|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
48-1269 |
0e+00 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 588.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 48 RLYMLVGTMAAIIHGAALPLMMLVFGnmtdsfanagisrnktfpVII-NESITNNTQHFInhleeemttyayyYSGIGAG 126
Cdd:PTZ00265 59 RKLLGVSFVCATISGGTLPFFVSVFG------------------VIMkNMNLGENVNDII-------------FSLVLIG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 127 VLVAAYIQVSFWCL-AAGRQILKIRK-QFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSIATFFT 204
Cdd:PTZ00265 108 IFQFILSFISSFCMdVVTTKILKTLKlEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 205 GFIVGFTRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLE 284
Cdd:PTZ00265 188 LYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 285 EAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTSLVLSS--------EYSIGQVLTVFFSVLIGAFSIGQASPSIEA 356
Cdd:PTZ00265 268 LYSKYILKANFMESLHIGMINGFILASYAFGFWYGTRIIISDlsnqqpnnDFHGGSVISILLGVLISMFMLTIILPNITE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 357 FANARGAAYEIFKIIDNKPSIDSySKSGHKPDNIKgNLEFKNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKS 436
Cdd:PTZ00265 348 YMKSLEATNSLYEIINRKPLVEN-NDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKS 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 437 TTVQLMQRLYDPTDGMVCI-DGQDIRTINVRHLREITGVVSQEPVLFATTIAENIRYG---------------------- 493
Cdd:PTZ00265 426 TILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsq 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 494 --------------------RENVTMDEIEKAVKEANA---------------YDFIMKLPNKFDTLVGERGAQLSGGQK 538
Cdd:PTZ00265 506 enknkrnscrakcagdlndmSNTTDSNELIEMRKNYQTikdsevvdvskkvliHDFVSALPDKYETLVGSNASKLSGGQK 585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 539 QRIAIARALVRNPKILLLDEATSALDTESEAVVQVALD--KARKGRTTIVIAHRLSTVRNADVI---------------- 600
Cdd:PTZ00265 586 QRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIfvlsnrergstvdvdi 665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 601 -------------------------------AGFDDGVIVEKGNHDELMKEK-GIYFKLVTMQ--------TRGNEIELE 640
Cdd:PTZ00265 666 igedptkdnkennnknnkddnnnnnnnnnnkINNAGSYIIEQGTHDALMKNKnGIYYTMINNQkvsskkssNNDNDKDSD 745
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 641 NATG---ESKSESDALEMS--PKDSGSSLIKRRSTRRSIH--APQGQDRKLGTKEDLNENVPPV-SFWRILKLNSTEWPY 712
Cdd:PTZ00265 746 MKSSaykDSERGYDPDEMNgnSKHENESASNKKSCKMSDEnaSENNAGGKLPFLRNLFKRKPKApNNLRIVYREIFSYKK 825
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 713 FVVGIFCAII-NGGLQPAFSIIFSRIIGIFTrdeDPETKRQNSNMFSVLFLVLGIISFITFFLQGFTFGKAGEILTKRLR 791
Cdd:PTZ00265 826 DVTIIALSILvAGGLYPVFALLYAKYVSTLF---DFANLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMK 902
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 792 YMVFRSMLRQDVSWFDDPKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIIS----------LIYGWQLTL 861
Cdd:PTZ00265 903 RRLFENILYQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSfyfcpivaavLTGTYFIFM 982
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 862 LLLAIVPIIAIAGVVEMKML--SGQAL---KDKKELEGAGKIATEAIENFRTVVSLTREQKFEYMYAQSLQVPYRNSLRK 936
Cdd:PTZ00265 983 RVFAIRARLTANKDVEKKEInqPGTVFaynSDDEIFKDPSFLIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRK 1062
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 937 AHIFGVSFSITQAMMYFSYAGCFRFGAYLVANEFMNFQDVLLVFSAIVFGAMAVGQVSSFAPDYAKAKVSAAHVIMIIEK 1016
Cdd:PTZ00265 1063 TLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIR 1142
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1017 SPLIDSYSPHGLK---PNTLEGNVTFNEVVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD--- 1090
Cdd:PTZ00265 1143 KSNIDVRDNGGIRiknKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkn 1222
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1091 ---------------------------------------------------PLAGSVLIDGKEIKHLNVQWLRAHLGIVS 1119
Cdd:PTZ00265 1223 dhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVS 1302
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1120 QEPILFDCSIAENIAYGDNSrvVSHEEIMQAAKEANIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHIL 1199
Cdd:PTZ00265 1303 QEPMLFNMSIYENIKFGKED--ATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKIL 1380
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1200 LLDEATSALDTESEKVVQEAL----DKAreGRTCIVIAHRLSTIQNADLIVVFQNGK-----VKEHGTHQQLL-AQKGIY 1269
Cdd:PTZ00265 1381 LLDEATSSLDSNSEKLIEKTIvdikDKA--DKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLsVQDGVY 1458
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
48-634 |
1.90e-179 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 542.06 E-value: 1.90e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 48 RLYMLVGTMAAIIHGAALPLMMLVFGNMTDSFANAGisrnktfpviinesitnNTQHFInhleeemtTYAYYYSGIGAGV 127
Cdd:COG1132 20 RGLLILALLLLLLSALLELLLPLLLGRIIDALLAGG-----------------DLSALL--------LLLLLLLGLALLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 128 LVAAYIQVSFWCLAAGRQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSIATFFTGFI 207
Cdd:COG1132 75 ALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 208 VGFTRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAK 287
Cdd:COG1132 155 VLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 288 RIGIKKAITANISIGAAFLLIYASYALAFWYGTSLVLSSEYSIGQVLTVFFSVLIGAFSIGQASPSIEAFANARGAAYEI 367
Cdd:COG1132 235 RANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 368 FKIIDNKPSIDSySKSGHKPDNIKGNLEFKNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD 447
Cdd:COG1132 315 FELLDEPPEIPD-PPGAVPLPPVRGEIEFENVSFSYPGDRPV--LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 448 PTDGMVCIDGQDIRTINVRHLREITGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPNKFDTLVG 527
Cdd:COG1132 392 PTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 528 ERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGV 607
Cdd:COG1132 472 ERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGR 551
|
570 580
....*....|....*....|....*..
gi 925114634 608 IVEKGNHDELMKEKGIYFKLVTMQTRG 634
Cdd:COG1132 552 IVEQGTHEELLARGGLYARLYRLQFGE 578
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
698-1279 |
3.88e-172 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 522.80 E-value: 3.88e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 698 SFWRILKLNSTEWPYFVVGIFCAIINGGLQPAFSIIFSRIIGIFTRDEDPETkrqnSNMFSVLFLVLGIISFITFFLQGF 777
Cdd:COG1132 8 LLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSA----LLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 778 TFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISLIYGW 857
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFD--RRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 858 QLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGAGKIATEAIENFRTVVSLTREQKFEYMYAQSLQVPYRNSLRKA 937
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 938 HIFGVSFSITQAMMYFSYAGCFRFGAYLVANEFMNFQDVLLVFSAIVFGAMAVGQVSSFAPDYAKAKVSAAHVIMIIEKS 1017
Cdd:COG1132 242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1018 PLIDSySPHGLKPNTLEGNVTFNEVVFNYPtrPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVL 1097
Cdd:COG1132 322 PEIPD-PPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1098 IDGKEIKHLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSHEEIMQAAKEANIHHFIETLPEKYNTRVGDKGTQ 1177
Cdd:COG1132 399 IDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPD--ATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVN 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1178 LSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHG 1257
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQG 556
|
570 580
....*....|....*....|..
gi 925114634 1258 THQQLLAQKGIYFSMVSVQAGA 1279
Cdd:COG1132 557 THEELLARGGLYARLYRLQFGE 578
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
51-367 |
1.48e-161 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 484.86 E-value: 1.48e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 51 MLVGTMAAIIHGAALPLMMLVFGNMTDSFANAGISRNKTfpviiNESITNNTQHFINHLEEEMTTYAYYYSGIGAGVLVA 130
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNITG-----NSSGLNSSAGPFEKLEEEMTLYAYYYLIIGAIVLIT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 131 AYIQVSFWCLAAGRQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSIATFFTGFIVGF 210
Cdd:cd18558 76 AYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 211 TRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIG 290
Cdd:cd18558 156 IRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNG 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 291 IKKAITANISIGAAFLLIYASYALAFWYGTSLVLSSEYSIGQVLTVFFSVLIGAFSIGQASPSIEAFANARGAAYEI 367
Cdd:cd18558 236 IKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1037-1276 |
3.79e-153 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 459.70 E-value: 3.79e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLG 1116
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1117 IVSQEPILFDCSIAENIAYGDNSRVVshEEIMQAAKEANIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQP 1196
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1197 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLAQKGIYFSMVSVQ 1276
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
395-631 |
1.32e-152 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 458.16 E-value: 1.32e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 395 EFKNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITGV 474
Cdd:cd03249 2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 475 VSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKIL 554
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 555 LLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQ 631
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
123-632 |
2.13e-145 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 457.37 E-value: 2.13e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 123 IGAGVLVAAYIQVSF-----WCLA-AGRQI-LKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDdVSKINEGIGDKIGMF 195
Cdd:COG2274 198 LAIGLLLALLFEGLLrllrsYLLLrLGQRIdLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRD-VESIREFLTGSLLTA 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 196 FQSIATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKE 275
Cdd:COG2274 277 LLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRF 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 276 LERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTSLVLSSEYSIGQVLTvfFSVLIGAF--SIGQASPS 353
Cdd:COG2274 357 RRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIA--FNILSGRFlaPVAQLIGL 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 354 IEAFANARGAAYEIFKIIDNKPSIDSYSKSGHKPdNIKGNLEFKNVHFSYPSRkEVKILKGLNLKVQSGQTVALVGNSGC 433
Cdd:COG2274 435 LQRFQDAKIALERLDDILDLPPEREEGRSKLSLP-RLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGS 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 434 GKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYD 513
Cdd:COG2274 513 GKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHD 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 514 FIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLST 593
Cdd:COG2274 593 FIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLST 672
|
490 500 510
....*....|....*....|....*....|....*....
gi 925114634 594 VRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQT 632
Cdd:COG2274 673 IRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
703-1020 |
5.38e-141 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 430.72 E-value: 5.38e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 703 LKLNSTEWPYFVVGIFCAIINGGLQPAFSIIFSRIIGIFTRDEDPETKRQnSNMFSVLFLVLGIISFITFFLQGFTFGKA 782
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSE-ANFWALMFLVLAIVAGIAYFLQGYLFGIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 783 GEILTKRLRYMVFRSMLRQDVSWFDDPKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISLIYGWQLTLL 862
Cdd:cd18578 80 GERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 863 LLAIVPIIAIAGVVEMKMLSGQALKDKKELEGAGKIATEAIENFRTVVSLTREQKFEYMYAQSLQVPYRNSLRKAHIFGV 942
Cdd:cd18578 160 GLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 943 SFSITQAMMYFSYAGCFRFGAYLVANEFMNFQDVLLVFSAIVFGAMAVGQVSSFAPDYAKAKVSAAHVIMIIEKSPLI 1020
Cdd:cd18578 240 GFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
141-628 |
1.99e-139 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 441.47 E-value: 1.99e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 141 AAGRQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSIATFFTGFIVGFTRGWKLTLVI 220
Cdd:TIGR00958 228 TMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVT 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 221 LAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANIS 300
Cdd:TIGR00958 308 LINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGY 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 301 IGAAFLLIYASYALAFWYGTSLVLSSEYSIGQVLtvffSVLIGAFSIGQASPSIEAFAN----ARGAAYEIFKIIDNKPS 376
Cdd:TIGR00958 388 LWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLV----SFLLYQEQLGEAVRVLSYVYSgmmqAVGASEKVFEYLDRKPN 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 377 IDSysKSGHKPDNIKGNLEFKNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCID 456
Cdd:TIGR00958 464 IPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 457 GQDIRTINVRHLREITGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPNKFDTLVGERGAQLSGG 536
Cdd:TIGR00958 542 GVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGG 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 537 QKQRIAIARALVRNPKILLLDEATSALDTESEAVVQValDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDE 616
Cdd:TIGR00958 622 QKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQ 699
|
490
....*....|..
gi 925114634 617 LMKEKGIYFKLV 628
Cdd:TIGR00958 700 LMEDQGCYKHLV 711
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
692-1277 |
2.77e-134 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 427.71 E-value: 2.77e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 692 ENVPPVSFWRILKLNSTEWPYFVVGIFCAIINGGLQ---PAFS-IIFSRIIGiftrdedpeTKRQNS-NMFSVLFLVLGI 766
Cdd:COG2274 137 RGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLAlatPLFTqVVIDRVLP---------NQDLSTlWVLAIGLLLALL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 767 ISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLaNDAAQVKGAIGSRLAVITQNIANLG 846
Cdd:COG2274 208 FEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFE--SRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 847 TGIIISLIYGWQLTLLLLAIVPIIAIAGVV---EMKMLSGQALKDKKELEGagkIATEAIENFRTVVSLTREQKFEYMYA 923
Cdd:COG2274 285 IFLIVLFFYSPPLALVVLLLIPLYVLLGLLfqpRLRRLSREESEASAKRQS---LLVETLRGIETIKALGAESRFRRRWE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 924 QSLQVPYRNSLRKAHIFGVSFSITQAMMYFSYAGCFRFGAYLVANEFMNFqDVLLVFSAIVFGAMA-VGQVSSFAPDYAK 1002
Cdd:COG2274 362 NLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTL-GQLIAFNILSGRFLApVAQLIGLLQRFQD 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1003 AKVSAAHVIMIIEKsPLIDSYSPHGLKPNTLEGNVTFNEVVFNYPTRpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVV 1082
Cdd:COG2274 441 AKIALERLDDILDL-PPEREEGRSKLSLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLL 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1083 QLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSHEEIMQAAKEANIHHFIET 1162
Cdd:COG2274 519 KLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPD--ATDEEIIEAARLAGLHDFIEA 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1163 LPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNA 1242
Cdd:COG2274 597 LPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLA 676
|
570 580 590
....*....|....*....|....*....|....*
gi 925114634 1243 DLIVVFQNGKVKEHGTHQQLLAQKGIYFSMVSVQA 1277
Cdd:COG2274 677 DRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
713-1010 |
4.71e-134 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 412.44 E-value: 4.71e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 713 FVVGIFCAIINGGLQPAFSIIFSRIIGIFT----------------RDEDPETKRQNSNMFSVLFLVLGIISFITFFLQG 776
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTnggmtnitgnssglnsSAGPFEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 777 FTFGKAGEILTKRLRYMVFRSMLRQDVSWFddPKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISLIYG 856
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWF--DVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 857 WQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGAGKIATEAIENFRTVVSLTREQKFEYMYAQSLQVPYRNSLRK 936
Cdd:cd18558 159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 937 AHIFGVSFSITQAMMYFSYAGCFRFGAYLV-ANEFMNFQDVLLVFSAIVFGAMAVGQVSSFAPdYAKAKVSAAHV 1010
Cdd:cd18558 239 AITFNISMGAAFLLIYASYALAFWYGTYLVtQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEA-FANARGAAYHI 312
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
103-631 |
1.21e-131 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 416.02 E-value: 1.21e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 103 QHFINHLEEEMTTYAYYYSGIGAGVLVAAYIQVSFWCLAAGRQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVS 182
Cdd:TIGR02204 47 HGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 183 KINEGIGDKIGMFFQSIATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAA 262
Cdd:TIGR02204 127 LLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 263 IRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTSLVLSSEYSIGQVLTVFFSVLI 342
Cdd:TIGR02204 207 IRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVM 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 343 GAFSIGQASPSIEAFANARGAAYEIFKIIDNKPSIDSYSKSGHKPDNIKGNLEFKNVHFSYPSRKEVKILKGLNLKVQSG 422
Cdd:TIGR02204 287 VAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 423 QTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITGVVSQEPVLFATTIAENIRYGRENVTMDEI 502
Cdd:TIGR02204 367 ETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEV 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 503 EKAVKEANAYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGR 582
Cdd:TIGR02204 447 EAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGR 526
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 925114634 583 TTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQ 631
Cdd:TIGR02204 527 TTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
51-367 |
3.45e-129 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 399.16 E-value: 3.45e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 51 MLVGTMAAIIHGAALPLMMLVFGNMTDSFANAGISRNKTfpviinesitnntqhfiNHLEEEMTTYAYYYSGIGAGVLVA 130
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSP-----------------DEFLDDVNKYALYFVYLGIGSFVL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 131 AYIQVSFWCLAAGRQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSIATFFTGFIVGF 210
Cdd:cd18577 64 SYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 211 TRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIG 290
Cdd:cd18577 144 IYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAG 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 291 IKKAITANISIGAAFLLIYASYALAFWYGTSLVLSSEYSIGQVLTVFFSVLIGAFSIGQASPSIEAFANARGAAYEI 367
Cdd:cd18577 224 IKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
677-1273 |
3.42e-125 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 403.33 E-value: 3.42e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 677 PQGQDRKLGTKEDLNeNVPPVsfWRILKLNSTEWPYFVVGIF---CAIINGGLQPAFSiifSRIIGIFTRDEDPETkrqn 753
Cdd:TIGR00958 130 SAGASEKEAEQGQSE-TADLL--FRLLGLSGRDWPWLISAFVfltLSSLGEMFIPFYT---GRVIDTLGGDKGPPA---- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 754 snmFSVLFLVLGIISFITFFLQGF---TFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGA 830
Cdd:TIGR00958 200 ---LASAIFFMCLLSIASSVSAGLrggSFNYTMARINLRIREDLFRSLLRQDLGFFD--ENKTGELTSRLSSDTQTMSRS 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 831 IGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGAGKIATEAIENFRTVV 910
Cdd:TIGR00958 275 LSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVR 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 911 SLTRE----QKFEYMYAQSLQVPYRNSLRKAhifgVSFSITQAMMYFSYAGCFRFGAYLVANEFMNfQDVLLVFsaiVFG 986
Cdd:TIGR00958 355 SFAAEegeaSRFKEALEETLQLNKRKALAYA----GYLWTTSVLGMLIQVLVLYYGGQLVLTGKVS-SGNLVSF---LLY 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 987 AMAVGQ----VSSFAPDYAKAKVSAAHVIMIIEKSPLIDSysPHGLKPNTLEGNVTFNEVVFNYPTRPDIPVLQGLSLEV 1062
Cdd:TIGR00958 427 QEQLGEavrvLSYVYSGMMQAVGASEKVFEYLDRKPNIPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTL 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1063 KKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvV 1142
Cdd:TIGR00958 505 HPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTD--T 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1143 SHEEIMQAAKEANIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEalDK 1222
Cdd:TIGR00958 583 PDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SR 660
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 925114634 1223 AREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLAQKGIYFSMV 1273
Cdd:TIGR00958 661 SRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
129-633 |
2.30e-118 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 380.60 E-value: 2.30e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 129 VAAYIQVSFWCLAAGRQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSIATFFTGFIV 208
Cdd:TIGR02203 69 ICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 209 GFTRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKR 288
Cdd:TIGR02203 149 LLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 289 IGIKKAITANISIGAAFLLIYASYALAFWYGTSLVLSSEYSIGQvLTVFFSvligafSIGQASPSIEAFANARG------ 362
Cdd:TIGR02203 229 LAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGD-FTAFIT------AMIALIRPLKSLTNVNApmqrgl 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 363 -AAYEIFKIIDNKPSIDsysKSGHKPDNIKGNLEFKNVHFSYPSRkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQL 441
Cdd:TIGR02203 302 aAAESLFTLLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNL 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 442 MQRLYDPTDGMVCIDGQDIRTINVRHLREITGVVSQEPVLFATTIAENIRYGR-ENVTMDEIEKAVKEANAYDFIMKLPN 520
Cdd:TIGR02203 378 IPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPL 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 521 KFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVI 600
Cdd:TIGR02203 458 GLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRI 537
|
490 500 510
....*....|....*....|....*....|...
gi 925114634 601 AGFDDGVIVEKGNHDELMKEKGIYFKLVTMQTR 633
Cdd:TIGR02203 538 VVMDDGRIVERGTHNELLARNGLYAQLHNMQFR 570
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
756-1276 |
5.39e-116 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 374.04 E-value: 5.39e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 756 MFSVLFLVLGIISFITFFLqgftFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRL 835
Cdd:TIGR02204 63 FLLVVALVLALGTAARFYL----VTWLGERVVADIRRAVFAHLISLSPSFFD--KNRSGEVVSRLTTDTTLLQSVIGSSL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 836 AVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGAGKIATEAIENFRTVVSLTRE 915
Cdd:TIGR02204 137 SMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 916 QKFEYMYAQSLQVPYRNSLRKAHIFGVSFSITQAMMYFSYAGCFRFGAYLV------ANEFMNFqdvllVFSAiVFGAMA 989
Cdd:TIGR02204 217 DAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDViagkmsAGTLGQF-----VFYA-VMVAGS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 990 VGQVSSFAPDYAKAKVSAAHVIMIIEKSPLIDSYSPHGLKPNTLEGNVTFNEVVFNYPTRPDIPVLQGLSLEVKKGQTLA 1069
Cdd:TIGR02204 291 IGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1070 LVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPILFDCSIAENIAYG--DNSRvvshEEI 1147
Cdd:TIGR02204 371 LVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGrpDATD----EEV 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1148 MQAAKEANIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGR 1227
Cdd:TIGR02204 447 EAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGR 526
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 925114634 1228 TCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLAQKGIYFSMVSVQ 1276
Cdd:TIGR02204 527 TTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
135-631 |
8.43e-115 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 371.27 E-value: 8.43e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 135 VSFWCLA--AGRQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDD------------VSKINEG---IGDKIGMFFQ 197
Cdd:PRK11176 84 ISSYCISwvSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDseqvassssgalITVVREGasiIGLFIMMFYY 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 198 SiatfftgfivgftrgWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELE 277
Cdd:PRK11176 164 S---------------WQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 278 RYNKNLEEAKRIGIKKAITANISIGAAFLLiyASYALAFwygtSLVLSSEYSIGQVL-----TVFFSVLIGAFSIGQASP 352
Cdd:PRK11176 229 RFDKVSNRMRQQGMKMVSASSISDPIIQLI--ASLALAF----VLYAASFPSVMDTLtagtiTVVFSSMIALMRPLKSLT 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 353 SIEA-FANARGAAYEIFKIIDNKPSIDSyskSGHKPDNIKGNLEFKNVHFSYPSrKEVKILKGLNLKVQSGQTVALVGNS 431
Cdd:PRK11176 303 NVNAqFQRGMAACQTLFAILDLEQEKDE---GKRVIERAKGDIEFRNVTFTYPG-KEVPALRNINFKIPAGKTVALVGRS 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 432 GCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITGVVSQEPVLFATTIAENIRYGRENV-TMDEIEKAVKEAN 510
Cdd:PRK11176 379 GSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAY 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 511 AYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHR 590
Cdd:PRK11176 459 AMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHR 538
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 925114634 591 LSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQ 631
Cdd:PRK11176 539 LSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
265-638 |
1.40e-112 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 366.07 E-value: 1.40e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 265 TVIAFGGQKKELERYNKNLEEAKRIGIKKAITAN-ISIGAAfLLIYASYALAFWYGTSLVLSSEYSIGQVltvffsVLIG 343
Cdd:COG5265 230 TVKYFGNEAREARRYDEALARYERAAVKSQTSLAlLNFGQA-LIIALGLTAMMLMAAQGVVAGTMTVGDF------VLVN 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 344 AFSIGQASPsieafANARGAAY-EI----------FKIIDNKPSIdsYSKSGHKPDNIK-GNLEFKNVHFSY-PSRKevk 410
Cdd:COG5265 303 AYLIQLYIP-----LNFLGFVYrEIrqaladmermFDLLDQPPEV--ADAPDAPPLVVGgGEVRFENVSFGYdPERP--- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 411 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITGVVSQEPVLFATTIAENI 490
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNI 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 491 RYGRENVTMDEIEKAVKEANAYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAV 570
Cdd:COG5265 453 AYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERA 532
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 571 VQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQTRGNEIE 638
Cdd:COG5265 533 IQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEAE 600
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
394-627 |
6.29e-110 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 344.60 E-value: 6.29e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITG 473
Cdd:cd03251 1 VEFKNVTFRYPG-DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKI 553
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 925114634 554 LLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKL 627
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
698-1276 |
7.67e-109 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 354.79 E-value: 7.67e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 698 SFWRILKLNSTEWPYFVVGIFCAIINGGLQPAFSIIFSRIIGIFTRDEDPETKRQNSNMFSVLFLVLGIISFITFFLQGF 777
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 778 TFGKageiLTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISLIYGW 857
Cdd:TIGR02203 81 VSNK----VVRDIRVRMFEKLLGLPVSFFD--RQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 858 QLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGAGKIATEAIENFRTVVSLTREQKFEYMYAQSLQVPYRNSLRKA 937
Cdd:TIGR02203 155 QLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 938 HIFGVSFSITQ-----AMMYFSYAGCFRFGA-YLVANEFMNF-QDVLLVFSAIvfgamavGQVSSFAPDYAKAKVSAAHV 1010
Cdd:TIGR02203 235 SAGSISSPITQliaslALAVVLFIALFQAQAgSLTAGDFTAFiTAMIALIRPL-------KSLTNVNAPMQRGLAAAESL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1011 IMIIEKSPLIDSyspHGLKPNTLEGNVTFNEVVFNYPTRpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD 1090
Cdd:TIGR02203 308 FTLLDSPPEKDT---GTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1091 PLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSRVVShEEIMQAAKEANIHHFIETLPEKYNTR 1170
Cdd:TIGR02203 384 PDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADR-AEIERALAAAYAQDFVDKLPLGLDTP 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1171 VGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQN 1250
Cdd:TIGR02203 463 IGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDD 542
|
570 580
....*....|....*....|....*.
gi 925114634 1251 GKVKEHGTHQQLLAQKGIYFSMVSVQ 1276
Cdd:TIGR02203 543 GRIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1037-1269 |
9.07e-107 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 336.13 E-value: 9.07e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPTRPDiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLG 1116
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1117 IVSQEPILFDCSIAENIAYGDnsRVVSHEEIMQAAKEANIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQP 1196
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGR--PGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 1197 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLAQKGIY 1269
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVY 230
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1034-1281 |
1.09e-104 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 344.50 E-value: 1.09e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1034 EGNVTFNEVVFNYptRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRA 1113
Cdd:COG5265 355 GGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1114 HLGIVSQEPILFDCSIAENIAYGDNSrvVSHEEIMQAAKEANIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALV 1193
Cdd:COG5265 433 AIGIVPQDTVLFNDTIAYNIAYGRPD--ASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLL 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1194 RQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLAQKGIYFSMV 1273
Cdd:COG5265 511 KNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMW 590
|
....*...
gi 925114634 1274 SVQAGAKR 1281
Cdd:COG5265 591 ARQQEEEE 598
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
394-631 |
5.76e-103 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 326.11 E-value: 5.76e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITG 473
Cdd:cd03253 1 IEFENVTFAYDPGR--PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKI 553
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 554 LLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQ 631
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
392-622 |
9.43e-101 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 319.56 E-value: 9.43e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 392 GNLEFKNVHFSYpsRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREI 471
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 472 TGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNP 551
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 925114634 552 KILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKG 622
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1037-1276 |
1.26e-100 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 319.56 E-value: 1.26e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPtrPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLG 1116
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1117 IVSQEPILFDCSIAENIAYGDNSrvVSHEEIMQAAKEANIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQP 1196
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPD--ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1197 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLAQKGIYFSMVSVQ 1276
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
141-622 |
1.54e-99 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 329.03 E-value: 1.54e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 141 AAGRQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSIATFFTGFIVGFTRGWKLTLVI 220
Cdd:COG4988 85 AAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLIL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 221 LAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANIS 300
Cdd:COG4988 165 LVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRVAFLS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 301 IGAAFLLIYASYALAfwygtSLVLSSEYSIGQV-LTVFFSVLIgafsigqASPsiEAF-------------ANARGAAYE 366
Cdd:COG4988 245 SAVLEFFASLSIALV-----AVYIGFRLLGGSLtLFAALFVLL-------LAP--EFFlplrdlgsfyharANGIAAAEK 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 367 IFKIIDNKPSIdsySKSGHKPDNIKGN--LEFKNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQR 444
Cdd:COG4988 311 IFALLDAPEPA---APAGTAPLPAAGPpsIELEDVSFSYPGGRPA--LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLG 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 445 LYDPTDGMVCIDGQDIRTINVRHLREITGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPNKFDT 524
Cdd:COG4988 386 FLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDT 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 525 LVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFD 604
Cdd:COG4988 466 PLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLD 545
|
490
....*....|....*...
gi 925114634 605 DGVIVEKGNHDELMKEKG 622
Cdd:COG4988 546 DGRIVEQGTHEELLAKNG 563
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
295-631 |
5.13e-98 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 325.76 E-value: 5.13e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 295 ITANISIGAAFLLiyasyalafwyGTSLVLSSEYSIGQVLTV--FFSVLIGAFSigqaspSIEAFAN----ARGAAYEIF 368
Cdd:PRK13657 248 AASTITMLAILVL-----------GAALVQKGQLRVGEVVAFvgFATLLIGRLD------QVVAFINqvfmAAPKLEEFF 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 369 KIIDNKPSIDSYSKSGhKPDNIKGNLEFKNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDP 448
Cdd:PRK13657 311 EVEDAVPDVRDPPGAI-DLGRVKGAVEFDDVSFSYDNSRQG--VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDP 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 449 TDGMVCIDGQDIRTINVRHLREITGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPNKFDTLVGE 528
Cdd:PRK13657 388 QSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 529 RGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVI 608
Cdd:PRK13657 468 RGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRV 547
|
330 340
....*....|....*....|...
gi 925114634 609 VEKGNHDELMKEKGIYFKLVTMQ 631
Cdd:PRK13657 548 VESGSFDELVARGGRFAALLRAQ 570
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1035-1267 |
1.02e-96 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 308.77 E-value: 1.02e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1035 GNVTFNEVVFNYptRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAH 1114
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1115 LGIVSQEPILFDCSIAENIAYGDNSrvVSHEEIMQAAKEANIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVR 1194
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPN--ATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 1195 QPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLAQKG 1267
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
759-1278 |
3.75e-94 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 314.65 E-value: 3.75e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 759 VLFLVLGIISFITFFLQGFTFGKageiLTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVI 838
Cdd:PRK11176 73 GLMILRGITSFISSYCISWVSGK----VVMTMRRRLFGHMMGMPVSFFD--KQSTGTLLSRITYDSEQVASSSSGALITV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 839 TQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIA-GVVE-------------MKMLSG---QALKDKKELEGAGKIATE 901
Cdd:PRK11176 147 VREGASIIGLFIMMFYYSWQLSLILIVIAPIVSIAiRVVSkrfrnisknmqntMGQVTTsaeQMLKGHKEVLIFGGQEVE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 902 aIENFRTVVSLTREQKFEYMYAQSLQVPyrnslrkahifgvsfsITQAMMYFSYAgcfrfgAYLVANEFMNFQDVL---- 977
Cdd:PRK11176 227 -TKRFDKVSNRMRQQGMKMVSASSISDP----------------IIQLIASLALA------FVLYAASFPSVMDTLtagt 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 978 --LVFSAIvFGAM----AVGQVSSfapDYAKAKVSAAHVIMIIEKSPLIDSYSphgLKPNTLEGNVTFNEVVFNYPTRpD 1051
Cdd:PRK11176 284 itVVFSSM-IALMrplkSLTNVNA---QFQRGMAACQTLFAILDLEQEKDEGK---RVIERAKGDIEFRNVTFTYPGK-E 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1052 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPILFDCSIAE 1131
Cdd:PRK11176 356 VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIAN 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1132 NIAYGDNSRVvSHEEIMQAAKEANIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1211
Cdd:PRK11176 436 NIAYARTEQY-SREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTE 514
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1212 SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLAQKGIYFSMVSVQAG 1278
Cdd:PRK11176 515 SERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQFG 581
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
141-627 |
3.66e-91 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 305.92 E-value: 3.66e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 141 AAGRQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVskinegigDKIGMFF-QSIATFFTGFIVGFTrgwkLTLV 219
Cdd:COG4987 82 ATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADV--------DALDNLYlRVLLPLLVALLVILA----AVAF 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 220 ILAISPVLGLS-------AAIWAKILSSFTDK---ELLAYAKAGAVAE--EVLAAIRTVIAFGGQKKELERYN---KNLE 284
Cdd:COG4987 150 LAFFSPALALVlalglllAGLLLPLLAARLGRragRRLAAARAALRARltDLLQGAAELAAYGALDRALARLDaaeARLA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 285 EAKRigiKKAITANISIGAAFLLIYASYALAFWYGTSLVLSSEYSIGQVLTVFFSVLiGAFSIgqASPSIEAFAN---AR 361
Cdd:COG4987 230 AAQR---RLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAAL-ALFEA--LAPLPAAAQHlgrVR 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 362 GAAYEIFKIIDNKPSIDSYSKSGHKPDNikGNLEFKNVHFSYPSRKEvKILKGLNLKVQSGQTVALVGNSGCGKSTTVQL 441
Cdd:COG4987 304 AAARRLNELLDAPPAVTEPAEPAPAPGG--PSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLAL 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 442 MQRLYDPTDGMVCIDGQDIRTINVRHLREITGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPNK 521
Cdd:COG4987 381 LLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDG 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 522 FDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIA 601
Cdd:COG4987 461 LDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRIL 540
|
490 500
....*....|....*....|....*.
gi 925114634 602 GFDDGVIVEKGNHDELMKEKGIYFKL 627
Cdd:COG4987 541 VLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
701-1267 |
3.90e-91 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 305.53 E-value: 3.90e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 701 RILKLNSTEWPYFVVGIFCAIINGGLQPAFSIIFSRII-GIFTRDEDPEtkrQNSNMFSVLFLVLGIISFITFFLQGFTF 779
Cdd:COG4988 7 RLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLaGLIIGGAPLS---ALLPLLGLLLAVLLLRALLAWLRERAAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 780 gKAGEILTKRLRYMVFRSMLRQDVSWFDDPKntTGALTTRLANDAAQVKGAIG-----SRLAVITQnianLGTGIIISLI 854
Cdd:COG4988 84 -RAAARVKRRLRRRLLEKLLALGPAWLRGKS--TGELATLLTEGVEALDGYFArylpqLFLAALVP----LLILVAVFPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 855 YgWQLTLLLLAIVPII----AIAGV----------VEMKMLSGQALKDKKELE-----GAGKIATEAI----ENFRTvvs 911
Cdd:COG4988 157 D-WLSGLILLVTAPLIplfmILVGKgaakasrrqwRALARLSGHFLDRLRGLTtlklfGRAKAEAERIaeasEDFRK--- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 912 ltreqkfeymyaQSLQVpyrnsLRKAhiFGVSFsITQAMMYFSYAgcfrfgayLVAnefmnfqdVLLVFSAI-----VFG 986
Cdd:COG4988 233 ------------RTMKV-----LRVA--FLSSA-VLEFFASLSIA--------LVA--------VYIGFRLLggsltLFA 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 987 AMAV-----------GQVSSFapdY-AKAK-VSAAHVIMIIEKSPLIDSYSPHGLKPNTLEGNVTFNEVVFNYPTRPdiP 1053
Cdd:COG4988 277 ALFVlllapefflplRDLGSF---YhARANgIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGR--P 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPILFDCSIAENI 1133
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENL 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1134 AYGDnsRVVSHEEIMQAAKEANIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESE 1213
Cdd:COG4988 432 RLGR--PDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETE 509
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 925114634 1214 KVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLAQKG 1267
Cdd:COG4988 510 AEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1028-1253 |
6.87e-89 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 287.06 E-value: 6.87e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1028 LKPNTLEGNVTFNEVVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLN 1107
Cdd:cd03248 3 LAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1108 VQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSHEEIMQAAKEANIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIA 1187
Cdd:cd03248 83 HKYLHSKVSLVGQEPVLFARSLQDNIAYGLQS--CSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 1188 IARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGKV 1253
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
152-632 |
6.54e-88 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 300.89 E-value: 6.54e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 152 QFFHAIMRQEIGWFDVHDVGELNTRLTDdVSKINEGIGDKIGMFFQSIATFFTGFIVGFTRGWKLTLVILAISPVLGLSA 231
Cdd:TIGR01846 217 RLYRHLLGLPLGYFESRRVGDTVARVRE-LEQIRNFLTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLS 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 232 AIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYAS 311
Cdd:TIGR01846 296 VFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLT 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 312 YALAFWYGTSLVLSSEYSIGQVltVFFSVLIGAFS--IGQASPSIEAFANARGAAYEIFKIIdNKPSiDSYSKSGHKPDN 389
Cdd:TIGR01846 376 FAILLWFGAHLVIGGALSPGQL--VAFNMLAGRVTqpVLRLAQLWQDFQQTGIALERLGDIL-NSPT-EPRSAGLAALPE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 390 IKGNLEFKNVHFSY-PSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHL 468
Cdd:TIGR01846 452 LRGAITFENIRFRYaPDSPEV--LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWL 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 469 REITGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALV 548
Cdd:TIGR01846 530 RRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALV 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 549 RNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLV 628
Cdd:TIGR01846 610 GNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLW 689
|
....
gi 925114634 629 TMQT 632
Cdd:TIGR01846 690 QQQS 693
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
786-1274 |
3.95e-86 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 292.06 E-value: 3.95e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 786 LTKRLRYMVFRSMLRQDVSWFDDPKntTGALTTRLANDAAQVKGAIgsrLAVITQNIANLGTGIIISLIYGWQLTLLLLA 865
Cdd:COG4987 86 LLADLRVRLYRRLEPLAPAGLARLR--SGDLLNRLVADVDALDNLY---LRVLLPLLVALLVILAAVAFLAFFSPALALV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 866 IVPIIAIAGVVE---MKMLSGQALKDKKELEGAGKI-ATEAIENFRTVVSLTREQKFEYMYAQSLQVPYRNSLRKAHIFG 941
Cdd:COG4987 161 LALGLLLAGLLLpllAARLGRRAGRRLAAARAALRArLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 942 VSFSITQAMMYFSYAGCFRFGAYLVANEFMNfqDVLLVfsAIVFGAMA----VGQVSSFAPDYAKAKVSAAHVIMIIEKS 1017
Cdd:COG4987 241 LAQALLQLAAGLAVVAVLWLAAPLVAAGALS--GPLLA--LLVLAALAlfeaLAPLPAAAQHLGRVRAAARRLNELLDAP 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1018 PLIDSysPHGLKPNTLEGNVTFNEVVFNYPTRPDiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVL 1097
Cdd:COG4987 317 PAVTE--PAEPAPAPGGPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSIT 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1098 IDGKEIKHLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSHEEIMQAAKEANIHHFIETLPEKYNTRVGDKGTQ 1177
Cdd:COG4987 394 LGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPD--ATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRR 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1178 LSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHG 1257
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQG 551
|
490
....*....|....*..
gi 925114634 1258 THQQLLAQKGIYFSMVS 1274
Cdd:COG4987 552 THEELLAQNGRYRQLYQ 568
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
44-377 |
4.93e-86 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 282.80 E-value: 4.93e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 44 NWLDRLYMLVGTMAAIIHGAALPLMMLVFGNMTDSFANAGISrnktfpviinesitnntqhfinHLEEEMTTYAYYYSGI 123
Cdd:cd18578 4 NKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDD----------------------ELRSEANFWALMFLVL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 124 GAGVLVAAYIQVSFWCLAAGRQILKIRKQFFHAIMRQEIGWFD--VHDVGELNTRLTDDVSKINEGIGDKIGMFFQSIAT 201
Cdd:cd18578 62 AIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 202 FFTGFIVGFTRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNK 281
Cdd:cd18578 142 LVAGLIIAFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 282 NLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTSLVLSSEYSIGQVLTVFFSVLIGAFSIGQASPSIEAFANAR 361
Cdd:cd18578 222 ALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAK 301
|
330
....*....|....*.
gi 925114634 362 GAAYEIFKIIDNKPSI 377
Cdd:cd18578 302 AAAARIFRLLDRKPEI 317
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
394-631 |
6.61e-84 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 273.59 E-value: 6.61e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITG 473
Cdd:cd03252 1 ITFEHVRFRYKP-DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKI 553
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 554 LLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQ 631
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
851-1267 |
1.85e-83 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 284.93 E-value: 1.85e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 851 ISLIYGWQLTLLLLAIVPI-IAIAGVVEMKMLSGQAlkdkkELE----GAGKIATEAIENFRTVVSLTREQKfeymYAQS 925
Cdd:PRK13657 150 LALFMNWRLSLVLVVLGIVyTLITTLVMRKTKDGQA-----AVEehyhDLFAHVSDAIGNVSVVQSYNRIEA----ETQA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 926 LQvPYRNSLRKAHI-----FGVSFSITQAMMYFSYAGCFRFGAYLVANEFMNFQDVLlvfSAIVFGAMAVG---QVSSFA 997
Cdd:PRK13657 221 LR-DIADNLLAAQMpvlswWALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVV---AFVGFATLLIGrldQVVAFI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 998 PDYAKAKVSAAHVIMIIEKSPLIDSySPHGLKPNTLEGNVTFNEVVFNYPTRPdiPVLQGLSLEVKKGQTLALVGSSGCG 1077
Cdd:PRK13657 297 NQVFMAAPKLEEFFEVEDAVPDVRD-PPGAIDLGRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAG 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1078 KSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSHEEIMQAAKEANIH 1157
Cdd:PRK13657 374 KSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPD--ATDEEMRAAAERAQAH 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1158 HFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLS 1237
Cdd:PRK13657 452 DFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLS 531
|
410 420 430
....*....|....*....|....*....|
gi 925114634 1238 TIQNADLIVVFQNGKVKEHGTHQQLLAQKG 1267
Cdd:PRK13657 532 TVRNADRILVFDNGRVVESGSFDELVARGG 561
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
713-1010 |
5.03e-83 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 273.58 E-value: 5.03e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 713 FVVGIFCAIINGGLQPAFSIIFSRIIGIFTR----DEDPETKRQNSNMFSVLFLVLGIISFITFFLQGFTFGKAGEILTK 788
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDfgsgESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 789 RLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVP 868
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFD--KNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 869 IIAIAGVVEMKMLSGQALKDKKELEGAGKIATEAIENFRTVVSLTREQKFEYMYAQSLQVPYRNSLRKAHIFGVSFSITQ 948
Cdd:cd18577 159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 949 AMMYFSYAGCFRFGAYLVANEFMNFQDVLLVFSAIVFGAMAVGQVSSFAPDYAKAKVSAAHV 1010
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
51-345 |
1.84e-82 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 271.05 E-value: 1.84e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 51 MLVGTMAAIIHGAALPLMMLVFGNMTDSFanagisrnktfpviinesITNNTQHFinhleEEMTTYAYYYSGIGAGVLVA 130
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVL------------------LPDGDPET-----QALNVYSLALLLLGLAQFIL 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 131 AYIQVSFWCLAAGRQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSIATFFTGFIVGF 210
Cdd:pfam00664 58 SFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 211 TRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIG 290
Cdd:pfam00664 138 YYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAG 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 291 IKKAITANISIGAAFLLIYASYALAFWYGTSLVLSSEYSIGQ--VLTVFFSVLIGAF 345
Cdd:pfam00664 218 IKKAVANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
387-608 |
1.44e-81 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 266.64 E-value: 1.44e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 387 PDNIKGNLEFKNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVR 466
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 467 HLREITGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARA 546
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 547 LVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVI 608
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1037-1276 |
3.38e-81 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 265.89 E-value: 3.38e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYptRPDIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHL 1115
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1116 GIVSQEPILFDCSIAENIAYGDNSrvVSHEEIMQAAKEANIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQ 1195
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPG--MSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1196 PHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLAQKGIYFSMVSV 1275
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236
|
.
gi 925114634 1276 Q 1276
Cdd:cd03252 237 Q 237
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
394-606 |
9.72e-80 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 259.24 E-value: 9.72e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITG 473
Cdd:cd03228 1 IEFKNVSFSYPGR-PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFATTIAENIrygrenvtmdeiekavkeanaydfimklpnkfdtlvgergaqLSGGQKQRIAIARALVRNPKI 553
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 925114634 554 LLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDG 606
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1037-1252 |
2.27e-79 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 258.08 E-value: 2.27e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPTRPDiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLG 1116
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1117 IVSQEPILFDCSIAENIaygdnsrvvsheeimqaakeanihhfietlpekyntrvgdkgtqLSGGQKQRIAIARALVRQP 1196
Cdd:cd03228 80 YVPQDPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 1197 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGK 1252
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
696-1269 |
2.29e-77 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 271.05 E-value: 2.29e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 696 PVSFWRILK--LNSTE--WPYFVVGIFCAIINGGLQPAFSIIFSRIIGIftrdedpetkRQNSNMFSVLFLVLGIISFIT 771
Cdd:TIGR03796 138 KPSLLRALWrrLRGSRgaLLYLLLAGLLLVLPGLVIPAFSQIFVDEILV----------QGRQDWLRPLLLGMGLTALLQ 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 772 FFLQGFtfgkageiltkRLRYMV--------------FRSMLRQDVSWFDdpKNTTGALTTRLANdAAQVKGAIGSRLAV 837
Cdd:TIGR03796 208 GVLTWL-----------QLYYLRrleiklavgmsarfLWHILRLPVRFFA--QRHAGDIASRVQL-NDQVAEFLSGQLAT 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 838 ITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGAGKIATEAIENFRTVVSLTREQK 917
Cdd:TIGR03796 274 TALDAVMLVFYALLMLLYDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKASGLESD 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 918 FEYMYA--QSLQVPYRNSL-RKAHIFGVsfsITQAMMYFSYAGCFRFGAYLVANEFMN------FQDVLLVFSAIVFGAM 988
Cdd:TIGR03796 354 FFSRWAgyQAKLLNAQQELgVLTQILGV---LPTLLTSLNSALILVVGGLRVMEGQLTigmlvaFQSLMSSFLEPVNNLV 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 989 AVGQ-VSSFAPDYAKAK-VSAAHVIMIIEKSPLIDSYSPHGLKpntLEGNVTFNEVVFNYpTRPDIPVLQGLSLEVKKGQ 1066
Cdd:TIGR03796 431 GFGGtLQELEGDLNRLDdVLRNPVDPLLEEPEGSAATSEPPRR---LSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQ 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1067 TLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSHEE 1146
Cdd:TIGR03796 507 RVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPT--IPDAD 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1147 IMQAAKEANIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALdkAREG 1226
Cdd:TIGR03796 585 LVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL--RRRG 662
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 925114634 1227 RTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLAQKGIY 1269
Cdd:TIGR03796 663 CTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAY 705
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
319-628 |
5.68e-77 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 266.75 E-value: 5.68e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 319 GTSLVLSSEYSIGQVLTV--FFSVLIGafSIGQASPSIEAFANARGAAYEIFKIIDNKPSIDSYSKSGHKPdNIKGNLEF 396
Cdd:TIGR01192 261 GTVLVIKGELSVGEVIAFigFANLLIG--RLDQMSGFITQIFEARAKLEDFFDLEDSVFQREEPADAPELP-NVKGAVEF 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 397 KNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITGVVS 476
Cdd:TIGR01192 338 RHITFEFANSSQG--VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVF 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 477 QEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLL 556
Cdd:TIGR01192 416 QDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVL 495
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 557 DEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLV 628
Cdd:TIGR01192 496 DEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLL 567
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
981-1278 |
9.20e-76 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 266.22 E-value: 9.20e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 981 SAIVFGAMAVGQVSSF--------AP---------DYAKAKVSAAHVIMIIEkSPlIDSYSPHGLKPNTLEGNVTFNEVV 1043
Cdd:TIGR01846 385 HLVIGGALSPGQLVAFnmlagrvtQPvlrlaqlwqDFQQTGIALERLGDILN-SP-TEPRSAGLAALPELRGAITFENIR 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1044 FNYptRPDIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEP 1122
Cdd:TIGR01846 463 FRY--APDSPeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQEN 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1123 ILFDCSIAENIAYGDNSrvVSHEEIMQAAKEANIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLD 1202
Cdd:TIGR01846 541 VLFSRSIRDNIALCNPG--APFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFD 618
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 1203 EATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLAQKGIYFSMVSVQAG 1278
Cdd:TIGR01846 619 EATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQSG 694
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
798-1276 |
1.58e-74 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 262.20 E-value: 1.58e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 798 MLRQDVSWFDdpKNTTGALTTRlANDAAQvkgaIGSRLAVITQNIANLGTGIIISL----IYGWQLTL--LLLAIVpIIA 871
Cdd:TIGR03797 219 LLRLPVSFFR--QYSTGDLASR-AMGISQ----IRRILSGSTLTTLLSGIFALLNLglmfYYSWKLALvaVALALV-AIA 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 872 IAGVVEMKMLSgqalKDKKELEGAGKIATEAIENFRTVVSLtR----EQKFEYMYAQ--SLQVPYRNSLRKAH----IFG 941
Cdd:TIGR03797 291 VTLVLGLLQVR----KERRLLELSGKISGLTVQLINGISKL-RvagaENRAFARWAKlfSRQRKLELSAQRIEnlltVFN 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 942 VSFSITQAMMYFSYAGCFRFGAYLVANEFMNFQDVLLVFSAIVFG-AMAVGQVSSFAPDYAKAKVsaahvimIIEKSPLI 1020
Cdd:TIGR03797 366 AVLPVLTSAALFAAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQlSNTLISILAVIPLWERAKP-------ILEALPEV 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1021 DSYSPHglkPNTLEGNVTFNEVVFNYptRPDIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLID 1099
Cdd:TIGR03797 439 DEAKTD---PGKLSGAIEVDRVTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYD 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1100 GKEIKHLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDnsrVVSHEEIMQAAKEANIHHFIETLPEKYNTRVGDKGTQLS 1179
Cdd:TIGR03797 514 GQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGA---PLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLS 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1180 GGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRtcIVIAHRLSTIQNADLIVVFQNGKVKEHGTH 1259
Cdd:TIGR03797 591 GGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTY 668
|
490
....*....|....*..
gi 925114634 1260 QQLLAQKGIYFSMVSVQ 1276
Cdd:TIGR03797 669 DELMAREGLFAQLARRQ 685
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
713-988 |
1.84e-73 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 245.63 E-value: 1.84e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 713 FVVGIFCAIINGGLQPAFSIIFSRIIGIFTRDEDPETkrQNSNMFSVLFLVLGIISFITFFLQGFTFGKAGEILTKRLRY 792
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPET--QALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 793 MVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAI 872
Cdd:pfam00664 79 KLFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 873 AGVVEMKMLSGQALKDKKELEGAGKIATEAIENFRTVVSLTREQKFEYMYAQSLQVPYRNSLRKAHIFGVSFSITQAMMY 952
Cdd:pfam00664 157 VSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGY 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 925114634 953 FSYAGCFRFGAYLVANEFMNFQD--VLLVFSAIVFGAM 988
Cdd:pfam00664 237 LSYALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
397-1272 |
2.81e-71 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 262.96 E-value: 2.81e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 397 KNVHFSYpSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQdirtinvrhlreiTGVVS 476
Cdd:TIGR00957 640 HNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVP 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 477 QEPVLFATTIAENIRYGREnvTMDEIEKAVKEANAY--DFIMkLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKIL 554
Cdd:TIGR00957 706 QQAWIQNDSLRENILFGKA--LNEKYYQQVLEACALlpDLEI-LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIY 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 555 LLDEATSALDTEseaVVQVALDKA------RKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFK-L 627
Cdd:TIGR00957 783 LFDDPLSAVDAH---VGKHIFEHVigpegvLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEfL 859
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 628 VTMQTRGNEIELEN--ATGESKSESDALE----MSPKDSGSSLIKRRSTRRSIHApQGQDRKLGTKEDLNENVPPVSFWR 701
Cdd:TIGR00957 860 RTYAPDEQQGHLEDswTALVSGEGKEAKLiengMLVTDVVGKQLQRQLSASSSDS-GDQSRHHGSSAELQKAEAKEETWK 938
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 702 ILKLN---------STEWPYF-VVGIFCAIINGGL---QPAFSIIFSRIIGIFTRDEDPETKRQNSNMFSVLFLVLGIIS 768
Cdd:TIGR00957 939 LMEADkaqtgqvelSVYWDYMkAIGLFITFLSIFLfvcNHVSALASNYWLSLWTDDPMVNGTQNNTSLRLSVYGALGILQ 1018
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 769 FITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIAN-LGT 847
Cdd:TIGR00957 1019 GFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFE--RTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNvIGA 1096
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 848 GIIISLIygwqlTLLLLAIVPIIAIAGVVEMKMLSGQAlKDKKELEGAGKIA-----TEAIENFRTVVSLTREQKFEYMY 922
Cdd:TIGR00957 1097 LIVILLA-----TPIAAVIIPPLGLLYFFVQRFYVASS-RQLKRLESVSRSPvyshfNETLLGVSVIRAFEEQERFIHQS 1170
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 923 ------AQSLQVPYRNSLRK---------------AHIFGV--SFSITQAMMYFSYAGCFRFGAYLvanefmNFqdVLLV 979
Cdd:TIGR00957 1171 dlkvdeNQKAYYPSIVANRWlavrlecvgncivlfAALFAVisRHSLSAGLVGLSVSYSLQVTFYL------NW--LVRM 1242
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 980 FSAIVFGAMAVGQVSsfapDYAKAKVSAAHVIMiiEKSPlidsysPHGLKPNtleGNVTFNEVVFNYptRPDIP-VLQGL 1058
Cdd:TIGR00957 1243 SSEMETNIVAVERLK----EYSETEKEAPWQIQ--ETAP------PSGWPPR---GRVEFRNYCLRY--REDLDlVLRHI 1305
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1059 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPILFDCSIAENIaygDN 1138
Cdd:TIGR00957 1306 NVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---DP 1382
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1139 SRVVSHEEIMQAAKEANIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQE 1218
Cdd:TIGR00957 1383 FSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQS 1462
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....
gi 925114634 1219 ALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLAQKGIYFSM 1272
Cdd:TIGR00957 1463 TIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
392-612 |
2.92e-69 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 231.71 E-value: 2.92e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 392 GNLEFKNVHFSYPSrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREI 471
Cdd:cd03245 1 GRIEFRNVSFSYPN-QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 472 TGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNP 551
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 925114634 552 KILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKG 612
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1035-1253 |
1.21e-66 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 224.01 E-value: 1.21e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1035 GNVTFNEVVFNYPTRPdIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAH 1114
Cdd:cd03245 1 GRIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1115 LGIVSQEPILFDCSIAENIAYGDnsRVVSHEEIMQAAKEANIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVR 1194
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGA--PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 1195 QPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGKV 1253
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
123-631 |
1.24e-66 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 239.47 E-value: 1.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 123 IGAGVLVAAYIQVSFWcLAAGRQILKIRKQFFHAIM--------RQEIGWFDVHDVGELNTRlTDDVSKINEGIGDK-IG 193
Cdd:TIGR03797 178 IALALLAAAVGAAAFQ-LAQSLAVLRLETRMDASLQaavwdrllRLPVSFFRQYSTGDLASR-AMGISQIRRILSGStLT 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 194 MFFQSIATFFTgFIVGFTRGWKLTLVILAISPVLGLSAAIWAKILssfTDKELLAYAKAGAVAEEVLAAIRTVIAF---G 270
Cdd:TIGR03797 256 TLLSGIFALLN-LGLMFYYSWKLALVAVALALVAIAVTLVLGLLQ---VRKERRLLELSGKISGLTVQLINGISKLrvaG 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 271 GQKKELERYNKNLEEAKRIGIKKAITANI--SIGAAFLLIyASYALaFWYGTSLVLSSEYSIGQVLTvfFSVLIGAF--S 346
Cdd:TIGR03797 332 AENRAFARWAKLFSRQRKLELSAQRIENLltVFNAVLPVL-TSAAL-FAAAISLLGGAGLSLGSFLA--FNTAFGSFsgA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 347 IGQASPSIEAfANARGAAYEIFK-IIDNKPSIDSYSKsghKPDNIKGNLEFKNVHFSYPSRKEVkILKGLNLKVQSGQTV 425
Cdd:TIGR03797 408 VTQLSNTLIS-ILAVIPLWERAKpILEALPEVDEAKT---DPGKLSGAIEVDRVTFRYRPDGPL-ILDDVSLQIEPGEFV 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 426 ALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITGVVSQEPVLFATTIAENIrYGRENVTMDEIEKA 505
Cdd:TIGR03797 483 AIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEA 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 506 VKEANAYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRttI 585
Cdd:TIGR03797 562 ARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--I 639
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 925114634 586 VIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQ 631
Cdd:TIGR03797 640 VIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQ 685
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
108-630 |
2.43e-66 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 246.86 E-value: 2.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 108 HLEEEMTTYAYYYSGIGAGVLVAAYIQvSFWCLAAGRQILK-IRKQFFHAIMRQEIGWFD--VHDVGELNTRLTDDVSKI 184
Cdd:PTZ00265 860 NLEANSNKYSLYILVIAIAMFISETLK-NYYNNVIGEKVEKtMKRRLFENILYQEISFFDqdKHAPGLLSAHINRDVHLL 938
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 185 NEGIGDKIGMFFQSIATFFTGFIVGF----------TRGWKLTLVILAISPVLGLSAAIWAK-------ILSSFTDKELl 247
Cdd:PTZ00265 939 KTGLVNNIVIFTHFIVLFLVSMVMSFyfcpivaavlTGTYFIFMRVFAIRARLTANKDVEKKeinqpgtVFAYNSDDEI- 1017
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 248 aYAKAGAVAEEVLAAIRTVIAFGgqkkeLERYNKNLEEA----KRIGIKKAITAN-----ISIGAAFLLiyasYALAFWY 318
Cdd:PTZ00265 1018 -FKDPSFLIQEAFYNMNTVIIYG-----LEDYFCNLIEKaidySNKGQKRKTLVNsmlwgFSQSAQLFI----NSFAYWF 1087
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 319 GTSLVLSSEYSIGQVLTVFFSVLIGAFSIGQASPSIEAFANARGAAYEIFKIIDNKPSIDSYSKSGHKPDN---IKGNLE 395
Cdd:PTZ00265 1088 GSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNkndIKGKIE 1167
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 396 FKNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD---------------------------- 447
Cdd:PTZ00265 1168 IMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdee 1247
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 448 --------------------------PTDGMVCIDGQDIRTINVRHLREITGVVSQEPVLFATTIAENIRYGRENVTMDE 501
Cdd:PTZ00265 1248 qnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATRED 1327
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 502 IEKAVKEANAYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVAL----DK 577
Cdd:PTZ00265 1328 VKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDK 1407
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 578 ARKgrTTIVIAHRLSTVRNADVIAGFDD----GVIVE-KGNHDELMK-EKGIYFKLVTM 630
Cdd:PTZ00265 1408 ADK--TIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSvQDGVYKKYVKL 1464
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
123-652 |
2.50e-66 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 235.38 E-value: 2.50e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 123 IGAGVLVAA--YIQVSFWCL----AAGRQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFF 196
Cdd:PRK10789 39 IGTMVLIAVvvYLLRYVWRVllfgASYQLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 197 QSIATFFTGFIVGFTR-GWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKE 275
Cdd:PRK10789 119 DSLVMGCAVLIVMSTQiSWQLTLLALLPMPVMAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 276 LERY--------NKNLEEAkRIGIKKAITANISIGAAFLLiyasyalAFWYGTSLVLSSEYSIGQvLTVFFSVLigafsi 347
Cdd:PRK10789 199 SALFaadaedtgKKNMRVA-RIDARFDPTIYIAIGMANLL-------AIGGGSWMVVNGSLTLGQ-LTSFVMYL------ 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 348 GQASPSIEAFA---N--ARG-AAY-EIFKIIDNKPSIdsysKSGHKP-DNIKGNLEFKNVHFSYPsRKEVKILKGLNLKV 419
Cdd:PRK10789 264 GLMIWPMLALAwmfNivERGsAAYsRIRAMLAEAPVV----KDGSEPvPEGRGELDVNIRQFTYP-QTDHPALENVNFTL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 420 QSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITGVVSQEPVLFATTIAENIRYGRENVTM 499
Cdd:PRK10789 339 KPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQ 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 500 DEIEKAVKEANAYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKAR 579
Cdd:PRK10789 419 QEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWG 498
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 580 KGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQTRgnEIELENATGESKSESDA 652
Cdd:PRK10789 499 EGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQQL--EAALDDAPEIREEAVDA 569
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
394-1273 |
4.70e-65 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 242.96 E-value: 4.70e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDgMVCIDgqdirtinvrhLREITG 473
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE-TSSVV-----------IRGSVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFATTIAENIRYGrENVTMDEIEKAVK-EANAYDFIMkLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPK 552
Cdd:PLN03232 683 YVPQVSWIFNATVRENILFG-SDFESERYWRAIDvTALQHDLDL-LPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 553 ILLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQ 631
Cdd:PLN03232 761 IYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENA 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 632 TRGNEIELENATGES---KSESDALEMSPKDSGSslIKRRSTRRSIHAPQgQDRKLGTkedlnenvppVSFWRILKLNST 708
Cdd:PLN03232 841 GKMDATQEVNTNDENilkLGPTVTIDVSERNLGS--TKQGKRGRSVLVKQ-EERETGI----------ISWNVLMRYNKA 907
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 709 EWPYFVVGIF--CAIinggLQPAFSIIFSRIIGIFTRDEDPETKRqnSNMFSVLFLVLGIISFITFFLQGFTFGKAGEIL 786
Cdd:PLN03232 908 VGGLWVVMILlvCYL----TTEVLRVSSSTWLSIWTDQSTPKSYS--PGFYIVVYALLGFGQVAVTFTNSFWLISSSLHA 981
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 787 TKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDaaqvkgaIGSrlavITQNIANLGTGIIISLiygWQL--TLLLL 864
Cdd:PLN03232 982 AKRLHDAMLNSILRAPMLFFH--TNPTGRVINRFSKD-------IGD----IDRNVANLMNMFMNQL---WQLlsTFALI 1045
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 865 AIVPIIAIAGVVEMKMLSGQAL-------KDKKELEGAGKIAT-----EAIENFRTVVSLTREQKFEYMYAQSLQVPYRN 932
Cdd:PLN03232 1046 GTVSTISLWAIMPLLILFYAAYlyyqstsREVRRLDSVTRSPIyaqfgEALNGLSSIRAYKAYDRMAKINGKSMDNNIRF 1125
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 933 SL-----------RKAHIFGV------SFSITQAMMYFSYAGcFRFGAYLVANEFMNFQDVLlvfsaivfgAMAVGQVSS 995
Cdd:PLN03232 1126 TLantssnrwltiRLETLGGVmiwltaTFAVLRNGNAENQAG-FASTMGLLLSYTLNITTLL---------SGVLRQASK 1195
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 996 FAPDYAKAKVSAAHVIMIIEKSPLIDSYSPHGLKPntLEGNVTFNEVVFNYptRPDIP-VLQGLSLEVKKGQTLALVGSS 1074
Cdd:PLN03232 1196 AENSLNSVERVGNYIDLPSEATAIIENNRPVSGWP--SRGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRT 1271
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1075 GCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPILFDCSIAENIaygDNSRVVSHEEIMQAAKEA 1154
Cdd:PLN03232 1272 GAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI---DPFSEHNDADLWEALERA 1348
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1155 NIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAH 1234
Cdd:PLN03232 1349 HIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAH 1428
|
890 900 910 920
....*....|....*....|....*....|....*....|
gi 925114634 1235 RLSTIQNADLIVVFQNGKVKEHGTHQQLLAQKG-IYFSMV 1273
Cdd:PLN03232 1429 RLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMV 1468
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
392-613 |
3.85e-64 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 216.98 E-value: 3.85e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 392 GNLEFKNVHFSYPSRKEVkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREI 471
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPP-VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 472 TGVVSQEPVLFATTIAENI----RYgrenvTMDEIEKAVKEANAYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARAL 547
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSNLdpfgEY-----SDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 548 VRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGN 613
Cdd:cd03244 155 LRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
356-600 |
6.26e-64 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 227.17 E-value: 6.26e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 356 AFANARGAAYEIFKIIDNKPSIDSYSKSghKPDNIKGNLEFKNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGK 435
Cdd:TIGR02857 286 ARADGVAAAEALFAVLDAAPRPLAGKAP--VTAAPASSLEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGK 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 436 STTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFI 515
Cdd:TIGR02857 362 STLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFV 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 516 MKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVR 595
Cdd:TIGR02857 442 AALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAA 521
|
....*
gi 925114634 596 NADVI 600
Cdd:TIGR02857 522 LADRI 526
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1034-1265 |
1.67e-63 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 226.94 E-value: 1.67e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1034 EGNVTFNEVVFNYPTRpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRA 1113
Cdd:COG4618 328 KGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1114 HLGIVSQEPILFDCSIAENIA-YGDnsrvVSHEEIMQAAKEANIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARAL 1192
Cdd:COG4618 407 HIGYLPQDVELFDGTIAENIArFGD----ADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARAL 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 925114634 1193 VRQPHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLAQ 1265
Cdd:COG4618 483 YGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1035-1258 |
3.83e-63 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 214.28 E-value: 3.83e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1035 GNVTFNEVVFNYptRPDI-PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRA 1113
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1114 HLGIVSQEPILFDCSIAENIaygDNSRVVSHEEIMQAAKEANIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALV 1193
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNL---DPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 1194 RQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGT 1258
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
759-1276 |
5.90e-63 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 225.36 E-value: 5.90e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 759 VLFLVLGIISFITFFLQGFTFGkAGEILTKRLRYMVFRSMLRQDVSWFddPKNTTGALTTRLANDAAQVKGAIGSR-LAV 837
Cdd:PRK10789 41 TMVLIAVVVYLLRYVWRVLLFG-ASYQLAVELREDFYRQLSRQHPEFY--LRHRTGDLMARATNDVDRVVFAAGEGvLTL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 838 ITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIagvveMKMLSGQALKDK-KELEGA----GKIATEAIENFRTVVSL 912
Cdd:PRK10789 118 VDSLVMGCAVLIVMSTQISWQLTLLALLPMPVMAI-----MIKRYGDQLHERfKLAQAAfsslNDRTQESLTSIRMIKAF 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 913 TREQKFEYMYAQSLQVPYRNSLRKAHI---FGVSFSITQAMMYFSYAGCfrfGAYLVANefmnfqdvllvfsaivfGAMA 989
Cdd:PRK10789 193 GLEDRQSALFAADAEDTGKKNMRVARIdarFDPTIYIAIGMANLLAIGG---GSWMVVN-----------------GSLT 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 990 VGQVSSFA--------PDYAKA-------KVSAAH--VIMIIEKSPLIDSYS---PHGlkpntlEGNVTFNEVVFNYPTR 1049
Cdd:PRK10789 253 LGQLTSFVmylglmiwPMLALAwmfniveRGSAAYsrIRAMLAEAPVVKDGSepvPEG------RGELDVNIRQFTYPQT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1050 pDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPILFDCSI 1129
Cdd:PRK10789 327 -DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1130 AENIAYGDNSrvVSHEEIMQAAKEANIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1209
Cdd:PRK10789 406 ANNIALGRPD--ATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVD 483
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1210 TESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLAQKGIYFSMVSVQ 1276
Cdd:PRK10789 484 GRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ 550
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
759-1276 |
1.05e-62 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 225.37 E-value: 1.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 759 VLFLVLGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVI 838
Cdd:PRK10790 69 AAYVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFD--TQPVGQLISRVTNDTEVIRDLYVTVVATV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 839 TQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAgvvemkMLSGQalkdkkelegagKIATEAIENFRTVVSLTREQKF 918
Cdd:PRK10790 147 LRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLVV------MVIYQ------------RYSTPIVRRVRAYLADINDGFN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 919 EYMYAQSLQVPYRNSLRkahiFGVSFSITQAMMYFSYAGCFRFGAYLVanefmnfQDVLLVFSAIVF------------G 986
Cdd:PRK10790 209 EVINGMSVIQQFRQQAR----FGERMGEASRSHYMARMQTLRLDGFLL-------RPLLSLFSALILcgllmlfgfsasG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 987 AMAVGQVSSFApDY------------------AKAKVSAAHVImiieksPLIDS-YSPHGLKPNTLE-GNVTFNEVVFNY 1046
Cdd:PRK10790 278 TIEVGVLYAFI-SYlgrlneplielttqqsmlQQAVVAGERVF------ELMDGpRQQYGNDDRPLQsGRIDIDNVSFAY 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1047 ptRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPILFD 1126
Cdd:PRK10790 351 --RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLA 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1127 CSIAENIAYGdnsRVVSHEEIMQAAKEANIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1206
Cdd:PRK10790 429 DTFLANVTLG---RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATA 505
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1207 ALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLAQKGIYFSMVSVQ 1276
Cdd:PRK10790 506 NIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
992-1247 |
4.69e-62 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 221.78 E-value: 4.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 992 QVSSFAPDYAKAKVSAAHVIMIIEKSPLIdsYSPHGLKPNTLEGNVTFNEVVFNYPTRPdiPVLQGLSLEVKKGQTLALV 1071
Cdd:TIGR02857 279 QLGAQYHARADGVAAAEALFAVLDAAPRP--LAGKAPVTAAPASSLEFSGVSVAYPGRR--PALRPVSFTVPPGERVALV 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1072 GSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDnsRVVSHEEIMQAA 1151
Cdd:TIGR02857 355 GPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLAR--PDASDAEIREAL 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1152 KEANIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIV 1231
Cdd:TIGR02857 433 ERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLL 512
|
250
....*....|....*.
gi 925114634 1232 IAHRLSTIQNADLIVV 1247
Cdd:TIGR02857 513 VTHRLALAALADRIVV 528
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
983-1272 |
1.52e-60 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 218.54 E-value: 1.52e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 983 IVFGAMA--------------VGQVSSfapdyakakvSAAHVIMIIEKSPLIDSYSPHGLKPNtlEGNVTFNEVVFNYPT 1048
Cdd:PRK11160 283 FVFAALAafealmpvagafqhLGQVIA----------SARRINEITEQKPEVTFPTTSTAAAD--QVSLTLNNVSFTYPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1049 RPDiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPILFDCS 1128
Cdd:PRK11160 351 QPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSAT 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1129 IAENIAYGDNSrvVSHEEIMQAAKEANIHHFIETlPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1208
Cdd:PRK11160 430 LRDNLLLAAPN--ASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 925114634 1209 DTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLAQKGIYFSM 1272
Cdd:PRK11160 507 DAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
397-1273 |
2.49e-60 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 228.08 E-value: 2.49e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 397 KNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIdgqdirtinvrhLREITGVVS 476
Cdd:PLN03130 618 KNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYVP 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 477 QEPVLFATTIAENIRYGREnVTMDEIEKAVKEANAYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLL 556
Cdd:PLN03130 686 QVSWIFNATVRDNILFGSP-FDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIF 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 557 DEATSALDTE-SEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLvtMQTRGN 635
Cdd:PLN03130 765 DDPLSALDAHvGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL--MENAGK 842
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 636 EIELENATGESKSESDALEMSPKDSGSSLikrrsTRRSIHAPQGQDRK--LGTKEDLNENVppVSfWRIL-KLNSTEWPY 712
Cdd:PLN03130 843 MEEYVEENGEEEDDQTSSKPVANGNANNL-----KKDSSSKKKSKEGKsvLIKQEERETGV--VS-WKVLeRYKNALGGA 914
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 713 FVVGI--FCAIinggLQPAFSIIFSRIIGIFTrdeDPETKRQNSNMFSVLflVLGIISF---ITFFLQGFTFGKAGEILT 787
Cdd:PLN03130 915 WVVMIlfLCYV----LTEVFRVSSSTWLSEWT---DQGTPKTHGPLFYNL--IYALLSFgqvLVTLLNSYWLIMSSLYAA 985
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 788 KRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDaaqvkgaigsrLAVITQNIANLGTGIIISLiygWQL--TLLLLA 865
Cdd:PLN03130 986 KRLHDAMLGSILRAPMSFFH--TNPLGRIINRFAKD-----------LGDIDRNVAVFVNMFLGQI---FQLlsTFVLIG 1049
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 866 IVPIIAIAGVVEMKMLSGQAL-------KDKKELEGAGKIAT-----EAIENFRTVVSLTREQKFEYMYAQSLQVPYRNS 933
Cdd:PLN03130 1050 IVSTISLWAIMPLLVLFYGAYlyyqstaREVKRLDSITRSPVyaqfgEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFT 1129
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 934 L---RKAHIFGVSFSITQAMMYFSYAGCFRFGAYLVAN--EFMNFQDVLLVFSAIVFGAM-AVGQVSSFAPDYAKAKVSA 1007
Cdd:PLN03130 1130 LvnmSSNRWLAIRLETLGGLMIWLTASFAVMQNGRAENqaAFASTMGLLLSYALNITSLLtAVLRLASLAENSLNAVERV 1209
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1008 AHVIMIIEKSPL-IDSYSPHGLKPNTleGNVTFNEVVFNYptRPDIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL 1085
Cdd:PLN03130 1210 GTYIDLPSEAPLvIENNRPPPGWPSS--GSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNAL 1285
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1086 ERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPILFDCSIAENIaygDNSRVVSHEEIMQAAKEANIHHFIETLPE 1165
Cdd:PLN03130 1286 FRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL---DPFNEHNDADLWESLERAHLKDVIRRNSL 1362
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1166 KYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKarEGRTC--IVIAHRLSTIQNAD 1243
Cdd:PLN03130 1363 GLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE--EFKSCtmLIIAHRLNTIIDCD 1440
|
890 900 910
....*....|....*....|....*....|.
gi 925114634 1244 LIVVFQNGKVKEHGTHQQLLAQKGIYFS-MV 1273
Cdd:PLN03130 1441 RILVLDAGRVVEFDTPENLLSNEGSAFSkMV 1471
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
391-620 |
1.48e-59 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 215.38 E-value: 1.48e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 391 KGNLEFKNVHFSYPSRKEVkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLRE 470
Cdd:COG4618 328 KGRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 471 ITGVVSQEPVLFATTIAENI-RYGreNVTMDEIEKAVKEANAYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVR 549
Cdd:COG4618 407 HIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 550 NPKILLLDEATSALDTESEAVVQVALDKARK-GRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKE 620
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
129-629 |
2.40e-58 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 215.37 E-value: 2.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 129 VAAYIQVSFWCLAAGRQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDdVSKINEGIGDKI-GMFFQSIATFFTGFI 207
Cdd:TIGR01193 211 ILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTD-ASSIIDALASTIlSLFLDMWILVIVGLF 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 208 VGFtRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGqkkELERYNK------ 281
Cdd:TIGR01193 290 LVR-QNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTS---EAERYSKidsefg 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 282 -NLEEAKRIGIKKAITANISIGAAFLLIyasyALAFWYGTSLVLSSEYSIGQVLTvfFSVLIGAF-----SIGQASPSIE 355
Cdd:TIGR01193 366 dYLNKSFKYQKADQGQQAIKAVTKLILN----VVILWTGAYLVMRGKLTLGQLIT--FNALLSYFltpleNIINLQPKLQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 356 AFANARGAAYEIFKIidnkPSIDSYSKSGHKPDNIKGNLEFKNVHFSYPSRKEvkILKGLNLKVQSGQTVALVGNSGCGK 435
Cdd:TIGR01193 440 AARVANNRLNEVYLV----DSEFINKKKRTELNNLNGDIVINDVSYSYGYGSN--ILSDISLTIKMNSKTTIVGMSGSGK 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 436 STTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITGVVSQEPVLFATTIAENIRYG-RENVTMDEIEKAVKEANAYDF 514
Cdd:TIGR01193 514 STLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDD 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 515 IMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKArKGRTTIVIAHRLSTV 594
Cdd:TIGR01193 594 IENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLSVA 672
|
490 500 510
....*....|....*....|....*....|....*
gi 925114634 595 RNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVT 629
Cdd:TIGR01193 673 KQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
104-638 |
6.67e-58 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 211.12 E-value: 6.67e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 104 HFINHleeeMTTYAYYYSGIGAGvLVAAYIQVSFwcLAAG---RQIL-----------KIRKQFFHAIMRQEIGWFDVHD 169
Cdd:PRK10790 48 YFIDN----MVAKGNLPLGLVAG-LAAAYVGLQL--LAAGlhyAQSLlfnraavgvvqQLRTDVMDAALRQPLSAFDTQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 170 VGELNTRLTDDVSKINEGIGDKIGMFFQSIATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAIWAKiLSSFTDKELLAY 249
Cdd:PRK10790 121 VGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQR-YSTPIVRRVRAY 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 250 -AKAGAVAEEVLAAIrTVIAfggQKKELERYNKNLEEAKRIGIKKAITA----------NISIGAAFLLIyasyALAFWY 318
Cdd:PRK10790 200 lADINDGFNEVINGM-SVIQ---QFRQQARFGERMGEASRSHYMARMQTlrldgfllrpLLSLFSALILC----GLLMLF 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 319 GtslvLSSEYSIG-QVLTVFFSVLiGAFSigqaSPSIE------AFANARGAAYEIFKIIDNkpsidsySKSGHKPDNI- 390
Cdd:PRK10790 272 G----FSASGTIEvGVLYAFISYL-GRLN----EPLIElttqqsMLQQAVVAGERVFELMDG-------PRQQYGNDDRp 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 391 --KGNLEFKNVHFSYpsRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHL 468
Cdd:PRK10790 336 lqSGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 469 REITGVVSQEPVLFATTIAENIRYGReNVTMDEIEKAVKEANAYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALV 548
Cdd:PRK10790 414 RQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLV 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 549 RNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLV 628
Cdd:PRK10790 493 QTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMY 572
|
570
....*....|
gi 925114634 629 TMQTRGNEIE 638
Cdd:PRK10790 573 QLQLAGEELA 582
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
1035-1273 |
1.01e-57 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 210.52 E-value: 1.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1035 GNVTFNEVVFNYPTRPdipvlQG---LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWL 1111
Cdd:TIGR01192 333 GAVEFRHITFEFANSS-----QGvfdVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1112 RAHLGIVSQEPILFDCSIAENIAYGDNSrvVSHEEIMQAAKEANIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARA 1191
Cdd:TIGR01192 408 RKSIATVFQDAGLFNRSIRENIRLGREG--ATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1192 LVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLAQKGIYFS 1271
Cdd:TIGR01192 486 ILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYK 565
|
..
gi 925114634 1272 MV 1273
Cdd:TIGR01192 566 LL 567
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
171-591 |
4.74e-56 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 204.13 E-value: 4.74e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 171 GELNTRLTDDVskinEGIGDKI-GMFFQSIATFFTGFIVgftrgwklTLVILAISPVLGLSAAI----------WAKILS 239
Cdd:TIGR02868 110 GDLLGRLGADV----DALQDLYvRVIVPAGVALVVGAAA--------VAAIAVLSVPAALILAAglllagfvapLVSLRA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 240 SFTDKELLAYAKaGAVAEEVLAAIR---TVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAF 316
Cdd:TIGR02868 178 ARAAEQALARLR-GELAAQLTDALDgaaELVASGALPAALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGAL 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 317 WYGTSLVLSSEYSiGQVLTVFFSVLIGAFSIGQA-SPSIEAFANARGAAYEIFKIIDNKPSIDSYSKSGHKPDNIKG-NL 394
Cdd:TIGR02868 257 WAGGPAVADGRLA-PVTLAVLVLLPLAAFEAFAAlPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKpTL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 395 EFKNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITGV 474
Cdd:TIGR02868 336 ELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSV 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 475 VSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKIL 554
Cdd:TIGR02868 414 CAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPIL 493
|
410 420 430
....*....|....*....|....*....|....*..
gi 925114634 555 LLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRL 591
Cdd:TIGR02868 494 LLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
363-627 |
6.63e-56 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 205.06 E-value: 6.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 363 AAYEIFKIIDNKPSIDSYSKSGHKPDniKGNLEFKNVHFSYPSRkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLM 442
Cdd:PRK11160 310 SARRINEITEQKPEVTFPTTSTAAAD--QVSLTLNNVSFTYPDQ-PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 443 QRLYDPTDGMVCIDGQDIRTINVRHLREITGVVSQEPVLFATTIAENIRYGRENVTmDEIEKAVKEANAYDFIMKLPNKF 522
Cdd:PRK11160 387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNAS-DEALIEVLQQVGLEKLLEDDKGL 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 523 DTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAG 602
Cdd:PRK11160 466 NAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICV 545
|
250 260
....*....|....*....|....*
gi 925114634 603 FDDGVIVEKGNHDELMKEKGIYFKL 627
Cdd:PRK11160 546 MDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
717-1275 |
7.24e-56 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 207.67 E-value: 7.24e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 717 IFCAIINGGLQPAFSIIFSRIIGIFTrdedPETKRQNSNMFSVLFLVLGIISFITFFLQGFTFGKAGEILTKRLRYMVFR 796
Cdd:TIGR01193 162 VIAAIIVTLISIAGSYYLQKIIDTYI----PHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 797 SMLRQDVSWFDDPKntTGALTTRLAnDAAQVKGAIGSrlaVITQNIANLGTGIIISLIYGWQ---LTLLLLAIVPIIAIA 873
Cdd:TIGR01193 238 HLFELPMSFFSTRR--TGEIVSRFT-DASSIIDALAS---TILSLFLDMWILVIVGLFLVRQnmlLFLLSLLSIPVYAVI 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 874 GVVEMKMLSGQalkDKKELEGAGKIATEAIENF---RTVVSLTRE----QKFEYMYAQSLQVPYRNSLRKAhIFGVSFSI 946
Cdd:TIGR01193 312 IILFKRTFNKL---NHDAMQANAVLNSSIIEDLngiETIKSLTSEaerySKIDSEFGDYLNKSFKYQKADQ-GQQAIKAV 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 947 TQAMMYFSyagCFRFGAYLVANEFMNFQDvLLVFSAIV-FGAMAVGQVSSFAPDYAKAKVSAAHV--IMIIEkSPLIDSY 1023
Cdd:TIGR01193 388 TKLILNVV---ILWTGAYLVMRGKLTLGQ-LITFNALLsYFLTPLENIINLQPKLQAARVANNRLneVYLVD-SEFINKK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1024 SPHGLkpNTLEGNVTFNEVVFNYPTRPdiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEI 1103
Cdd:TIGR01193 463 KRTEL--NNLNGDIVINDVSYSYGYGS--NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1104 KHLNVQWLRAHLGIVSQEPILFDCSIAENIAYGdNSRVVSHEEIMQAAKEANIHHFIETLPEKYNTRVGDKGTQLSGGQK 1183
Cdd:TIGR01193 539 KDIDRHTLRQFINYLPQEPYIFSGSILENLLLG-AKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQK 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1184 QRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREgRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLL 1263
Cdd:TIGR01193 618 QRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELL 696
|
570
....*....|..
gi 925114634 1264 AQKGIYFSMVSV 1275
Cdd:TIGR01193 697 DRNGFYASLIHN 708
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1001-1272 |
7.43e-56 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 205.08 E-value: 7.43e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1001 AKAK-VSAAHVIMIIEKSPLIDSYS----PHGLKPNTLEGNvtfNEVVFNyptrPDIPVLQG-LSLEVKKGQTLALVGSS 1074
Cdd:PRK11174 313 AKAQaVGAAESLVTFLETPLAHPQQgekeLASNDPVTIEAE---DLEILS----PDGKTLAGpLNFTLPAGQRIALVGPS 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1075 GCGKSTVVQLLERFYdPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSHEEIMQAAKEA 1154
Cdd:PRK11174 386 GAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPD--ASDEQLQQALENA 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1155 NIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAH 1234
Cdd:PRK11174 463 WVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTH 542
|
250 260 270
....*....|....*....|....*....|....*...
gi 925114634 1235 RLSTIQNADLIVVFQNGKVKEHGTHQQLLAQKGIYFSM 1272
Cdd:PRK11174 543 QLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
319-620 |
2.14e-52 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 193.72 E-value: 2.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 319 GTSLVLSSEYSIGQVLTVffSVLIG-AFS-IGQASPSIEAFANARGAAYEIFKIIDNKPSIDSYSKSghkPdNIKGNLEF 396
Cdd:TIGR01842 246 GAYLAIDGEITPGMMIAG--SILVGrALApIDGAIGGWKQFSGARQAYKRLNELLANYPSRDPAMPL---P-EPEGHLSV 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 397 KNVHFSYPSRKEVkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITGVVS 476
Cdd:TIGR01842 320 ENVTIVPPGGKKP-TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLP 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 477 QEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLL 556
Cdd:TIGR01842 399 QDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVL 478
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 557 DEATSALDTESEAVVQVALDKARK-GRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKE 620
Cdd:TIGR01842 479 DEPNSNLDEEGEQALANAIKALKArGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
356-624 |
3.48e-52 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 194.29 E-value: 3.48e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 356 AFANARGAAYEIFKIIDnkpSIDSYSKSGHKPDNIKGNLEFKNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGK 435
Cdd:PRK11174 313 AKAQAVGAAESLVTFLE---TPLAHPQQGEKELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGK 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 436 STtvqLMQRL--YDPTDGMVCIDGQDIRTINVRHLREITGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYD 513
Cdd:PRK11174 390 TS---LLNALlgFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSE 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 514 FIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLST 593
Cdd:PRK11174 467 FLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLED 546
|
250 260 270
....*....|....*....|....*....|.
gi 925114634 594 VRNADVIAGFDDGVIVEKGNHDELMKEKGIY 624
Cdd:PRK11174 547 LAQWDQIWVMQDGQIVQQGDYAELSQAGGLF 577
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1034-1265 |
1.20e-50 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 188.71 E-value: 1.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1034 EGNVTFNEVVFnYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRA 1113
Cdd:TIGR01842 314 EGHLSVENVTI-VPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1114 HLGIVSQEPILFDCSIAENIA-YGDNsrvVSHEEIMQAAKEANIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARAL 1192
Cdd:TIGR01842 393 HIGYLPQDVELFPGTVAENIArFGEN---ADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARAL 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 925114634 1193 VRQPHILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLAQ 1265
Cdd:TIGR01842 470 YGDPKLVVLDEPNSNLDEEGEQALANAIKALKaRGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
394-621 |
5.06e-50 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 176.75 E-value: 5.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITG 473
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPV--LFATTIAENIRYGREN--VTMDEIEKAVKEA----NAYDFIMKLPNkfdtlvgergaQLSGGQKQRIAIAR 545
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPENlgLPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 546 ALVRNPKILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELMKEK 621
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGrRELLELLKRLNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
395-606 |
1.45e-49 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 174.96 E-value: 1.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 395 EFKNVHFSYPSRKEvKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITGV 474
Cdd:cd03225 1 ELKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 475 VSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEANAydfIMKLPNKFDTLVgergAQLSGGQKQRIAIARALVRN 550
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENlgLPEEEIEERVEEALE---LVGLEGLRDRSP----FTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 551 PKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLSTVRN-ADVIAGFDDG 606
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
394-618 |
1.82e-49 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 184.34 E-value: 1.82e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRK--EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREI 471
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 472 T---GVVSQEPV--LFAT-TIAENIRYGREN---VTMDEIEKAVKEANA-----YDFIMKLPnkfdtlvgergAQLSGGQ 537
Cdd:COG1123 341 RrrvQMVFQDPYssLNPRmTVGDIIAEPLRLhglLSRAERRERVAELLErvglpPDLADRYP-----------HELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 538 KQRIAIARALVRNPKILLLDEATSALDTESEAVVqvaLD-----KARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEK 611
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQI---LNllrdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVED 486
|
....*..
gi 925114634 612 GNHDELM 618
Cdd:COG1123 487 GPTEEVF 493
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
394-617 |
4.34e-49 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 174.29 E-value: 4.34e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD-----PTDGMVCIDGQDIRTINVR-- 466
Cdd:cd03260 1 IELRDLNVYY---GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 467 HLREITGVVSQEPVLFATTIAENIRYG------RENVTMDEI-EKAVKEANaydfimkLPNKFDTLVGERGaqLSGGQKQ 539
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERvEEALRKAA-------LWDEVKDRLHALG--LSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 540 RIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDEL 617
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
394-608 |
9.60e-49 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 171.25 E-value: 9.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKEVkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITG 473
Cdd:cd03246 1 LEVENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFATTIAENIrygrenvtmdeiekavkeanaydfimklpnkfdtlvgergaqLSGGQKQRIAIARALVRNPKI 553
Cdd:cd03246 80 YLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 554 LLLDEATSALDTESEAVVQVALDKARK-GRTTIVIAHRLSTVRNADVIAGFDDGVI 608
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1037-1266 |
1.50e-48 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 172.52 E-value: 1.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPtrPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLG 1116
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1117 IVSQEPI--LFDCSIAENIAYGDNSRVVSHEEIMQAAKEA----NIHHFIETLPekyntrvgdkgTQLSGGQKQRIAIAR 1190
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPENLGLPREEIRERVEEAlelvGLEHLADRPP-----------HELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 1191 ALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVFQNGKVKEHGTHQQLLAQK 1266
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
105-367 |
4.15e-48 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 173.52 E-value: 4.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 105 FINHLEEEM-----TTYAYYYSGIGAGVLVAAYIQVSFWCLAAGRQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTD 179
Cdd:cd18557 22 LIDTIIKGGdldvlNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 180 DVSKINEGIGDKIGMFFQSIATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEV 259
Cdd:cd18557 102 DTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEES 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 260 LAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTSLVLSSEYSIGQVLT-VFF 338
Cdd:cd18557 182 LSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSfILY 261
|
250 260
....*....|....*....|....*....
gi 925114634 339 SVLIgAFSIGQASPSIEAFANARGAAYEI 367
Cdd:cd18557 262 TIMV-ASSVGGLSSLLADIMKALGASERV 289
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1051-1262 |
2.72e-47 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 168.90 E-value: 2.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1051 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PLAGSVLIDGKEIKHL--NVQWLRAHLGIVSQEPI 1123
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLdvDVLELRRRVGMVFQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1124 LFDCSIAENIAYGDNSR-VVSHEEIMQAAKEAnihhfIET--LPEKYNTRVgdKGTQLSGGQKQRIAIARALVRQPHILL 1200
Cdd:cd03260 92 PFPGSIYDNVAYGLRLHgIKLKEELDERVEEA-----LRKaaLWDEVKDRL--HALGLSGGQQQRLCLARALANEPEVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 1201 LDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQL 1262
Cdd:cd03260 165 LDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1037-1265 |
2.87e-47 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 177.79 E-value: 2.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPTRP--DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLN---VQWL 1111
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1112 RAHLGIVSQEPIL-FDC--SIAENIAYG-DNSRVVSHEEIMQAAKEAnihhfIET--LPEKYNTRvgdKGTQLSGGQKQR 1185
Cdd:COG1123 341 RRRVQMVFQDPYSsLNPrmTVGDIIAEPlRLHGLLSRAERRERVAEL-----LERvgLPPDLADR---YPHELSGGQRQR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1186 IAIARALVRQPHILLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQL 1262
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEV 492
|
...
gi 925114634 1263 LAQ 1265
Cdd:COG1123 493 FAN 495
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1042-1253 |
4.26e-47 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 166.24 E-value: 4.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1042 VVFNYP-TRPdiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQ 1120
Cdd:cd03246 6 VSFRYPgAEP--PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1121 EPILFDCSIAENIaygdnsrvvsheeimqaakeanihhfietlpekyntrvgdkgtqLSGGQKQRIAIARALVRQPHILL 1200
Cdd:cd03246 84 DDELFSGSIAENI--------------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 925114634 1201 LDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVFQNGKV 1253
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1039-1252 |
5.99e-47 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 167.26 E-value: 5.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1039 FNEVVFNYPTRpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIV 1118
Cdd:cd03225 2 LKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1119 SQEP--ILFDCSIAENIAYGDNSRVVSHEEIMQAAKEA----NIHHFIETLPEkyntrvgdkgtQLSGGQKQRIAIARAL 1192
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGLENLGLPEEEIEERVEEAlelvGLEGLRDRSPF-----------TLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 1193 VRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGK 1252
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1035-1258 |
1.86e-46 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 165.66 E-value: 1.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1035 GNVTFNEVVFNYptRPDIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRA 1113
Cdd:cd03369 5 GEIEVENLSVRY--APDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1114 HLGIVSQEPILFDCSIAENIaygDNSRVVSHEEIMQAakeanihhfietlpekynTRVGDKGTQLSGGQKQRIAIARALV 1193
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 1194 RQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGT 1258
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
394-589 |
2.72e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 165.37 E-value: 2.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITG 473
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFATTIAENI----RYGRENVTMDEIEKAVKEANaydfimkLPNKF-DTLVGErgaqLSGGQKQRIAIARALV 548
Cdd:COG4619 78 YVPQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLG-------LPPDIlDKPVER----LSGGERQRLALIRALL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 925114634 549 RNPKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAH 589
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSH 189
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
976-1236 |
1.44e-45 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 173.32 E-value: 1.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 976 VLLVFSAivFGAMAVgqVSSFAPDYAKAKVSAAHVIMIIEKSPLIDSYSPHGLKPNTLEG-NVTFNEVVFNYPTRPdiPV 1054
Cdd:TIGR02868 277 VLLPLAA--FEAFAA--LPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKpTLELRDLSAGYPGAP--PV 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1055 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPILFDCSIAEN-- 1132
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENlr 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1133 IAYGDnsrvVSHEEIMQAAKEANIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1212
Cdd:TIGR02868 431 LARPD----ATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAET 506
|
250 260
....*....|....*....|....
gi 925114634 1213 EKVVQEALDKAREGRTCIVIAHRL 1236
Cdd:TIGR02868 507 ADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
394-617 |
3.74e-45 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 163.14 E-value: 3.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSR-KEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREI- 471
Cdd:cd03258 2 IELKNVSKVFGDTgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 472 --TGVVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKE----------ANAYdfimklPnkfdtlvgergAQLSGG 536
Cdd:cd03258 82 rrIGMIFQHFNLLSSrTVFENVALPLEiaGVPKAEIEERVLEllelvgledkADAY------P-----------AQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 537 QKQRIAIARALVRNPKILLLDEATSALDTES-EAVVQVALDKARKGRTTIV-IAHRLSTVRN-ADVIAGFDDGVIVEKGN 613
Cdd:cd03258 145 QKQRVGIARALANNPKVLLCDEATSALDPETtQSILALLRDINRELGLTIVlITHEMEVVKRiCDRVAVMEKGEVVEEGT 224
|
....
gi 925114634 614 HDEL 617
Cdd:cd03258 225 VEEV 228
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
412-561 |
7.02e-45 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 158.97 E-value: 7.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 412 LKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITGVVSQEPVLF-ATTIAENI 490
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 491 RYGREnvtMDEIEKAVKEANAYDFI--MKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATS 561
Cdd:pfam00005 81 RLGLL---LKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1037-1257 |
8.33e-45 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 160.17 E-value: 8.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPTRpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQwLRAHLG 1116
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1117 IVSQEPILFDCSIAENIaygdnsrvvsheeimqaakeanihhfietlpekyntrvgdkGTQLSGGQKQRIAIARALVRQP 1196
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL-----------------------------------------GRRFSGGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 925114634 1197 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHG 1257
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1048-1257 |
1.16e-44 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 160.76 E-value: 1.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1048 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQwlRAHLGIVSQEPILFD- 1126
Cdd:cd03259 9 TYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPh 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1127 CSIAENIAYGDNSRVVSHEEI----MQAAKEANIHHFIETLPEkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLD 1202
Cdd:cd03259 87 LTVAENIAFGLKLRGVPKAEIrarvRELLELVGLEGLLNRYPH-----------ELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 1203 EATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGKVKEHG 1257
Cdd:cd03259 156 EPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
394-613 |
2.06e-44 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 164.48 E-value: 2.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRK-EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREI- 471
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 472 --TGVVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKE----------ANAYdfimklPnkfdtlvgergAQLSGG 536
Cdd:COG1135 82 rkIGMIFQHFNLLSSrTVAENVALPLEiaGVPKAEIRKRVAEllelvglsdkADAY------P-----------SQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 537 QKQRIAIARALVRNPKILLLDEATSALDTES-EAVVQVaLDKARK--GRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKG 612
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPETtRSILDL-LKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQG 223
|
.
gi 925114634 613 N 613
Cdd:COG1135 224 P 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
394-619 |
2.99e-44 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 160.53 E-value: 2.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREI-- 471
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 472 -TGVVSQEPVLF-ATTIAENIRYG-RENVTM--DEIEKAVkeanaydfIMKLpnkfdTLVGERGA------QLSGGQKQR 540
Cdd:COG1127 83 rIGMLFQGGALFdSLTVFENVAFPlREHTDLseAEIRELV--------LEKL-----ELVGLPGAadkmpsELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 541 IAIARALVRNPKILLLDEATSALD--TeSEAVVQVALD-KARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDE 616
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDpiT-SAVIDELIRElRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEE 228
|
...
gi 925114634 617 LMK 619
Cdd:COG1127 229 LLA 231
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
394-617 |
3.07e-44 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 160.54 E-value: 3.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDI--RTINVRHLREI 471
Cdd:COG1126 2 IEIENLHKSF---GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 472 TGVVSQEPVLFA-TTIAENIRYGRENVT-MDEiEKAVKEANAY-------DFIMKLPnkfdtlvgergAQLSGGQKQRIA 542
Cdd:COG1126 79 VGMVFQQFNLFPhLTVLENVTLAPIKVKkMSK-AEAEERAMELlervglaDKADAYP-----------AQLSGGQQQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 543 IARALVRNPKILLLDEATSALDTE--SEaVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDEL 617
Cdd:COG1126 147 IARALAMEPKVMLFDEPTSALDPElvGE-VLDVMRDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1055-1206 |
6.77e-44 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 156.27 E-value: 6.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1055 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPILF-DCSIAENI 1133
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 1134 AYGdnsrvVSHEEIMQAAKEANIHHFIETL--PEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1206
Cdd:pfam00005 81 RLG-----LLLKGLSKREKDARAEEALEKLglGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1053-1234 |
8.26e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 158.44 E-value: 8.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1053 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPILFDCSIAEN 1132
Cdd:COG4619 14 PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALWGGTVRDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1133 IAYGDNSRvvsheeiMQAAKEANIHHFIET--LPEKY-NTRVgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1209
Cdd:COG4619 94 LPFPFQLR-------ERKFDRERALELLERlgLPPDIlDKPV----ERLSGGERQRLALIRALLLQPDVLLLDEPTSALD 162
|
170 180
....*....|....*....|....*..
gi 925114634 1210 TESEKVVQEALDK--AREGRTCIVIAH 1234
Cdd:COG4619 163 PENTRRVEELLREylAEEGRAVLWVSH 189
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
394-612 |
9.46e-44 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 158.82 E-value: 9.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRK-EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIrTINVRHLREIT 472
Cdd:cd03257 2 LEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDL-LKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 473 G----VVSQEPvlFAT-----TIAENIRYGRENVTMDEIEKAVKEANAYDFiMKLPNKfDTLVGERGAQLSGGQKQRIAI 543
Cdd:cd03257 81 RkeiqMVFQDP--MSSlnprmTIGEQIAEPLRIHGKLSKKEARKEAVLLLL-VGVGLP-EEVLNRYPHELSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 544 ARALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKG 612
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1037-1255 |
1.43e-43 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 158.28 E-value: 1.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPT-RPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPLAGSVLIDGKEIKHLN----V 1108
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDISSLSerelA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1109 QWLRAHLGIVSQEPILFDC-SIAENIA----YGDNSRVVSHEEIMQAAKEANIHHFIETLPekyntrvgdkgTQLSGGQK 1183
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPElTALENVAlpllLAGVSRKERRERARELLERVGLGDRLDHRP-----------SQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 925114634 1184 QRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVFQNGKVKE 1255
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
394-619 |
2.33e-43 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 158.05 E-value: 2.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREI-- 471
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 472 -TGVVSQEPVLF-ATTIAENIRYG-RENVTMDE--IEKAVKeanaydfiMKLpnkfdTLVGERG------AQLSGGQKQR 540
Cdd:cd03261 78 rMGMLFQSGALFdSLTVFENVAFPlREHTRLSEeeIREIVL--------EKL-----EAVGLRGaedlypAELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 541 IAIARALVRNPKILLLDEATSALD-TESEAVVQVALD-KARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDEL 617
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
..
gi 925114634 618 MK 619
Cdd:cd03261 225 RA 226
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
392-612 |
3.22e-43 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 156.42 E-value: 3.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 392 GNLEFKNVHFSYPSRKEvKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREI 471
Cdd:cd03369 5 GEIEVENLSVRYAPDLP-PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 472 TGVVSQEPVLFATTIAENI-RYGREnvTMDEIEKAVKeanaydfimklpnkfdtlVGERGAQLSGGQKQRIAIARALVRN 550
Cdd:cd03369 84 LTIIPQDPTLFSGTIRSNLdPFDEY--SDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 551 PKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKG 612
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
401-1274 |
4.32e-43 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 172.40 E-value: 4.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 401 FSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGmvcidgqdirtiNVRHLREITgVVSQEPV 480
Cdd:TIGR01271 431 FSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEG------------KIKHSGRIS-FSPQTSW 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 481 LFATTIAENIRYGrenVTMDEIE--KAVKEANAYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDE 558
Cdd:TIGR01271 498 IMPGTIKDNIIFG---LSYDEYRytSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 559 ATSALD--TESEaVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIY------------ 624
Cdd:TIGR01271 575 PFTHLDvvTEKE-IFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFsslllgleafdn 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 625 -------------------------------------------------------------FKLVTM-QTRGNEIELENA 642
Cdd:TIGR01271 654 fsaerrnsiltetlrrvsidgdstvfsgpetikqsfkqpppefaekrkqsiilnpiasarkFSFVQMgPQKAQATTIEDA 733
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 643 TGESKS-------ESDALE--------------------------MSPKDSGSSLIKRR--STRRSIHAPQ--------- 678
Cdd:TIGR01271 734 VREPSErkfslvpEDEQGEeslprgnqyhhglqhqaqrrqsvlqlMTHSNRGENRREQLqtSFRKKSSITQqnelaseld 813
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 679 ------GQDRKLGTKEDLNE------------NVPPVSFWRI-LKLNSTEWPYFVVGIFCAII-----NGGLQPAFsIIF 734
Cdd:TIGR01271 814 iysrrlSKDSVYEISEEINEedlkecfadereNVFETTTWNTyLRYITTNRNLVFVLIFCLVIflaevAASLLGLW-LIT 892
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 735 SRIIGIFTRDEDPETKRQNSNMFSVL----------FLVLGII-SFITF-FLQGFTFGKAGEILTKRLRYMVFRSMLRQD 802
Cdd:TIGR01271 893 DNPSAPNYVDQQHANASSPDVQKPVIitptsayyifYIYVGTAdSVLALgFFRGLPLVHTLLTVSKRLHEQMLHSVLQAP 972
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 803 VSWFDDPKntTGALTTRLANDAAQVKGAIGSRLAVITQ-NIANLGTGIIISLIYGWqltlLLLAIVPIIAIAGVVEMKML 881
Cdd:TIGR01271 973 MAVLNTMK--AGRILNRFTKDMAIIDDMLPLTLFDFIQlTLIVLGAIFVVSVLQPY----IFIAAIPVAVIFIMLRAYFL 1046
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 882 -SGQALKdKKELEGAGKIATEAIENFR---TVVSLTREQKFEYMYAQSLQVP------YRNSLR----KAHIFGVSFSIt 947
Cdd:TIGR01271 1047 rTSQQLK-QLESEARSPIFSHLITSLKglwTIRAFGRQSYFETLFHKALNLHtanwflYLSTLRwfqmRIDIIFVFFFI- 1124
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 948 qAMMYFSYA----GCFRFGAYLVANefMNFQDVL--LVFSAI-VFGAM-AVGQVSSF---APDYAKAKVSAAHV----IM 1012
Cdd:TIGR01271 1125 -AVTFIAIGtnqdGEGEVGIILTLA--MNILSTLqwAVNSSIdVDGLMrSVSRVFKFidlPQEEPRPSGGGGKYqlstVL 1201
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1013 IIEKSPLIDSYsPHGlkpntleGNVTFNEVVFNYpTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPl 1092
Cdd:TIGR01271 1202 VIENPHAQKCW-PSG-------GQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST- 1271
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1093 AGSVLIDGKEIKHLNVQWLRAHLGIVSQEPILFDCSIAENIaygDNSRVVSHEEIMQAAKEANIHHFIETLPEKYNTRVG 1172
Cdd:TIGR01271 1272 EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL---DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLV 1348
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1173 DKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGK 1252
Cdd:TIGR01271 1349 DGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSS 1428
|
1050 1060
....*....|....*....|..
gi 925114634 1253 VKEHGTHQQLLAQKGIYFSMVS 1274
Cdd:TIGR01271 1429 VKQYDSIQKLLNETSLFKQAMS 1450
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
54-363 |
7.79e-43 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 158.57 E-value: 7.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 54 GTMAAIIHGAALPLMMLVFGNMTDSfanagisrnktfpviinesITNNTQHFINHLEEEMTTYAYYYSGIGAGVLVAAYI 133
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDA-------------------VTNHSGSGGEEALRALNQAVLILLGVVLIGSIATFL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 134 QVSFWCLAAGRQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSIATFFTGFIVGFTRG 213
Cdd:cd18780 62 RSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 214 WKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKK 293
Cdd:cd18780 142 WKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKL 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 294 AITANISIGAAFLLIYASYALAFWYGTSLVLSSEYSIGQvLTVF--FSVLIgAFSIGQASPSIEAFANARGA 363
Cdd:cd18780 222 ARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTGL-LTSFllYTLTV-AMSFAFLSSLYGDFMQAVGA 291
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
394-610 |
1.25e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 155.59 E-value: 1.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRK-EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHL---- 468
Cdd:COG1136 5 LELRNLTKSYGTGEgEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 469 -REItGVVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKEANAY----DFIMKLPNkfdtlvgergaQLSGGQKQR 540
Cdd:COG1136 85 rRHI-GFVFQFFNLLPElTALENVALPLLlaGVSRKERRERARELLERvglgDRLDHRPS-----------QLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 541 IAIARALVRNPKILLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIA-HRLSTVRNADVIAGFDDGVIVE 610
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKtGEEVLELLRELNRELGTTIVMVtHDPELAARADRVIRLRDGRIVS 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
394-612 |
1.47e-42 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 153.62 E-value: 1.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINvRHLREITG 473
Cdd:cd03247 1 LSINNVSFSYPE-QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFATTIAENIrygrenvtmdeiekavkeanaydfimklpnkfdtlvgerGAQLSGGQKQRIAIARALVRNPKI 553
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 554 LLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKG 612
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
410-1273 |
1.89e-42 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 170.34 E-value: 1.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 410 KILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDgqdiRTInvrhlreitGVVSQEPVLFATTIAEN 489
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE----RSI---------AYVPQQAWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 490 IRYGRENVTMDeIEKAVK----EANaydfIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 565
Cdd:PTZ00243 741 ILFFDEEDAAR-LADAVRvsqlEAD----LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 566 E-SEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMkEKGIYFKLvTMQTRGNEIELENATG 644
Cdd:PTZ00243 816 HvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFM-RTSLYATL-AAELKENKDSKEGDAD 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 645 ESKSESDALEMSPKDSGSSLIK--RRSTRRSIHAPQGQDRKLGTKED-LNENVPPVSFWRILKL-NSTEWPYFVVGIFca 720
Cdd:PTZ00243 894 AEVAEVDAAPGGAVDHEPPVAKqeGNAEGGDGAALDAAAGRLMTREEkASGSVPWSTYVAYLRFcGGLHAAGFVLATF-- 971
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 721 iingGLQPAFSIIFSRIIGIFTRDEdpETKRQNSNMFSVLFLV-LGIISFITFFLQGFTFGKAGeilTKRLRYMVFRSML 799
Cdd:PTZ00243 972 ----AVTELVTVSSGVWLSMWSTRS--FKLSAATYLYVYLGIVlLGTFSVPLRFFLSYEAMRRG---SRNMHRDLLRSVS 1042
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 800 RQDVSWFDdpknTT--GALTTRLANDAaqvkGAIGSRLAVITQNIANLGTGIIIS-LIYGWQLTLLLLAIVP-------- 868
Cdd:PTZ00243 1043 RGTMSFFD----TTplGRILNRFSRDI----DILDNTLPMSYLYLLQCLFSICSSiLVTSASQPFVLVALVPcgylyyrl 1114
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 869 ----------IIAIAGVVEMKMLS--GQALKDKKELEGAGK---IATEAIENFRTVVSLTREQ---------KFEYM--- 921
Cdd:PTZ00243 1115 mqfynsanreIRRIKSVAKSPVFTllEEALQGSATITAYGKahlVMQEALRRLDVVYSCSYLEnvanrwlgvRVEFLsni 1194
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 922 --YAQSLQVPYRNSLRKAH--IFGVSFSITQAMMYFSYAG-CFRFGAYLVANefMNFQDVLLVFSAIVfGAMAVGQVSSF 996
Cdd:PTZ00243 1195 vvTVIALIGVIGTMLRATSqeIGLVSLSLTMAMQTTATLNwLVRQVATVEAD--MNSVERLLYYTDEV-PHEDMPELDEE 1271
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 997 APDYAKAKVSAAHVImiieKSPLIDSYSPHGLKPNTLE-GNVTFNEVVFNYptRPDIP-VLQGLSLEVKKGQTLALVGSS 1074
Cdd:PTZ00243 1272 VDALERRTGMAADVT----GTVVIEPASPTSAAPHPVQaGSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRT 1345
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1075 GCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPILFDCSIAENIaygDNSRVVSHEEIMQAAKEA 1154
Cdd:PTZ00243 1346 GSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV---DPFLEASSAEVWAALELV 1422
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1155 NIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALV-RQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIA 1233
Cdd:PTZ00243 1423 GLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIA 1502
|
890 900 910 920
....*....|....*....|....*....|....*....|.
gi 925114634 1234 HRLSTIQNADLIVVFQNGKVKEHGTHQQL-LAQKGIYFSMV 1273
Cdd:PTZ00243 1503 HRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSMV 1543
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1037-1255 |
1.93e-42 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 154.94 E-value: 1.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPT-RPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNvqwlrAHL 1115
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1116 GIVSQEPILFD-CSIAENIAYGDNSRVVSHEEIMQAAkeaniHHFIEtlpekyntRVGDKGT------QLSGGQKQRIAI 1188
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERA-----EELLE--------LVGLSGFenayphQLSGGMRQRVAL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 1189 ARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQN--GKVKE 1255
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1037-1258 |
2.56e-42 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 158.72 E-value: 2.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPtrpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQwlRAHLG 1116
Cdd:COG3842 6 LELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1117 IVSQEPILF-DCSIAENIAYGDNSRVVSHEEIMQAAKEA----NIHHFIETLPekyntrvgdkgTQLSGGQKQRIAIARA 1191
Cdd:COG3842 81 MVFQDYALFpHLTVAENVAFGLRMRGVPKAEIRARVAELlelvGLEGLADRYP-----------HQLSGGQQQRVALARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 1192 LVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS---TIqnADLIVVFQNGKVKEHGT 1258
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
394-618 |
3.11e-42 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 162.77 E-value: 3.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPT---DGMVCIDGQDIRTINVRHLRE 470
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 471 ITGVVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEANAYDFImklpnkfDTLVGERGAQLSGGQKQRIAIARA 546
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEALENlgLSRAEARARVLELLEAVGL-------ERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 547 LVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELM 618
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEIL 231
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1046-1257 |
3.91e-42 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 154.20 E-value: 3.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1046 YPTRPD-IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWL---RAHLGIVSQE 1121
Cdd:cd03257 11 FPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirRKEIQMVFQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1122 PI-----LFdcSIAENIAygdnsrvvsheEIMQAAKEANIHHFIETLPEKYNTRVGDKGT-------QLSGGQKQRIAIA 1189
Cdd:cd03257 91 PMsslnpRM--TIGEQIA-----------EPLRIHGKLSKKEARKEAVLLLLVGVGLPEEvlnryphELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 925114634 1190 RALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHG 1257
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
394-623 |
5.79e-42 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 155.28 E-value: 5.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTI-NVRHLREIT 472
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEeNLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 473 GVVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEA----NAYDFIMKLPnkfdtlvgergAQLSGGQKQRIAIA 544
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENlgVPREEMRKRVDEAlklvGMEDFRDREP-----------HLLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 545 RALVRNPKILLLDEATSALDTES-EAVVQVALD-KARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKG------NHDE 616
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGrKEVLETIRKlNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGtpreifSQVE 228
|
....*..
gi 925114634 617 LMKEKGI 623
Cdd:TIGR04520 229 LLKEIGL 235
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1046-1264 |
6.62e-42 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 154.19 E-value: 6.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1046 YPTRP-DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPIL 1124
Cdd:COG1124 11 YGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPYA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1125 -------FDCSIAE--NIAYGDNSRvvshEEIMQAAKEANihhfietLPEKYNTRVGDkgtQLSGGQKQRIAIARALVRQ 1195
Cdd:COG1124 91 slhprhtVDRILAEplRIHGLPDRE----ERIAELLEQVG-------LPPSFLDRYPH---QLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 1196 PHILLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQLLA 1264
Cdd:COG1124 157 PELLLLDEPTSALDV----SVQaEILNllkdlREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
394-620 |
7.23e-42 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 153.68 E-value: 7.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTiNVRHLREITG 473
Cdd:COG1131 1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKEANAydfIMKLPNKFDTLVGergaQLSGGQKQRIAIARALVRN 550
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRFFARlyGLPRKEARERIDELLE---LFGLTDAADRKVG----TLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 551 PKILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELMKE 620
Cdd:COG1131 150 PELLILDEPTSGLDPEArRELWELLRELAAEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
394-608 |
9.54e-42 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 152.64 E-value: 9.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKE-VKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREI- 471
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 472 ---TGVVSQEPVLFAT-TIAENIRYGrenVTMDEIEKAVKEANAYDFI--MKLPNKFDTLVgergAQLSGGQKQRIAIAR 545
Cdd:cd03255 81 rrhIGFVFQSFNLLPDlTALENVELP---LLLAGVPKKERRERAEELLerVGLGDRLNHYP----SELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 546 ALVRNPKILLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIA-HRLSTVRNADVIAGFDDGVI 608
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSEtGKEVMELLRELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
394-612 |
1.48e-41 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 151.90 E-value: 1.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVrHLREItG 473
Cdd:cd03259 1 LELKGLSKTY---GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP-ERRNI-G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFAT-TIAENIRYGRENVTM--DEIEKAVKEANAydfIMKLPNkfdtLVGERGAQLSGGQKQRIAIARALVRN 550
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGLKLRGVpkAEIRARVRELLE---LVGLEG----LLNRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 551 PKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKG 612
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1051-1265 |
2.58e-41 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 152.07 E-value: 2.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1051 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTV---VQLLERfydPLAGSVLIDGKEI--KHLNVQWLRAHLGIVSQEPILF 1125
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTITVDGEDLtdSKKDINKLRRKVGMVFQQFNLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1126 -DCSIAENIAYGdnSRVV---SHEEIMQAAKEAnihhfietLpekynTRVG--DKG----TQLSGGQKQRIAIARALVRQ 1195
Cdd:COG1126 90 pHLTVLENVTLA--PIKVkkmSKAEAEERAMEL--------L-----ERVGlaDKAdaypAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 1196 PHILLLDEATSALDTEsekVVQEALD--K--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQLLAQ 1265
Cdd:COG1126 155 PKVMLFDEPTSALDPE---LVGEVLDvmRdlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1042-1263 |
4.49e-41 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 152.12 E-value: 4.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1042 VVFNYPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQE 1121
Cdd:COG1120 7 LSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1122 PIL-FDCSIAENIAYG--------DNSRVVSHEEIMQAAKEANIHHFIEtlpekynTRVgdkgTQLSGGQKQRIAIARAL 1192
Cdd:COG1120 84 PPApFGLTVRELVALGryphlglfGRPSAEDREAVEEALERTGLEHLAD-------RPV----DELSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 925114634 1193 VRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGKVKEHGTHQQLL 1263
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
394-589 |
5.49e-41 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 150.70 E-value: 5.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRK-EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRhlreiT 472
Cdd:cd03293 1 LEVRNVSKTYGGGGgAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 473 GVVSQEPVLFA-TTIAENIRYGRE--NVTMDEIEKAVKEANAydfimklpnkfdtLVGERGA------QLSGGQKQRIAI 543
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLElqGVPKAEARERAEELLE-------------LVGLSGFenayphQLSGGMRQRVAL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 925114634 544 ARALVRNPKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAH 589
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTH 190
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
394-618 |
7.31e-41 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 150.91 E-value: 7.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITG 473
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFA-TTIAENI-------RYGREnvtmdEIEKAVKEANAydfIMKLPNKfdTLVGERGAQLSGGQKQRIAIAR 545
Cdd:cd03295 79 YVIQQIGLFPhMTVEENIalvpkllKWPKE-----KIRERADELLA---LVGLDPA--EFADRYPHELSGGQQQRVGVAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 546 ALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRL-STVRNADVIAGFDDGVIVEKGNHDELM 618
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
394-589 |
8.24e-41 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 151.40 E-value: 8.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRK-EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRhlreiT 472
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 473 GVVSQEPVLFA-TTIAENIRYGRENVTMDEiEKAVKEANAY-------DFIMKLPnkfdtlvgergAQLSGGQKQRIAIA 544
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLELRGVPK-AERRERARELlelvglaGFEDAYP-----------HQLSGGMRQRVAIA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 925114634 545 RALVRNPKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAH 589
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTH 197
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
111-335 |
9.74e-41 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 152.31 E-value: 9.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 111 EEMTTYAYYYSGIGAGVLVAAYIQVSFWCLAAGRQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGD 190
Cdd:cd18572 33 EAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLST 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 191 KIGMFFQSIATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFG 270
Cdd:cd18572 113 NLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 271 GQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTSLVLSSEYSIGQVLT 335
Cdd:cd18572 193 TEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLVT 257
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
51-367 |
1.07e-40 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 152.32 E-value: 1.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 51 MLVGTMAAIIHGAALPLMMLVFGNMTDSFANAGisrnktfpviinesitnntqhfinhleeEMTTYAYYYSGIGAGVLVA 130
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAG----------------------------DLSLLLWIALLLLLLALLR 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 131 A---YIQVSFWCLAAGRQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSIATFFTGFI 207
Cdd:cd07346 53 AllsYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 208 VGFTRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAK 287
Cdd:cd07346 133 ILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLR 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 288 RIGIKKAITANISIGAAFLLIYASYALAFWYGTSLVLSSEYSIGQvLTVFFSVLIGAFS-IGQASPSIEAFANARGAAYE 366
Cdd:cd07346 213 DANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIGE-LVAFLAYLGMLFGpIQRLANLYNQLQQALASLER 291
|
.
gi 925114634 367 I 367
Cdd:cd07346 292 I 292
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
394-606 |
1.70e-40 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 147.72 E-value: 1.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRT--INVRHLREI 471
Cdd:cd03229 1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDleDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 472 TGVVSQEPVLFAT-TIAENIRYGrenvtmdeiekavkeanaydfimklpnkfdtlvgergaqLSGGQKQRIAIARALVRN 550
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 551 PKILLLDEATSALDTESEAVVQVALD--KARKGRTTIVIAHRLSTVRN-ADVIAGFDDG 606
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
394-619 |
1.83e-40 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 149.95 E-value: 1.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSR-KEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREIT 472
Cdd:COG1124 2 LEVRNLSVSYGQGgRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 473 GVVSQEP---------VlfATTIAENIRYGRENVTMDEIEKAVKEANaydfimkLPnkfDTLVGERGAQLSGGQKQRIAI 543
Cdd:COG1124 82 QMVFQDPyaslhprhtV--DRILAEPLRIHGLPDREERIAELLEQVG-------LP---PSFLDRYPHQLSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 544 ARALVRNPKILLLDEATSALDteseAVVQVA-LD-----KARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDE 616
Cdd:COG1124 150 ARALILEPELLLLDEPTSALD----VSVQAEiLNllkdlREERGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVAD 225
|
...
gi 925114634 617 LMK 619
Cdd:COG1124 226 LLA 228
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
713-1010 |
2.05e-40 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 151.55 E-value: 2.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 713 FVVGIFCAIINGGLQPAFSIIFSRIIGiftrDEDPETKRQNSNMFSVLFLVLGIISFITFFLQGFTFGKAGEILTKRLRY 792
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLID----DVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 793 MVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAI 872
Cdd:cd07346 77 DLFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 873 AGVVEMKMLSGQALKDKKELEGAGKIATEAIENFRTVVSLTREQKFEYMYAQSLQVPYRNSLRKAHIFGVSFSITQAMMY 952
Cdd:cd07346 155 ILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTA 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 953 FSYAGCFRFGAYLVANEFMNFQDVLLVFSAIVFGAMAVGQVSSFAPDYAKAKVSAAHV 1010
Cdd:cd07346 235 LGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1037-1265 |
2.87e-40 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 156.99 E-value: 2.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPTRpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP---LAGSVLIDGKEIKHLNVQWLRA 1113
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1114 HLGIVSQEPI--LFDCSIAENIAYGDNSRVVSHEEIMQAAKEANIHHFIETLPEKYNTrvgdkgtQLSGGQKQRIAIARA 1191
Cdd:COG1123 84 RIGMVFQDPMtqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPH-------QLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1192 LVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTI-QNADLIVVFQNGKVKEHGTHQQLLAQ 1265
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
394-608 |
2.90e-40 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 148.45 E-value: 2.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDI--RTINVRHLREI 471
Cdd:cd03262 1 IEIKNLHKSF---GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 472 TGVVSQEPVLFA-TTIAENIRYGRENVT-MDEIEKavkEANAYDFIMK--LPNKFDtlvgERGAQLSGGQKQRIAIARAL 547
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLAPIKVKgMSKAEA---EERALELLEKvgLADKAD----AYPAQLSGGQQQRVAIARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 548 VRNPKILLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVI 608
Cdd:cd03262 151 AMNPKVMLFDEPTSALDPElVGEVLDVMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
116-647 |
4.08e-40 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 162.84 E-value: 4.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 116 YAYYYSGIGAGvLVAAYIQVSFWCLAAGRQILK-IRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGM 194
Cdd:PLN03232 952 YIVVYALLGFG-QVAVTFTNSFWLISSSLHAAKrLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNM 1030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 195 FFQSIATFFTGFIVgftRGWKLTLVILAISPVLGLSAAIW---------AKILSSFTDKELlaYAKAGavaeEVLAAIRT 265
Cdd:PLN03232 1031 FMNQLWQLLSTFAL---IGTVSTISLWAIMPLLILFYAAYlyyqstsreVRRLDSVTRSPI--YAQFG----EALNGLSS 1101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 266 VIAFGGQKKELERYNKNLEEAKRIGIKkAITAN-------ISIGAAFLLIYASYAL----------AFWYGTSLVLSSEY 328
Cdd:PLN03232 1102 IRAYKAYDRMAKINGKSMDNNIRFTLA-NTSSNrwltirlETLGGVMIWLTATFAVlrngnaenqaGFASTMGLLLSYTL 1180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 329 SIGQVLTvffSVLIGAFSIGQASPSIEAFANARGAAYEIFKIIDNKPSIDSYSKSGhkpdnikgNLEFKNVHFSYpsRKE 408
Cdd:PLN03232 1181 NITTLLS---GVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRG--------SIKFEDVHLRY--RPG 1247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 409 VK-ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITGVVSQEPVLFATTIA 487
Cdd:PLN03232 1248 LPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVR 1327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 488 ENIRYGRENVTMDeIEKAVKEANAYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 567
Cdd:PLN03232 1328 FNIDPFSEHNDAD-LWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT 1406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 568 EAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELM-KEKGIYFKLVTMQTRGNEIELENATGES 646
Cdd:PLN03232 1407 DSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLsRDTSAFFRMVHSTGPANAQYLSNLVFER 1486
|
.
gi 925114634 647 K 647
Cdd:PLN03232 1487 R 1487
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1037-1265 |
6.55e-40 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 148.11 E-value: 6.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPTRP-DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ---LLERfydPLAGSVLIDGKEIKHLN---VQ 1109
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRcinGLER---PTSGSVLVDGTDLTLLSgkeLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1110 WLRAHLGIVSQEPILFDC-SIAENIAYGDNSRVVSHEEImqaakEANIHHFIETlpekyntrVG--DKG----TQLSGGQ 1182
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEI-----EERVLELLEL--------VGleDKAdaypAQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1183 KQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTH 1259
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTV 225
|
....*.
gi 925114634 1260 QQLLAQ 1265
Cdd:cd03258 226 EEVFAN 231
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1051-1265 |
6.74e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 147.90 E-value: 6.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1051 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWlRAHLGIVSQEPILF-DCSI 1129
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIGYVPQEPALYpDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1130 AENIAYGDNSRVVSHEEIMQAAKEAnihhfIET--LPEKYNTRVGdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSA 1207
Cdd:COG1131 91 RENLRFFARLYGLPRKEARERIDEL-----LELfgLTDAADRKVG----TLSGGMKQRLGLALALLHDPELLILDEPTSG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1208 LDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQLLAQ 1265
Cdd:COG1131 162 LDPEARRELWELLRElAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
394-612 |
1.02e-39 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 151.40 E-value: 1.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVrHLREItG 473
Cdd:COG3842 6 LELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP-EKRNV-G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFA-TTIAENIRYG--RENVTMDEIEKAVKEAnaydfimkLpnkfdTLVGERG------AQLSGGQKQRIAIA 544
Cdd:COG3842 81 MVFQDYALFPhLTVAENVAFGlrMRGVPKAEIRARVAEL--------L-----ELVGLEGladrypHQLSGGQQQRVALA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 545 RALVRNPKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAHRLS---TVrnADVIAGFDDGVIVEKG 612
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVG 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
395-606 |
1.35e-39 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 144.31 E-value: 1.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 395 EFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITGV 474
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 475 VSQepvlfattiaenirygrenvtmdeiekavkeanaydfimklpnkfdtlvgergaqLSGGQKQRIAIARALVRNPKIL 554
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 925114634 555 LLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTVRNA-DVIAGFDDG 606
Cdd:cd00267 103 LLDEPTSGLDPASrERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
394-620 |
1.43e-39 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 147.88 E-value: 1.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITG 473
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVL-FATTIAENIRYGR---------ENVTMDEI-EKAVKEANAYDFIMKLpnkFDTlvgergaqLSGGQKQRIA 542
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGRyphlglfgrPSAEDREAvEEALERTGLEHLADRP---VDE--------LSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 543 IARALVRNPKILLLDEATSALDteseavV--QVA-LD-----KARKGRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKGN 613
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLD------LahQLEvLEllrrlARERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGP 221
|
....*..
gi 925114634 614 HDELMKE 620
Cdd:COG1120 222 PEEVLTP 228
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
82-627 |
1.85e-39 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 160.50 E-value: 1.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 82 AGISRNKTFPVIINESITNNTQhfiNHLEEEMTTYAYYysGIGAGVLVAAY-IQVSFWCLAAGRqilKIRKQFFHAIMRQ 160
Cdd:TIGR00957 980 SALASNYWLSLWTDDPMVNGTQ---NNTSLRLSVYGAL--GILQGFAVFGYsMAVSIGGIQASR---VLHQDLLHNKLRS 1051
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 161 EIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSIATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAIWAKilSS 240
Cdd:TIGR00957 1052 PMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVA--SS 1129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 241 FTDKELLAYAKAGAVAE--EVLAAIRTVIAFGGQKKELERYNKNLEEAKRiGIKKAITAN--ISIGAAFL-----LIYAS 311
Cdd:TIGR00957 1130 RQLKRLESVSRSPVYSHfnETLLGVSVIRAFEEQERFIHQSDLKVDENQK-AYYPSIVANrwLAVRLECVgncivLFAAL 1208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 312 YALAFWYGTS--LV-LSSEYSIgQVlTVFFSVLIgafsigQASPSIEAFANARGAAYEIFKIIDNKPSI--DSYSKSGHK 386
Cdd:TIGR00957 1209 FAVISRHSLSagLVgLSVSYSL-QV-TFYLNWLV------RMSSEMETNIVAVERLKEYSETEKEAPWQiqETAPPSGWP 1280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 387 PdniKGNLEFKNVHFSYpsRKEVK-ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINV 465
Cdd:TIGR00957 1281 P---RGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGL 1355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 466 RHLREITGVVSQEPVLFATTIAENI----RYGRENVTMdeiekAVKEANAYDFIMKLPNKFDTLVGERGAQLSGGQKQRI 541
Cdd:TIGR00957 1356 HDLRFKITIIPQDPVLFSGSLRMNLdpfsQYSDEEVWW-----ALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLV 1430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 542 AIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEK 621
Cdd:TIGR00957 1431 CLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQR 1510
|
....*.
gi 925114634 622 GIYFKL 627
Cdd:TIGR00957 1511 GIFYSM 1516
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1037-1255 |
2.00e-39 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 147.54 E-value: 2.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPTRP-DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLnvqwlRAHL 1115
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP-----GPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1116 GIVSQEPILFD-CSIAENIAYGDNSRVVSHEEIMQAAKEA----NIHHFIETLPekyntrvgdkgTQLSGGQKQRIAIAR 1190
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERARELlelvGLAGFEDAYP-----------HQLSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 1191 ALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH------RLstiqnADLIVVFQN--GKVKE 1255
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
394-620 |
9.15e-39 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 147.51 E-value: 9.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRK-EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDP---TDGMVCIDGQDIRTINVRHLR 469
Cdd:COG0444 2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 470 EITG----VVSQEPvlFA---------TTIAENIRYgRENVTMDEIEKAVKEA-------NAYDFIMKLPNkfdtlvger 529
Cdd:COG0444 82 KIRGreiqMIFQDP--MTslnpvmtvgDQIAEPLRI-HGGLSKAEARERAIELlervglpDPERRLDRYPH--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 530 gaQLSGGQKQRIAIARALVRNPKILLLDEATSALDteseAVVQVA-LD-----KARKGRTTIVIAHRLSTVRN-ADVIA- 601
Cdd:COG0444 150 --ELSGGMRQRVMIARALALEPKLLIADEPTTALD----VTIQAQiLNllkdlQRELGLAILFITHDLGVVAEiADRVAv 223
|
250 260
....*....|....*....|.
gi 925114634 602 --GfddGVIVEKGNHDELMKE 620
Cdd:COG0444 224 myA---GRIVEEGPVEELFEN 241
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1038-1252 |
1.77e-38 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 141.23 E-value: 1.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1038 TFNEVVFNYPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGI 1117
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1118 VSQepilfdcsiaeniaygdnsrvvsheeimqaakeanihhfietlpekyntrvgdkgtqLSGGQKQRIAIARALVRQPH 1197
Cdd:cd00267 78 VPQ---------------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1198 ILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNA-DLIVVFQNGK 1252
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
716-1003 |
1.96e-38 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 145.78 E-value: 1.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 716 GIFCAIINGGLQPAFSIIFSRIIGIFTRDEDPETKRQNSNMFSVLFLVLGIISFITFFLqgftFGKAGEILTKRLRYMVF 795
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYL----FNIAGERIVARLRRDLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 796 RSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGV 875
Cdd:cd18557 77 SSLLRQEIAFFD--KHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 876 V---EMKMLSGQALkdkKELEGAGKIATEAIENFRTVVSLTREQKFEYMYAQSLQVPYRNSLRKAHIFGVSFSITQAMMY 952
Cdd:cd18557 155 IygrYIRKLSKEVQ---DALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIY 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 925114634 953 FSYAGCFRFGAYLVANEFMNFQDVL--LVFSAIVfgAMAVGQVSSFAPDYAKA 1003
Cdd:cd18557 232 LSLLLVLWYGGYLVLSGQLTVGELTsfILYTIMV--ASSVGGLSSLLADIMKA 282
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1048-1252 |
2.20e-38 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 141.56 E-value: 2.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1048 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLN--VQWLRAHLGIVSQEPILF 1125
Cdd:cd03229 9 RYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFALF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1126 -DCSIAENIAYGdnsrvvsheeimqaakeanihhfietlpekyntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEA 1204
Cdd:cd03229 89 pHLTVLENIALG-----------------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 925114634 1205 TSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGK 1252
Cdd:cd03229 128 TSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1053-1273 |
2.55e-38 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 144.28 E-value: 2.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1053 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPILFDCSIAEN 1132
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1133 IaygDNSRVVSHEEIMQAAKEANIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1212
Cdd:cd03288 115 L---DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 1213 EKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLAQK-GIYFSMV 1273
Cdd:cd03288 192 ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLV 253
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
394-564 |
3.45e-38 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 146.76 E-value: 3.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHlREItG 473
Cdd:COG3839 4 LELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-RNI-A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLF-ATTIAENIRYG--RENVTMDEIEKAVKEANAydfIMKLpnkfDTLVGERGAQLSGGQKQRIAIARALVRN 550
Cdd:COG3839 79 MVFQSYALYpHMTVYENIAFPlkLRKVPKAEIDRRVREAAE---LLGL----EDLLDRKPKQLSGGQRQRVALGRALVRE 151
|
170
....*....|....
gi 925114634 551 PKILLLDEATSALD 564
Cdd:COG3839 152 PKVFLLDEPLSNLD 165
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1037-1266 |
3.67e-38 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 144.11 E-value: 3.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPtRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQW-LRAHL 1115
Cdd:TIGR04520 1 IEVENVSFSYP-ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1116 GIVSQEPilfD----CSIAEN-IAYGDNSRVVSHEEIMQ----AAKEANIHHFIETLPEKyntrvgdkgtqLSGGQKQRI 1186
Cdd:TIGR04520 80 GMVFQNP---DnqfvGATVEDdVAFGLENLGVPREEMRKrvdeALKLVGMEDFRDREPHL-----------LSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1187 AIARALVRQPHILLLDEATSALDTESEKVVQEALDKAR--EGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLA 1264
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFS 225
|
..
gi 925114634 1265 QK 1266
Cdd:TIGR04520 226 QV 227
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1046-1258 |
4.95e-38 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 145.99 E-value: 4.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1046 YPTRP-DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ---LLERfydPLAGSVLIDGKEIKHLNVQWLRA---HLGIV 1118
Cdd:COG1135 11 FPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRcinLLER---PTSGSVLVDGVDLTALSERELRAarrKIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1119 SQEPILFD-CSIAENIAY-----GdnsrvVSHEEIMQAAKEanihhfietLPEkyntRVG--DKG----TQLSGGQKQRI 1186
Cdd:COG1135 88 FQHFNLLSsRTVAENVALpleiaG-----VPKAEIRKRVAE---------LLE----LVGlsDKAdaypSQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 1187 AIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGT 1258
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1053-1264 |
6.56e-38 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 142.43 E-value: 6.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1053 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNV---QWLRAHLGIVSQEPILFDC-S 1128
Cdd:COG1127 19 VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELRRRIGMLFQGGALFDSlT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1129 IAENIAYG-DNSRVVSHEEIMQAAKEA----NIHHFIETLPEkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDE 1203
Cdd:COG1127 99 VFENVAFPlREHTDLSEAEIRELVLEKlelvGLPGAADKMPS-----------ELSGGMRKRVALARALALDPEILLYDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 925114634 1204 ATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQLLA 1264
Cdd:COG1127 168 PTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
394-622 |
9.35e-38 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 142.30 E-value: 9.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREItG 473
Cdd:COG4555 2 IEVENLSKKY---GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI-G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKEanaYDFIMKLPNKFDTLVGErgaqLSGGQKQRIAIARALVRN 550
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRYFAElyGLFDEELKKRIEE---LIELLGLEEFLDRRVGE----LSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 925114634 551 PKILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELMKEKG 622
Cdd:COG4555 151 PKVLLLDEPTNGLDVMArRLLREILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
89-351 |
9.83e-38 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 143.81 E-value: 9.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 89 TFPVIINESITNNTQHFINHLEEEMTTYAYYYSGIGAGVLVAAYIQVSFWCL--AAGRQILKIRKQFFHAIMRQEIGWFD 166
Cdd:cd18573 14 SVPFAIGKLIDVASKESGDIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLriAGERIVARLRKRLFKSILRQDAAFFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 167 VHDVGELNTRLTDDVSKINEGIGDKIGMFFQSIATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKEL 246
Cdd:cd18573 94 KNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 247 LAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTSLVLSS 326
Cdd:cd18573 174 DALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASG 253
|
250 260
....*....|....*....|....*..
gi 925114634 327 EYSIGQvLTVF--FSVLIGAfSIGQAS 351
Cdd:cd18573 254 ELTVGD-LTSFlmYAVYVGS-SVSGLS 278
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1037-1264 |
1.13e-37 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 142.05 E-value: 1.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPTRPdiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLG 1116
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1117 IVSQEPILF-DCSIAENIAYGDNSRVVSHEEIMQAAKEanIHHFIETLPEKYNTRVGDkgtQLSGGQKQRIAIARALVRQ 1195
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIALVPKLLKWPKEKIRERADE--LLALVGLDPAEFADRYPH---ELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 1196 PHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRL-STIQNADLIVVFQNGKVKEHGTHQQLLA 1264
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1038-1267 |
1.50e-37 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 141.53 E-value: 1.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1038 TFNEVVFNYPtrpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNvQWLRAHLGI 1117
Cdd:COG4555 3 EVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1118 VSQEPILFD-CSIAENIAYGDNSRVVSHEEIMQAAKEAnIHHFIetLPEKYNTRVGDkgtqLSGGQKQRIAIARALVRQP 1196
Cdd:COG4555 79 LPDERGLYDrLTVRENIRYFAELYGLFDEELKKRIEEL-IELLG--LEEFLDRRVGE----LSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 1197 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQN-ADLIVVFQNGKVKEHGTHQQLLAQKG 1267
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1039-1268 |
1.55e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 142.44 E-value: 1.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1039 FNEVVFNYPTRpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIV 1118
Cdd:PRK13632 10 VENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1119 SQEPilfD-----CSIAENIAYGDNSRVVSHEE----IMQAAKEANIHHFIETLPEKyntrvgdkgtqLSGGQKQRIAIA 1189
Cdd:PRK13632 89 FQNP---DnqfigATVEDDIAFGLENKKVPPKKmkdiIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1190 RALVRQPHILLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLAQKG 1267
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKE 234
|
.
gi 925114634 1268 I 1268
Cdd:PRK13632 235 I 235
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
394-610 |
2.21e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 140.19 E-value: 2.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTIN---VRHLRE 470
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 471 ITGVVSQE-PVLFATTIAENIRY-----GRENvtmDEIEKAVKEAnaydfIMK--LPNKFDTLVgergAQLSGGQKQRIA 542
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSR---KEIRRRVREV-----LDLvgLSDKAKALP----HELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 543 IARALVRNPKILLLDEATSALDTE-SEAVVQVaLDKARKGRTTIVIA-HRLSTVRNAD--VIAgFDDGVIVE 610
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPEtSWEIMEL-LEEINRRGTTVLIAtHDLELVDRMPkrVLE-LEDGRLVR 217
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
394-617 |
3.04e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 140.94 E-value: 3.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD--P---TDGMVCIDGQDI--RTINVR 466
Cdd:COG1117 12 IEVRNLNVYY---GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 467 HLREITGVVSQEPVLFATTIAENIRYG------RENVTMDEI-EKAVKEANAYDFImklpnKfDTLvGERGAQLSGGQKQ 539
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIvEESLRKAALWDEV-----K-DRL-KKSALGLSGGQQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 540 RIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKgRTTIVI-------AHRLStvrnaDVIAGFDDGVIVEKG 612
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGELVEFG 235
|
....*
gi 925114634 613 NHDEL 617
Cdd:COG1117 236 PTEQI 240
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
395-612 |
4.27e-37 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 143.40 E-value: 4.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 395 EFKNVHFSYP-SRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLRE--- 470
Cdd:PRK11153 3 ELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 471 -ItGVVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKE----------ANAYdfimklPnkfdtlvgergAQLSGG 536
Cdd:PRK11153 83 qI-GMIFQHFNLLSSrTVFDNVALPLElaGTPKAEIKARVTEllelvglsdkADRY------P-----------AQLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 537 QKQRIAIARALVRNPKILLLDEATSALDTE-SEAVVQVALDKARKGRTTIV-IAHRLSTVRN-ADVIAGFDDGVIVEKG 612
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPAtTRSILELLKDINRELGLTIVlITHEMDVVKRiCDRVAVIDAGRLVEQG 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1037-1253 |
5.19e-37 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 139.16 E-value: 5.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPTRPD-IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWL---- 1111
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1112 RAHLGIVSQE----PILfdcSIAENIAYGDNSRVVSHEEIMQAAKEAnihhfIET--LPEKYNTRVGdkgtQLSGGQKQR 1185
Cdd:cd03255 81 RRHIGFVFQSfnllPDL---TALENVELPLLLAGVPKKERRERAEEL-----LERvgLGDRLNHYPS----ELSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1186 IAIARALVRQPHILLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIA-HRLSTIQNADLIVVFQNGKV 1253
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLrELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1037-1252 |
6.51e-37 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 138.37 E-value: 6.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPTRPDI--PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ErfYDPLAGSVLIDGKeikhlnvqwlr 1112
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPGS----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1113 ahLGIVSQEPILFDCSIAENIAYG---DNSRVvshEEIMQA-AKEANIhhfiETLPEKYNTRVGDKGTQLSGGQKQRIAI 1188
Cdd:cd03250 68 --IAYVSQEPWIQNGTIRENILFGkpfDEERY---EKVIKAcALEPDL----EILPDGDLTEIGEKGINLSGGQKQRISL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 1189 ARALVRQPHILLLDEATSALDTES-----EKVVQEALdkaREGRTCIVIAHRLSTIQNADLIVVFQNGK 1252
Cdd:cd03250 139 ARAVYSDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1051-1262 |
9.16e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 139.79 E-value: 9.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1051 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD--PLA---GSVLIDGKEI--KHLNVQWLRAHLGIVSQEPI 1123
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGArveGEILLDGEDIydPDVDVVELRRRVGMVFQKPN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1124 LFDCSIAENIAYG-----DNSRVVSHEEIMQAAKEANihhfietLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHI 1198
Cdd:COG1117 103 PFPKSIYDNVAYGlrlhgIKSKSELDEIVEESLRKAA-------LWDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEV 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 925114634 1199 LLLDEATSALDTESEKVVQEALDKAREgRTCIVI-------AHRLStiqnaDLIVVFQNGKVKEHGTHQQL 1262
Cdd:COG1117 176 LLMDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGELVEFGPTEQI 240
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
394-609 |
2.04e-36 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 138.27 E-value: 2.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREI-- 471
Cdd:COG3638 3 LELRNLSKRYPGGT--PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 472 -TGVVSQEPVLFA-TTIAENI---RYGREN--------VTMDEIEKAvkeanaydfimklpnkFDTL--VG------ERG 530
Cdd:COG3638 81 rIGMIFQQFNLVPrLSVLTNVlagRLGRTStwrsllglFPPEDRERA----------------LEALerVGladkayQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 531 AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE-SEAVVQVALDKAR-KGRTTIVIAHRLSTVRN-ADVIAGFDDGV 607
Cdd:COG3638 145 DQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKtARQVMDLLRRIAReDGITVVVNLHQVDLARRyADRIIGLRDGR 224
|
..
gi 925114634 608 IV 609
Cdd:COG3638 225 VV 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
394-606 |
3.39e-36 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 136.06 E-value: 3.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKEV--KILKGLNLKVQSGQTVALVGNSGCGKSTTVQ-LMQRLyDPTDGMVCIDGQdirtinvrhlre 470
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGEL-EKLSGSVSVPGS------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 471 iTGVVSQEPVLFATTIAENIRYGREnvtMDEIE-KAVKEANA--YDFIMkLPNKFDTLVGERGAQLSGGQKQRIAIARAL 547
Cdd:cd03250 68 -IAYVSQEPWIQNGTIRENILFGKP---FDEERyEKVIKACAlePDLEI-LPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 925114634 548 VRNPKILLLDEATSALDTESEAVV--QVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDG 606
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVGRHIfeNCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1037-1264 |
3.70e-36 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 137.25 E-value: 3.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNV---QWLRA 1113
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1114 HLGIVSQEPILFDC-SIAENIAYG--DNSRvVSHEEIMQAAKE----ANIHHFIETLPEkyntrvgdkgtQLSGGQKQRI 1186
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPlrEHTR-LSEEEIREIVLEkleaVGLRGAEDLYPA-----------ELSGGMKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1187 AIARALVRQPHILLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTI-QNADLIVVFQNGKVKEHGTHQQLL 1263
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELR 225
|
.
gi 925114634 1264 A 1264
Cdd:cd03261 226 A 226
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
394-621 |
1.05e-35 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 136.16 E-value: 1.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREI-- 471
Cdd:cd03256 1 IEVENLSKTYPNGK--KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 472 -TGVVSQEPVLFA-TTIAENIRYGR-----------ENVTMDEIEKAVKEANAYDfIMKLPNKfdtlvgeRGAQLSGGQK 538
Cdd:cd03256 79 qIGMIFQQFNLIErLSVLENVLSGRlgrrstwrslfGLFPKEEKQRALAALERVG-LLDKAYQ-------RADQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 539 QRIAIARALVRNPKILLLDEATSALDTE-SEAVVQVALDKAR-KGRTTIVIAHRLSTVR-NADVIAGFDDGVIVEKGNHD 615
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPAsSRQVMDLLKRINReEGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPA 230
|
....*.
gi 925114634 616 ELMKEK 621
Cdd:cd03256 231 ELTDEV 236
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
395-623 |
1.41e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 136.66 E-value: 1.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 395 EFKNVHFSYPSrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITGV 474
Cdd:PRK13632 9 KVENVSFSYPN-SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 475 VSQEP--VLFATTIAENIRYGREN--VTMDE----IEKAVKEANAYDFIMKLPNKfdtlvgergaqLSGGQKQRIAIARA 546
Cdd:PRK13632 88 IFQNPdnQFIGATVEDDIAFGLENkkVPPKKmkdiIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 547 LVRNPKILLLDEATSALDTES-EAVVQVALDKARKG-RTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGI 623
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGkREIKKIMVDLRKTRkKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEI 235
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
394-618 |
1.43e-35 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 135.61 E-value: 1.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNV--HFSypsrkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIR--TINVRHLR 469
Cdd:PRK09493 2 IEFKNVskHFG-----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 470 EITGVVSQEPVLFATTIA-ENIRYGRENVtmdeieKAVKEANAYDFIMKLPNKfdtlVG--ERG----AQLSGGQKQRIA 542
Cdd:PRK09493 77 QEAGMVFQQFYLFPHLTAlENVMFGPLRV------RGASKEEAEKQARELLAK----VGlaERAhhypSELSGGQQQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 543 IARALVRNPKILLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELM 618
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1040-1265 |
1.43e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 137.07 E-value: 1.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1040 NEVVFNYPTRPDiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVS 1119
Cdd:PRK13635 9 EHISFRYPDAAT-YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1120 QEPilfD-----CSIAENIAYGDNSRVVSHEE----IMQAAKEANIHHFIETLPEKyntrvgdkgtqLSGGQKQRIAIAR 1190
Cdd:PRK13635 88 QNP---DnqfvgATVQDDVAFGLENIGVPREEmverVDQALRQVGMEDFLNREPHR-----------LSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1191 ALVRQPHILLLDEATSALDTESEkvvQEALD-----KAREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLAQ 1265
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGR---REVLEtvrqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
394-608 |
1.70e-35 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 132.91 E-value: 1.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREItG 473
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRI-G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFAT-TIAENIRYgrenvtmdeiekavkeanaydfimklpnkfdtlvgergaqlSGGQKQRIAIARALVRNPK 552
Cdd:cd03230 77 YLPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 553 ILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVI 608
Cdd:cd03230 116 LLILDEPTSGLDPESrREFWELLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1051-1253 |
2.07e-35 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 134.19 E-value: 2.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1051 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEI--KHLNVQWLRAHLGIVSQEPILF-DC 1127
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFpHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1128 SIAENIAYGdnSRVVSHEEIMQAAKEAnihhfietlpEKYNTRVG--DKGT----QLSGGQKQRIAIARALVRQPHILLL 1201
Cdd:cd03262 92 TVLENITLA--PIKVKGMSKAEAEERA----------LELLEKVGlaDKADaypaQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1202 DEATSALDTEsekVVQEALDK----AREGRTCIVIAHRLSTIQN-ADLIVVFQNGKV 1253
Cdd:cd03262 160 DEPTSALDPE---LVGEVLDVmkdlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1054-1263 |
2.13e-35 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 135.16 E-value: 2.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQwlRAHLGIVSQEPILF-DCSIAEN 1132
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1133 IAYG----DNSRVVSHEEIMQAAKEANIHHFIETLPEKyntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATSAL 1208
Cdd:cd03299 92 IAYGlkkrKVDKKEIERKVLEIAEMLGIDHLLNRKPET-----------LSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 1209 DTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQLL 1263
Cdd:cd03299 161 DVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
119-628 |
2.18e-35 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 147.19 E-value: 2.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 119 YYSGIGAGVlvaAYIQV------SFW----CLAAGRqilKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGI 188
Cdd:PLN03130 954 FYNLIYALL---SFGQVlvtllnSYWlimsSLYAAK---RLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNV 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 189 GDKIGMFFQSIATFFTGFI-VGFTRgwklTLVILAISPVLGL---------SAAIWAKILSSFTDKELlaYAKAGavaeE 258
Cdd:PLN03130 1028 AVFVNMFLGQIFQLLSTFVlIGIVS----TISLWAIMPLLVLfygaylyyqSTAREVKRLDSITRSPV--YAQFG----E 1097
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 259 VLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIkkaitANIS-----------IGAAFLLIYASYAL----------AFW 317
Cdd:PLN03130 1098 ALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTL-----VNMSsnrwlairletLGGLMIWLTASFAVmqngraenqaAFA 1172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 318 YGTSLVLSSEYSIGQVLTvffSVLIGAfSIGQAS-PSIEAFANARGAAYEIFKIIDNKPSIDSYSKSGhkpdnikgNLEF 396
Cdd:PLN03130 1173 STMGLLLSYALNITSLLT---AVLRLA-SLAENSlNAVERVGTYIDLPSEAPLVIENNRPPPGWPSSG--------SIKF 1240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 397 KNVHFSYpsRKEVK-ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITGVV 475
Cdd:PLN03130 1241 EDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGII 1318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 476 SQEPVLFATTIAENIRYGRENVTMDEIEkAVKEANAYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILL 555
Cdd:PLN03130 1319 PQAPVLFSGTVRFNLDPFNEHNDADLWE-SLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILV 1397
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 925114634 556 LDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDEL-MKEKGIYFKLV 628
Cdd:PLN03130 1398 LDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLlSNEGSAFSKMV 1471
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1037-1257 |
3.14e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 134.02 E-value: 3.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPtrPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLN---VQWLRA 1113
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1114 HLGIVSQE-PILFDCSIAENIAY-----GdnsrvVSHEEIMQAAKEA----NIHHFIETLPEkyntrvgdkgtQLSGGQK 1183
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtG-----KSRKEIRRRVREVldlvGLSDKAKALPH-----------ELSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1184 QRIAIARALVRQPHILLLDEATSALDTE-SEKVVqEALDKAREGRTCIVIA-HRLSTIQNADL-IVVFQNGKVKEHG 1257
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1037-1265 |
6.36e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 134.06 E-value: 6.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLnvqwlRAHLG 1116
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1117 IVSQE-------PIlfdcSIAENIAYGDNSRV--------VSHEEIMQAAKEANIHHFIetlpekyNTRVGdkgtQLSGG 1181
Cdd:COG1121 79 YVPQRaevdwdfPI----TVRDVVLMGRYGRRglfrrpsrADREAVDEALERVGLEDLA-------DRPIG----ELSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1182 QKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVFqNGKVKEHGTH 1259
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVrEYFDRVLLL-NRGLVAHGPP 222
|
....*.
gi 925114634 1260 QQLLAQ 1265
Cdd:COG1121 223 EEVLTP 228
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
125-364 |
8.70e-35 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 134.92 E-value: 8.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 125 AGVLVA----AYIQVSFWCLAAGRQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSIA 200
Cdd:cd18576 43 LGLFLLqavfSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQIL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 201 TFFTGFIVGFTRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYN 280
Cdd:cd18576 123 TLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 281 KNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTSLVLSSEYSIGQVLT-VFFSVLIGAfSIGQASPSIEAFAN 359
Cdd:cd18576 203 KALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAfLLYTLFIAG-SIGSLADLYGQLQK 281
|
....*
gi 925114634 360 ARGAA 364
Cdd:cd18576 282 ALGAS 286
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1059-1265 |
9.81e-35 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 134.31 E-value: 9.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1059 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRA----HLGIVSQEPILF-DCSIAENI 1133
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1134 AYGDNSRVVSHEEIMQAAKEA----NIHHFIETLPekyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1209
Cdd:cd03294 124 AFGLEVQGVPRAEREERAAEAlelvGLEGWEHKYP-----------DELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 1210 TESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGKVKEHGTHQQLLAQ 1265
Cdd:cd03294 193 PLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
416-618 |
1.28e-34 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 133.92 E-value: 1.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 416 NLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREI----TGVVSQEPVLFA-TTIAENI 490
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLPhRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 491 RYGRENVTMDEIEKAVKEANAY------DFIMKLPNkfdtlvgergaQLSGGQKQRIAIARALVRNPKILLLDEATSALD 564
Cdd:cd03294 124 AFGLEVQGVPRAEREERAAEALelvgleGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 565 TESEAVVQVALDK--ARKGRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKGNHDELM 618
Cdd:cd03294 193 PLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1037-1253 |
2.55e-34 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 132.49 E-value: 2.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPTrpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLN---VQWLRA 1113
Cdd:COG3638 3 LELRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1114 HLGIVSQEPILFD-CSIAENI---AYGDNS------RVVSHEEIMQAakeaniHHFIET--LPEKYNTRVGdkgtQLSGG 1181
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVlagRLGRTStwrsllGLFPPEDRERA------LEALERvgLADKAYQRAD----QLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 1182 QKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTIQN-ADLIVVFQNGKV 1253
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrRIAREdGITVVVNLHQVDLARRyADRIIGLRDGRV 225
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
406-620 |
3.27e-34 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 134.47 E-value: 3.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 406 RKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREI---TGVVSQEPvlF 482
Cdd:COG4608 28 VGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLrrrMQMVFQDP--Y 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 483 A---------TTIAENIRYgRENVTMDEIEKAVKEA------NAyDFIMKLPNKFdtlvgergaqlSGGQKQRIAIARAL 547
Cdd:COG4608 106 AslnprmtvgDIIAEPLRI-HGLASKAERRERVAELlelvglRP-EHADRYPHEF-----------SGGQRQRIGIARAL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 548 VRNPKILLLDEATSALDTESEA-VVQVALD-KARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELMKE 620
Cdd:COG4608 173 ALNPKLIVCDEPVSALDVSIQAqVLNLLEDlQDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1051-1262 |
3.69e-34 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 131.21 E-value: 3.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1051 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQwlRAHLGIVSQEPILF-DCSI 1129
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVFQNYALFpHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1130 AENIAYGDNSRVVSHEEIMQAAKEAniHHFIETlpEKYNTRvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1209
Cdd:cd03300 90 FENIAFGLRLKKLPKAEIKERVAEA--LDLVQL--EGYANR---KPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 1210 TESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGKVKEHGTHQQL 1262
Cdd:cd03300 163 LKLRKDMQLELKRlqKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
411-628 |
8.05e-34 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 131.18 E-value: 8.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 411 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITGVVSQEPVLFATTIAENI 490
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 491 RYGREnVTMDEIEKAVKEANAYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAV 570
Cdd:cd03288 116 DPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENI 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 571 VQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELM-KEKGIYFKLV 628
Cdd:cd03288 195 LQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLV 253
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1048-1265 |
8.86e-34 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 133.73 E-value: 8.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1048 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPLAGSVLIDGKEIK-HLNVQwlRAHLGIVSQEPI 1123
Cdd:COG1118 11 RFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDLFtNLPPR--ERRVGFVFQHYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1124 LF-DCSIAENIAYGDNSRVVSHEEIMQAAKE----ANIHHFIETLPekyntrvgdkgTQLSGGQKQRIAIARALVRQPHI 1198
Cdd:COG1118 86 LFpHMTVAENIAFGLRVRPPSKAEIRARVEEllelVQLEGLADRYP-----------SQLSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1199 LLLDEATSALDT----ESEKVVQEALDkaREGRTCIVIAH------RLstiqnADLIVVFQNGKVKEHGTHQQLLAQ 1265
Cdd:COG1118 155 LLLDEPFGALDAkvrkELRRWLRRLHD--ELGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1051-1258 |
1.59e-33 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 133.92 E-value: 1.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1051 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQwlRAHLGIVSQEPILF-DCSI 1129
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFpHMTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1130 AENIAYGDNSRVVSHEEI----MQAAKEANIHHFIETLPekyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEAT 1205
Cdd:PRK09452 104 FENVAFGLRMQKTPAAEItprvMEALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1206 SALDTESEKVVQEALdKA--RE-GRTCIVIAH-RLSTIQNADLIVVFQNGKVKEHGT 1258
Cdd:PRK09452 173 SALDYKLRKQMQNEL-KAlqRKlGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1037-1253 |
3.13e-33 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 128.29 E-value: 3.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPtrPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLN---VQWLRA 1113
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1114 HLGIVSQE-PILFDCSIAENIAYGDNSRVVSHEEIMQAAKEA----NIHHFIETLPEkyntrvgdkgtQLSGGQKQRIAI 1188
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFALEVTGVPPREIRKRVPAAlelvGLSHKHRALPA-----------ELSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1189 ARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNA--DLIVVFQNGKV 1253
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTtrHRVIALERGKL 214
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
731-997 |
3.62e-33 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 130.33 E-value: 3.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 731 SIIFSRIIG-----IFTRDEDPETKRQNSNMFSVLFLVLGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSW 805
Cdd:cd18573 12 TMSVPFAIGklidvASKESGDIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 806 FDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQA 885
Cdd:cd18573 92 FD--KNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 886 LKDKKELEGAGKIATEAIENFRTVVSLTREQKFEYMYAQSLQVPYRNSLRKAHIFGVSFSITQAMMYFSYAGCFRFGAYL 965
Cdd:cd18573 170 KQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSL 249
|
250 260 270
....*....|....*....|....*....|..
gi 925114634 966 VANefmnfqdvllvfsaivfGAMAVGQVSSFA 997
Cdd:cd18573 250 VAS-----------------GELTVGDLTSFL 264
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1048-1247 |
4.74e-33 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 127.21 E-value: 4.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1048 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWlRAHLGIVSQEPILF-D 1126
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLAYLGHADGLKpE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1127 CSIAENIA-----YGdnsRVVSHEEIMQAAKEANIHHFIETLPEkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLL 1201
Cdd:COG4133 90 LTVRENLRfwaalYG---LRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 925114634 1202 DEATSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQNADLIVV 1247
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1046-1265 |
7.45e-33 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 130.17 E-value: 7.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1046 YPTRP-DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLA---GSVLIDGKEIKHLNVQWLRA----HLGI 1117
Cdd:COG0444 11 FPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKELRKirgrEIQM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1118 VSQEP---------ILFdcSIAENIAYgdnSRVVSHEEIMQAAKEA----NIHHfietlPEKyntRVGDKGTQLSGGQKQ 1184
Cdd:COG0444 91 IFQDPmtslnpvmtVGD--QIAEPLRI---HGGLSKAEARERAIELlervGLPD-----PER---RLDRYPHELSGGMRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1185 RIAIARALVRQPHILLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTI-QNADLIVVFQNGKVKEHG 1257
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDV----TIQaQILNllkdlQRELGLAILFITHDLGVVaEIADRVAVMYAGRIVEEG 233
|
....*...
gi 925114634 1258 THQQLLAQ 1265
Cdd:COG0444 234 PVEELFEN 241
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1037-1262 |
8.13e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 130.96 E-value: 8.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPtrpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQwlRAHLG 1116
Cdd:COG3839 4 LELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1117 IVSQEPILFD-CSIAENIAYGDNSRVVSHEEIMQAAKEA----NIHHFIETLPekyntrvgdkgTQLSGGQKQRIAIARA 1191
Cdd:COG3839 79 MVFQSYALYPhMTVYENIAFPLKLRKVPKAEIDRRVREAaellGLEDLLDRKP-----------KQLSGGQRQRVALGRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1192 LVRQPHILLLDEATSALD------TESE-KVVQEALdkareGRTCIVIAHRLS---TIqnADLIVVFQNGKVKEHGTHQQ 1261
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDaklrveMRAEiKRLHRRL-----GTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQVGTPEE 220
|
.
gi 925114634 1262 L 1262
Cdd:COG3839 221 L 221
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
394-617 |
1.10e-32 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 130.65 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRT-INVRHLReiT 472
Cdd:COG1118 3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnLPPRERR--V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 473 GVVSQEPVLFA-TTIAENIRYG--RENVTMDEIEKAVKE----------ANAYdfimklPnkfdtlvgergAQLSGGQKQ 539
Cdd:COG1118 78 GFVFQHYALFPhMTVAENIAFGlrVRPPSKAEIRARVEEllelvqleglADRY------P-----------SQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 540 RIAIARALVRNPKILLLDEATSALDTeseavvqvaldKARK-------------GRTTIVIAH-RLSTVRNADVIAGFDD 605
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALDA-----------KVRKelrrwlrrlhdelGGTTVFVTHdQEEALELADRVVVMNQ 209
|
250
....*....|..
gi 925114634 606 GVIVEKGNHDEL 617
Cdd:COG1118 210 GRIEQVGTPDEV 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
394-612 |
1.28e-32 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 126.22 E-value: 1.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPsrkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHlREItG 473
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-RDI-A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFA-TTIAENIRYG--RENVTMDEIEKAVKEANAydfIMKLpnkfDTLVGERGAQLSGGQKQRIAIARALVRN 550
Cdd:cd03301 76 MVFQNYALYPhMTVYDNIAFGlkLRKVPKDEIDERVREVAE---LLQI----EHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 551 PKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAH-RLSTVRNADVIAGFDDGVIVEKG 612
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1037-1265 |
1.33e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 128.31 E-value: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLG 1116
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1117 IVSQEP--ILFDCSIAENIAYGDNSRVVSHEEIMQAAKEA----NIHHFIETLPEKyntrvgdkgtqLSGGQKQRIAIAR 1190
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENKGIPHEEMKERVNEAlelvGMQDFKEREPAR-----------LSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1191 ALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLAQ 1265
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
394-620 |
1.83e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 126.74 E-value: 1.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRtinvRHLREItG 473
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR----RARRRI-G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVL---FATTIAENI---RYGRENVTM-------DEIEKAVKEANAYDFImklpnkfDTLVGErgaqLSGGQKQR 540
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVlmgRYGRRGLFRrpsradrEAVDEALERVGLEDLA-------DRPIGE----LSGGQQQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 541 IAIARALVRNPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLSTVR-NADVIAGFDDGVIVEkGNHDELM 618
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDRVLLLNRGLVAH-GPPEEVL 226
|
..
gi 925114634 619 KE 620
Cdd:COG1121 227 TP 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
394-588 |
2.45e-32 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 125.60 E-value: 2.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSrkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDI---RTINVRHLRE 470
Cdd:cd03292 1 IEFINVTKTYPN--GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlRGRAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 471 ITGVVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKEANAydfIMKLPNKFDTLvgerGAQLSGGQKQRIAIARAL 547
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALEvtGVPPREIRKRVPAALE---LVGLSHKHRAL----PAELSGGEQQRVAIARAI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 925114634 548 VRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIA 588
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1053-1253 |
2.71e-32 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 126.14 E-value: 2.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1053 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEI---KHLNVQWLRAHLGIVSQEPILFD-CS 1128
Cdd:cd03256 15 KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklKGKALRQLRRQIGMIFQQFNLIErLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1129 IAENIAYGDNSRV---------VSHEEImQAAKEAnihhfIET--LPEKYNTRVGdkgtQLSGGQKQRIAIARALVRQPH 1197
Cdd:cd03256 95 VLENVLSGRLGRRstwrslfglFPKEEK-QRALAA-----LERvgLLDKAYQRAD----QLSGGQQQRVAIARALMQQPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 1198 ILLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTI-QNADLIVVFQNGKV 1253
Cdd:cd03256 165 LILADEPVASLDPASSRQVMDLLkRINREeGITVIVSLHQVDLArEYADRIVGLKDGRI 223
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1042-1257 |
3.32e-32 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 124.08 E-value: 3.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1042 VVFNYPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQe 1121
Cdd:cd03214 5 LSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1122 pilfdcsiaeniaygdnsrvvsheeimqAAKEANIHHFIetlpekyntrvgDKG-TQLSGGQKQRIAIARALVRQPHILL 1200
Cdd:cd03214 81 ----------------------------ALELLGLAHLA------------DRPfNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1201 LDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGKVKEHG 1257
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1040-1253 |
4.13e-32 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 123.28 E-value: 4.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1040 NEVVFNYPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQwLRAHLGIVS 1119
Cdd:cd03230 4 RNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1120 QEPILF-DCSIAENIaygdnsrvvsheeimqaakeanihhfietlpekyntrvgdkgtQLSGGQKQRIAIARALVRQPHI 1198
Cdd:cd03230 80 EEPSLYeNLTVRENL-------------------------------------------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1199 LLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGKV 1253
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
394-618 |
5.73e-32 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 132.50 E-value: 5.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRK--------EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLyDPTDGMVCIDGQDIRTIN- 464
Cdd:COG4172 276 LEARDLKVWFPIKRglfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSr 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 465 --VRHLREITGVVSQEPvlFAT-----TIAENIRYG----RENVTMDEIEKAVKEA-----------NAYdfimklPNKF 522
Cdd:COG4172 355 raLRPLRRRMQVVFQDP--FGSlsprmTVGQIIAEGlrvhGPGLSAAERRARVAEAleevgldpaarHRY------PHEF 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 523 dtlvgergaqlSGGQKQRIAIARALVRNPKILLLDEATSALDteseAVVQ---VALDK---ARKGRTTIVIAHRLSTVRN 596
Cdd:COG4172 427 -----------SGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQaqiLDLLRdlqREHGLAYLFISHDLAVVRA 491
|
250 260
....*....|....*....|...
gi 925114634 597 -ADVIAGFDDGVIVEKGNHDELM 618
Cdd:COG4172 492 lAHRVMVMKDGKVVEQGPTEQVF 514
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
397-589 |
6.61e-32 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 123.91 E-value: 6.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 397 KNVHFSYpsRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIrtiNVRHLREITGVVS 476
Cdd:cd03226 3 ENISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 477 QEP--VLFATTIAENIRYGRENVTMD--EIEKAVKEANAYDFIMKLPnkfdtlvgergAQLSGGQKQRIAIARALVRNPK 552
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKELDAGneQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 925114634 553 ILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAH 589
Cdd:cd03226 147 LLIFDEPTSGLDYKNmERVGELIRELAAQGKAVIVITH 184
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
394-619 |
7.03e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 126.28 E-value: 7.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKEVKiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITG 473
Cdd:PRK13635 6 IRVEHISFRYPDAATYA-LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEP--VLFATTIAENIRYGREN--VTMDE----IEKAVKEANAYDFIMKLPnkfdtlvgergAQLSGGQKQRIAIAR 545
Cdd:PRK13635 85 MVFQNPdnQFVGATVQDDVAFGLENigVPREEmverVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 546 ALVRNPKILLLDEATSALDTE--SEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMK 619
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRgrREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
394-620 |
7.58e-32 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 124.66 E-value: 7.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVrHLREItG 473
Cdd:cd03300 1 IELENVSKFYGG---FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP-HKRPV-N 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFA-TTIAENIRYG--RENVTMDEIEKAVKEAnaydfiMKLPnKFDTLVGERGAQLSGGQKQRIAIARALVRN 550
Cdd:cd03300 76 TVFQNYALFPhLTVFENIAFGlrLKKLPKAEIKERVAEA------LDLV-QLEGYANRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 551 PKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLS---TVrnADVIAGFDDGVIVEKGNHDELMKE 620
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEealTM--SDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
716-996 |
7.99e-32 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 126.60 E-value: 7.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 716 GIFCAIINGGLQPAFSIIFSRIIGIFTRDEDPETKRQNSNMFSVLFLVLGIISF--ITFFLQGFTFGKAGEILTKRLRYM 793
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTNHSGSGGEEALRALNQAVLILLGVVLIgsIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 794 VFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIA 873
Cdd:cd18780 81 LFSAIIAQEIAFFD--VTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 874 GVVEMKMLSGQALKDKKELEGAGKIATEAIENFRTVVSLTREQKFEYMYAQSLQVPYRNSLRKAHIFGVSFSITQAMMYF 953
Cdd:cd18780 159 AVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 925114634 954 SYAGCFRFGAYLVanefmnfqdvllvfsaiVFGAMAVGQVSSF 996
Cdd:cd18780 239 AIVLVLWYGGRLV-----------------IDGELTTGLLTSF 264
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
394-617 |
8.69e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 125.96 E-value: 8.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTIN--VRHLREI 471
Cdd:PRK13639 2 LETRDLKYSYPDGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKksLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 472 TGVVSQEP--VLFATTIAENIRYGRENV--TMDEIEKAVKEA----NAYDFIMKLPNkfdtlvgergaQLSGGQKQRIAI 543
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGPLNLglSKEEVEKRVKEAlkavGMEGFENKPPH-----------HLSGGQKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 544 ARALVRNPKILLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDEL 617
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
412-619 |
1.39e-31 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 123.99 E-value: 1.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 412 LKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHlREItGVVSQEPVLFA-TTIAENI 490
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK-RDI-SYVPQNYALFPhMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 491 RYGRENVTMD--EIEKAVKEanaydfIMKLPNkFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESE 568
Cdd:cd03299 93 AYGLKKRKVDkkEIERKVLE------IAEMLG-IDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 925114634 569 AVVQVALDKARK--GRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELMK 619
Cdd:cd03299 166 EKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1055-1262 |
1.53e-31 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 126.77 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1055 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLN---VQWLRAHLGIVSQEPilFDC---- 1127
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP--YASlnpr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1128 -SIAENIAYG-DNSRVVSHEEIMQAAKEAnihhfIETL---PEKYNtRVGDkgtQLSGGQKQRIAIARALVRQPHILLLD 1202
Cdd:COG4608 112 mTVGDIIAEPlRIHGLASKAERRERVAEL-----LELVglrPEHAD-RYPH---EFSGGQRQRIGIARALALNPKLIVCD 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 1203 EATSALDtesekV-VQ-------EALdKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQL 1262
Cdd:COG4608 183 EPVSALD-----VsIQaqvlnllEDL-QDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
408-620 |
2.75e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 124.77 E-value: 2.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 408 EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDI--RTINVRHLREITGVVSQEP--VLFA 483
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 484 TTIAENIRYGRENVTM--DEIEKAVKEAnaydfiMKLPN-KFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEAT 560
Cdd:PRK13637 99 ETIEKDIAFGPINLGLseEEIENRVKRA------MNIVGlDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 561 SALD--TESEAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELMKE 620
Cdd:PRK13637 173 AGLDpkGRDEILNKIKELHKEYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1051-1264 |
2.90e-31 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 122.54 E-value: 2.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1051 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQwLRAHLGI--VSQEPILF-DC 1127
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPH-ERARAGIgyVPEGRRIFpEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1128 SIAENIAYGDNSRVvsheeimQAAKEANIHHFIETLPEKYnTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1207
Cdd:cd03224 91 TVEENLLLGAYARR-------RAKRKARLERVYELFPRLK-ERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1208 LdteSEKVVQE---ALDKAREGRTCIVIAHrlstiQNADLI-------VVFQNGKVKEHGTHQQLLA 1264
Cdd:cd03224 163 L---APKIVEEifeAIRELRDEGVTILLVE-----QNARFAleiadraYVLERGRVVLEGTAAELLA 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1048-1265 |
3.87e-31 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 129.80 E-value: 3.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1048 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFyDPLAGSVLIDGKEIKHLN---VQWLRAHLGIVSQEPil 1124
Cdd:COG4172 295 TVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP-- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1125 FDC-----SIAENIAYGdnsrVVSHEEIMQAA-KEANIhhfIETLpekynTRVG-DKGT------QLSGGQKQRIAIARA 1191
Cdd:COG4172 372 FGSlsprmTVGQIIAEG----LRVHGPGLSAAeRRARV---AEAL-----EEVGlDPAArhryphEFSGGQRQRIAIARA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1192 LVRQPHILLLDEATSALDteseKVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQLLA 1264
Cdd:COG4172 440 LILEPKLLVLDEPTSALD----VSVQaQILDllrdlQREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFD 515
|
.
gi 925114634 1265 Q 1265
Cdd:COG4172 516 A 516
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1050-1253 |
5.10e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 128.98 E-value: 5.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1050 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNV-QWLRAHLGIVSQEPILF-DC 1127
Cdd:COG1129 15 GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrDAQAAGIAIIHQELNLVpNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1128 SIAENIAYGD---NSRVVSHEEIMQAAKEAnihhfIETL-----PekyNTRVGDkgtqLSGGQKQRIAIARALVRQPHIL 1199
Cdd:COG1129 95 SVAENIFLGReprRGGLIDWRAMRRRAREL-----LARLgldidP---DTPVGD----LSVAQQQLVEIARALSRDARVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 1200 LLDEATSAL-DTESE---KVVQEaLdkAREGRTCIVIAHRLSTIQN-ADLIVVFQNGKV 1253
Cdd:COG1129 163 ILDEPTASLtEREVErlfRIIRR-L--KAQGVAIIYISHRLDEVFEiADRVTVLRDGRL 218
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
395-612 |
5.58e-31 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 120.23 E-value: 5.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 395 EFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITGV 474
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 475 VSQepvlfattiaenirygrenvtmdeiekAVKEANAYDFIMKLpnkFDTlvgergaqLSGGQKQRIAIARALVRNPKIL 554
Cdd:cd03214 78 VPQ---------------------------ALELLGLAHLADRP---FNE--------LSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 555 LLDEATSALDTESeavvQVALDK------ARKGRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKG 612
Cdd:cd03214 120 LLDEPTSHLDIAH----QIELLEllrrlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
716-971 |
1.15e-30 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 123.04 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 716 GIFCAIINGGLQ---PAFSiifSRIIGIFTRDEDPETKRQNSNMFSVLFLVLGIISFitffLQGFTFGKAGEILTKRLRY 792
Cdd:cd18572 1 AFVFLVVAALSElaiPHYT---GAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSG----LRGGCFSYAGTRLVRRLRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 793 MVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAI 872
Cdd:cd18572 74 DLFRSLLRQDIAFFD--ATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 873 AGVVE---MKMLSGQAlkdKKELEGAGKIATEAIENFRTVVSLTREQKFEYMYAQSLQVPYRNSLRKAHIFGVSFSITQA 949
Cdd:cd18572 152 ITKVYgryYRKLSKEI---QDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTL 228
|
250 260
....*....|....*....|..
gi 925114634 950 MMYFSYAGCFRFGAYLVANEFM 971
Cdd:cd18572 229 LQNGTQVLVLFYGGHLVLSGRM 250
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1039-1257 |
1.57e-30 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 120.33 E-value: 1.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1039 FNEVVFNYPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLnvqwlRAHLGIV 1118
Cdd:cd03235 2 VEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1119 SQEPIL---FDCSIAENIAYGDNSRVVSHEEIMQAAKEAnIHHFIET--LPEKYNTRVGdkgtQLSGGQKQRIAIARALV 1193
Cdd:cd03235 74 PQRRSIdrdFPISVRDVVLMGLYGHKGLFRRLSKADKAK-VDEALERvgLSELADRQIG----ELSGGQQQRVLLARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 1194 RQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFqNGKVKEHG 1257
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1048-1211 |
2.28e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 119.89 E-value: 2.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1048 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP---LAGSVLIDGKEIKHLNVQwlRAHLGIVSQEPIL 1124
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1125 FD-CSIAENIAYG---DNSRVVSHEEIMQAAKEANIHHFIETLPEkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILL 1200
Cdd:COG4136 88 FPhLSVGENLAFAlppTIGRAQRRARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRALL 156
|
170
....*....|.
gi 925114634 1201 LDEATSALDTE 1211
Cdd:COG4136 157 LDEPFSKLDAA 167
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1059-1265 |
2.90e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 120.24 E-value: 2.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1059 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQwLRAhLGIVSQEPILFD-CSIAENIAYGD 1137
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA-ERP-VSMLFQENNLFPhLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1138 NSR----VVSHEEIMQAAKEANIHHFIETLPEkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALD---- 1209
Cdd:COG3840 97 RPGlkltAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalr 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1210 TESEKVVQEALDkaREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQLLAQ 1265
Cdd:COG3840 166 QEMLDLVDELCR--ERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
394-564 |
3.98e-30 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 123.90 E-value: 3.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDI-------RTINVr 466
Cdd:PRK09452 15 VELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIthvpaenRHVNT- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 467 hlreitgvVSQEPVLFA-TTIAENIRYG--RENVTMDEIEKAVKEAnaydfiMKLPnKFDTLVGERGAQLSGGQKQRIAI 543
Cdd:PRK09452 91 --------VFQSYALFPhMTVFENVAFGlrMQKTPAAEITPRVMEA------LRMV-QLEEFAQRKPHQLSGGQQQRVAI 155
|
170 180
....*....|....*....|.
gi 925114634 544 ARALVRNPKILLLDEATSALD 564
Cdd:PRK09452 156 ARAVVNKPKVLLLDESLSALD 176
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1042-1254 |
5.45e-30 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 118.51 E-value: 5.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1042 VVFNYPTRPDIpvLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKhlnvQWLRAH-LGIVSQ 1120
Cdd:cd03226 5 ISFSYKKGTEI--LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK----AKERRKsIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1121 EP--ILFDCSIAENIAYGDNSRVVSHEEIMQAAKEANIHHFIETLPekyntrvgdkgTQLSGGQKQRIAIARALVRQPHI 1198
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 1199 LLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVK 1254
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
394-617 |
6.89e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 119.88 E-value: 6.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKEvkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD-----PTDGMVCIDGQDI---RTINV 465
Cdd:PRK14239 6 LQVSDLSVYYNKKKA---LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIyspRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 466 RHLREItGVVSQEPVLFATTIAENIRYG------RENVTMDE-IEKAVKEANAYDFIMKlpNKFDTLVGergaqLSGGQK 538
Cdd:PRK14239 83 DLRKEI-GMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVLDEaVEKSLKGASIWDEVKD--RLHDSALG-----LSGGQQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 539 QRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDEL 617
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
394-598 |
7.23e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 120.61 E-value: 7.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITG 473
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEA----NAYDFIMKLPnkfdtlvgergAQLSGGQKQRIAIAR 545
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENkgIPHEEMKERVNEAlelvGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 546 ALVRNPKILLLDEATSALDTES--EAVVQVALDKARKGRTTIVIAHRLSTVRNAD 598
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGrlELIKTIKGIRDDYQMTVISITHDLDEVALSD 208
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1054-1258 |
8.40e-30 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 119.08 E-value: 8.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQwLRAHLGIVS--QEPILF-DCSIA 1130
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFpELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1131 ENI----------AYGDNSRVVSHEEIMQAAKEAnihhfIET--LPEKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHI 1198
Cdd:cd03219 94 ENVmvaaqartgsGLLLARARREEREARERAEEL-----LERvgLADLADRPAGE----LSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 1199 LLLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGT 1258
Cdd:cd03219 165 LLLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
394-620 |
1.17e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 119.81 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKEVK---ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTI-NVRHLR 469
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 470 EITGVVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEA----NAYDFIMKLPNkfdtlvgergaQLSGGQKQRI 541
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGPENlgIPPEEIRERVDESlkkvGMYEYRRHAPH-----------LLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 542 AIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMK 619
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFK 233
|
.
gi 925114634 620 E 620
Cdd:PRK13633 234 E 234
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
395-597 |
1.50e-29 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 117.25 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 395 EFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRhlreiTGV 474
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 475 VSQEPVL---FATTIAENIRYGREN----------VTMDEIEKAVKEANAYDFImklpnkfDTLVGErgaqLSGGQKQRI 541
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMGLYGhkglfrrlskADKAKVDEALERVGLSELA-------DRQIGE----LSGGQQQRV 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 542 AIARALVRNPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLSTVRNA 597
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEY 198
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
394-600 |
1.54e-29 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 117.19 E-value: 1.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREItG 473
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRL-A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFAT-TIAENIR-----YGREnVTMDEIEKAVKEanaydfiMKLPNKFDTLVGergaQLSGGQKQRIAIARAL 547
Cdd:COG4133 79 YLGHADGLKPElTVRENLRfwaalYGLR-ADREAIDEALEA-------VGLAGLADLPVR----QLSAGQKRRVALARLL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 925114634 548 VRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIA-HRLSTVRNADVI 600
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVL 200
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
394-617 |
2.31e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 123.98 E-value: 2.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLRE--I 471
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAagI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 472 tGVVSQEPVLFAT-TIAENIRYGRENVT---MD--EIEKAVKEANAYdfiMKLPNKFDTLVGErgaqLSGGQKQRIAIAR 545
Cdd:COG1129 82 -AIIHQELNLVPNlSVAENIFLGREPRRgglIDwrAMRRRARELLAR---LGLDIDPDTPVGD----LSVAQQQLVEIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 925114634 546 ALVRNPKILLLDEATSAL-DTESEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDEL 617
Cdd:COG1129 154 ALSRDARVLILDEPTASLtEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1050-1253 |
2.38e-29 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 115.22 E-value: 2.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1050 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQwlRAH-LGIvsqepilfdcs 1128
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR--DARrAGI----------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1129 iaeniaygdnsrvvsheeimqaakeANIHhfietlpekyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1208
Cdd:cd03216 78 -------------------------AMVY-------------------QLSVGERQMVEIARALARNARLLILDEPTAAL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 925114634 1209 -DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGKV 1253
Cdd:cd03216 114 tPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1050-1262 |
3.25e-29 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 117.44 E-value: 3.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1050 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQwlRAHLGIVSQEPILF-DCS 1128
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFrHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1129 IAENIAYGDNSRVVShEEIMQAAKEANIHHFIETLP-EKYNTRVGdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1207
Cdd:cd03296 91 VFDNVAFGLRVKPRS-ERPPEAEIRAKVHELLKLVQlDWLADRYP---AQLSGGQRQRVALARALAVEPKVLLLDEPFGA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 1208 LDTESEKVVQEALDKARE--GRTCIVIAHRLS-TIQNADLIVVFQNGKVKEHGTHQQL 1262
Cdd:cd03296 167 LDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
393-618 |
3.39e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 117.16 E-value: 3.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 393 NLEFKNVHFSYPSRkevkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVrHLREIT 472
Cdd:COG3840 1 MLRLDDLTYRYGDF-----PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP-AERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 473 gVVSQEPVLFA-TTIAENI--------RYGRENVTmdEIEKAVKEANAYDFIMKLPnkfdtlvgergAQLSGGQKQRIAI 543
Cdd:COG3840 75 -MLFQENNLFPhLTVAQNIglglrpglKLTAEQRA--QVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 544 ARALVRNPKILLLDEATSALD----TESEAVV-QVAldkARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDEL 617
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDpalrQEMLDLVdELC---RERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAAL 217
|
.
gi 925114634 618 M 618
Cdd:COG3840 218 L 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1046-1262 |
4.48e-29 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 116.45 E-value: 4.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1046 YPTRPDiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIkHLNVQWLRAHLGIVSQEPILF 1125
Cdd:cd03263 10 YKKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1126 D-CSIAENIAYgdNSRV--VSHEEImqaakEANIHHFIET--LPEKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILL 1200
Cdd:cd03263 88 DeLTVREHLRF--YARLkgLPKSEI-----KEEVELLLRVlgLTDKANKRART----LSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 1201 LDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQL 1262
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
394-609 |
4.97e-29 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 114.06 E-value: 4.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLRE--I 471
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRagI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 472 tGVVSQepvlfattiaenirygrenvtmdeiekavkeanaydfimklpnkfdtlvgergaqLSGGQKQRIAIARALVRNP 551
Cdd:cd03216 78 -AMVYQ-------------------------------------------------------LSVGERQMVEIARALARNA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 552 KILLLDEATSAL-DTESEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIV 609
Cdd:cd03216 102 RLLILDEPTAALtPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
394-629 |
5.25e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 117.45 E-value: 5.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD-----PTDGMVCIDGQDI--RTINVR 466
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyeRRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 467 HLREITGVVSQEPVLFATTIAENIRYG------RENVTMDEI-EKAVKEANAYDfimKLPNKfdtlVGERGAQLSGGQKQ 539
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIvESALKDADLWD---EIKHK----IHKSALDLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 540 RIAIARALVRNPKILLLDEATSALDTESEAVVQ--VALDKARKGRTTIVIAHRLSTV-RNADVIAGFddgviveKGNHDE 616
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVEslIQSLRLRSELTMVIVSHNLHQVsRLSDFTAFF-------KGNENR 230
|
250
....*....|....*
gi 925114634 617 L--MKEKGIYFKLVT 629
Cdd:PRK14258 231 IgqLVEFGLTKKIFN 245
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
816-1269 |
5.82e-29 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 126.21 E-value: 5.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 816 LTTRLANDAAQVkGAIGSRLAVITQNIANLGT----------GIIISLIYGWQ-LTLLLLA----IVPIIAIAGVVEMKM 880
Cdd:TIGR00957 403 VITNSARKSSTV-GEIVNLMSVDAQRFMDLATyinmiwsaplQVILALYFLWLnLGPSVLAgvavMVLMVPLNAVMAMKT 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 881 LSGQaLKDKKELEGAGKIATEAIENFRTVV----SLTREQKFEYMYAQSLQVpyrnsLRKAHIFGVSFSITQAMMYFSYA 956
Cdd:TIGR00957 482 KTYQ-VAHMKSKDNRIKLMNEILNGIKVLKlyawELAFLDKVEGIRQEELKV-----LKKSAYLHAVGTFTWVCTPFLVA 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 957 GCfRFGAYLVANEfMNFQDV------LLVFSAIVFGAMAVGQVSSfapDYAKAKVSAAHVIMIIEKSPL-IDSYSPHGLK 1029
Cdd:TIGR00957 556 LI-TFAVYVTVDE-NNILDAekafvsLALFNILRFPLNILPMVIS---SIVQASVSLKRLRIFLSHEELePDSIERRTIK 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1030 PNtlEGN-VTFNEVVFNYpTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKeikhlnv 1108
Cdd:TIGR00957 631 PG--EGNsITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS------- 700
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1109 qwlrahLGIVSQEPILFDCSIAENIAYGDNSRVVSHEEIMQAAKeanIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAI 1188
Cdd:TIGR00957 701 ------VAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACA---LLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSL 771
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1189 ARALVRQPHILLLDEATSALDTESEKVVQEAL---DKAREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLAQ 1265
Cdd:TIGR00957 772 ARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQR 851
|
....
gi 925114634 1266 KGIY 1269
Cdd:TIGR00957 852 DGAF 855
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
388-628 |
5.90e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 117.98 E-value: 5.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 388 DNIkgnLEFKNVHFSYPSRKEvKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTD---GMVCIDGQDIRTIN 464
Cdd:PRK13640 3 DNI---VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 465 VRHLREITGVVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEANA----YDFIMKLPnkfdtlvgergAQLSGG 536
Cdd:PRK13640 79 VWDIREKVGIVFQNPdnQFVGATVGDDVAFGLENraVPRPEMIKIVRDVLAdvgmLDYIDSEP-----------ANLSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 537 QKQRIAIARALVRNPKILLLDEATSALDTES-EAVVQVALD-KARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKG-- 612
Cdd:PRK13640 148 QKQRVAIAGILAVEPKIIILDESTSMLDPAGkEQILKLIRKlKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGsp 227
|
250 260
....*....|....*....|
gi 925114634 613 ----NHDELMKEKGIYFKLV 628
Cdd:PRK13640 228 veifSKVEMLKEIGLDIPFV 247
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1054-1265 |
7.33e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 119.44 E-value: 7.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQwlRAHLGIVSQEPILF-DCSIAEN 1132
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFpHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1133 IAYGDNSRVVSHEEIMQAAKEAnihhfIETLP-EKYNTRVGDkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1211
Cdd:PRK11432 99 VGYGLKMLGVPKEERKQRVKEA-----LELVDlAGFEDRYVD---QISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1212 SEKVVQEaldKARE-----GRTCIVIAHRLS-TIQNADLIVVFQNGKVKEHGTHQQLLAQ 1265
Cdd:PRK11432 171 LRRSMRE---KIRElqqqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
394-610 |
1.10e-28 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 115.61 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSR-KEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTIN----VRHL 468
Cdd:COG4181 9 IELRGLTKTVGTGaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 469 REITGVVSQEPVLFATTIAEnirygrENVTM--------DEIEKAVKEANAYDfimklpnkfdtlVGERG----AQLSGG 536
Cdd:COG4181 89 ARHVGFVFQSFQLLPTLTAL------ENVMLplelagrrDARARARALLERVG------------LGHRLdhypAQLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 537 QKQRIAIARALVRNPKILLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIA-HRLSTVRNADVIAGFDDGVIVE 610
Cdd:COG4181 151 EQQRVALARAFATEPAILFADEPTGNLDAAtGEQIIDLLFELNRERGTTLVLVtHDPALAARCDRVLRLRAGRLVE 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
394-617 |
1.31e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 116.73 E-value: 1.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITG 473
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEA----NAYDFIMKLPnkfdtlvgergAQLSGGQKQRIAIAR 545
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENqgIPREEMIKRVDEAllavNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 925114634 546 ALVRNPKILLLDEATSALDT--ESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDEL 617
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPtgRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
411-617 |
2.03e-28 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 115.23 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 411 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDI---RTIN-----VRHLREITGVVSQEPVLF 482
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSqqkglIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 483 A-TTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPNKFDTLvgerGAQLSGGQKQRIAIARALVRNPKILLLDEATS 561
Cdd:PRK11264 98 PhRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSY----PRRLSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 562 ALDTESEAVVQVALDK-ARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDEL 617
Cdd:PRK11264 174 ALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1049-1258 |
2.29e-28 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 117.98 E-value: 2.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1049 RPDIPVLQGLSLEVKKGQTLALVGSSGCGKST---VVQLLERfydPLAGSVLIDGKEIKHLNVQWLRA---HLGIVSQE- 1121
Cdd:PRK11153 15 GRTIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELRKarrQIGMIFQHf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1122 PILFDCSIAENIAY-----GdnsrvVSHEEImqaakEANIHHFIEtlpekyntRVG--DKG----TQLSGGQKQRIAIAR 1190
Cdd:PRK11153 92 NLLSSRTVFDNVALplelaG-----TPKAEI-----KARVTELLE--------LVGlsDKAdrypAQLSGGQKQRVAIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 925114634 1191 ALVRQPHILLLDEATSALDTESEKVVQEALDKA-RE-GRTCIVIAHRLSTI-QNADLIVVFQNGKVKEHGT 1258
Cdd:PRK11153 154 ALASNPKVLLCDEATSALDPATTRSILELLKDInRElGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGT 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
394-620 |
2.35e-28 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 114.45 E-value: 2.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVrHLREITG 473
Cdd:cd03224 1 LEVENLNAGY---GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPP-HERARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 V--VSQEPVLFAT-TIAENIRYGRENVTMDEIEKAVKEAnaYDFIMKLPNKFDTLVGergaQLSGGQKQRIAIARALVRN 550
Cdd:cd03224 77 IgyVPEGRRIFPElTVEENLLLGAYARRRAKRKARLERV--YELFPRLKERRKQLAG----TLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 551 PKILLLDEATSALdteSEAVVQV---ALDKARKGRTTIVI----AHRLSTVrnADVIAGFDDGVIVEKGNHDELMKE 620
Cdd:cd03224 151 PKLLLLDEPSEGL---APKIVEEifeAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1050-1257 |
2.70e-28 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 113.89 E-value: 2.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1050 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEI-----KHLNVqwlrahlGIVSQEPIL 1124
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVtdlppKDRDI-------AMVFQNYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1125 F-DCSIAENIAYGDNSRVVSHEEI----MQAAKEANIHHFIETLPekyntrvgdkgTQLSGGQKQRIAIARALVRQPHIL 1199
Cdd:cd03301 84 YpHMTVYDNIAFGLKLRKVPKDEIdervREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 925114634 1200 LLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH-RLSTIQNADLIVVFQNGKVKEHG 1257
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1037-1264 |
3.37e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 115.47 E-value: 3.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPTrpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLN-VQWLRAHL 1115
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1116 GIVSQEP--ILFDCSIAENIAYGDNSRVVSHEEIMQAAKEAnihhFIETLPEKYNTRvgdKGTQLSGGQKQRIAIARALV 1193
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRA----LAEIGLEKYRHR---SPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 1194 RQPHILLLDEATSALDTESEKVVQEALDKA-REGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLA 1264
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
410-612 |
3.50e-28 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 113.54 E-value: 3.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 410 KILKGLNLKVQ---SGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQ---DIR-TINVR-HLREItGVVSQEPVL 481
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRkKINLPpQQRKI-GLVFQQYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 482 FA-TTIAENIRYGRENVTMDEIEKAVKEANAYdfiMKLpnkfDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEAT 560
Cdd:cd03297 87 FPhLNVRENLAFGLKRKRNREDRISVDELLDL---LGL----DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 561 SALDTESEAVVQVALDKARK--GRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKG 612
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1055-1253 |
3.74e-28 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 113.54 E-value: 3.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1055 LQGLSLEVK---KGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGK-----EIK-HLNVQwlRAHLGIVSQEPILF 1125
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsRKKiNLPPQ--QRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1126 -DCSIAENIAYG-----DNSRVVSHEEIMQAAkeaNIHHFIETLPEkyntrvgdkgtQLSGGQKQRIAIARALVRQPHIL 1199
Cdd:cd03297 88 pHLNVRENLAFGlkrkrNREDRISVDELLDLL---GLDHLLNRYPA-----------QLSGGEKQRVALARALAAQPELL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1200 LLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGKV 1253
Cdd:cd03297 154 LLDEPFSALDRALRLQLLPELKQikKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRL 210
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
388-619 |
4.48e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 114.85 E-value: 4.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 388 DNIkgnLEFKNVHFSYPSrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRH 467
Cdd:PRK13648 5 NSI---IVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 468 LREITGVVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEA----NAYDFIMKLPNkfdtlvgergaQLSGGQKQ 539
Cdd:PRK13648 81 LRKHIGIVFQNPdnQFVGSIVKYDVAFGLENhaVPYDEMHRRVSEAlkqvDMLERADYEPN-----------ALSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 540 RIAIARALVRNPKILLLDEATSALDTE--SEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDEL 617
Cdd:PRK13648 150 RVAIAGVLALNPSVIILDEATSMLDPDarQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
..
gi 925114634 618 MK 619
Cdd:PRK13648 230 FD 231
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1055-1265 |
6.05e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 114.49 E-value: 6.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1055 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLA-----GSVLIDGKEI--KHLNVQWLRAHLGIVSQEPILFDC 1127
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPgfrveGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1128 SIAENIAYGdnSRVVSHEEIMQAAKEANIHHfiETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1207
Cdd:PRK14243 106 SIYDNIAYG--ARINGYKGDMDELVERSLRQ--AALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 1208 LDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLAQ 1265
Cdd:PRK14243 182 LDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYLVE 239
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1042-1264 |
6.85e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 114.80 E-value: 6.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1042 VVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQE 1121
Cdd:PRK13642 10 LVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1122 P--ILFDCSIAENIAYGDNSRVVSHEEIMQAAKEAnihhFIETLPEKYNTRvgdKGTQLSGGQKQRIAIARALVRQPHIL 1199
Cdd:PRK13642 90 PdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEA----LLAVNMLDFKTR---EPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 1200 LLDEATSALD----TESEKVVQEALDKARegRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLA 1264
Cdd:PRK13642 163 ILDESTSMLDptgrQEIMRVIHEIKEKYQ--LTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1055-1274 |
8.04e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 114.45 E-value: 8.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1055 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEP--ILFDCSIAEN 1132
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPddQVFSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1133 IAYGDNSRVVSHEEIMQAAKEA----NIHHFIETLPEkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1208
Cdd:PRK13647 101 VAFGPVNMGLDKDEVERRVEEAlkavRMWDFRDKPPY-----------HLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 1209 DTESEKVVQEALDK-AREGRTCIVIAHRLS-TIQNADLIVVFQNGKVKEHG-----THQQLLAQKGIYFSMVS 1274
Cdd:PRK13647 170 DPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIVEQAGLRLPLVA 242
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
394-566 |
8.46e-28 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 113.20 E-value: 8.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHlREItG 473
Cdd:cd03296 3 IEVRNVSKRFGD---FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-RNV-G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFA-TTIAENIRYG------RENVTMDEIEKAVKEanaydfIMKLPnKFDTLVGERGAQLSGGQKQRIAIARA 546
Cdd:cd03296 78 FVFQHYALFRhMTVFDNVAFGlrvkprSERPPEAEIRAKVHE------LLKLV-QLDWLADRYPAQLSGGQRQRVALARA 150
|
170 180
....*....|....*....|
gi 925114634 547 LVRNPKILLLDEATSALDTE 566
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAK 170
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
388-629 |
9.64e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 114.06 E-value: 9.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 388 DNIkgnLEFKNVHFSYpsRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRH 467
Cdd:PRK13647 2 DNI---IEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 468 LREITGVVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEA----NAYDFIMKLPNkfdtlvgergaQLSGGQKQ 539
Cdd:PRK13647 77 VRSKVGLVFQDPddQVFSSTVWDDVAFGPVNmgLDKDEVERRVEEAlkavRMWDFRDKPPY-----------HLSYGQKK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 540 RIAIARALVRNPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKG----- 612
Cdd:PRK13647 146 RVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGdksll 225
|
250
....*....|....*..
gi 925114634 613 NHDELMKEKGIYFKLVT 629
Cdd:PRK13647 226 TDEDIVEQAGLRLPLVA 242
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
716-989 |
1.04e-27 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 114.50 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 716 GIFCAIINGGLQPAFSIIFSRIIGIFTRDEDPETKRQNSNMFSVLFLVLGIISFItfflQGFTFGKAGEILTKRLRYMVF 795
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFF----RIYLFARVGERVVADLRKDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 796 RSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGV 875
Cdd:cd18576 77 RHLQRLPLSFFH--ERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 876 V---EMKMLSGQALkdkKELEGAGKIATEAIENFRTVVSLTREQkFEYM-YAQSLQVPYRNSLRKAHIFGVSFSITQAMM 951
Cdd:cd18576 155 LfgrRIRKLSKKVQ---DELAEANTIVEETLQGIRVVKAFTRED-YEIErYRKALERVVKLALKRARIRALFSSFIIFLL 230
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 925114634 952 YFSYAGCFRFGAYLVANEFMNFQDV--LLVFSAIVFGAMA 989
Cdd:cd18576 231 FGAIVAVLWYGGRLVLAGELTAGDLvaFLLYTLFIAGSIG 270
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1037-1262 |
1.21e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 113.69 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYptRPDIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHL 1115
Cdd:PRK13648 8 IVFKNVSFQY--QSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1116 GIVSQEPI-LFDCSIAE-NIAYGDNSRVVSHEE----IMQAAKEANIHHFIETLPEkyntrvgdkgtQLSGGQKQRIAIA 1189
Cdd:PRK13648 86 GIVFQNPDnQFVGSIVKyDVAFGLENHAVPYDEmhrrVSEALKQVDMLERADYEPN-----------ALSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 1190 RALVRQPHILLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQL 1262
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1051-1263 |
1.82e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 112.49 E-value: 1.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1051 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIK--HLNVQWLRAHLGIVSQEPILFDCS 1128
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAGMVFQQFYLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1129 IA-ENIAYGD-NSRVVSHEEIMQAAKE--------ANIHHFietlPekyntrvgdkgTQLSGGQKQRIAIARALVRQPHI 1198
Cdd:PRK09493 93 TAlENVMFGPlRVRGASKEEAEKQAREllakvglaERAHHY----P-----------SELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1199 LLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVF-QNGKVKEHGTHQQLL 1263
Cdd:PRK09493 158 MLFDEPTSALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFiDKGRIAEDGDPQVLI 224
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
393-615 |
1.97e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 112.41 E-value: 1.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 393 NLEFKNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDG------QDIRTINVR 466
Cdd:COG4161 2 SIQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 467 HLREITGVVSQE----PVLfatTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPNKFDTLvgerGAQLSGGQKQRIA 542
Cdd:COG4161 79 LLRQKVGMVFQQynlwPHL---TVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRF----PLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 543 IARALVRNPKILLLDEATSALDTESEA-VVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHD 615
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAqVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDAS 226
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1040-1266 |
2.79e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 112.86 E-value: 2.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1040 NEVVFNYPTrpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWL--RAHLGI 1117
Cdd:PRK13639 5 RDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1118 VSQEP--ILFDCSIAENIAYGDNSRVVSHEEIMQAAKEAnihhfietlpekyNTRVGDKGTQ------LSGGQKQRIAIA 1189
Cdd:PRK13639 83 VFQNPddQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEA-------------LKAVGMEGFEnkpphhLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 1190 RALVRQPHILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQ-NADLIVVFQNGKVKEHGTHQQLLAQK 1266
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
387-621 |
2.91e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 113.02 E-value: 2.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 387 PDNIkgnLEFKNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQ--DIRTIN 464
Cdd:PRK13636 2 EDYI---LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 465 VRHLREITGVVSQEP--VLFATTIAENIRYGRENVTM--DEIEKAVKEANAYDFIMKLPNKfdtlvgeRGAQLSGGQKQR 540
Cdd:PRK13636 77 LMKLRESVGMVFQDPdnQLFSASVYQDVSFGAVNLKLpeDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 541 IAIARALVRNPKILLLDEATSALDTE--SEaVVQVALDKARKGRTTIVIA-HRLSTVR-NADVIAGFDDGVIVEKGNHDE 616
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMgvSE-IMKLLVEMQKELGLTIIIAtHDIDIVPlYCDNVFVMKEGRVILQGNPKE 228
|
....*
gi 925114634 617 LMKEK 621
Cdd:PRK13636 229 VFAEK 233
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1055-1262 |
2.96e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 112.18 E-value: 2.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1055 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PLAGSVLIDGKEI---KHLNVQwLRAHLGIVSQEPILFD 1126
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIyspRTDTVD-LRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1127 CSIAENIAYGDNSRVVSHEEIMQAAKEANIHHfiETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1206
Cdd:PRK14239 100 MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKG--ASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 1207 ALDTESEKVVQEALDKAREGRTCIVIAHRL---STIqnADLIVVFQNGKVKEHGTHQQL 1262
Cdd:PRK14239 178 ALDPISAGKIEETLLGLKDDYTMLLVTRSMqqaSRI--SDRTGFFLDGDLIEYNDTKQM 234
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
394-619 |
3.52e-27 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 111.37 E-value: 3.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVrHLREITG 473
Cdd:cd03219 1 LEVRGLTKRF---GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPP-HEIARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVS--QEPVLFAT-TIAENIRYG-----RENVTMDEIEKAVKEANAYDF----IMKLPNKFDTLVGErgaqLSGGQKQRI 541
Cdd:cd03219 77 IGRtfQIPRLFPElTVLENVMVAaqartGSGLLLARARREEREARERAEelleRVGLADLADRPAGE----LSYGQQRRL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 542 AIARALVRNPKILLLDEATSAL-DTESEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELMK 619
Cdd:cd03219 153 EIARALATDPKLLLLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
394-621 |
4.06e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 112.57 E-value: 4.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYP--SRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDI----RTINVRH 467
Cdd:PRK13646 3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 468 LREITGVVSQ--EPVLFATTIAENIRYGRENVTMDeIEKAvkEANAYDFIMKLPNKFDTLvGERGAQLSGGQKQRIAIAR 545
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMN-LDEV--KNYAHRLLMDLGFSRDVM-SQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 546 ALVRNPKILLLDEATSALDTESEAVVQVALDKAR--KGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELMKEK 621
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDK 237
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
411-610 |
4.60e-27 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 112.09 E-value: 4.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 411 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTIN---VRHLREITGVVSQEP---VLFAT 484
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDSisaVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 485 TIAENIRYG-RENVTMDEIEKAVKEANAYDfIMKLPnkfDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 563
Cdd:PRK10419 107 TVREIIREPlRHLLSLDKAERLARASEMLR-AVDLD---DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 925114634 564 DTESEAVVQVALDKARKGRTT--IVIAHRLSTV-RNADVIAGFDDGVIVE 610
Cdd:PRK10419 183 DLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1037-1257 |
5.50e-27 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 109.89 E-value: 5.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPTRPdipvlQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQwlRAHLG 1116
Cdd:cd03298 1 VRLDKIRFSYGEQP-----MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1117 IVSQEPILF-DCSIAENIAYGDNSRV----VSHEEIMQAAKEANIHHFIETLPEkyntrvgdkgtQLSGGQKQRIAIARA 1191
Cdd:cd03298 74 MLFQENNLFaHLTVEQNVGLGLSPGLkltaEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 1192 LVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHG 1257
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1055-1258 |
5.50e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 112.45 E-value: 5.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1055 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEI--KHLNVQWLRAHLGIVSQEP--ILFDCSIA 1130
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1131 ENIAYGDNSRVVSHEEIMQAAKEAnihhfIETLPEKYNTrVGDKGT-QLSGGQKQRIAIARALVRQPHILLLDEATSALD 1209
Cdd:PRK13637 103 KDIAFGPINLGLSEEEIENRVKRA-----MNIVGLDYED-YKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 1210 TeseKVVQEALDKARE-----GRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGT 1258
Cdd:PRK13637 177 P---KGRDEILNKIKElhkeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
394-613 |
5.62e-27 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 109.56 E-value: 5.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHF---SYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTtvqLM-----QRLYDPTDGMVCIDGQDIRTINv 465
Cdd:cd03213 4 LSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKST---LLnalagRRTGLGVSGEVLINGRPLDKRS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 466 rhLREITGVVSQEPVLFAT-TIAENIrygrenvtmdeiekavkeanayDFIMKLpnkfdtlvgeRGaqLSGGQKQRIAIA 544
Cdd:cd03213 80 --FRKIIGYVPQDDILHPTlTVRETL----------------------MFAAKL----------RG--LSGGERKRVSIA 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 545 RALVRNPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLSTvrnaDVIAGFDDGVIVEKGN 613
Cdd:cd03213 124 LELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSS----EIFELFDKLLLLSQGR 189
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
394-564 |
5.71e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 114.05 E-value: 5.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDI--RTInvrHLREI 471
Cdd:PRK11432 7 VVLKNITKRFGS---NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSI---QQRDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 472 TgVVSQEPVLFA-TTIAENIRYG--RENVTMDEIEKAVKEANAydfIMKLPNKFDTLVGergaQLSGGQKQRIAIARALV 548
Cdd:PRK11432 81 C-MVFQSYALFPhMSLGENVGYGlkMLGVPKEERKQRVKEALE---LVDLAGFEDRYVD----QISGGQQQRVALARALI 152
|
170
....*....|....*.
gi 925114634 549 RNPKILLLDEATSALD 564
Cdd:PRK11432 153 LKPKVLLFDEPLSNLD 168
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
411-610 |
8.39e-27 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 111.05 E-value: 8.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 411 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTIN---VRHLREITGVVSQE---PVLFAT 484
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqRRAFRRDVQLVFQDspsAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 485 TIAENIRYGRENVT-MDEIEKAVKEANAYDfIMKLPnkfDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 563
Cdd:TIGR02769 106 TVRQIIGEPLRHLTsLDESEQKARIAELLD-MVGLR---SEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 925114634 564 DTESEAVVQVALDK--ARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVE 610
Cdd:TIGR02769 182 DMVLQAVILELLRKlqQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVE 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1053-1265 |
1.00e-26 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 116.32 E-value: 1.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1053 PVLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRA----HLGIVSQEPI- 1123
Cdd:COG4172 24 EAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPMt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1124 ----LFdcSIAENIAygdnsrvvsheEIM---------QAAKEAnihhfIETL-------PEKyntRVGDKGTQLSGGQK 1183
Cdd:COG4172 104 slnpLH--TIGKQIA-----------EVLrlhrglsgaAARARA-----LELLervgipdPER---RLDAYPHQLSGGQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1184 QRIAIARALVRQPHILLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEH 1256
Cdd:COG4172 163 QRVMIAMALANEPDLLIADEPTTALDV----TVQaQILDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQ 238
|
....*....
gi 925114634 1257 GTHQQLLAQ 1265
Cdd:COG4172 239 GPTAELFAA 247
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1054-1264 |
1.04e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 110.61 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEI---KHLNVQW-----LRAHLGIVSQEPILF 1125
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSQQKglirqLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1126 DC-SIAENIAYGDnsrVVSHEEIMQAAkeanihhfiETLPEKYNTRVGDKGTQ------LSGGQKQRIAIARALVRQPHI 1198
Cdd:PRK11264 98 PHrTVLENIIEGP---VIVKGEPKEEA---------TARARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 925114634 1199 LLLDEATSALDTEsekVVQEALDK----AREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQLLA 1264
Cdd:PRK11264 166 ILFDEPTSALDPE---LVGEVLNTirqlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1053-1251 |
1.09e-26 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 116.83 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1053 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLI-DGKEIkhlnvqwlrahLgIVSQEPILFDCSIAE 1131
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV-----------L-FLPQRPYLPLGTLRE 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1132 NIAYGDNSRVVSHEEIMQAAKEANIHHFIETLPEkyntrVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1211
Cdd:COG4178 445 ALLYPATAEAFSDAELREALEAVGLGHLAERLDE-----EADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 925114634 1212 SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNG 1251
Cdd:COG4178 520 NEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
394-617 |
1.37e-26 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 112.49 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKN--VHFSYPSRKE--------VKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTI 463
Cdd:PRK15079 9 LEVADlkVHFDIKDGKQwfwqppktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 464 NVRHLREITG---VVSQEPV-------LFATTIAENIRYGRENVTMDEIEKAVKEanaydFIMK---LPNkfdtLVGERG 530
Cdd:PRK15079 89 KDDEWRAVRSdiqMIFQDPLaslnprmTIGEIIAEPLRTYHPKLSRQEVKDRVKA-----MMLKvglLPN----LINRYP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 531 AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTVRN-ADVIAGFDDGV 607
Cdd:PRK15079 160 HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGH 239
|
250
....*....|
gi 925114634 608 IVEKGNHDEL 617
Cdd:PRK15079 240 AVELGTYDEV 249
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
394-589 |
1.68e-26 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 108.75 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTiNVRHLREITG 473
Cdd:cd03263 1 LQIRNLTKTYKK-GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFAT-TIAENIRY-----GRENVTMDEiekavkEANAYDFIMKLPNKFDTLVGergaQLSGGQKQRIAIARAL 547
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKE------EVELLLRVLGLTDKANKRAR----TLSGGMKRKLSLAIAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 925114634 548 VRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAH 589
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTH 190
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
394-564 |
2.12e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 108.65 E-value: 2.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITG 473
Cdd:PRK10247 8 LQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFATTIAENIRYGRenvtmdEIEKAVKEANAY-DFIMK--LPnkfDTLVGERGAQLSGGQKQRIAIARALVRN 550
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIFPW------QIRNQQPDPAIFlDDLERfaLP---DTILTKNIAELSGGEKQRISLIRNLQFM 155
|
170
....*....|....
gi 925114634 551 PKILLLDEATSALD 564
Cdd:PRK10247 156 PKVLLLDEITSALD 169
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
394-621 |
2.19e-26 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 109.40 E-value: 2.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGM-VCIDGQDIRTINVRHLREIT 472
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 473 GVVS---------QEPVL-------FATTiaeniryGR-ENVTMDEIEKAVKEANAYDFimklpnkfDTLVGERGAQLSG 535
Cdd:COG1119 81 GLVSpalqlrfprDETVLdvvlsgfFDSI-------GLyREPTDEQRERARELLELLGL--------AHLADRPFGTLSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 536 GQKQRIAIARALVRNPKILLLDEATSALDTES-EAVVQVaLDK-ARKGRTTIV-IAHRLStvrnaDVIAGFD------DG 606
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGArELLLAL-LDKlAAEGAPTLVlVTHHVE-----EIPPGIThvlllkDG 219
|
250
....*....|....*
gi 925114634 607 VIVEKGNHDELMKEK 621
Cdd:COG1119 220 RVVAAGPKEEVLTSE 234
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1051-1264 |
2.36e-26 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 108.92 E-value: 2.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1051 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVqWLRAHLGI--VSQEPILF-DC 1127
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPP-HRIARLGIgyVPEGRRIFpSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1128 SIAENI---AYGDNSRVVSHEEImqaakeANIHHFIETLPEKYNTRvgdkGTQLSGGQKQRIAIARALVRQPHILLLDEA 1204
Cdd:COG0410 94 TVEENLllgAYARRDRAEVRADL------ERVYELFPRLKERRRQR----AGTLSGGEQQMLAIGRALMSRPKLLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1205 TSALdteSEKVVQEALDK----AREGRTCIVI---AHRLSTIqnADLIVVFQNGKVKEHGTHQQLLA 1264
Cdd:COG0410 164 SLGL---APLIVEEIFEIirrlNREGVTILLVeqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
394-609 |
2.62e-26 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 115.98 E-value: 2.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKE-VKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHL---- 468
Cdd:PRK10535 5 LELKDIRRSYPSGEEqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 469 REITGVVSQEPVLFATTIAEnirygrENVTMDEI----EKAVKEANAYDFIMKLpnKFDTLVGERGAQLSGGQKQRIAIA 544
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAA------QNVEVPAVyaglERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 545 RALVRNPKILLLDEATSALDTESEAVVQVALDKAR-KGRTTIVIAHRLSTVRNADVIAGFDDGVIV 609
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
105-364 |
2.99e-26 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 110.27 E-value: 2.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 105 FINHLEEEMTTYAYYYSGIGAGVLVAAYIQVSFWCLAAGRQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKI 184
Cdd:cd18575 27 FAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 185 NEGIGDKIGMFFQSIATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAI---WAKILSSFTDKELlayAKAGAVAEEVLA 261
Cdd:cd18575 107 QTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILfgrRVRRLSRASQDRL---ADLSAFAEETLS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 262 AIRTVIAFGGQKKELERYNKNLEEA-----KRIGIKKAITAnisigAAFLLIYASYALAFWYGTSLVLSSEYSIGQvLTV 336
Cdd:cd18575 184 AIKTVQAFTREDAERQRFATAVEAAfaaalRRIRARALLTA-----LVIFLVFGAIVFVLWLGAHDVLAGRMSAGE-LSQ 257
|
250 260
....*....|....*....|....*....
gi 925114634 337 F-FSVLIGAFSIGQASPSIEAFANARGAA 364
Cdd:cd18575 258 FvFYAVLAAGSVGALSEVWGDLQRAAGAA 286
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
394-612 |
3.27e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 109.92 E-value: 3.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYP--SRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIR----TINVRH 467
Cdd:PRK13641 3 IKFENVDYIYSpgTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 468 LREITGVVSQ--EPVLFATTIAENIRYGRENVTMDEIEKAVKeanAYDFIMKLPNKfDTLVGERGAQLSGGQKQRIAIAR 545
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDEAKEK---ALKWLKKVGLS-EDLISKSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 546 ALVRNPKILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHrlstvrNADVIAGFDDGVIV-EKG 612
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTH------NMDDVAEYADDVLVlEHG 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
393-612 |
3.69e-26 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 108.13 E-value: 3.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 393 NLEFKNVHFSYPS-RKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQL-MQRLYDP--TDGMVCIDGQDIRtinvRHL 468
Cdd:cd03234 3 VLPWWDVGLKAKNwNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAiSGRVEGGgtTSGQILFNGQPRK----PDQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 469 -REITGVVSQEPVLFAT-TIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPNkfDTLVG-ERGAQLSGGQKQRIAIAR 545
Cdd:cd03234 79 fQKCVAYVRQDDILLPGlTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLA--LTRIGgNLVKGISGGERRRVSIAV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 546 ALVRNPKILLLDEATSALDTESE-AVVQVALDKARKGRTTIVIAH--RLSTVRNADVIAGFDDGVIVEKG 612
Cdd:cd03234 157 QLLWDPKVLILDEPTSGLDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1037-1258 |
5.09e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 109.50 E-value: 5.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPTRPDiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGS---VLIDGKEIKHLNVQWLRA 1113
Cdd:PRK13640 6 VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1114 HLGIVSQEP--ILFDCSIAENIAYGDNSRVVSHEEIM----QAAKEANIHHFIETLPEkyntrvgdkgtQLSGGQKQRIA 1187
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEMIkivrDVLADVGMLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 1188 IARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGT 1258
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1037-1264 |
6.85e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 109.34 E-value: 6.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYptRPDIP----VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEI----KHLNV 1108
Cdd:PRK13634 3 ITFQKVEHRY--QYKTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1109 QWLRAHLGIVSQ--EPILFDCSIAENIAYGDNSRVVSHEEIMQAAKEAnihhfIET--LPEKYNTRvgdKGTQLSGGQKQ 1184
Cdd:PRK13634 81 KPLRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREM-----IELvgLPEELLAR---SPFELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1185 RIAIARALVRQPHILLLDEATSALDTESEKVVQE---ALDKaREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQ 1260
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEmfyKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPR 231
|
....
gi 925114634 1261 QLLA 1264
Cdd:PRK13634 232 EIFA 235
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1037-1258 |
7.55e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 108.68 E-value: 7.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYP--TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEI----KHLNVQW 1110
Cdd:PRK13649 3 INLQNVSYTYQagTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1111 LRAHLGIVSQ--EPILFDCSIAENIAYGDNSRVVSHEEIMQAAKEA-NIHHFIETLPEKyntrvgdKGTQLSGGQKQRIA 1187
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKlALVGISESLFEK-------NPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 1188 IARALVRQPHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGT 1258
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1035-1274 |
1.02e-25 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 108.40 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1035 GNVTFNEVVFNYpTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDpLAGSVLIDGKEIKHLNVQWLRAH 1114
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1115 LGIVSQEPILFDCSIAENI-AYGDNSrvvsHEEIMQAAKEANIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALV 1193
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLdPYGKWS----DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1194 RQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLAQKGIYFSMV 1273
Cdd:cd03289 155 SKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAI 234
|
.
gi 925114634 1274 S 1274
Cdd:cd03289 235 S 235
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1053-1263 |
1.20e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 107.55 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1053 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPIL-FDCSIAE 1131
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1132 NIAYG----DNSRVVSHEEIMQAAKEANIHHFIETLpekYntrvgdkgTQLSGGQKQRIAIARALVR------QPHILLL 1201
Cdd:PRK13548 96 VVAMGraphGLSRAEDDALVAAALAQVDLAHLAGRD---Y--------PQLSGGEQQRVQLARVLAQlwepdgPPRWLLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 1202 DEATSALD-TESEKVVQEALDKARE-GRTCIVIAHRLS-TIQNADLIVVFQNGKVKEHGTHQQLL 1263
Cdd:PRK13548 165 DEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1054-1255 |
1.21e-25 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 106.75 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPLAGSVLIDGKEIKHLN----VQWLRAHLGIVSQE----P 1122
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALDedarARLRARHVGFVFQSfqllP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1123 ILfdcSIAENIAygdnsrV----VSHEEIMQAAKEA--------NIHHFietlPekyntrvgdkgTQLSGGQKQRIAIAR 1190
Cdd:COG4181 104 TL---TALENVM------LplelAGRRDARARARALlervglghRLDHY----P-----------AQLSGGEQQRVALAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1191 ALVRQPHILLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTIQNADLIVVFQNGKVKE 1255
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAATGEQIIDLLfELNRErGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1038-1234 |
1.36e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 107.64 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1038 TFNEVVFNYP-TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNvqwlrAHLG 1116
Cdd:COG4525 5 TVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG-----ADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1117 IVSQEPILFD-CSIAENIAYGDNSRVVSHEEIMQAAkeanihhfietlpEKYNTRVGDKGT------QLSGGQKQRIAIA 1189
Cdd:COG4525 80 VVFQKDALLPwLNVLDNVAFGLRLRGVPKAERRARA-------------EELLALVGLADFarrriwQLSGGMRQRVGIA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 925114634 1190 RALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH 1234
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1050-1251 |
1.44e-25 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 106.26 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1050 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAH----LGIVSQEPILF 1125
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1126 DCSIAENIAYGDNSRVVSHEEIMQAAkeaNIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEAT 1205
Cdd:cd03290 92 NATVEENITFGSPFNKQRYKAVTDAC---SLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 925114634 1206 SALDTE-SEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVFQNG 1251
Cdd:cd03290 169 SALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
393-564 |
1.55e-25 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 109.93 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 393 NLEFKNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHlREIt 472
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQV--IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-RDI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 473 GVVSQEPVLFA-TTIAENIRYGRENVTM--DEIEKAVKEANAydfIMKLpnkfDTLVGERGAQLSGGQKQRIAIARALVR 549
Cdd:PRK11650 79 AMVFQNYALYPhMSVRENMAYGLKIRGMpkAEIEERVAEAAR---ILEL----EPLLDRKPRELSGGQRQRVAMGRAIVR 151
|
170
....*....|....*
gi 925114634 550 NPKILLLDEATSALD 564
Cdd:PRK11650 152 EPAVFLFDEPLSNLD 166
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
129-347 |
1.86e-25 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 107.89 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 129 VAAYIQVsfWCLA-AGRQILK-IRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSIATFFTGF 206
Cdd:cd18552 54 LASYLQT--YLMAyVGQRVVRdLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 207 IVGFTRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEA 286
Cdd:cd18552 132 GVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERL 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 925114634 287 KRIGIKKAITANISIGAAFLLIYASYALAFWYGTSLVLSSEYSIGQvltvFFSVLIGAFSI 347
Cdd:cd18552 212 RRLSMKIARARALSSPLMELLGAIAIALVLWYGGYQVISGELTPGE----FISFITALLLL 268
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1051-1257 |
2.03e-25 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 105.38 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1051 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWlrAHLGIVSQEPILFD-CSI 1129
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIGALIEAPGFYPnLTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1130 AENIAYGDNSRVVSHEEIMQAAKEANIHHfietlpekyntRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1209
Cdd:cd03268 90 RENLRLLARLLGIRKKRIDEVLDVVGLKD-----------SAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 925114634 1210 TESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHG 1257
Cdd:cd03268 159 PDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1054-1257 |
2.48e-25 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 105.35 E-value: 2.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTlALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHlNVQWLRAHLGIVSQEPILFDcsiaeni 1133
Cdd:cd03264 15 ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQEFGVYP------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1134 aygdNSRVVSHEEIMQAAKE---ANIHHFIETLPEKYN--TRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1208
Cdd:cd03264 86 ----NFTVREFLDYIAWLKGipsKEVKARVDEVLELVNlgDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 925114634 1209 DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHG 1257
Cdd:cd03264 162 DPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1051-1257 |
3.22e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 106.15 E-value: 3.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1051 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEP-IL 1124
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1125 FDCSIAENIAYGD--NSRVVSHEEIMQAAKEAnihhfIET--LPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILL 1200
Cdd:PRK14247 95 PNLSIFENVALGLklNRLVKSKKELQERVRWA-----LEKaqLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 1201 LDEATSALDTESEKVVQEALDKAREGRTCIVIAH------RLStiqnaDLIVVFQNGKVKEHG 1257
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWG 227
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1054-1265 |
3.41e-25 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 106.21 E-value: 3.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIK-------HLNV------QWLRAHLGIVSQ 1120
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgQLKVadknqlRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1121 EPILFdcsiaeniaygdnsrvvSHEEIMQAAKEANIH------HFIETLPEKYNTRVG-DKGTQ------LSGGQKQRIA 1187
Cdd:PRK10619 100 HFNLW-----------------SHMTVLENVMEAPIQvlglskQEARERAVKYLAKVGiDERAQgkypvhLSGGQQQRVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1188 IARALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNADLIVVF-QNGKVKEHGTHQQLLAQ 1265
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVSSHVIFlHQGKIEEEGAPEQLFGN 242
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1055-1251 |
3.51e-25 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 105.24 E-value: 3.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1055 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLrahlgIVSQEPILFD-CSIAENI 1133
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1134 AYGDNsRVVSHeeIMQAAKEANIHHFIETLPEkynTRVGDKG-TQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1212
Cdd:TIGR01184 76 ALAVD-RVLPD--LSKSERRAIVEEHIALVGL---TEAADKRpGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 925114634 1213 EKVVQEALDKARE--GRTCIVIAHRL-STIQNADLIVVFQNG 1251
Cdd:TIGR01184 150 RGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
713-1010 |
4.15e-25 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 106.75 E-value: 4.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 713 FVVGIFCAIINGGLQPAFSIIFSRIIGIFTRdedpetkrQNSNMFSVLFLV-LGIISFITFFLQGFTFGKAGEILTKRLR 791
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSA--------GGSSGGLLALLVaLFLLQAVLSALSSYLLGRTGERVVLDLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 792 YMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKgaigsrlAVITQNIANLGTGII-------ISLIYGWQLTLLLL 864
Cdd:cd18551 73 RRLWRRLLRLPVSFFD--RRRSGDLVSRVTNDTTLLR-------ELITSGLPQLVTGVLtvvgavvLMFLLDWVLTLVTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 865 AIVPIIAIAGVVEMKMLSGQALKDKKELEGAGKIATEAIENFRTVVSLTREQKFEYMYAQSLQVPYRNSLRKAHIFGVSF 944
Cdd:cd18551 144 AVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIG 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 945 SITQAMMYFSYAGCFRFGAYLVAN------EFMNFqdVLLVFSAIvfgaMAVGQVSSFAPDYAKAKVSAAHV 1010
Cdd:cd18551 224 PLMGLAVQLALLVVLGVGGARVASgaltvgTLVAF--LLYLFQLI----TPLSQLSSFFTQLQKALGALERI 289
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1054-1253 |
4.33e-25 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 105.89 E-value: 4.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVqWLRAHLGIVS--QEPILF-DCSIA 1130
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIARLGIARtfQNPRLFpELTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1131 ENIA----YGDNSRVVS---------------HEEIMQAAKEANIHHfietlpeKYNTRVGDkgtqLSGGQKQRIAIARA 1191
Cdd:COG0411 98 ENVLvaahARLGRGLLAallrlprarreereaRERAEELLERVGLAD-------RADEPAGN----LSYGQQRRLEIARA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 1192 LVRQPHILLLDEATSAL-DTESEKVVqEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGKV 1253
Cdd:COG0411 167 LATEPKLLLLDEPAAGLnPEETEELA-ELIRRLRDerGITILLIEHDMDLVMGlADRIVVLDFGRV 231
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1053-1266 |
4.85e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 105.87 E-value: 4.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1053 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPIL-FDCSIAE 1131
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1132 NIAYG--------------DNSRVVSHEEIMQaakeanihhfIETLPEKyntRVgdkgTQLSGGQKQRIAIARALVRQPH 1197
Cdd:PRK11231 96 LVAYGrspwlslwgrlsaeDNARVNQAMEQTR----------INHLADR---RL----TDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 925114634 1198 ILLLDEATSALD----TESEKVVQEAldkAREGRTCIVIAHRLS-TIQNADLIVVFQNGKVKEHGTHQQLLAQK 1266
Cdd:PRK11231 159 VVLLDEPTTYLDinhqVELMRLMREL---NTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1037-1263 |
4.97e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 105.89 E-value: 4.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDpLAGSVLIDGK-EI-------KHLNV 1108
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRvEFfnqniyeRRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1109 QWLRAHLGIVSQEPILFDCSIAENIAYGDN----SRVVSHEEIMQAA-KEANihhfietLPEKYNTRVGDKGTQLSGGQK 1183
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwRPKLEIDDIVESAlKDAD-------LWDEIKHKIHKSALDLSGGQQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1184 QRIAIARALVRQPHILLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVFQN-----GKVKE 1255
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVE 236
|
....*...
gi 925114634 1256 HGTHQQLL 1263
Cdd:PRK14258 237 FGLTKKIF 244
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
394-612 |
5.09e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 105.38 E-value: 5.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD-----PTDGMVCIDGQDIRTINVRHL 468
Cdd:PRK14247 4 IEIRDLKVSFGQ---VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 469 REITGVVSQEPVLFAT-TIAENIRYG----RENVTMDEIEKAVKEA-NAYDFIMKLPNKFDTLVGergaQLSGGQKQRIA 542
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNlSIFENVALGlklnRLVKSKKELQERVRWAlEKAQLWDEVKDRLDAPAG----KLSGGQQQRLC 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 925114634 543 IARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAH-RLSTVRNADVIAGFDDGVIVEKG 612
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWG 227
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
394-621 |
6.76e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 105.98 E-value: 6.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRK--EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTI----NVRH 467
Cdd:PRK13649 3 INLQNVSYTYQAGTpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 468 LREITGVVSQ--EPVLFATTIAENIRYGREN--VTMDEIEKAVKEAnaydfiMKLPNKFDTLVGERGAQLSGGQKQRIAI 543
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAREK------LALVGISESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 544 ARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIV-IAHRLSTVRN-ADVIAGFDDGVIVEKG------NHD 615
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGkpkdifQDV 236
|
....*.
gi 925114634 616 ELMKEK 621
Cdd:PRK13649 237 DFLEEK 242
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1052-1234 |
7.77e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 108.00 E-value: 7.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1052 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHlnVQWLRAHLGIVSQEPILF-DCSIA 1130
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH--VPPYQRPINMMFQSYALFpHMTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1131 ENIAYGDNSRVVSHEEIMQAAKEA-NIHHFIEtlpekYNTRvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1209
Cdd:PRK11607 110 QNIAFGLKQDKLPKAEIASRVNEMlGLVHMQE-----FAKR---KPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
170 180
....*....|....*....|....*..
gi 925114634 1210 TESEKVVQ-EALD-KAREGRTCIVIAH 1234
Cdd:PRK11607 182 KKLRDRMQlEVVDiLERVGVTCVMVTH 208
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
713-1008 |
8.19e-25 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 105.98 E-value: 8.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 713 FVVGIFCAIINGglqpAFSIIFSRIIGIFTRDEDPETKRQNSNMFSVLFLVLGIISFITFFLQGFTFGKAGEILTKRLRY 792
Cdd:cd18542 1 YLLAILALLLAT----ALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 793 MVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAI 872
Cdd:cd18542 77 DLYDHLQRLSFSFHD--KARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 873 AGVVEMKMLsGQALKDKKELEGA-GKIATEAIENFRTVVSLTRE----QKFEYMYAQslqvpYRN-SLRKAHIFGVSFSI 946
Cdd:cd18542 155 FSYVFFKKV-RPAFEEIREQEGElNTVLQENLTGVRVVKAFAREdyeiEKFDKENEE-----YRDlNIKLAKLLAKYWPL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 947 TQAMMYFSYAGCFRFGAYLVANEFMNFQDvLLVFSAIVFG-AMAVGQVSSFAPDYAKAKVSAA 1008
Cdd:cd18542 229 MDFLSGLQIVLVLWVGGYLVINGEITLGE-LVAFISYLWMlIWPVRQLGRLINDMSRASASAE 290
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
410-566 |
9.39e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 107.48 E-value: 9.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 410 KILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLReiTGVVSQEPVLFA-TTIAE 488
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VGFVFQHYALFRhMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 489 NIRYG------RENVTMDEIEKAVkeanaydfiMKLPN--KFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEAT 560
Cdd:PRK10851 94 NIAFGltvlprRERPNAAAIKAKV---------TQLLEmvQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPF 164
|
....*.
gi 925114634 561 SALDTE 566
Cdd:PRK10851 165 GALDAQ 170
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1053-1266 |
9.80e-25 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 105.27 E-value: 9.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1053 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRA---HLGIVSQepilfDC-- 1127
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrDVQLVFQ-----DSps 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1128 ------SIAENIAygdnsRVVSHEEIM-QAAKEANIHHFIET--LPEKYNTRVGdkgTQLSGGQKQRIAIARALVRQPHI 1198
Cdd:TIGR02769 100 avnprmTVRQIIG-----EPLRHLTSLdESEQKARIAELLDMvgLRSEDADKLP---RQLSGGQLQRINIARALAVKPKL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 925114634 1199 LLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQLLAQK 1266
Cdd:TIGR02769 172 IVLDEAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLLSFK 242
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1037-1263 |
1.09e-24 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 104.40 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAG-SVLIDGKEIKHLNVQWLRAHL 1115
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1116 GIVS---QEPILFDCSIAENIAYGDNS-----RVVSHEEIMQAA---KEANIHHFIETLpekYNTrvgdkgtqLSGGQKQ 1184
Cdd:COG1119 81 GLVSpalQLRFPRDETVLDVVLSGFFDsiglyREPTDEQRERARellELLGLAHLADRP---FGT--------LSQGEQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1185 RIAIARALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIV-IAHRL----STIQNAdliVVFQNGKVKEHGT 1258
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVeeipPGITHV---LLLKDGRVVAAGP 226
|
....*
gi 925114634 1259 HQQLL 1263
Cdd:COG1119 227 KEEVL 231
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
394-612 |
1.22e-24 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 103.04 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevkILKGLNLKVQSGQTvALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRtINVRHLREITG 473
Cdd:cd03264 1 LQLENLTKRYGKKR---ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL-KQPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFAT-TIAENIRY-----GRENVTMD-EIEKAVKEANAYDFimklpnkfdtlVGERGAQLSGGQKQRIAIARA 546
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYiawlkGIPSKEVKaRVDEVLELVNLGDR-----------AKKKIGSLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 547 LVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKG 612
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1058-1266 |
1.45e-24 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 106.73 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1058 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEI----KHLNVQWLRAHLGIVSQEPILF-DCSIAEN 1132
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrKGIFLPPEKRRIGYVFQEARLFpHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1133 IAYG-----DNSRVVSHEEIMQAAkeaNIHHFIETLPEKyntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATSA 1207
Cdd:TIGR02142 96 LRYGmkrarPSERRISFERVIELL---GIGHLLGRLPGR-----------LSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 1208 LDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQLLAQK 1266
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1054-1257 |
1.54e-24 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 102.74 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNvqwlRAHLGIVSQEPILF-DCSIAEN 1132
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYpKMKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1133 IAYGDNSRVVSHEEImqaakEANIHHFIET--LPEKYNTRVgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1210
Cdd:cd03269 91 LVYLAQLKGLKKEEA-----RRRIDEWLERleLSEYANKRV----EELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 925114634 1211 ESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHG 1257
Cdd:cd03269 162 VNVELLKDVIrELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
123-339 |
1.63e-24 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 105.21 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 123 IGAGVL--VAAYIQvSFWCLAAGRQILK-IRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSI 199
Cdd:cd18542 46 LGVALLrgVFRYLQ-GYLAEKASQKVAYdLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 200 ATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERY 279
Cdd:cd18542 125 LLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKF 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 280 NKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTSLVLSSEYSIGQvLTVFFS 339
Cdd:cd18542 205 DKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEITLGE-LVAFIS 263
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
394-564 |
2.02e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 104.17 E-value: 2.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKEVK-ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHlreit 472
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 473 GVVSQEPVLFA-TTIAENIRYGrenVTMDEIEKAVKEANAYDFImklpnkfdTLVGERGA------QLSGGQKQRIAIAR 545
Cdd:COG4525 79 GVVFQKDALLPwLNVLDNVAFG---LRLRGVPKAERRARAEELL--------ALVGLADFarrriwQLSGGMRQRVGIAR 147
|
170
....*....|....*....
gi 925114634 546 ALVRNPKILLLDEATSALD 564
Cdd:COG4525 148 ALAADPRFLLMDEPFGALD 166
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
394-615 |
2.63e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 103.17 E-value: 2.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDG------QDIRTINVRH 467
Cdd:PRK11124 3 IQLNGINCFYGAHQ---ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 468 LREITGVVSQEPVLFA-TTIAENIRYGRENVT-MDEiEKAVKEAnaydfiMKLpnkFDTLVGERGA-----QLSGGQKQR 540
Cdd:PRK11124 80 LRRNVGMVFQQYNLWPhLTVQQNLIEAPCRVLgLSK-DQALARA------EKL---LERLRLKPYAdrfplHLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 541 IAIARALVRNPKILLLDEATSALDTESEA-VVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHD 615
Cdd:PRK11124 150 VAIARALMMEPQVLLFDEPTAALDPEITAqIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
394-620 |
2.69e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 104.30 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTIN-VRHLREIT 472
Cdd:PRK13644 2 IRLENVSYSYPDGTPA--LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 473 GVVSQEP--VLFATTIAENIRYGRENVTMD--EIEKAVKEANAYDFIMKLPNKfdtlvgeRGAQLSGGQKQRIAIARALV 548
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPpiEIRKRVDRALAEIGLEKYRHR-------SPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 549 RNPKILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKE 620
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
144-367 |
3.09e-24 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 104.44 E-value: 3.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 144 RQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSIATFFTGFIVGFTRGWKLTLVILAI 223
Cdd:cd18551 66 RVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 224 SPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGA 303
Cdd:cd18551 146 VPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPL 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 925114634 304 AFLLIYASYALAFWYGTSLVLSSEYSIGQVLTVFFSVLIGAFSIGQASPSIEAFANARGAAYEI 367
Cdd:cd18551 226 MGLAVQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
394-612 |
3.49e-24 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 102.75 E-value: 3.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPsrkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTIN----VRHlr 469
Cdd:COG0410 4 LEVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPphriARL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 470 eitGV--VSQEPVLFAT-TIAENIRYGRENVTMDEIEKAVKEAnAYDFimklpnkFDTLvGER----GAQLSGGQKQRIA 542
Cdd:COG0410 79 ---GIgyVPEGRRIFPSlTVEENLLLGAYARRDRAEVRADLER-VYEL-------FPRL-KERrrqrAGTLSGGEQQMLA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 543 IARALVRNPKILLLDEATSALdteSEAVVQV---ALDKARKGRTTIVIahrlstV-RNADVIAGF-DDGVIVEKG 612
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGL---APLIVEEifeIIRRLNREGVTILL------VeQNARFALEIaDRAYVLERG 212
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1041-1266 |
3.66e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.16 E-value: 3.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1041 EVVFNYPTRPDipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKH--LNVQWLRAHLGIV 1118
Cdd:PRK13636 10 ELNYNYSDGTH--ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYsrKGLMKLRESVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1119 SQEP--ILFDCSIAENIAYGDNSRVVSHEEIMQAAKEANIHHFIETLPekyntrvgDKGTQ-LSGGQKQRIAIARALVRQ 1195
Cdd:PRK13636 88 FQDPdnQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLK--------DKPTHcLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 1196 PHILLLDEATSALD----TESEKVVQEALDKAreGRTCIVIAHRLSTIQ-NADLIVVFQNGKVKEHGTHQQLLAQK 1266
Cdd:PRK13636 160 PKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1055-1265 |
3.72e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 105.05 E-value: 3.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1055 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIK---HLNVQWLRAHLGIVSQEPilfdcsiae 1131
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQKIQIVFQNP--------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1132 niaYGD-NSR----------VVSHEEIMQAAKEANIHHFIETL---PEKYNtRVGDkgtQLSGGQKQRIAIARALVRQPH 1197
Cdd:PRK11308 102 ---YGSlNPRkkvgqileepLLINTSLSAAERREKALAMMAKVglrPEHYD-RYPH---MFSGGQRQRIAIARALMLDPD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 925114634 1198 ILLLDEATSALDTESE-KVVQEALDKAREGRTCIV-IAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQLLAQ 1265
Cdd:PRK11308 175 VVVADEPVSALDVSVQaQVLNLMMDLQQELGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1055-1265 |
3.78e-24 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 105.57 E-value: 3.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1055 LQGLSLEVK-----KGQTlALVGSSGCGKSTVVQL---LERfydPLAGSVLIDGKeikhlnV-------QWLRAH---LG 1116
Cdd:COG4148 11 RGGFTLDVDftlpgRGVT-ALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGE------VlqdsargIFLPPHrrrIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1117 IVSQEPILFD-CSIAENIAYG-----DNSRVVSHEEIMQAAkeaNIHHFIETLPEkyntrvgdkgtQLSGGQKQRIAIAR 1190
Cdd:COG4148 81 YVFQEARLFPhLSVRGNLLYGrkrapRAERRISFDEVVELL---GIGHLLDRRPA-----------TLSGGERQRVAIGR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1191 ALVRQPHILLLDEATSALDTESeKvvQEALDK----AREGRTCIV-IAH------RLstiqnADLIVVFQNGKVKEHGTH 1259
Cdd:COG4148 147 ALLSSPRLLLMDEPLAALDLAR-K--AEILPYlerlRDELDIPILyVSHsldevaRL-----ADHVVLLEQGRVVASGPL 218
|
....*.
gi 925114634 1260 QQLLAQ 1265
Cdd:COG4148 219 AEVLSR 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
412-604 |
3.87e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 103.32 E-value: 3.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 412 LKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD--PT---DGMVCIDGQDI--RTINVRHLREITGVVSQEPVLFAT 484
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 485 TIAENIRYG-REN---VTMDE-IEKAVKEANAYDFIMklpnkfDTLvGERGAQLSGGQKQRIAIARALVRNPKILLLDEA 559
Cdd:PRK14243 106 SIYDNIAYGaRINgykGDMDElVERSLRQAALWDEVK------DKL-KQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 925114634 560 TSALDTESEAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFD 604
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAaRVSDMTAFFN 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
415-612 |
3.92e-24 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 101.80 E-value: 3.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 415 LNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRhlREITGVVSQEPVLFA-TTIAENIRYG 493
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAhLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 494 RE-NVTMDEIE-KAVKEANAYdfiMKLPNKFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDT--ESEA 569
Cdd:cd03298 95 LSpGLKLTAEDrQAIEVALAR---VGLAGLEKRLPGE----LSGGERQRVALARVLVRDKPVLLLDEPFAALDPalRAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 925114634 570 VVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKG 612
Cdd:cd03298 168 LDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1045-1266 |
3.95e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 104.14 E-value: 3.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1045 NYPTRPDIPV----LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIK----HLNVQWLRAHLG 1116
Cdd:PRK13641 9 DYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKKLRKKVS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1117 IVSQ--EPILFDCSIAENIAYGDNSRVVSHEEimqaAKEANIhhfietlpeKYNTRVG------DKGT-QLSGGQKQRIA 1187
Cdd:PRK13641 89 LVFQfpEAQLFENTVLKDVEFGPKNFGFSEDE----AKEKAL---------KWLKKVGlsedliSKSPfELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1188 IARALVRQPHILLLDEATSALDTESEK-VVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVFQNGKVKEHGTHQQLLAQ 1265
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKeMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFSD 235
|
.
gi 925114634 1266 K 1266
Cdd:PRK13641 236 K 236
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1037-1265 |
4.38e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 103.63 E-value: 4.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPTRPD---IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQW-LR 1112
Cdd:PRK13633 5 IKCKNVSYKYESNEEsteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1113 AHLGIVSQEPilfDCSIA-----ENIAYGDNSRVVSHEEIM----QAAKEANIHHFIETLPEkyntrvgdkgtQLSGGQK 1183
Cdd:PRK13633 85 NKAGMVFQNP---DNQIVativeEDVAFGPENLGIPPEEIRervdESLKKVGMYEYRRHAPH-----------LLSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1184 QRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQ 1261
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
....
gi 925114634 1262 LLAQ 1265
Cdd:PRK13633 231 IFKE 234
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1052-1251 |
4.47e-24 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 102.13 E-value: 4.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1052 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEikhlnvQW-------------LRAH-LGI 1117
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDG------GWvdlaqaspreilaLRRRtIGY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1118 VSQ---------------EPILfdcsiaeniaygdnSRVVSHEEIMQAAKEAnIHHFieTLPEKY-----NTrvgdkgtq 1177
Cdd:COG4778 98 VSQflrviprvsaldvvaEPLL--------------ERGVDREEARARAREL-LARL--NLPERLwdlppAT-------- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 1178 LSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIV-IAHRLSTIQN-ADLIVVFQNG 1251
Cdd:COG4778 153 FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAvADRVVDVTPF 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
408-618 |
6.53e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 102.74 E-value: 6.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 408 EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTI-------------NVRHLREITGV 474
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 475 VSQEPVLFA-TTIAENIRygRENVTMDEIEKAVKEANAYDFIMKLPNKfDTLVGERGAQLSGGQKQRIAIARALVRNPKI 553
Cdd:PRK10619 97 VFQHFNLWShMTVLENVM--EAPIQVLGLSKQEARERAVKYLAKVGID-ERAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 554 LLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGF-DDGVIVEKGNHDELM 618
Cdd:PRK10619 174 LLFDEPTSALDPElVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFlHQGKIEEEGAPEQLF 240
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
394-617 |
8.03e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 103.89 E-value: 8.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRK-------EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTIN-- 464
Cdd:PRK11308 6 LQAIDLKKHYPVKRglfkperLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 465 -VRHLREITGVVSQEPvlFA---------TTIAENIRYgreNVTMDEIEKAVKEANaydfIMKLpnkfdtlVGERGAQ-- 532
Cdd:PRK11308 86 aQKLLRQKIQIVFQNP--YGslnprkkvgQILEEPLLI---NTSLSAAERREKALA----MMAK-------VGLRPEHyd 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 533 -----LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQVALDKARKGRTTIV-IAHRLSTVRNadvIAgfDD 605
Cdd:PRK11308 150 ryphmFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAqVLNLMMDLQQELGLSYVfISHDLSVVEH---IA--DE 224
|
250
....*....|....*...
gi 925114634 606 ------GVIVEKGNHDEL 617
Cdd:PRK11308 225 vmvmylGRCVEKGTKEQI 242
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
412-618 |
9.30e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 105.50 E-value: 9.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 412 LKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREI----TGVVSQEPVLFA-TTI 486
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPhMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 487 AENIRYGREnvtMDEIEKAVKEANAYDFIMKLpnKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 566
Cdd:PRK10070 124 LDNTAFGME---LAGINAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 567 SEAVVQVALDK--ARKGRTTIVIAHRL-STVRNADVIAGFDDGVIVEKGNHDELM 618
Cdd:PRK10070 199 IRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
393-617 |
9.35e-24 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 104.73 E-value: 9.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 393 NLEFKNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQdiRTINVRHLREIT 472
Cdd:PRK11000 3 SVTLRNVTKAY---GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK--RMNDVPPAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 473 GVVSQEPVLFA-TTIAENIRYGRE--NVTMDEIEKAVKEANAydfIMKLpnkfDTLVGERGAQLSGGQKQRIAIARALVR 549
Cdd:PRK11000 78 GMVFQSYALYPhLSVAENMSFGLKlaGAKKEEINQRVNQVAE---VLQL----AHLLDRKPKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 925114634 550 NPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAH-RLSTVRNADVIAGFDDGVIVEKGNHDEL 617
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1053-1257 |
9.51e-24 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 99.93 E-value: 9.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1053 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPLAGSVLIDGKEIKhlnVQWLRAHLGIVSQEPILFDC-SI 1129
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLD---KRSFRKIIGYVPQDDILHPTlTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1130 AENIAYgdnsrvvsheeimqAAKeanihhfietLpekyntrvgdKGtqLSGGQKQRIAIARALVRQPHILLLDEATSALD 1209
Cdd:cd03213 100 RETLMF--------------AAK----------L----------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 925114634 1210 TESEKVVQEALDK-AREGRTCIVIAHRLST--IQNADLIVVFQNGKVKEHG 1257
Cdd:cd03213 144 SSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
426-567 |
1.04e-23 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 104.41 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 426 ALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDG---QDIRT-INV-RHLREItGVVSQEPVLFAT-TIAENIRYGRenvtm 499
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARgIFLpPHRRRI-GYVFQEARLFPHlSVRGNLLYGR----- 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 500 deieKAVKEANAYDfimklpnKFDTLVG--------ERG-AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 567
Cdd:COG4148 103 ----KRAPRAERRI-------SFDEVVEllgighllDRRpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1041-1263 |
1.28e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 101.66 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1041 EVVFN----YPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF---YDP---LAGSVLIDGKEIKHLNVQW 1110
Cdd:PRK14246 8 EDVFNisrlYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1111 LRAHLGIVSQEPILF-DCSIAENIAYGDNSRVVSHEEIMQAAKEANIHHFieTLPEKYNTRVGDKGTQLSGGQKQRIAIA 1189
Cdd:PRK14246 88 LRKEVGMVFQQPNPFpHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKV--GLWKEVYDRLNSPASQLSGGQQQRLTIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 1190 RALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQLL 1263
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1043-1269 |
1.28e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 103.39 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1043 VFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLI------------------DGKEIK 1104
Cdd:PRK13631 30 VFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnhelitnpYSKKIK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1105 hlNVQWLRAHLGIVSQEP--ILFDCSIAENIAYGDNSRVVSHEEIMQAAKeanihhfietlpeKYNTRVGDKGT------ 1176
Cdd:PRK13631 110 --NFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSEAKKLAK-------------FYLNKMGLDDSylersp 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1177 -QLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEK-VVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVFQNGKV 1253
Cdd:PRK13631 175 fGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKI 254
|
250
....*....|....*.
gi 925114634 1254 KEHGTHQQLLAQKGIY 1269
Cdd:PRK13631 255 LKTGTPYEIFTDQHII 270
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
387-624 |
1.38e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 103.39 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 387 PDNIKGN--LEFKNVH--FSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCID----GQ 458
Cdd:PRK13631 13 PNPLSDDiiLRVKNLYcvFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 459 DIRTI------------NVRHLREITGVVSQEP--VLFATTIAENIRYGRENVTMDEIEkAVKEANAYDFIMKLpnKFDT 524
Cdd:PRK13631 93 KKNNHelitnpyskkikNFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSE-AKKLAKFYLNKMGL--DDSY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 525 LvgERGA-QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQVALDKARKGRTTIVIAHRLSTVRN-ADVIA 601
Cdd:PRK13631 170 L--ERSPfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvADEVI 247
|
250 260
....*....|....*....|...
gi 925114634 602 GFDDGVIVEKGNHDELMKEKGIY 624
Cdd:PRK13631 248 VMDKGKILKTGTPYEIFTDQHII 270
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1054-1257 |
1.39e-23 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 100.52 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHlNVQWLRAHLGIVSQEPILFD-CSIAEN 1132
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDrLTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1133 IAY--------GDNSrvvsHEEIMQAAKEANIHHFIETlpekyntRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEA 1204
Cdd:cd03266 99 LEYfaglyglkGDEL----TARLEELADRLGMEELLDR-------RVGG----FSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 1205 TSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQN-ADLIVVFQNGKVKEHG 1257
Cdd:cd03266 164 TTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
412-617 |
1.59e-23 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 100.14 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 412 LKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDI--RTINVRhlREItGVVSQEPvlfattIAEN 489
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvrEPREVR--RRI-GIVFQDL------SVDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 490 IRYGRENVTM---------DEIEKAVKEANAYdfiMKLPNKFDTLVGergaQLSGGQKQRIAIARALVRNPKILLLDEAT 560
Cdd:cd03265 87 ELTGWENLYIharlygvpgAERRERIDELLDF---VGLLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 561 SALDTESEAVVQVALDK--ARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDEL 617
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
377-628 |
1.98e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 108.33 E-value: 1.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 377 IDSYSKSGHKPDNIK-GNLEFKNVHFSYpsRKEVK-ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVC 454
Cdd:PTZ00243 1291 IEPASPTSAAPHPVQaGSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIR 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 455 IDGQDIRTINVRHLREITGVVSQEPVLFATTIAENIRYGREnVTMDEIEKAVKEANAYDFIMKLPNKFDTLVGERGAQLS 534
Cdd:PTZ00243 1369 VNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLE-ASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYS 1447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 535 GGQKQRIAIARALV-RNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGN 613
Cdd:PTZ00243 1448 VGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGS 1527
|
250
....*....|....*.
gi 925114634 614 HDEL-MKEKGIYFKLV 628
Cdd:PTZ00243 1528 PRELvMNRQSIFHSMV 1543
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
111-354 |
2.00e-23 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 102.00 E-value: 2.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 111 EEMTTYAYYYSGIGAGVLVAAYIQVSFWCLAAGRQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGD 190
Cdd:cd18784 33 DKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 191 KIGMFFQSIATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFG 270
Cdd:cd18784 113 NLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 271 GQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTSLVLSSEYSIGQvltvFFSVLIGAFSIGQA 350
Cdd:cd18784 193 NEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQISGGN----LISFILYQLELGSC 268
|
....
gi 925114634 351 SPSI 354
Cdd:cd18784 269 LESV 272
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1054-1262 |
2.45e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 103.24 E-value: 2.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQwlRAHLGIVSQEPILF-DCSIAEN 1132
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFrHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1133 IAYGDN--------SRVVSHEEIMQAAKEANIHHFIETLPekyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEA 1204
Cdd:PRK10851 95 IAFGLTvlprrerpNAAAIKAKVTQLLEMVQLAHLADRYP-----------AQLSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 925114634 1205 TSALDTESEKVVQEALDKARE--GRTCIVIAH-RLSTIQNADLIVVFQNGKVKEHGTHQQL 1262
Cdd:PRK10851 164 FGALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
394-621 |
2.84e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 101.64 E-value: 2.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRK--EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDI----RTINVRH 467
Cdd:PRK13634 3 ITFQKVEHRYQYKTpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 468 LREITGVVSQ--EPVLFATTIAENIRYGRENVTMDEiEKAVKEANAYDFIMKLPNK------FDtlvgergaqLSGGQKQ 539
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSE-EDAKQKAREMIELVGLPEEllarspFE---------LSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 540 RIAIARALVRNPKILLLDEATSALDTES--EAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDE 616
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGrkEMMEMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPRE 232
|
....*
gi 925114634 617 LMKEK 621
Cdd:PRK13634 233 IFADP 237
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
394-612 |
3.03e-23 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 99.36 E-value: 3.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSY-PSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTiNVRHLREIT 472
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 473 GVVSQEPVLFA-TTIAENIRY--GRENVTMDEIEKAVKEanaydfimkLPNKFDT--LVGERGAQLSGGQKQRIAIARAL 547
Cdd:cd03266 81 GFVSDSTGLYDrLTARENLEYfaGLYGLKGDELTARLEE---------LADRLGMeeLLDRRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 548 VRNPKILLLDEATSALD-TESEAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKG 612
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1051-1258 |
3.25e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 100.14 E-value: 3.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1051 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL---ERfYDPLAGSVLIDGKEIKHLNVQwLRAHLGI-VS-QEPI-- 1123
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDILELSPD-ERARAGIfLAfQYPVei 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1124 --------LfdcSIAENIAYGDNSRVV-SHEEIMQAAKEANihhfietLPEKYNTR---VGdkgtqLSGGQKQRIAIARA 1191
Cdd:COG0396 90 pgvsvsnfL---RTALNARRGEELSAReFLKLLKEKMKELG-------LDEDFLDRyvnEG-----FSGGEKKRNEILQM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1192 LVRQPHILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAH--RLSTIQNADLIVVFQNGKVKEHGT 1258
Cdd:COG0396 155 LLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1059-1209 |
3.63e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 99.66 E-value: 3.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1059 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEikHLNVQWLRAHLGIVSQEPILFD-CSIAENIAYGD 1137
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD--HTTTPPSRRPVSMLFQENNLFShLTVAQNIGLGL 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 1138 NS----RVVSHEEIMQAAKEANIHHFIETLPekyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1209
Cdd:PRK10771 97 NPglklNAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
411-617 |
4.78e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 100.12 E-value: 4.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 411 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRL---YDP---TDGMVCIDGQDIRTINVRHLREITGVVSQEPVLFA- 483
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPh 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 484 TTIAENIRYGRENVTMD---EIEKAVKEANAYDFIMKlpNKFDTLvGERGAQLSGGQKQRIAIARALVRNPKILLLDEAT 560
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKekrEIKKIVEECLRKVGLWK--EVYDRL-NSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 561 SALDTESEAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDEL 617
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
412-589 |
5.70e-23 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 99.08 E-value: 5.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 412 LKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLreitgVVSQEPVLFA-TTIAENI 490
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 491 RYGRENVtMDEIEKAVKEANAYDFImklpnkfdTLVG------ERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 564
Cdd:TIGR01184 76 ALAVDRV-LPDLSKSERRAIVEEHI--------ALVGlteaadKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180
....*....|....*....|....*..
gi 925114634 565 TESEAVVQVALDK--ARKGRTTIVIAH 589
Cdd:TIGR01184 147 ALTRGNLQEELMQiwEEHRVTVLMVTH 173
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
394-612 |
6.89e-23 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 104.38 E-value: 6.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPS-RKEVKILKGLNLKVQSGQTVALVGNSGCGKSTT----VQLMQRLYDPTDGMVCIDGQDIRTINVRHL 468
Cdd:COG4172 7 LSVEDLSVAFGQgGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 469 REITG----VVSQEPV-----LFatTI----AENIRYGReNVTMDEIEKAVKEAnaydfimkLpnkfdTLVGERGA---- 531
Cdd:COG4172 87 RRIRGnriaMIFQEPMtslnpLH--TIgkqiAEVLRLHR-GLSGAAARARALEL--------L-----ERVGIPDPerrl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 532 -----QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAvvQVaLD-----KARKGRTTIVIAHRLSTVRN-ADVI 600
Cdd:COG4172 151 dayphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQA--QI-LDllkdlQRELGMALLLITHDLGVVRRfADRV 227
|
250
....*....|..
gi 925114634 601 AGFDDGVIVEKG 612
Cdd:COG4172 228 AVMRQGEIVEQG 239
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
410-621 |
7.19e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 99.32 E-value: 7.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 410 KILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHL-REITGVVSQEPVLFATTIAE 488
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLaRRLALLPQHHLTPEGITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 489 NIRYGRE------NVTMDEIEKAVKEANAYDFImklpnkfDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 562
Cdd:PRK11231 96 LVAYGRSpwlslwGRLSAEDNARVNQAMEQTRI-------NHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 563 LDTESeavvQVALDK-----ARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELMKEK 621
Cdd:PRK11231 169 LDINH----QVELMRlmrelNTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1054-1253 |
7.61e-23 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 98.50 E-value: 7.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE---RFYDPLAGSVLIDGKEIKhlNVQWLRaHLGIVSQEPILFDC-SI 1129
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQPRK--PDQFQK-CVAYVRQDDILLPGlTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1130 AENIAYGDNSRVVSHEEIMQAAKEANIhhfiETLPEKYNTRVGDKG-TQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1208
Cdd:cd03234 99 RETLTYTAILRLPRKSSDAIRKKRVED----VLLRDLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 925114634 1209 DTESE-KVVQEALDKAREGRTCIVIAH--RLSTIQNADLIVVFQNGKV 1253
Cdd:cd03234 175 DSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEI 222
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
710-1266 |
8.05e-23 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 106.15 E-value: 8.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 710 WPYFVVGIFCAI--INGGLQPafsIIFSRIIGIFTRDEDPETKRqnsnmfsVLFLVLGI-ISFI--TFFLQGFTFG--KA 782
Cdd:TIGR01271 80 WRFVFYGILLYFgeATKAVQP---LLLGRIIASYDPFNAPEREI-------AYYLALGLcLLFIvrTLLLHPAIFGlhHL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 783 GEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVItqnIANLGTGIIISLIygWQLT-- 860
Cdd:TIGR01271 150 GMQMRIALFSLIYKKTLKLSSRVLD--KISTGQLVSLLSNNLNKFDEGLALAHFVW---IAPLQVILLMGLI--WELLev 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 861 --------LLLLAIVPiiaiAGVVEMKMlsgqALKDKKelegAGKIA------TEAIENFRTVVSLTREQKFEYMYaqsl 926
Cdd:TIGR01271 223 ngfcglgfLILLALFQ----ACLGQKMM----PYRDKR----AGKISerlaitSEIIENIQSVKAYCWEEAMEKII---- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 927 qvpyrNSLRKahifgVSFSITQAMMYFSYagcFRFGAYLVANEFMNFQDVL-----------LVFSAIVFGAMAVGQVSS 995
Cdd:TIGR01271 287 -----KNIRQ-----DELKLTRKIAYLRY---FYSSAFFFSGFFVVFLSVVpyalikgiilrRIFTTISYCIVLRMTVTR 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 996 FAPDYAKAKVSAAHVIMIIEKSPLIDSYSphglkpnTLEGNVTFNEVV-------------------------------- 1043
Cdd:TIGR01271 354 QFPGAIQTWYDSLGAITKIQDFLCKEEYK-------TLEYNLTTTEVEmvnvtaswdegigelfekikqnnkarkqpngd 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1044 ----FNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPlagsvlIDGKeIKHlnvqwlRAHLGIVS 1119
Cdd:TIGR01271 427 dglfFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEP------SEGK-IKH------SGRISFSP 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1120 QEPILFDCSIAENIAYGdnsrvVSHEEIMQAA--KEANIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPH 1197
Cdd:TIGR01271 494 QTSWIMPGTIKDNIIFG-----LSYDEYRYTSviKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDAD 568
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1198 ILLLDEATSALDTESEKVVQEA-LDKAREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLAQK 1266
Cdd:TIGR01271 569 LYLLDSPFTHLDVVTEKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
392-590 |
8.23e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 104.50 E-value: 8.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 392 GNLEFKNVHFSYPSRKEvkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGmvcidgqdirTINVRHLREI 471
Cdd:COG4178 361 GALALEDLTLRTPDGRP--LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSG----------RIARPAGARV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 472 TgVVSQEPVLFATTIAENIRY--GRENVTMDEIEKAVKEANaydfIMKLPNKFDTlVGERGAQLSGGQKQRIAIARALVR 549
Cdd:COG4178 429 L-FLPQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVG----LGHLAERLDE-EADWDQVLSLGEQQRLAFARLLLH 502
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 925114634 550 NPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHR 590
Cdd:COG4178 503 KPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1054-1257 |
8.85e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 99.15 E-value: 8.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PLAGSVLIDGKEIKHLNVQWL--RAHLGIVSQEPILF- 1125
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIevRREVGMVFQYPNPFp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1126 DCSIAENIAYGD--NSRVVSHEEIMQ----AAKEAnihhfieTLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHIL 1199
Cdd:PRK14267 99 HLTIYDNVAIGVklNGLVKSKKELDErvewALKKA-------ALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 925114634 1200 LLDEATSALDTESEKVVQEALDKAREGRTCIVIAHrlSTIQNA---DLIVVFQNGKVKEHG 1257
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH--SPAQAArvsDYVAFLYLGKLIEVG 230
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1059-1263 |
1.11e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 102.03 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1059 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWL----RAHLGIVSQE-PILFDCSIAENI 1133
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSfALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1134 AYGDNSRVVSHEEIMQAAKEANIHHFIETLPEKYNtrvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESE 1213
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYP-------DELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 925114634 1214 KVVQEALDK--AREGRTCIVIAHRL-STIQNADLIVVFQNGKVKEHGTHQQLL 1263
Cdd:PRK10070 201 TEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
394-617 |
1.36e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 99.11 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITG 473
Cdd:PRK13652 4 IETRDLCYSYSGSKEA--LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEP--VLFATTIAENIRYGRENVTMDE------IEKAVKEANAYDFIMKLPNkfdtlvgergaQLSGGQKQRIAIAR 545
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEetvahrVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 546 ALVRNPKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDEL 617
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDlpETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
411-566 |
1.37e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 97.17 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 411 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDP---TDGMVCIDGQDIRTINVrHLREItGVVSQEPVLFA-TTI 486
Cdd:COG4136 16 LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPA-EQRRI-GILFQDDLLFPhLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 487 AENIRYG-RENVTM----DEIEKAVKEANAYDFIMKLPnkfdtlvgergAQLSGGQKQRIAIARALVRNPKILLLDEATS 561
Cdd:COG4136 94 GENLAFAlPPTIGRaqrrARVEQALEEAGLAGFADRDP-----------ATLSGGQRARVALLRALLAEPRALLLDEPFS 162
|
....*
gi 925114634 562 ALDTE 566
Cdd:COG4136 163 KLDAA 167
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1055-1253 |
1.42e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 103.18 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1055 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLN-VQWLRAHLGIVSQEPILFDC-SIAEN 1132
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSpRDAIALGIGMVHQHFMLVPNlTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1133 IAYGDNSRVVSHEEIMQAAKEanihhfIETLPEKY------NTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATS 1206
Cdd:COG3845 101 IVLGLEPTKGGRLDRKAARAR------IRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARILILDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 925114634 1207 AL-DTESEKVVqEALDK-AREGRTCIVIAHRLSTI-QNADLIVVFQNGKV 1253
Cdd:COG3845 171 VLtPQEADELF-EILRRlAAEGKSIIFITHKLREVmAIADRVTVLRRGKV 219
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1053-1266 |
1.51e-22 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 99.16 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1053 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGsvlidgkEIKHlnvqwlRAHLGIVSQEPILFDCSIAEN 1132
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG-------KIKH------SGRISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1133 IAYGdnsrvVSHEEI--MQAAKEANIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1210
Cdd:cd03291 118 IIFG-----VSYDEYryKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1211 ESEKVVQEA-LDKAREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQLLAQK 1266
Cdd:cd03291 193 FTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1053-1234 |
1.52e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 98.62 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1053 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNvqwlrAHLGIVSQ-EPILFDCSIAE 1131
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGVVFQnEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1132 NIAYGDNSRVVSHEEIMQAAKEANIhhfietlpekyntRVGDKGT------QLSGGQKQRIAIARALVRQPHILLLDEAT 1205
Cdd:PRK11248 90 NVAFGLQLAGVEKMQRLEIAHQMLK-------------KVGLEGAekryiwQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190
....*....|....*....|....*....|.
gi 925114634 1206 SALDTESEKVVQEALDK--AREGRTCIVIAH 1234
Cdd:PRK11248 157 GALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1036-1209 |
1.59e-22 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 100.69 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1036 NVTFNEVVFNYPTrpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERFydpLAGSVLIDGKEIKHLnvqwlr 1112
Cdd:PRK11650 3 GLKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMvagLERI---TSGEIWIGGRVVNEL------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1113 ahlgivsqEPILFDC-------------SIAENIAYGDNSRVVSHEEIMQ----AAKEANIHHFIETLPEkyntrvgdkg 1175
Cdd:PRK11650 72 --------EPADRDIamvfqnyalyphmSVRENMAYGLKIRGMPKAEIEErvaeAARILELEPLLDRKPR---------- 133
|
170 180 190
....*....|....*....|....*....|....
gi 925114634 1176 tQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1209
Cdd:PRK11650 134 -ELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1042-1253 |
1.98e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 98.23 E-value: 1.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1042 VVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVqWLRA-HLGIVSQ 1120
Cdd:COG1101 9 KTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE-YKRAkYIGRVFQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1121 EPILFDC---SIAEN--IAYGDNSRvvshEEIMQAAKEANIHHFIET-------LPEKYNTRVGdkgtQLSGGQKQRIAI 1188
Cdd:COG1101 88 DPMMGTApsmTIEENlaLAYRRGKR----RGLRRGLTKKRRELFRELlatlglgLENRLDTKVG----LLSGGQRQALSL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 1189 ARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGKV 1253
Cdd:COG1101 160 LMATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNMEqALDYGNRLIMMHEGRI 227
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
367-591 |
1.98e-22 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 104.99 E-value: 1.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 367 IFKIIDnKPSIDSYSKSGHKPDNIKGNLEFKNVHFS--YPSRKEV--------------KILKGLNLKVQSGQTVALVGN 430
Cdd:TIGR01271 1175 VFKFID-LPQEEPRPSGGGGKYQLSTVLVIENPHAQkcWPSGGQMdvqgltakyteagrAVLQDLSFSVEGGQRVGLLGR 1253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 431 SGCGKSTTVQLMQRLYDpTDGMVCIDGQDIRTINVRHLREITGVVSQEPVLFATTIAENIRyGRENVTMDEIEKAVKEAN 510
Cdd:TIGR01271 1254 TGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD-PYEQWSDEEIWKVAEEVG 1331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 511 AYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHR 590
Cdd:TIGR01271 1332 LKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHR 1411
|
.
gi 925114634 591 L 591
Cdd:TIGR01271 1412 V 1412
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1054-1260 |
2.08e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 97.78 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDG------KEIKHLNVQWLRAHLGIVSQE----PI 1123
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQynlwPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1124 LfdcSIAENIAYGDnSRV--VSHEEIMQAAKEanihhFIETLpekyntRVGDKGT----QLSGGQKQRIAIARALVRQPH 1197
Cdd:PRK11124 97 L---TVQQNLIEAP-CRVlgLSKDQALARAEK-----LLERL------RLKPYADrfplHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 1198 ILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQ 1260
Cdd:PRK11124 162 VLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
407-612 |
2.09e-22 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 96.52 E-value: 2.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 407 KEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIrTINVRHLREItGVVSQEPVLFAT-T 485
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALRRI-GALIEAPGFYPNlT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 486 IAENIR-----YGRENVTMDEIEKAVKEANAYDfimklpnkfdtlvgERGAQLSGGQKQRIAIARALVRNPKILLLDEAT 560
Cdd:cd03268 89 ARENLRllarlLGIRKKRIDEVLDVVGLKDSAK--------------KKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 925114634 561 SALDTES-EAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKG 612
Cdd:cd03268 155 NGLDPDGiKELRELILSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1043-1262 |
2.21e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 99.39 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1043 VFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHL---------------- 1106
Cdd:PRK13651 11 IFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekekvleklviq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1107 --------NVQWLRAHLGIVSQ--EPILFDCSIAENIAYGDNSRVVSHEEIMQAAKEanihhFIET--LPEKYNTRvgdK 1174
Cdd:PRK13651 91 ktrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAK-----YIELvgLDESYLQR---S 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1175 GTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKA-REGRTCIVIAHRL-STIQNADLIVVFQNGK 1252
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKRTIFFKDGK 242
|
250
....*....|.
gi 925114634 1253 -VKEHGTHQQL 1262
Cdd:PRK13651 243 iIKDGDTYDIL 253
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1046-1265 |
2.45e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 98.34 E-value: 2.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1046 YPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEP--I 1123
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1124 LFDCSIAENIAYGDNSRVVSHEEIMQAAKEAnihhfIETLP-EKYNTRVGDkgtQLSGGQKQRIAIARALVRQPHILLLD 1202
Cdd:PRK13652 91 IFSPTVEQDIAFGPINLGLDEETVAHRVSSA-----LHMLGlEELRDRVPH---HLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 1203 EATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVFQNGKVKEHGTHQQLLAQ 1265
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
394-612 |
2.47e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 97.99 E-value: 2.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD-----PTDGMVCIDGQDIRTINVR-- 466
Cdd:PRK14267 5 IETVNLRVYYGSNH---VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDpi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 467 HLREITGVVSQEPVLFA-TTIAENIRYG-------RENVTMDE-IEKAVKEANAYDFIMKLPNKFdtlvgerGAQLSGGQ 537
Cdd:PRK14267 82 EVRREVGMVFQYPNPFPhLTIYDNVAIGvklnglvKSKKELDErVEWALKKAALWDEVKDRLNDY-------PSNLSGGQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 538 KQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHR-LSTVRNADVIAGFDDGVIVEKG 612
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
392-692 |
2.57e-22 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 98.39 E-value: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 392 GNLEFKNVHFSYPSRKEVkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDpTDGMVCIDGQDIRTINVRHLREI 471
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 472 TGVVSQEPVLFATTIAENIR-YGRENvtMDEIEKAVKEANAYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRN 550
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLDpYGKWS--DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 551 PKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVtm 630
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAI-- 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 631 qtrgneielenatgeskSESDALEMSPKdsgssliKRRSTRRSIHAPQGQDRKLGTKEDLNE 692
Cdd:cd03289 235 -----------------SPSDRLKLFPR-------RNSSKSKRKPRPQIQALQEETEEEVQD 272
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
396-621 |
2.58e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.45 E-value: 2.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 396 FKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGqdirtiNVRhlreiTGVV 475
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------GLR-----IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 476 SQEPVLFAT-TIAENIRYGRENVT-----MDEIEKAVK-----------------EANAYDF-------IMKL---PNKF 522
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGDAELRaleaeLEELEAKLAepdedlerlaelqeefeALGGWEAearaeeiLSGLgfpEEDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 523 DTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTES----EAVVqvaldKARKGrTTIVIAH-R--LSTVr 595
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFL-----KNYPG-TVLVVSHdRyfLDRV- 215
|
250 260
....*....|....*....|....*..
gi 925114634 596 nADVIAGFDDGVIVE-KGNHDELMKEK 621
Cdd:COG0488 216 -ATRILELDRGKLTLyPGNYSAYLEQR 241
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
394-618 |
2.58e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 97.99 E-value: 2.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSY------PSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTIN--- 464
Cdd:COG4167 5 LEVRNLSKTFkyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDyky 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 465 -VRHLREITgvvsQEPvlfATTIAENIRYG-------RENVTMDEIEKAVKeanaydfImklpnkFDTL--VGERGAQ-- 532
Cdd:COG4167 85 rCKHIRMIF----QDP---NTSLNPRLNIGqileeplRLNTDLTAEEREER-------I------FATLrlVGLLPEHan 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 533 -----LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQVALD-KARKGRTTIVIAHRLSTVRN-ADVIAGFD 604
Cdd:COG4167 145 fyphmLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSqIINLMLElQEKLGISYIYVSQHLGIVKHiSDKVLVMH 224
|
250
....*....|....
gi 925114634 605 DGVIVEKGNHDELM 618
Cdd:COG4167 225 QGEVVEYGKTAEVF 238
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
394-621 |
3.36e-22 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 96.83 E-value: 3.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVrHLREITG 473
Cdd:TIGR03410 1 LEVSNLNVYY---GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPP-HERARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 V--VSQEPVLFAT-TIAENIRYGREnvTMDEIEKAVKeanayDFIMKL-PNKFDTLvGERGAQLSGGQKQRIAIARALVR 549
Cdd:TIGR03410 77 IayVPQGREIFPRlTVEENLLTGLA--ALPRRSRKIP-----DEIYELfPVLKEML-GRRGGDLSGGQQQQLAIARALVT 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 550 NPKILLLDEATSALD----TESEAVVQvaLDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELMKEK 621
Cdd:TIGR03410 149 RPKLLLLDEPTEGIQpsiiKDIGRVIR--RLRAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDELDEDK 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1048-1263 |
4.11e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 100.30 E-value: 4.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1048 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPIL-FD 1126
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1127 CSIAENIAYGDN---SRVVSHEEIMQAAKEanihhfiETLPEKYNTRVGDKG-TQLSGGQKQRIAIARALVRQPHILLLD 1202
Cdd:PRK09536 92 FDVRQVVEMGRTphrSRFDTWTETDRAAVE-------RAMERTGVAQFADRPvTSLSGGERQRVLLARALAQATPVLLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 1203 EATSALDTESE----KVVQEALDkarEGRTCIVIAHRLS-TIQNADLIVVFQNGKVKEHGTHQQLL 1263
Cdd:PRK09536 165 EPTASLDINHQvrtlELVRRLVD---DGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
398-606 |
4.17e-22 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 96.25 E-value: 4.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 398 NVHFSYPSrkEVKILKGLNLKVQSGQTVALVGNSGCGKST----TVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITG 473
Cdd:cd03290 5 NGYFSWGS--GLATLSNINIRIPTGQLTMIVGQVGCGKSSlllaILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFATTIAENIRYGreNVTMDEIEKAVKEANAYD-FIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPK 552
Cdd:cd03290 83 YAAQKPWLLNATVEENITFG--SPFNKQRYKAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 553 ILLLDEATSALDTE-SEAVVQVALDKARKG--RTTIVIAHRLSTVRNADVIAGFDDG 606
Cdd:cd03290 161 IVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
394-617 |
4.29e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 99.91 E-value: 4.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKEVKilkGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINvRHLREITg 473
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-PYQRPIN- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFA-TTIAENIRYG--RENVTMDEIEKAVKE----ANAYDFIMKLPNkfdtlvgergaQLSGGQKQRIAIARA 546
Cdd:PRK11607 95 MMFQSYALFPhMTVEQNIAFGlkQDKLPKAEIASRVNEmlglVHMQEFAKRKPH-----------QLSGGQRQRVALARS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 925114634 547 LVRNPKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAH-RLSTVRNADVIAGFDDGVIVEKGNHDEL 617
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDKKLRDRMQLEVVDilERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1053-1259 |
4.73e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 96.62 E-value: 4.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1053 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDG------KEIKHLNVQWLRAHLGIVSQE----P 1122
Cdd:COG4161 16 QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLLRQKVGMVFQQynlwP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1123 ILfdcSIAENIAYGDnSRVV--SHEEIMQAAKEanihhFIETLpekyntRVGDKGT----QLSGGQKQRIAIARALVRQP 1196
Cdd:COG4161 96 HL---TVMENLIEAP-CKVLglSKEQAREKAMK-----LLARL------RLTDKADrfplHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 1197 HILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTH 1259
Cdd:COG4161 161 QVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDA 225
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
394-620 |
5.95e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 96.29 E-value: 5.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSypsRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQ-LMQR-LYDPTDGMVCIDGQDI--RTINVRHLR 469
Cdd:COG0396 1 LEIKNLHVS---VEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKvLMGHpKYEVTSGSILLDGEDIleLSPDERARA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 470 ----------EITGV-VSQepvlFATTIAENIRygRENVTMDEIEKAVKEANAydfIMKLPNKFdtlvGERG--AQLSGG 536
Cdd:COG0396 78 giflafqypvEIPGVsVSN----FLRTALNARR--GEELSAREFLKLLKEKMK---ELGLDEDF----LDRYvnEGFSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 537 QKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKAR-KGRTTIVIAH--RLSTVRNADVIAGFDDGVIVEKGN 613
Cdd:COG0396 145 EKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
....*..
gi 925114634 614 HdELMKE 620
Cdd:COG0396 225 K-ELALE 230
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1053-1264 |
7.19e-22 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 95.69 E-value: 7.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1053 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVqWLRAHLGI--VSQEPILF-DCSI 1129
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIgyLPQEASIFrKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1130 AENIAYGDNSRVVSHEEIMQAAkEANIHHF-IETLPEKyntrvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1208
Cdd:cd03218 93 EENILAVLEIRGLSKKEREEKL-EELLEEFhITHLRKS-------KASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 1209 DTESEKVVQEALDKAREGRTCIVIA-HRLS-TIQNADLIVVFQNGKVKEHGTHQQLLA 1264
Cdd:cd03218 165 DPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
394-606 |
1.95e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 99.62 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTtvqLMQRL-----YDPTDGMVCIDGQDIRTINVRHl 468
Cdd:PRK13549 6 LEMKNITKTFGG---VKALDNVSLKVRAGEIVSLCGENGAGKST---LMKVLsgvypHGTYEGEIIFEGEELQASNIRD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 469 REITGVV--SQEPVLFAT-TIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLpnKFDTLVGERGAQLSGGQKQRIAIAR 545
Cdd:PRK13549 79 TERAGIAiiHQELALVKElSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 925114634 546 ALVRNPKILLLDEATSALdTESEAVVQVAL--DKARKGRTTIVIAHRLSTVRN-ADVIAGFDDG 606
Cdd:PRK13549 157 ALNKQARLLILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
407-608 |
2.34e-21 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 94.42 E-value: 2.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 407 KEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQ----DIRTINVR---HLREIT-GVVSQe 478
Cdd:COG4778 22 KRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPReilALRRRTiGYVSQ- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 479 pvlFATTIAeniRYGRENVTMDE-IEKAVKEANAYDFIMKLPNKFDtlVGERGAQL-----SGGQKQRIAIARALVRNPK 552
Cdd:COG4778 101 ---FLRVIP---RVSALDVVAEPlLERGVDREEARARARELLARLN--LPERLWDLppatfSGGEQQRVNIARGFIADPP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 553 ILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHrlstvrNADVIAGFDDGVI 608
Cdd:COG4778 173 LLLLDEPTASLDAANrAVVVELIEEAKARGTAIIGIFH------DEEVREAVADRVV 223
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1037-1258 |
2.36e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 95.96 E-value: 2.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVvfNYPTRPDIP----VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSV----LIDGKEIKHLNV 1108
Cdd:PRK13643 2 IKFEKV--NYTYQPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1109 QWLRAHLGIVSQEP--ILFDCSIAENIAYGDNSRVVSHEEIMQAAKE-----ANIHHFIETLPekyntrvgdkgTQLSGG 1181
Cdd:PRK13643 80 KPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEklemvGLADEFWEKSP-----------FELSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 1182 QKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGT 1258
Cdd:PRK13643 149 QMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1037-1266 |
2.54e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 95.62 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYP--TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLN----VQW 1110
Cdd:PRK13646 3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1111 LRAHLGIVSQ--EPILFDCSIAENIAYG--------DNSRVVSHEEIMQAAKEANIhhfIETLPekyntrvgdkgTQLSG 1180
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGpknfkmnlDEVKNYAHRLLMDLGFSRDV---MSQSP-----------FQMSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1181 GQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAR--EGRTCIVIAHRLSTI-QNADLIVVFQNGKVKEHG 1257
Cdd:PRK13646 149 GQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQT 228
|
....*....
gi 925114634 1258 THQQLLAQK 1266
Cdd:PRK13646 229 SPKELFKDK 237
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
394-595 |
2.69e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 99.33 E-value: 2.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTtvqLMQRL---YDPTDGMVCIDGQDIRTINVRHLRE 470
Cdd:COG3845 6 LELRGITKRFGG---VVANDDVSLTVRPGEIHALLGENGAGKST---LMKILyglYQPDSGEILIDGKPVRIRSPRDAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 471 --ItGVVSQEPVLFAT-TIAENIRYGRENVT-----MDEIEKAVKE-ANAYDFIMKLpnkfDTLVGergaQLSGGQKQRI 541
Cdd:COG3845 80 lgI-GMVHQHFMLVPNlTVAENIVLGLEPTKggrldRKAARARIRElSERYGLDVDP----DAKVE----DLSVGEQQRV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 542 AIARALVRNPKILLLDEATSAL-DTESEAVVQVaLDK-ARKGRTTIVIAHRLSTVR 595
Cdd:COG3845 151 EILKALYRGARILILDEPTAVLtPQEADELFEI-LRRlAAEGKSIIFITHKLREVM 205
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1036-1257 |
3.39e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 97.02 E-value: 3.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1036 NVTFNEVVFNYPtrpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKhlNVQWLRAHL 1115
Cdd:PRK11000 3 SVTLRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVPPAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1116 GIVSQEPILF-DCSIAENIAYG----------DNSRVVSHEEIMQAAkeanihHFIETLPEkyntrvgdkgtQLSGGQKQ 1184
Cdd:PRK11000 78 GMVFQSYALYpHLSVAENMSFGlklagakkeeINQRVNQVAEVLQLA------HLLDRKPK-----------ALSGGQRQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 1185 RIAIARALVRQPHILLLDEATSALDTESEkvVQEALDKA----REGRTCIVIAH-RLSTIQNADLIVVFQNGKVKEHG 1257
Cdd:PRK11000 141 RVAIGRTLVAEPSVFLLDEPLSNLDAALR--VQMRIEISrlhkRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
713-971 |
3.70e-21 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 95.18 E-value: 3.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 713 FVVGIFCAIINGGLQPAFSIIFSRIIGIFTRDEDPETKRqnsnMFSVLFLVLGIISFITFFLQGFTFGKAGEILTKRLRY 792
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALL----LVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 793 MVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGtGIIISLIY-GWQLTLLLLAIVPIIA 871
Cdd:cd18552 77 DLFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVI-GLLGVLFYlDWKLTLIALVVLPLAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 872 IAGVV---EMKMLSgqalkdKKELEGAGKIAT---EAIENFRTVVSLTREQKFEYMYAQSLQVPYRNSLRKAHIFGVSFS 945
Cdd:cd18552 154 LPIRRigkRLRKIS------RRSQESMGDLTSvlqETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSP 227
|
250 260
....*....|....*....|....*.
gi 925114634 946 ITQAMMYFSYAGCFRFGAYLVANEFM 971
Cdd:cd18552 228 LMELLGAIAIALVLWYGGYQVISGEL 253
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1053-1249 |
4.63e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.24 E-value: 4.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1053 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPILFDCSIAEN 1132
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1133 IAYGDNSRvvsHEEIMQAAKEANIHHFieTLPEKyntrVGDKG-TQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1211
Cdd:PRK10247 101 LIFPWQIR---NQQPDPAIFLDDLERF--ALPDT----ILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 925114634 1212 SEKVVQEALDK-AREGRTCIV-IAHRLSTIQNADLIVVFQ 1249
Cdd:PRK10247 172 NKHNVNEIIHRyVREQNIAVLwVTHDKDEINHADKVITLQ 211
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
394-591 |
4.78e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 94.38 E-value: 4.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVH--FSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDI-------RTIN 464
Cdd:COG1101 2 LELKNLSktFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtklpeykRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 465 VrhlreitGVVSQEPVL---FATTIAEN------------IRYGRENVTMDEIEKAVKEANaydfiMKLPNKFDTLVGer 529
Cdd:COG1101 82 I-------GRVFQDPMMgtaPSMTIEENlalayrrgkrrgLRRGLTKKRRELFRELLATLG-----LGLENRLDTKVG-- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 925114634 530 gaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAHRL 591
Cdd:COG1101 148 --LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNM 209
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1051-1264 |
4.88e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 94.69 E-value: 4.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1051 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKH--LNVQWLRAHLGIVSQEP--ILFD 1126
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYskRGLLALRQQVATVFQDPeqQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1127 CSIAENIAYGDNSRVVSHEEIMQAAKEAnihhfiETLPEKYNTRvgDKGTQ-LSGGQKQRIAIARALVRQPHILLLDEAT 1205
Cdd:PRK13638 93 TDIDSDIAFSLRNLGVPEAEITRRVDEA------LTLVDAQHFR--HQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 925114634 1206 SALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVFQNGKVKEHGTHQQLLA 1264
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
415-618 |
4.99e-21 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 96.33 E-value: 4.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 415 LNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDG---QDIR--TINVRHLREItGVVSQEPVLFA-TTIAE 488
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRkgIFLPPEKRRI-GYVFQEARLFPhLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 489 NIRYGRENVTMDEiekavkEANAYDFIMKLPNkFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESE 568
Cdd:TIGR02142 95 NLRYGMKRARPSE------RRISFERVIELLG-IGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 925114634 569 AVVQVALDKARK--GRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELM 618
Cdd:TIGR02142 168 YEILPYLERLHAefGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1050-1256 |
5.78e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.21 E-value: 5.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1050 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIdGKEIKhlnvqwlrahLGIVSQEPILFDcsi 1129
Cdd:COG0488 326 GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IGYFDQHQEELD--- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1130 aeniaygDNSRVVshEEIMQAAKEANIHHFIETL------PEKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDE 1203
Cdd:COG0488 392 -------PDKTVL--DELRDGAPGGTEQEVRGYLgrflfsGDDAFKPVGV----LSGGEKARLALAKLLLSPPNVLLLDE 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 1204 ATSALDTESEKVVQEALDkAREGrTCIVIAH-R--LSTIqnADLIVVFQNGKVKEH 1256
Cdd:COG0488 459 PTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREY 510
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1044-1278 |
6.04e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 100.05 E-value: 6.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1044 FNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIdgkeikhlnvqwLRAHLGIVSQEPI 1123
Cdd:PLN03232 622 FSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVAYVPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1124 LFDCSIAENIAYGDNsrvVSHEEIMQAAKEANIHHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDE 1203
Cdd:PLN03232 690 IFNATVRENILFGSD---FESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 1204 ATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQlLAQKGIYFSMVSVQAG 1278
Cdd:PLN03232 767 PLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAE-LSKSGSLFKKLMENAG 841
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1050-1252 |
6.05e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 98.08 E-value: 6.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1050 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdP---LAGSVLIDGKEIKHLNVQWL-RAHLGIVSQEPILF 1125
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PhgtYEGEIIFEGEELQASNIRDTeRAGIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1126 -DCSIAENIAYGD---NSRVVSHEEIMQAAKE--ANIHHFIETlpekyNTRVGDkgtqLSGGQKQRIAIARALVRQPHIL 1199
Cdd:PRK13549 95 kELSVLENIFLGNeitPGGIMDYDAMYLRAQKllAQLKLDINP-----ATPVGN----LGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 1200 LLDEATSALdTESEKVVQEAL--DKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGK 1252
Cdd:PRK13549 166 ILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1050-1248 |
9.13e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.53 E-value: 9.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1050 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQwlrahlgiVSQEPILFDCSI 1129
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ--------RSEVPDSLPLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1130 AENIAYG-------------DNSRVVshEEIMQAAKeanihhfIETLPEKyntRVGDkgtqLSGGQKQRIAIARALVRQP 1196
Cdd:NF040873 75 RDLVAMGrwarrglwrrltrDDRAAV--DDALERVG-------LADLAGR---QLGE----LSGGQRQRALLAQGLAQEA 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 925114634 1197 HILLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQNADLIVVF 1248
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
409-610 |
1.03e-20 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 93.18 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 409 VKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRhlrEIT--GVVS--QEPVLFAT 484
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH---RIArlGIARtfQNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 485 -TIAENIRYGRENVTMDEIEKAV--------KEANAYDFIM------KLPNKFDTLVGErgaqLSGGQKQRIAIARALVR 549
Cdd:COG0411 94 lTVLENVLVAAHARLGRGLLAALlrlprarrEEREARERAEellervGLADRADEPAGN----LSYGQQRRLEIARALAT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 550 NPKILLLDEATSAL-DTESEAVVQVALD-KARKGRTTIVIAHRLSTVRN-ADVIAGFDDG-VIVE 610
Cdd:COG0411 170 EPKLLLLDEPAAGLnPEETEELAELIRRlRDERGITILLIEHDMDLVMGlADRIVVLDFGrVIAE 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1053-1265 |
1.08e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.47 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1053 PVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP----LAGSVLIDGKEIKHLNVQWLRAHLG----IVSQEPI 1123
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVRGnkiaMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1124 L-------FDCSIAENIA-YGDNSRVVSHEEIMQAAKEANIHHfietlpekYNTRVGDKGTQLSGGQKQRIAIARALVRQ 1195
Cdd:PRK15134 103 VslnplhtLEKQLYEVLSlHRGMRREAARGEILNCLDRVGIRQ--------AAKRLTDYPHQLSGGERQRVMIAMALLTR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 1196 PHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVFQNGKVKEHGTHQQLLAQ 1265
Cdd:PRK15134 175 PELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQNRAATLFSA 247
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1054-1258 |
1.10e-20 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 92.20 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWlRAHLGI--VSQEPILF-DCSIA 1130
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE-RARAGIayVPQGREIFpRLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1131 ENIAYGDNSRVVSHEEImqaakEANIHHFIETLPEKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1210
Cdd:TIGR03410 94 ENLLTGLAALPRRSRKI-----PDEIYELFPVLKEMLGRRGGD----LSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 925114634 1211 ESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGKVKEHGT 1258
Cdd:TIGR03410 165 SIIKDIGRVIRRlrAEGGMAILLVEQYLDfARELADRYYVMERGRVVASGA 215
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
394-612 |
1.36e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.08 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRK--------EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYdPTDGMVCIDGQDIRTINV 465
Cdd:PRK15134 276 LDVEQLQVAFPIRKgilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 466 RHL---REITGVVSQEP---------VLfaTTIAENIRYGRENVTMDEIEKAVKEAnaydfiMKlpnkfdtlvgERG--- 530
Cdd:PRK15134 355 RQLlpvRHRIQVVFQDPnsslnprlnVL--QIIEEGLRVHQPTLSAAQREQQVIAV------ME----------EVGldp 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 531 -------AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVqVALDKARKGR---TTIVIAHRLSTVRNA--D 598
Cdd:PRK15134 417 etrhrypAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQI-LALLKSLQQKhqlAYLFISHDLHVVRALchQ 495
|
250
....*....|....
gi 925114634 599 VIAgFDDGVIVEKG 612
Cdd:PRK15134 496 VIV-LRQGEVVEQG 508
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1054-1264 |
1.61e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.08 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPLAGSVLIDGKEIKHLNVQWL---RAHLGIVSQEP---ILFDC 1127
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnssLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1128 SIAENIAYGDNsrvVSHEEIMQAAKEANIhhfIETLPEkyntrVG-DKGT------QLSGGQKQRIAIARALVRQPHILL 1200
Cdd:PRK15134 380 NVLQIIEEGLR---VHQPTLSAAQREQQV---IAVMEE-----VGlDPETrhrypaEFSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 925114634 1201 LDEATSALDteseKVVQE---ALDKAREGR---TCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQLLA 1264
Cdd:PRK15134 449 LDEPTSSLD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1044-1265 |
1.72e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 92.59 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1044 FNYPT----RPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVS 1119
Cdd:COG4167 14 FKYRTglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1120 QEPilfdcsiaeNIAYGDNSRVVS--------HEEIMQAAKEANIhhfIETLpekynTRVG-------DKGTQLSGGQKQ 1184
Cdd:COG4167 94 QDP---------NTSLNPRLNIGQileeplrlNTDLTAEEREERI---FATL-----RLVGllpehanFYPHMLSSGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1185 RIAIARALVRQPHILLLDEATSALD--TESEKV-----VQEaldkaREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEH 1256
Cdd:COG4167 157 RVALARALILQPKIIIADEALAALDmsVRSQIInlmleLQE-----KLGISYIYVSQHLGIVKHiSDKVLVMHQGEVVEY 231
|
....*....
gi 925114634 1257 GTHQQLLAQ 1265
Cdd:COG4167 232 GKTAEVFAN 240
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1048-1255 |
2.24e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 92.44 E-value: 2.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1048 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLN----------VQWL------ 1111
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrkafrrdIQMVfqdsis 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1112 ----RAHLGIVSQEPI--LFDCSIAENIAygdnsRVvshEEIMQAakeanihhfIETLPEKYNTRVGdkgtQLSGGQKQR 1185
Cdd:PRK10419 101 avnpRKTVREIIREPLrhLLSLDKAERLA-----RA---SEMLRA---------VDLDDSVLDKRPP----QLSGGQLQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1186 IAIARALVRQPHILLLDEATSALDteseKVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKE 1255
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLD----LVLQaGVIRllkklQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
394-612 |
2.26e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 92.14 E-value: 2.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITG 473
Cdd:PRK13548 3 LEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVL-FATTIAENIRYGR-----ENVTMDEI-EKAVKEANAydfimklpnkfDTLVGERGAQLSGGQKQRIAIARA 546
Cdd:PRK13548 80 VLPQHSSLsFPFTVEEVVAMGRaphglSRAEDDALvAAALAQVDL-----------AHLAGRDYPQLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 547 LVR------NPKILLLDEATSALD-TESEAVVQVALDKARK-GRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKG 612
Cdd:PRK13548 149 LAQlwepdgPPRWLLLDEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADG 223
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
394-591 |
2.28e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 96.23 E-value: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREI-T 472
Cdd:PRK10762 5 LQLKGIDKAFPG---VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 473 GVVSQEPVLFAT-TIAENIRYGRENVT-MDEIE--KAVKEANAYDFIMKLPNKFDTLVGErgaqLSGGQKQRIAIARALV 548
Cdd:PRK10762 82 GIIHQELNLIPQlTIAENIFLGREFVNrFGRIDwkKMYAEADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAKVLS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 925114634 549 RNPKILLLDEATSAL-DTESEAVVQVALDKARKGRTTIVIAHRL 591
Cdd:PRK10762 158 FESKVIIMDEPTDALtDTETESLFRVIRELKSQGRGIVYISHRL 201
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
144-337 |
2.32e-20 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 92.79 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 144 RQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSIATFFTGFIVGFTRGWKLTLVILAI 223
Cdd:cd18590 66 RLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 224 SPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGA 303
Cdd:cd18590 146 MPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLV 225
|
170 180 190
....*....|....*....|....*....|....
gi 925114634 304 AFLLIYASYALAFWYGTSLVLSSEYSIGQVLTVF 337
Cdd:cd18590 226 RRVLQLGVQVLMLYCGRQLIQSGHLTTGSLVSFI 259
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1050-1265 |
2.39e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 96.13 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1050 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQ-WLRAHLGIVSQEPILF-DC 1127
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAIIYQELHLVpEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1128 SIAENIAYGD--NSR-VVSHEEIMQAAKEANIHHFIETLPekyNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEA 1204
Cdd:PRK11288 95 TVAENLYLGQlpHKGgIVNRRLLNYEAREQLEHLGVDIDP---DTPLKY----LSIGQRQMVEIAKALARNARVIAFDEP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 1205 TSALDT-ESE---KVVQEALDkarEGRTCIVIAHRLSTI-QNADLIVVFQNG-KVKEHG-----THQQLLAQ 1265
Cdd:PRK11288 168 TSSLSArEIEqlfRVIRELRA---EGRVILYVSHRMEEIfALCDAITVFKDGrYVATFDdmaqvDRDQLVQA 236
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
394-564 |
2.91e-20 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 91.07 E-value: 2.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVrHLREITG 473
Cdd:cd03218 1 LRAENLSKRYGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 V--VSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKEANAYDFIMKLPNKFdtlvgerGAQLSGGQKQRIAIARALV 548
Cdd:cd03218 77 IgyLPQEASIFRKlTVEENILAVLEirGLSKKEREEKLEELLEEFHITHLRKSK-------ASSLSGGERRRVEIARALA 149
|
170
....*....|....*.
gi 925114634 549 RNPKILLLDEATSALD 564
Cdd:cd03218 150 TNPKFLLLDEPFAGVD 165
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1054-1264 |
3.35e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 92.08 E-value: 3.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAG-----SVLIDGKEI-KHLNVQWLRAHLGIVSQEPILFDC 1127
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1128 SIAENIAYGDNSRVVSHEEIMQAAKEANIHHFieTLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1207
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 1208 LDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQLLA 1264
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS 251
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
394-564 |
4.62e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 91.28 E-value: 4.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVcIDGqdirTINVRHLREITG 473
Cdd:PRK11247 13 LLLNAVSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG----TAPLAEAREDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFA-TTIAENIRYGRENVTMDEIEKAVKEANaydfimkLPNKfdtlVGERGAQLSGGQKQRIAIARALVRNPK 552
Cdd:PRK11247 85 LMFQDARLLPwKKVIDNVGLGLKGQWRDAALQALAAVG-------LADR----ANEWPAALSGGQKQRVALARALIHRPG 153
|
170
....*....|..
gi 925114634 553 ILLLDEATSALD 564
Cdd:PRK11247 154 LLLLDEPLGALD 165
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1053-1203 |
6.38e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 90.47 E-value: 6.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1053 PVLQGLSLEVKKGQTLALVGSSGCGKSTVvqllerFY------DPLAGSVLIDGKEIKHLNVqWLRAHLGI--VSQEPIL 1124
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-HKRARLGIgyLPQEASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1125 F-DCSIAENIAYGDNSRVVSHEEIMQAA----KEANIHHFIETlpekyntrvgdKGTQLSGGQKQRIAIARALVRQPHIL 1199
Cdd:COG1137 90 FrKLTVEDNILAVLELRKLSKKEREERLeellEEFGITHLRKS-----------KAYSLSGGERRRVEIARALATNPKFI 158
|
....
gi 925114634 1200 LLDE 1203
Cdd:COG1137 159 LLDE 162
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1054-1237 |
6.72e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 90.26 E-value: 6.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQW---LRAH-LGIVSQ-EPILFDCS 1128
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1129 IAENIAY----GDNSRVVSHEEIMQAAKEANIHHfietlpekyntRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEA 1204
Cdd:PRK11629 104 ALENVAMplliGKKKPAEINSRALEMLAAVGLEH-----------RANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190
....*....|....*....|....*....|....*
gi 925114634 1205 TSALDTESEKVVQEALDK--AREGRTCIVIAHRLS 1237
Cdd:PRK11629 173 TGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQ 207
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
416-618 |
6.83e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 90.03 E-value: 6.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 416 NLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTInvrhlreitgVVSQEPV--------LFA-TTI 486
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTT----------PPSRRPVsmlfqennLFShLTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 487 AENIRYG-RENVTMDEIEKAVKEANAY-----DFIMKLPnkfdtlvgergAQLSGGQKQRIAIARALVRNPKILLLDEAT 560
Cdd:PRK10771 89 AQNIGLGlNPGLKLNAAQREKLHAIARqmgieDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 925114634 561 SALDT--ESEAVVQVALDKARKGRTTIVIAHRLS-TVRNAD---VIAgfdDGVIVEKGNHDELM 618
Cdd:PRK10771 158 SALDPalRQEMLTLVSQVCQERQLTLLMVSHSLEdAARIAPrslVVA---DGRIAWDGPTDELL 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
394-651 |
7.08e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 91.71 E-value: 7.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIrtiNVRHLREItG 473
Cdd:COG4152 2 LELKGLTKRF---GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL---DPEDRRRI-G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFAT-TIAENIRY-GR-ENVTMDEIEKAVKEanaydfimkLPNKFDtlVGERGA----QLSGGQKQRIAIARA 546
Cdd:COG4152 75 YLPEERGLYPKmKVGEQLVYlARlKGLSKAEAKRRADE---------WLERLG--LGDRANkkveELSKGNQQKVQLIAA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 547 LVRNPKILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELMKEKGIy 624
Cdd:COG4152 144 LLHDPELLILDEPFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQFGR- 222
|
250 260
....*....|....*....|....*..
gi 925114634 625 fKLVTMQTRGNEIELENATGESKSESD 651
Cdd:COG4152 223 -NTLRLEADGDAGWLRALPGVTVVEED 248
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
394-620 |
7.96e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 91.33 E-value: 7.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKEV--KILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTIN----VRH 467
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 468 LREITGVVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKE-----ANAYDFIMKLPnkfdtlvgergAQLSGGQK 538
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNfgIPKEKAEKIAAEklemvGLADEFWEKSP-----------FELSGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 539 QRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK-GRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDE 616
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSD 230
|
....
gi 925114634 617 LMKE 620
Cdd:PRK13643 231 VFQE 234
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
394-590 |
8.68e-20 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 87.59 E-value: 8.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVcidgqdirtinVRHLREITG 473
Cdd:cd03223 1 IELENLSLATPDGR--VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFATTIAENIRYGRENVtmdeiekavkeanaydfimklpnkfdtlvgergaqLSGGQKQRIAIARALVRNPKI 553
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*...
gi 925114634 554 LLLDEATSALDTESEAVVqvaLDKARKGRTTIV-IAHR 590
Cdd:cd03223 113 VFLDEATSALDEESEDRL---YQLLKELGITVIsVGHR 147
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
405-612 |
8.75e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 93.37 E-value: 8.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 405 SRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITGVVSQEPVL-FA 483
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 484 TTIAENIRYGREN-----VTMDE-----IEKAVKEANAYDFIMKlpnKFDTlvgergaqLSGGQKQRIAIARALVRNPKI 553
Cdd:PRK09536 92 FDVRQVVEMGRTPhrsrfDTWTEtdraaVERAMERTGVAQFADR---PVTS--------LSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 925114634 554 LLLDEATSALDTESEA-VVQVALDKARKGRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKG 612
Cdd:PRK09536 161 LLLDEPTASLDINHQVrTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
103-339 |
9.92e-20 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 91.32 E-value: 9.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 103 QHFINHLE------EEMTTYAYYYSGIGAGVLVAAYIQVSFWcLAAGRQI-LKIRKQFFHAIMRQEIGWFDVHDVGELNT 175
Cdd:cd18541 23 GRAIDALTagtltaSQLLRYALLILLLALLIGIFRFLWRYLI-FGASRRIeYDLRNDLFAHLLTLSPSFYQKNRTGDLMA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 176 RLTDDVSKINEGIGDKIGMFFQSIATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAV 255
Cdd:cd18541 102 RATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 256 AEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTSLVLSSEYSIGQvLT 335
Cdd:cd18541 182 VQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITLGD-LV 260
|
....
gi 925114634 336 VFFS 339
Cdd:cd18541 261 AFNS 264
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1054-1253 |
1.28e-19 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 87.87 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNV-QWLRAHLGIVSQEP----ILFDCS 1128
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVPEDRkregLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1129 IAENIAYGDnsrvvsheeimqaakeanihhfietlpekyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1208
Cdd:cd03215 95 VAENIALSS---------------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 925114634 1209 DTES-EKVVQEALDKAREGRTCIVIahrlST-----IQNADLIVVFQNGKV 1253
Cdd:cd03215 136 DVGAkAEIYRLIRELADAGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1039-1234 |
1.49e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.98 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1039 FNEVVFNYPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGkeikhlnvqwlRAHLGIV 1118
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1119 SQEPILFD-CSIAENIAYGDNSRVVSHEEIMQA-----------AKEANIHHFIETL-------------------PEKY 1167
Cdd:COG0488 67 PQEPPLDDdLTVLDTVLDGDAELRALEAELEELeaklaepdedlERLAELQEEFEALggweaearaeeilsglgfpEEDL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 1168 NTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTESekvVQ--EALDKAREGrTCIVIAH 1234
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEwlEEFLKNYPG-TVLVVSH 207
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
395-624 |
1.86e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 89.37 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 395 EFKNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITGV 474
Cdd:COG4604 3 EIKNVSKRY---GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 475 VSQEPVlFAT--TIAENIRYGR-----ENVTmDEIEKAVKEANAYDFIMKLPNKF-DtlvgergaQLSGGQKQRIAIARA 546
Cdd:COG4604 80 LRQENH-INSrlTVRELVAFGRfpyskGRLT-AEDREIIDEAIAYLDLEDLADRYlD--------ELSGGQRQRAFIAMV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 547 LVRNPKILLLDEATSALDTesEAVVQV--ALDKA--RKGRTTIVIAHRLstvrN-----ADVIAGFDDGVIVEKGNHDEL 617
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDM--KHSVQMmkLLRRLadELGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQGTPEEI 223
|
250
....*....|
gi 925114634 618 MKE---KGIY 624
Cdd:COG4604 224 ITPevlSDIY 233
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1051-1265 |
1.89e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 90.55 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1051 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNvqwlRAHLGIVSQEPILF-DCSI 1129
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLPEERGLYpKMKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1130 AENIAY-----GdnsrvVSHEEIMQAAKEanihhFIET--LPEKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLD 1202
Cdd:COG4152 89 GEQLVYlarlkG-----LSKAEAKRRADE-----WLERlgLGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 1203 EATSALDTES-EKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQLLAQ 1265
Cdd:COG4152 155 EPFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
759-1255 |
2.30e-19 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 93.32 E-value: 2.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 759 VLFLVLGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIgSRLAVI 838
Cdd:COG4615 52 LLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLE--RIGAARLLAALTEDVRTISQAF-VRLPEL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 839 TQNIANlgtgIIISLIY-GWQLTLLLLAIVPIIAIAGVVEMKMLSgqalKDKKELEGAGKIATEAIENFRTVVSLTREQK 917
Cdd:COG4615 129 LQSVAL----VLGCLAYlAWLSPPLFLLTLVLLGLGVAGYRLLVR----RARRHLRRAREAEDRLFKHFRALLEGFKELK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 918 F-----EYMYAQSLQVP---YRNSLRKAH-IFGVSFSITQAMMYFSYAGCFrfgaYLVANEFMNFQDVLLVFS-AIVFGA 987
Cdd:COG4615 201 LnrrrrRAFFDEDLQPTaerYRDLRIRADtIFALANNWGNLLFFALIGLIL----FLLPALGWADPAVLSGFVlVLLFLR 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 988 MAVGQVSSFAPDYAKAKVSAAHvIMIIEKSplIDSYSPHGLKPNTLEGNVTFNE-----VVFNYPTRPDIP--VLQGLSL 1060
Cdd:COG4615 277 GPLSQLVGALPTLSRANVALRK-IEELELA--LAAAEPAAADAAAPPAPADFQTlelrgVTYRYPGEDGDEgfTLGPIDL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1061 EVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPILFDcsiaenIAYGDNSr 1140
Cdd:COG4615 354 TIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD------RLLGLDG- 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1141 vvsheeimqAAKEANIHHFIETLPEKYNTRVGDKG---TQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQ 1217
Cdd:COG4615 427 ---------EADPARARELLERLELDHKVSVEDGRfstTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRVFY 497
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 925114634 1218 EAL---DKAReGRTCIVIAHRLSTIQNADLIVVFQNGKVKE 1255
Cdd:COG4615 498 TELlpeLKAR-GKTVIAISHDDRYFDLADRVLKMDYGKLVE 537
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
122-355 |
2.40e-19 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 90.26 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 122 GIGAGVLVAAYIQVSFWCLAAGRQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSIAT 201
Cdd:cd18564 62 GIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 202 FFTGFIVGFTRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNK 281
Cdd:cd18564 142 LVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFAR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 282 NLEEAKRIGIK-KAITANISIGAAfLLIYASYALAFWYGTSLVLSSEYSIGQvLTVFFSVLIGAF-----------SIGQ 349
Cdd:cd18564 222 ENRKSLRAGLRaARLQALLSPVVD-VLVAVGTALVLWFGAWLVLAGRLTPGD-LLVFLAYLKNLYkpvrdlakltgRIAK 299
|
....*.
gi 925114634 350 ASPSIE 355
Cdd:cd18564 300 ASASAE 305
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
402-598 |
2.74e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 87.29 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 402 SYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGmvcidgqdirTINVRHLREITGVV--SQEP 479
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSG----------TVRRAGGARVAYVPqrSEVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 480 VLFATTIAENIRYGR-------ENVTMDEiEKAVKEAnaydfIMKLpnKFDTLVGERGAQLSGGQKQRIAIARALVRNPK 552
Cdd:NF040873 68 DSLPLTVRDLVAMGRwarrglwRRLTRDD-RAAVDDA-----LERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 925114634 553 ILLLDEATSALDTESEAVVQVAL-DKARKGRTTIVIAHRLSTVRNAD 598
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRAD 186
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
398-621 |
2.75e-19 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 89.53 E-value: 2.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 398 NVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGmvcidgqdirtiNVRHLREITgVVSQ 477
Cdd:cd03291 39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG------------KIKHSGRIS-FSSQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 478 EPVLFATTIAENIRYGrenVTMDEI--EKAVKEANAYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILL 555
Cdd:cd03291 106 FSWIMPGTIKENIIFG---VSYDEYryKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 556 LDEATSALD--TESEaVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEK 621
Cdd:cd03291 183 LDSPFGYLDvfTEKE-IFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
394-612 |
2.98e-19 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 87.72 E-value: 2.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIrTINVRHLreiTG 473
Cdd:cd03269 1 LEVENVTKRF---GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAARNR---IG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLF-ATTIAENIRY-GREnvtmdeieKAVKEANAYDFIMKLPNKFD--TLVGERGAQLSGGQKQRIAIARALVR 549
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVYlAQL--------KGLKKEEARRRIDEWLERLElsEYANKRVEELSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 550 NPKILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKG 612
Cdd:cd03269 146 DPELLILDEPFSGLDPVNvELLKDVIRELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
92-339 |
3.44e-19 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 89.75 E-value: 3.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 92 VIINESITNNTQHFinhleEEMTTYAYYYSGIGAGVLVAAYIQVSFWCLAAGRQILKIRKQFFHAIMRQEIGWFDVHDVG 171
Cdd:cd18544 24 RAIDDYIVPGQGDL-----QGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 172 ELNTRLTDDVSKINEGIGDKIGMFFQSIATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAK 251
Cdd:cd18544 99 RLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 252 AGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKkaitaNISIGAAF-----LLIYASYALAFWYGTSLVLSS 326
Cdd:cd18544 179 LNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLK-----SIKLFALFrplveLLSSLALALVLWYGGGQVLSG 253
|
250
....*....|...
gi 925114634 327 EYSIGqVLTVFFS 339
Cdd:cd18544 254 AVTLG-VLYAFIQ 265
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
392-627 |
4.65e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 89.30 E-value: 4.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 392 GNLEFKNVHFSYPSRK--EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDI-----RTIN 464
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 465 VRHLREITGVVSQEP--VLFATTIAENIRYGRENVTMDEiEKAVKEANAYDFIMKLPNKFdtlVGERGAQLSGGQKQRIA 542
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENK-QEAYKKVPELLKLVQLPEDY---VKRSPFELSGGQKRRVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 543 IARALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELMK 619
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFEIFS 240
|
....*...
gi 925114634 620 EKGIYFKL 627
Cdd:PRK13645 241 NQELLTKI 248
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
394-620 |
4.75e-19 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 86.81 E-value: 4.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSypsRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTtvqLMQRL-----YDPTDGMVCIDGQDIR--TINVR 466
Cdd:cd03217 1 LEIKDLHVS---VGGKEILKGVNLTIKKGEVHALMGPNGSGKST---LAKTImghpkYEVTEGEILFKGEDITdlPPEER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 467 HLREITgVVSQEPVLFA-TTIAENIRYGRENvtmdeiekavkeanaydfimklpnkfdtlvgergaqLSGGQKQRIAIAR 545
Cdd:cd03217 75 ARLGIF-LAFQYPPEIPgVKNADFLRYVNEG------------------------------------FSGGEKKRNEILQ 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 546 ALVRNPKILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAH--RLSTVRNADVIAGFDDGVIVEKGNhDELMKE 620
Cdd:cd03217 118 LLLLEPDLAILDEPDSGLDIDAlRLVAEVINKLREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELALE 194
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1046-1280 |
5.65e-19 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 93.69 E-value: 5.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1046 YPTRPDIpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVlidgkeikhlnvqWLRAHLGIVSQEPILF 1125
Cdd:PTZ00243 668 FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1126 DCSIAENIAYGDNSRVVS-HEEIMQAAKEANIhhfiETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEA 1204
Cdd:PTZ00243 734 NATVRGNILFFDEEDAARlADAVRVSQLEADL----AQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1205 TSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGKVKEHGTHQQlLAQKGIYFSMVSVQAGAK 1280
Cdd:PTZ00243 810 LSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSAD-FMRTSLYATLAAELKENK 885
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
394-589 |
6.31e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 87.83 E-value: 6.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHlreitG 473
Cdd:PRK11248 2 LQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQ-EPVLFATTIAENIRYGREnvtMDEIEKAVKEANAYDFIMKlpnkfdtlVGERGA------QLSGGQKQRIAIARA 546
Cdd:PRK11248 74 VVFQnEGLLPWRNVQDNVAFGLQ---LAGVEKMQRLEIAHQMLKK--------VGLEGAekryiwQLSGGQRQRVGIARA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 925114634 547 LVRNPKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAH 589
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1037-1235 |
6.33e-19 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 85.28 E-value: 6.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPTrpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPLAGsvlidGKEIKHLnvqwlRAHLG 1116
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLW-PWGS-----GRIGMPE-----GEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1117 IVSQEPILFDCSIAENIAYgdnsrvvsheeimqaakeanihhfietlPEkyntrvgdkGTQLSGGQKQRIAIARALVRQP 1196
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIY----------------------------PW---------DDVLSGGEQQRLAFARLLLHKP 110
|
170 180 190
....*....|....*....|....*....|....*....
gi 925114634 1197 HILLLDEATSALDTESEKVVQEALDKarEGRTCIVIAHR 1235
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKE--LGITVISVGHR 147
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
713-973 |
6.51e-19 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 88.60 E-value: 6.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 713 FVVGIFCAIINGGLQPAFSIIFSRII--GIFTRDEDPetkrQNSNMFSVLFLVLGIISFITFFLQGFTFGKAGEILTKRL 790
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIddYIVPGQGDL----QGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 791 RYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLgTGIIISLIY-GWQLTLLLLAIVPI 869
Cdd:cd18544 77 RRDLFSHIQRLPLSFFD--RTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLL-IGILIAMFLlNWRLALISLLVLPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 870 IAIAGVVeMKMLSGQALKDKKELEGA--GKIAtEAIENFRTVVSLTREQKFEYMYAQSLQVPYRNSLRKAHIFGVSFSIT 947
Cdd:cd18544 154 LLLATYL-FRKKSRKAYREVREKLSRlnAFLQ-ESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLV 231
|
250 260
....*....|....*....|....*.
gi 925114634 948 QAMMYFSYAGCFRFGAYLVANEFMNF 973
Cdd:cd18544 232 ELLSSLALALVLWYGGGQVLSGAVTL 257
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
394-620 |
7.00e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 88.99 E-value: 7.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRK--EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTI-------- 463
Cdd:PRK13651 3 IKVKNIVKIFNKKLptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 464 ----------------NVRHLREITGVVSQ--EPVLFATTIAENIRYGRENVTMDEiEKAVKEANAYDFIMKLPNKFDtl 525
Cdd:PRK13651 83 vleklviqktrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSK-EEAKKRAAKYIELVGLDESYL-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 526 vgERGA-QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK-GRTTIVIAHRLSTV--RNADVIA 601
Cdd:PRK13651 160 --QRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKqGKTIILVTHDLDNVleWTKRTIF 237
|
250
....*....|....*....
gi 925114634 602 gFDDGVIVEKGNHDELMKE 620
Cdd:PRK13651 238 -FKDGKIIKDGDTYDILSD 255
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1052-1255 |
7.15e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 87.14 E-value: 7.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1052 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQW---LRA-HLGIVSQEPILFDC 1127
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRAkHVGFVFQSFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1128 SIA-ENIAY-----GDNSRvVSHEEIMQAAKEANIHHFIETLPekyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLL 1201
Cdd:PRK10584 103 LNAlENVELpallrGESSR-QSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 1202 DEATSALDTES-EKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVFQNGKVKE 1255
Cdd:PRK10584 171 DEPTGNLDRQTgDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
376-613 |
1.19e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 91.65 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 376 SIDSYSKSGHKPDNIKGNLEFKNVHFSYPSRKEVK-ILKGLNLKVQSGQTVALVGNSGCGKSTtvqLMQRL--YDPTD-- 450
Cdd:TIGR00955 4 SWRNSDVFGRVAQDGSWKQLVSRLRGCFCRERPRKhLLKNVSGVAKPGELLAVMGSSGAGKTT---LMNALafRSPKGvk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 451 --GMVCIDGqdiRTINVRHLREITGVVSQEPVLFAT-TIAENI------RYGReNVTMDEIEKAVKEanaydFI--MKLP 519
Cdd:TIGR00955 81 gsGSVLLNG---MPIDAKEMRAISAYVQQDDLFIPTlTVREHLmfqahlRMPR-RVTKKEKRERVDE-----VLqaLGLR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 520 NKFDTLVGERGAQ--LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQVALDKARKGRTTIVIAHRLStvrn 596
Cdd:TIGR00955 152 KCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYsVVQVLKGLAQKGKTIICTIHQPS---- 227
|
250
....*....|....*..
gi 925114634 597 ADVIAGFDDGVIVEKGN 613
Cdd:TIGR00955 228 SELFELFDKIILMAEGR 244
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
394-558 |
1.37e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 86.62 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRT--INVRHLREI 471
Cdd:COG1137 4 LEAENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpMHKRARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 472 tGVVSQEPVLFAT-TIAENIRYGRENVTMDEIEKAvkeanaydfimklpNKFDTLVGE---------RGAQLSGGQKQRI 541
Cdd:COG1137 81 -GYLPQEASIFRKlTVEDNILAVLELRKLSKKERE--------------ERLEELLEEfgithlrksKAYSLSGGERRRV 145
|
170
....*....|....*..
gi 925114634 542 AIARALVRNPKILLLDE 558
Cdd:COG1137 146 EIARALATNPKFILLDE 162
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
394-589 |
1.43e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 87.94 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTiNVRHLREITG 473
Cdd:PRK13537 8 IDFRNVEKRY---GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQ----EPVLfatTIAENIR-YGRE-NVTMDEIEKAVkeANAYDFiMKLPNKFDTLVGErgaqLSGGQKQRIAIARAL 547
Cdd:PRK13537 84 VVPQfdnlDPDF---TVRENLLvFGRYfGLSAAAARALV--PPLLEF-AKLENKADAKVGE----LSGGMKRRLTLARAL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 925114634 548 VRNPKILLLDEATSALDTESEAVVQVALDK--ARkGRTTIVIAH 589
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSllAR-GKTILLTTH 196
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
394-616 |
1.52e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.89 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVcidgqdIRTINVRhlreiTG 473
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV------KLGETVK-----IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFAT--TIAENIRYGRENVTmdeiekavkEANAYDFIMKL---PNKFDTLVGErgaqLSGGQKQRIAIARALV 548
Cdd:COG0488 382 YFDQHQEELDPdkTVLDELRDGAPGGT---------EQEVRGYLGRFlfsGDDAFKPVGV----LSGGEKARLALAKLLL 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 549 RNPKILLLDEATSALDTESEAVVQVALDkARKGrTTIVIAH-R--LSTVrnADVIAGFDDGVIVEK-GNHDE 616
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREYpGGYDD 516
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1051-1259 |
1.54e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 88.73 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1051 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHlNVQWLRAHLGIVSQepilFD---- 1126
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQ----FDnldl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1127 -CSIAEN-IAYGDNSRVvSHEEImqaakEANIHHFIE--TLPEKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLD 1202
Cdd:PRK13536 128 eFTVRENlLVFGRYFGM-STREI-----EAVIPSLLEfaRLESKADARVSD----LSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 925114634 1203 EATSALDTESEKVVQEALDK--AReGRTCIVIAHRLSTIQN-ADLIVVFQNG-KVKEHGTH 1259
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVLEAGrKIAEGRPH 257
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1051-1253 |
1.85e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 90.94 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1051 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWL----RAHLGIVSQE-PILF 1125
Cdd:PRK10535 20 QVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRyHLLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1126 DCSIAENI----AYGDNSRvvsheeimqAAKEANIHHFIETLpeKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLL 1201
Cdd:PRK10535 100 HLTAAQNVevpaVYAGLER---------KQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 925114634 1202 DEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVFQNGKV 1253
Cdd:PRK10535 169 DEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
408-589 |
2.06e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 85.60 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 408 EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRH---LR-EITGVVSQEPVLFA 483
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRaKHVGFVFQSFMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 484 TTIAenirygRENVTMDEIEKAVKEANAYDFIMKLPNKFDtlVGER----GAQLSGGQKQRIAIARALVRNPKILLLDEA 559
Cdd:PRK10584 102 TLNA------LENVELPALLRGESSRQSRNGAKALLEQLG--LGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190
....*....|....*....|....*....|..
gi 925114634 560 TSALDTES-EAVVQVALDKARKGRTT-IVIAH 589
Cdd:PRK10584 174 TGNLDRQTgDKIADLLFSLNREHGTTlILVTH 205
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
394-620 |
2.57e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 89.97 E-value: 2.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRH-LREIT 472
Cdd:PRK11288 5 LSFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 473 GVVSQE----PVLfatTIAENIRYGRenvtmdeiekavkeanaydfimkLPNKF-----DTLVGERGAQL---------- 533
Cdd:PRK11288 82 AIIYQElhlvPEM---TVAENLYLGQ-----------------------LPHKGgivnrRLLNYEAREQLehlgvdidpd 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 534 ------SGGQKQRIAIARALVRNPKILLLDEATSALDT-ESEAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDD 605
Cdd:PRK11288 136 tplkylSIGQRQMVEIAKALARNARVIAFDEPTSSLSArEIEQLFRVIRELRAEGRVILYVSHRMEEIfALCDAITVFKD 215
|
250 260
....*....|....*....|.
gi 925114634 606 GVIVE------KGNHDELMKE 620
Cdd:PRK11288 216 GRYVAtfddmaQVDRDQLVQA 236
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1055-1280 |
2.64e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 86.22 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1055 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydplagSVLIDGKEIKHLNVQWL-----------------RAHLGI 1117
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHL---------SGLITGDKSAGSHIELLgrtvqregrlardirksRANTGY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1118 VSQEPILFD-CSIAENIAYGDNSRVVSHEEIMQAAKEANIHHFIETLpekynTRVG------DKGTQLSGGQKQRIAIAR 1190
Cdd:PRK09984 91 IFQQFNLVNrLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1191 ALVRQPHILLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLS-TIQNADLIVVFQNGKVKEHGTHQQLLAQK- 1266
Cdd:PRK09984 166 ALMQQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNERf 245
|
250
....*....|....*
gi 925114634 1267 -GIYFSMVSVQAGAK 1280
Cdd:PRK09984 246 dHLYRSINRVEENAK 260
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1053-1258 |
2.91e-18 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 91.61 E-value: 2.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1053 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKhLNVQWLRAHLGIVSQEPILFD-CSIAE 1131
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE-TNLDAVRQSLGMCPQHNILFHhLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1132 NIAYGDNSRVVSHEEI---MQAAKE-ANIHHfietlpeKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSA 1207
Cdd:TIGR01257 1023 HILFYAQLKGRSWEEAqleMEAMLEdTGLHH-------KRNEEAQD----LSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 1208 LDTESEKVVQEALDKAREGRTCIVIAHRLStiqNADL----IVVFQNGKVKEHGT 1258
Cdd:TIGR01257 1092 VDPYSRRSIWDLLLKYRSGRTIIMSTHHMD---EADLlgdrIAIISQGRLYCSGT 1143
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
411-592 |
3.11e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 85.25 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 411 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTIN------VRHlREItGVVSQEPVLFAT 484
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaakaeLRN-QKL-GFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 485 TIAenirygRENVTMDEI--EKAVKEANAYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 562
Cdd:PRK11629 102 FTA------LENVAMPLLigKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190
....*....|....*....|....*....|..
gi 925114634 563 LDTE-SEAVVQVALD-KARKGRTTIVIAHRLS 592
Cdd:PRK11629 176 LDARnADSIFQLLGElNRLQGTAFLVVTHDLQ 207
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1055-1259 |
3.59e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 84.93 E-value: 3.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1055 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLN---VQWLRAHLGIVSQEP-ILFDCSIA 1130
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnreVPFLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1131 ENIAYgdnsrvvshEEIMQAAKEANIHHFIETLPEKyntrVG--DKG----TQLSGGQKQRIAIARALVRQPHILLLDEA 1204
Cdd:PRK10908 98 DNVAI---------PLIIAGASGDDIRRRVSAALDK----VGllDKAknfpIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1205 TSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADL-IVVFQNGKVkeHGTH 1259
Cdd:PRK10908 165 TGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYrMLTLSDGHL--HGGV 219
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1048-1233 |
4.10e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.16 E-value: 4.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1048 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQ-EPILfd 1126
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRNAmKPAL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1127 cSIAENIA-----YGDNSRvvsheEIMQAAKEANIHHfIETLPEKYntrvgdkgtqLSGGQKQRIAIARALVRQPHILLL 1201
Cdd:PRK13539 89 -TVAENLEfwaafLGGEEL-----DIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWIL 151
|
170 180 190
....*....|....*....|....*....|..
gi 925114634 1202 DEATSALDTESEKVVQEALdKAREGRTCIVIA 1233
Cdd:PRK13539 152 DEPTAALDAAAVALFAELI-RAHLAQGGIVIA 182
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
713-996 |
4.43e-18 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 86.30 E-value: 4.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 713 FVVGIFCAIINGGLQPAFSIIFSRIIGIFTRDEDPETKRQNSNMFSVLFLVLGI--ISFITFFLQGFTFGKAGEILTKRL 790
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVDFSGLLRILLLLLGLylLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 791 RYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPII 870
Cdd:cd18547 81 RKDLFEKLQRLPLSYFD--THSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 871 AIAgvveMKMLSGQALKD-KKELEGAGKI---ATEAIENFRTVVSLTRE----QKFEYMYAQslqvpYRNSLRKAHIF-G 941
Cdd:cd18547 159 LLV----TKFIAKRSQKYfRKQQKALGELngyIEEMISGQKVVKAFNREeeaiEEFDEINEE-----LYKASFKAQFYsG 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 942 VSFSITQAMMYFSYAGCFRFGAYLVANefmnfqdvllvfsaivfGAMAVGQVSSF 996
Cdd:cd18547 230 LLMPIMNFINNLGYVLVAVVGGLLVIN-----------------GALTVGVIQAF 267
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1054-1258 |
4.50e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.13 E-value: 4.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKeikhlnVQWLrahLGI-VSQEPILfdcSIAEN 1132
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR------VSAL---LELgAGFHPEL---TGREN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1133 I-----AYGdnsrvVSHEEIMQAAKE----ANIHHFIETlPEKYntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDE 1203
Cdd:COG1134 109 IylngrLLG-----LSRKEIDEKFDEivefAELGDFIDQ-PVKT----------YSSGMRARLAFAVATAVDPDILLVDE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1204 ATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGT 1258
Cdd:COG1134 173 VLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
401-623 |
4.56e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 85.83 E-value: 4.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 401 FSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQ--DIRTINVRHLREITGVVSQE 478
Cdd:PRK13638 9 FRY---QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 479 P--VLFATTIAENIRYGREN--VTMDEIEKAVKEANaydfimklpnkfdTLVGERGAQ------LSGGQKQRIAIARALV 548
Cdd:PRK13638 86 PeqQIFYTDIDSDIAFSLRNlgVPEAEITRRVDEAL-------------TLVDAQHFRhqpiqcLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 549 RNPKILLLDEATSALDTESEA-VVQVALDKARKGRTTIVIAHRLSTV----------RNADVIAGFDDGVIVEKGnhdEL 617
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTqMIAIIRRIVAQGNHVIISSHDIDLIyeisdavyvlRQGQILTHGAPGEVFACT---EA 229
|
....*.
gi 925114634 618 MKEKGI 623
Cdd:PRK13638 230 MEQAGL 235
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1051-1252 |
4.68e-18 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 89.11 E-value: 4.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1051 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY--DPLAGSVLIDGKEIKHLNVQWL-RAHLGIVSQEPILF-D 1126
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1127 CSIAENIAYG-----------DNSRVVSHEEIMQAAKeanihhfietLPEKYNTR-VGDKGtqlsGGQKQRIAIARALVR 1194
Cdd:TIGR02633 93 LSVAENIFLGneitlpggrmaYNAMYLRAKNLLRELQ----------LDADNVTRpVGDYG----GGQQQLVEIAKALNK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1195 QPHILLLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGK 1252
Cdd:TIGR02633 159 QARLLILDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1044-1257 |
4.73e-18 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 84.51 E-value: 4.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1044 FNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKeikhlnVQW-LRAHLGIVSQ-- 1120
Cdd:cd03220 27 GRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------VSSlLGLGGGFNPElt 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1121 --EPILFDCSIaeniaYGdnsrvVSHEEImqAAKEANIHHFIEtLPEKYNTRVGdkgtQLSGGQKQRIAIARALVRQPHI 1198
Cdd:cd03220 101 grENIYLNGRL-----LG-----LSRKEI--DEKIDEIIEFSE-LGDFIDLPVK----TYSSGMKARLAFAIATALEPDI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 925114634 1199 LLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVFQNGKVKEHG 1257
Cdd:cd03220 164 LLIDEVLAVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1035-1265 |
6.29e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.83 E-value: 6.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1035 GNVTFNEVVFNYPTRP--DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDG-------KEIKH 1105
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1106 lnVQWLRAHLGIVSQEP--ILFDCSIAENIAYGDNSRVVSHEEIMQAAKEAnihHFIETLPEKYNTRvgdKGTQLSGGQK 1183
Cdd:PRK13645 85 --VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPEL---LKLVQLPEDYVKR---SPFELSGGQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1184 QRIAIARALVRQPHILLLDEATSALDTESEK---VVQEALDKaREGRTCIVIAHRLSTI-QNADLIVVFQNGKVKEHG-- 1257
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNK-EYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGsp 235
|
250
....*....|..
gi 925114634 1258 ----THQQLLAQ 1265
Cdd:PRK13645 236 feifSNQELLTK 247
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1054-1253 |
6.82e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 85.11 E-value: 6.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP-----LAGSV-LIDGKEIKHLNVQWLRahlgivsqepILFDC 1127
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPsagelLAGTApLAEAREDTRLMFQDAR----------LLPWK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1128 SIAENIAYG--DNSRvvsheeimQAAKEAnihhfIET--LPEkyntRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDE 1203
Cdd:PRK11247 97 KVIDNVGLGlkGQWR--------DAALQA-----LAAvgLAD----RANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 925114634 1204 ATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGKV 1253
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1053-1253 |
8.27e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.15 E-value: 8.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1053 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNV-QWLRAHLGIVS----QEPILFDC 1127
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPrDAIRAGIAYVPedrkGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1128 SIAENI---AYGDNSR--VVSHEEIMQAAKEanihhFIETLpekyNTRVGDKGT---QLSGGQKQRIAIARALVRQPHIL 1199
Cdd:COG1129 346 SIRENItlaSLDRLSRggLLDRRRERALAEE-----YIKRL----RIKTPSPEQpvgNLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 1200 LLDEATSALD--TESE--KVVQEAldkAREGRTCIVIahrlST-----IQNADLIVVFQNGKV 1253
Cdd:COG1129 417 ILDEPTRGIDvgAKAEiyRLIREL---AAEGKAVIVI----SSelpelLGLSDRILVMREGRI 472
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1052-1253 |
1.11e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.80 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1052 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVqwLRAH-LGI--VSQEPILF-DC 1127
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP--AKAHqLGIylVPQEPLLFpNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1128 SIAENIAYGDNSRVVSHEEIMQAAKEANIHHFIETlpekyntrvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1207
Cdd:PRK15439 102 SVKENILFGLPKRQASMQKMKQLLAALGCQLDLDS-----------SAGSLEVADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 925114634 1208 LD-TESEKV---VQEALDKareGRTCIVIAHRLSTI-QNADLIVVFQNGKV 1253
Cdd:PRK15439 171 LTpAETERLfsrIRELLAQ---GVGIVFISHKLPEIrQLADRISVMRDGTI 218
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
756-996 |
1.18e-17 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 84.84 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 756 MFSVLFLVLGIISFITFFLqgftFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRL 835
Cdd:cd18575 41 LLLAVALVLALASALRFYL----VSWLGERVVADLRKAVFAHLLRLSPSFFE--TTRTGEVLSRLTTDTTLIQTVVGSSL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 836 AVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVV---EMKMLSGQAlKDKkeLEGAGKIATEAIENFRTVVSL 912
Cdd:cd18575 115 SIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILfgrRVRRLSRAS-QDR--LADLSAFAEETLSAIKTVQAF 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 913 TREQKFEYMYAQSLQVPYRNSLRKAHIfgvsfsitQAMMYFsyagcfrfgayLVanefmnfqdVLLVFSAIVF------- 985
Cdd:cd18575 192 TREDAERQRFATAVEAAFAAALRRIRA--------RALLTA-----------LV---------IFLVFGAIVFvlwlgah 243
|
250
....*....|....*
gi 925114634 986 ----GAMAVGQVSSF 996
Cdd:cd18575 244 dvlaGRMSAGELSQF 258
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
394-620 |
1.25e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 87.94 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPS--RKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVC-------IDGQDIRTIN 464
Cdd:TIGR03269 280 IKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 465 VRHLREITGVVSQEPVLFA-TTIAENIRygrENVTM---DEI--EKAV--------KEANAYDFIMKLPNkfdtlvgerg 530
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYPhRTVLDNLT---EAIGLelpDELarMKAVitlkmvgfDEEKAEEILDKYPD---------- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 531 aQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTVRN-ADVIAGFDDGV 607
Cdd:TIGR03269 427 -ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGK 505
|
250
....*....|...
gi 925114634 608 IVEKGNHDELMKE 620
Cdd:TIGR03269 506 IVKIGDPEEIVEE 518
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
394-623 |
1.46e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.41 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREItG 473
Cdd:PRK15439 12 LCARSISKQYSG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL-G 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 V--VSQEPVLFAT-TIAENIRYG--RENVTMDEIEKAVKEANAYdfiMKLPNKFDTL-VGERgaqlsggqkQRIAIARAL 547
Cdd:PRK15439 88 IylVPQEPLLFPNlSVKENILFGlpKRQASMQKMKQLLAALGCQ---LDLDSSAGSLeVADR---------QIVEILRGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 548 VRNPKILLLDEATSALD-TESEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELMKEKGI 623
Cdd:PRK15439 156 MRDSRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLSTDDII 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1052-1265 |
1.85e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 87.17 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1052 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSV-------LIDGKEIKHLNVQWLRAHLGIVSQEPIL 1124
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDGRGRAKRYIGILHQEYDL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1125 F-DCSIAENIaygdnSRVVSHEEIMQAAKEANIHHFIET-LPEKYNTRVGDKGT-QLSGGQKQRIAIARALVRQPHILLL 1201
Cdd:TIGR03269 377 YpHRTVLDNL-----TEAIGLELPDELARMKAVITLKMVgFDEEKAEEILDKYPdELSEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1202 DEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQLLAQ 1265
Cdd:TIGR03269 452 DEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1054-1264 |
1.89e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.86 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHlNVQWLRAHLGIVSQ----EPilfDCSI 1129
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVVPQfdnlDP---DFTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1130 AENIaygdnsRVVSHEEIMQAAK-EANIHHFIE--TLPEKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATS 1206
Cdd:PRK13537 98 RENL------LVFGRYFGLSAAAaRALVPPLLEfaKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 925114634 1207 ALDTESEKVVQEALDK--AReGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQLLA 1264
Cdd:PRK13537 168 GLDPQARHLMWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
386-587 |
2.29e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 82.77 E-value: 2.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 386 KPDNIKGNLEfknvHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINV 465
Cdd:cd03267 15 KEPGLIGSLK----SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 466 RHLREITGVVSQEPVL-FATTIAENIRYGRE--NVTMDEIEKAVKEANAydfIMKLPNKFDTLVgergAQLSGGQKQRIA 542
Cdd:cd03267 91 KFLRRIGVVFGQKTQLwWDLPVIDSFYLLAAiyDLPPARFKKRLDELSE---LLDLEELLDTPV----RQLSLGQRMRAE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 925114634 543 IARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVI 587
Cdd:cd03267 164 IAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVL 208
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1055-1262 |
2.57e-17 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 82.42 E-value: 2.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1055 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHlNVQWLRAHLGIVSQEPILFDCSIA-ENI 1133
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDELTGwENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1134 A-----YGdnsrvVSHEEIMQAAKEAniHHFIEtLPEKYNTRVGdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1208
Cdd:cd03265 95 YiharlYG-----VPGAERRERIDEL--LDFVG-LLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1209 DTESEKVVQEALDK--AREGRTCIVIAHRLSTI-QNADLIVVFQNGKVKEHGTHQQL 1262
Cdd:cd03265 163 DPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
415-612 |
2.61e-17 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 88.53 E-value: 2.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 415 LNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTiNVRHLREITGVVSQEPVLFA-TTIAENIRYg 493
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHhLTVAEHILF- 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 494 RENVTMDEIEKAVKEANAYDFIMKLPNKFDtlvgERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQV 573
Cdd:TIGR01257 1027 YAQLKGRSWEEAQLEMEAMLEDTGLHHKRN----EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
|
170 180 190
....*....|....*....|....*....|....*....
gi 925114634 574 ALDKARKGRTTIVIAHRLStvrNADVIAgfDDGVIVEKG 612
Cdd:TIGR01257 1103 LLLKYRSGRTIIMSTHHMD---EADLLG--DRIAIISQG 1136
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1051-1257 |
3.00e-17 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 81.42 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1051 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPLAGSVLIDGKEIKHLNVQwLRAHLGI--VSQEPILFD 1126
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGIflAFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1127 csiaeniaygdnsrvvsheeimqaakEANIHHFIETLPEKyntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATS 1206
Cdd:cd03217 91 --------------------------GVKNADFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 925114634 1207 ALDTESEKVVQEALDKAR-EGRTCIVIAH--RLSTIQNADLIVVFQNGKVKEHG 1257
Cdd:cd03217 134 GLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1057-1262 |
3.50e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 82.73 E-value: 3.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1057 GLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLrAHLGIVS--QEPILF-DCSIAENI 1133
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVRtfQHVRLFrEMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1134 AygdnsrVVSHEEI--------------MQAAKEA--NIHHFIET--LPEKYNTRVGDkgtqLSGGQKQRIAIARALVRQ 1195
Cdd:PRK11300 102 L------VAQHQQLktglfsgllktpafRRAESEAldRAATWLERvgLLEHANRQAGN----LAYGQQRRLEIARCMVTQ 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1196 PHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQL 1262
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
394-621 |
3.57e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 84.50 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTiNVRHLREITG 473
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVL-FATTIAEN-IRYGRE-NVTMDEIEKAVkeANAYDFiMKLPNKFDTLVgergAQLSGGQKQRIAIARALVRN 550
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENlLVFGRYfGMSTREIEAVI--PSLLEF-ARLESKADARV----SDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 551 PKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELMKEK 621
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1053-1258 |
3.83e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 82.44 E-value: 3.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1053 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPILfdcsiaen 1132
Cdd:COG4604 15 VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQENHI-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1133 iaygdNSRV-----VS---------------HEEIMQAakeanIHHF-IETLPEKYNTrvgdkgtQLSGGQKQRIAIARA 1191
Cdd:COG4604 87 -----NSRLtvrelVAfgrfpyskgrltaedREIIDEA-----IAYLdLEDLADRYLD-------ELSGGQRQRAFIAMV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1192 LVRQPHILLLDEATSALD----TESEKVVQEAldkARE-GRTCIVIAHRLstiqN-----ADLIVVFQNGKVKEHGT 1258
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRL---ADElGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQGT 219
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
126-332 |
4.10e-17 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 83.36 E-value: 4.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 126 GVLVAAYIqvSFWCLAAGRQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSK--------INEGIgdkigmffQ 197
Cdd:cd18574 56 SLLTFAYI--SLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEfkssfkqcVSQGL--------R 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 198 SIATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELE 277
Cdd:cd18574 126 SVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELE 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 278 RYNKNLEEAKR--------IGIKKAITaNISIGAAFLLIYasyalafWYGTSLVLSSEYSIGQ 332
Cdd:cd18574 206 LYEEEVEKAAKlneklglgIGIFQGLS-NLALNGIVLGVL-------YYGGSLVSRGELTAGD 260
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
749-971 |
4.35e-17 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 83.13 E-value: 4.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 749 TKRQNSNMFSVLFLVLGIISFITFFLQG-----FTFGKAGeiLTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLAND 823
Cdd:cd18784 27 VIEKSQDKFSRAIIIMGLLAIASSVAAGirgglFTLAMAR--LNIRIRNLLFRSIVSQEIGFFD--TVKTGDITSRLTSD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 824 AAQVKGAIGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGAGKIATEAI 903
Cdd:cd18784 103 TTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETI 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 904 ENFRTVVSLTREQKFEYMYAQSLQVPYRNSLRKAHIFGvSFSITQAMMYFS-YAGCFRFGAYLVANEFM 971
Cdd:cd18784 183 SSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYG-GYVWSNELTELAlTVSTLYYGGHLVITGQI 250
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
394-589 |
4.50e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 79.41 E-value: 4.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVcidgQDIRTINVRHLreitg 473
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----TWGSTVKIGYF----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 vvsqepvlfattiaenirygrenvtmdeiekavkeanaydfimklpnkfdtlvgergAQLSGGQKQRIAIARALVRNPKI 553
Cdd:cd03221 69 ---------------------------------------------------------EQLSGGEKMRLALAKLLLENPNL 91
|
170 180 190
....*....|....*....|....*....|....*.
gi 925114634 554 LLLDEATSALDTESEAVVQVALdKARKGrTTIVIAH 589
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSH 125
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
149-339 |
5.00e-17 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 83.33 E-value: 5.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 149 IRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSIATFFTGFIVGFTRGWKLTLVILAISPVLG 228
Cdd:cd18563 78 LRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 229 -LSAAIWAKILSSFTdKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLL 307
Cdd:cd18563 158 wGSYFFWKKIRRLFH-RQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFL 236
|
170 180 190
....*....|....*....|....*....|..
gi 925114634 308 IYASYALAFWYGTSLVLSSEYSIGqVLTVFFS 339
Cdd:cd18563 237 TSLGTLIVWYFGGRQVLSGTMTLG-TLVAFLS 267
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1054-1220 |
6.09e-17 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 80.61 E-value: 6.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPILFDCSIAENI 1133
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1134 AY--GDNSRvvshEEIMQAAKEANIHHFiETLPekyntrvgdkGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1211
Cdd:cd03231 95 RFwhADHSD----EQVEEALARVGLNGF-EDRP----------VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
....*....
gi 925114634 1212 SEKVVQEAL 1220
Cdd:cd03231 160 GVARFAEAM 168
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1054-1263 |
7.38e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.96 E-value: 7.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPIL-FDCSIAEN 1132
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1133 IAYG--------DNSRVVSHEEIMQAAKEANIHHFietlpekyntrVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEA 1204
Cdd:PRK10253 102 VARGryphqplfTRWRKEDEEAVTKAMQATGITHL-----------ADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 1205 TSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGKVKEHGTHQQLL 1263
Cdd:PRK10253 171 TTWLDISHQIDLLELLSElnREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1037-1252 |
8.44e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 78.64 E-value: 8.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLErfydplagsvlidGKeikhlnvqwLRAHLG 1116
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIA-------------GE---------LEPDEG 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1117 IVSQepilfdcsiaeniaygdnsrvvsheeimqaAKEANIHHFietlpekyntrvgdkgTQLSGGQKQRIAIARALVRQP 1196
Cdd:cd03221 56 IVTW------------------------------GSTVKIGYF----------------EQLSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1197 HILLLDEATSALDTESEKVVQEALdKAREGrTCIVIAHRLSTIQN-ADLIVVFQNGK 1252
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
394-612 |
1.15e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 85.29 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSR--------KEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTIN- 464
Cdd:PRK10261 314 LQVRNLVTRFPLRsgllnrvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSp 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 465 --VRHLREITGVVSQEPvlFAT---------TIAENIRY--------GRENVTMDEIEKAVKEANAYDFimklPNKFdtl 525
Cdd:PRK10261 394 gkLQALRRDIQFIFQDP--YASldprqtvgdSIMEPLRVhgllpgkaAAARVAWLLERVGLLPEHAWRY----PHEF--- 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 526 vgergaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQVALDKARK-GRTTIVIAHRLSTV-RNADVIAG 602
Cdd:PRK10261 465 --------SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGqIINLLLDLQRDfGIAYLFISHDMAVVeRISHRVAV 536
|
250
....*....|
gi 925114634 603 FDDGVIVEKG 612
Cdd:PRK10261 537 MYLGQIVEIG 546
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
411-618 |
1.27e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.57 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 411 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITGVVSQEPVLFA-TTIAEN 489
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGdITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 490 IRYGRE------NVTMDEIEKAVKEANAYDFIMKLPNK-FDTlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSA 562
Cdd:PRK10253 102 VARGRYphqplfTRWRKEDEEAVTKAMQATGITHLADQsVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 563 LDTESEA-VVQVALDKAR-KGRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKGNHDELM 618
Cdd:PRK10253 174 LDISHQIdLLELLSELNReKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1057-1262 |
1.32e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 82.45 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1057 GLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLN-VQWL--RAHLGIVSQEPILF---DCSIA 1130
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKdDEWRavRSDIQMIFQDPLASlnpRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1131 ENIA------YGDNSRvvshEEIMQAAKEANIHhfIETLPEKYNTRvgdkGTQLSGGQKQRIAIARALVRQPHILLLDEA 1204
Cdd:PRK15079 119 EIIAeplrtyHPKLSR----QEVKDRVKAMMLK--VGLLPNLINRY----PHEFSGGQCQRIGIARALILEPKLIICDEP 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 925114634 1205 TSALDTESE-KVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQL 1262
Cdd:PRK15079 189 VSALDVSIQaQVVNLLQQLQREmGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
397-619 |
1.83e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.99 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 397 KNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHL-REITGVV 475
Cdd:PRK10575 15 RNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFaRKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 476 SQEPVLFATTIAENI------------RYGRENvtMDEIEKAVKEANAYDFIMKLPNkfdtlvgergaQLSGGQKQRIAI 543
Cdd:PRK10575 92 QQLPAAEGMTVRELVaigrypwhgalgRFGAAD--REKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 544 ARALVRNPKILLLDEATSALD----TESEAVVQvALDKARkGRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKGNHDELM 618
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDiahqVDVLALVH-RLSQER-GLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELM 236
|
.
gi 925114634 619 K 619
Cdd:PRK10575 237 R 237
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1048-1255 |
1.96e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 84.07 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1048 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdP---LAGSVLIDGKEIKHLNvqwLRA--HLGIV--SQ 1120
Cdd:NF040905 10 TFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PhgsYEGEILFDGEVCRFKD---IRDseALGIViiHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1121 E----PILfdcSIAENIAYGdNSR----VVSHEEIMQAAKEanihhFIET--LPEKYNTRVGDKGTqlsgGQKQRIAIAR 1190
Cdd:NF040905 86 ElaliPYL---SIAENIFLG-NERakrgVIDWNETNRRARE-----LLAKvgLDESPDTLVTDIGV----GKQQLVEIAK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1191 ALVRQPHILLLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVFQNGKVKE 1255
Cdd:NF040905 153 ALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1049-1233 |
2.01e-16 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 78.94 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1049 RPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQEPILFDCS 1128
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1129 IAENIAY-----GDNSRVVSheeimQAAKEANIHHFiETLPekyntrvgdkGTQLSGGQKQRIAIARALVRQPHILLLDE 1203
Cdd:TIGR01189 90 ALENLHFwaaihGGAQRTIE-----DALAAVGLTGF-EDLP----------AAQLSAGQQRRLALARLWLSRRPLWILDE 153
|
170 180 190
....*....|....*....|....*....|
gi 925114634 1204 ATSALDTESEKVVQEALDkAREGRTCIVIA 1233
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLR-AHLARGGIVLL 182
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1037-1268 |
2.40e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 79.92 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPtrpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHL-NVQWLRAHL 1115
Cdd:PRK11614 6 LSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1116 GIVSQEPILFD-CSIAENIAYGdnSRVVSHEEIMQaakeaNIHHFIETLPEKYNTRVGDKGTqLSGGQKQRIAIARALVR 1194
Cdd:PRK11614 83 AIVPEGRRVFSrMTVEENLAMG--GFFAERDQFQE-----RIKWVYELFPRLHERRIQRAGT-MSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 1195 QPHILLLDEATSALdteSEKVVQEALDKAR----EGRTCIVIAHRLS-TIQNADLIVVFQNGKVKEHGTHQQLLAQKGI 1268
Cdd:PRK11614 155 QPRLLLLDEPSLGL---APIIIQQIFDTIEqlreQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
122-339 |
2.88e-16 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 80.91 E-value: 2.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 122 GIGAGVLVAAYIQvSFWCLAAGRQILK-IRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSIA 200
Cdd:cd18547 53 GLYLLSALFSYLQ-NRLMARVSQRTVYdLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSIL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 201 TFFTGFIVGFTRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYN 280
Cdd:cd18547 132 TIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFD 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 281 KNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTSLVLSSEYSIGqVLTVFFS 339
Cdd:cd18547 212 EINEELYKASFKAQFYSGLLMPIMNFINNLGYVLVAVVGGLLVINGALTVG-VIQAFLQ 269
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
406-588 |
2.96e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.76 E-value: 2.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 406 RKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLreITGVVSQEPVLFATT 485
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA--CHYLGHRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 486 IAENIR-----YGRENVTMDEIEKAVKEANAYDfimkLPNKFdtlvgergaqLSGGQKQRIAIARALVRNPKILLLDEAT 560
Cdd:PRK13539 90 VAENLEfwaafLGGEELDIAAALEAVGLAPLAH----LPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPT 155
|
170 180
....*....|....*....|....*...
gi 925114634 561 SALDTESEAVVQvALDKARKGRTTIVIA 588
Cdd:PRK13539 156 AALDAAAVALFA-ELIRAHLAQGGIVIA 182
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1023-1265 |
3.09e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 83.48 E-value: 3.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1023 YSPHGLKPNTLEG--NVTFNEVVFNYPTR-----PdipvlqgLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGS 1095
Cdd:PRK10522 307 YKAEFPRPQAFPDwqTLELRNVTFAYQDNgfsvgP-------INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1096 VLIDGKEIKHLNVQWLRAHLGIVSQEPILFDcsiaeniaygdnsRVVSHEEimQAAKEANIHHFIETLPEKYNTRVGD-- 1173
Cdd:PRK10522 380 ILLDGKPVTAEQPEDYRKLFSAVFTDFHLFD-------------QLLGPEG--KPANPALVEKWLERLKMAHKLELEDgr 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1174 -KGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVV-QEALDKARE-GRTCIVIAHRLSTIQNADLIVVFQN 1250
Cdd:PRK10522 445 iSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFyQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRN 524
|
250
....*....|....*.
gi 925114634 1251 GKVKE-HGTHQQLLAQ 1265
Cdd:PRK10522 525 GQLSElTGEERDAASR 540
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
394-620 |
3.66e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 79.36 E-value: 3.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYP-------------------SRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVC 454
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 455 IDGqdirtiNVRHLREITGVVSQEpvlfaTTIAENIR-----YGrenVTMDEIEKAVKEANAY----DFImklpnkfDTL 525
Cdd:COG1134 85 VNG------RVSALLELGAGFHPE-----LTGRENIYlngrlLG---LSRKEIDEKFDEIVEFaelgDFI-------DQP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 526 VGergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE----SEAVVQvalDKARKGRTTIVIAHRLSTVRN-ADVI 600
Cdd:COG1134 144 VK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIR---ELRESGRTVIFVSHSMGAVRRlCDRA 216
|
250 260
....*....|....*....|
gi 925114634 601 AGFDDGVIVEKGNHDELMKE 620
Cdd:COG1134 217 IWLEKGRLVMDGDPEEVIAA 236
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1049-1262 |
4.80e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 83.37 E-value: 4.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1049 RPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSV-------------LIDGKEIKHLNVQWLR-AH 1114
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQSAAQMRHVRgAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1115 LGIVSQEPI-----LFDC--SIAENIAYGDNsrvVSHEEIMQAAKEanihhFIET--LPEKyNTRVGDKGTQLSGGQKQR 1185
Cdd:PRK10261 106 MAMIFQEPMtslnpVFTVgeQIAESIRLHQG---ASREEAMVEAKR-----MLDQvrIPEA-QTILSRYPHQLSGGMRQR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1186 IAIARALVRQPHILLLDEATSALDTESE-------KVVQEALDKAregrtCIVIAHRLSTIQN-ADLIVVFQNGKVKEHG 1257
Cdd:PRK10261 177 VMIAMALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMSMG-----VIFITHDMGVVAEiADRVLVMYQGEAVETG 251
|
....*
gi 925114634 1258 THQQL 1262
Cdd:PRK10261 252 SVEQI 256
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
394-610 |
7.38e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 82.14 E-value: 7.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTtvqLMQRL-----YDPTDGMVCIDGQdirtinVRHL 468
Cdd:NF040905 2 LEMRGITKTFPG---VKALDDVNLSVREGEIHALCGENGAGKST---LMKVLsgvypHGSYEGEILFDGE------VCRF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 469 REIT-----GVV--SQE----PVLfatTIAENIRYGRENVTMDEI--EKAVKEANAYDFIMKLPNKFDTLVGERGAqlsg 535
Cdd:NF040905 70 KDIRdsealGIViiHQElaliPYL---SIAENIFLGNERAKRGVIdwNETNRRARELLAKVGLDESPDTLVTDIGV---- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 536 GQKQRIAIARALVRNPKILLLDEATSAL-DTESEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVE 610
Cdd:NF040905 143 GKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
138-335 |
7.49e-16 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 79.44 E-value: 7.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 138 WCLAAGRQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSIATFFTGFIVGFTRGWKLT 217
Cdd:cd18589 60 YNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 218 LVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITA 297
Cdd:cd18589 140 LLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAY 219
|
170 180 190
....*....|....*....|....*....|....*...
gi 925114634 298 NISIGAAFLLIYASYALAFWYGTSLVLSSEYSIGQVLT 335
Cdd:cd18589 220 AVSMWTSSFSGLALKVGILYYGGQLVTAGTVSSGDLVT 257
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1043-1257 |
8.12e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.60 E-value: 8.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1043 VFNYPTRpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLN---VQWLRAHLGIVS 1119
Cdd:PRK10261 329 LLNRVTR-EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIF 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1120 QEPILfDCSIAENIAYGDNSRVVSHEEIMQAAKEANIHHFIEtlpekyntRVGDKGT-------QLSGGQKQRIAIARAL 1192
Cdd:PRK10261 408 QDPYA-SLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLE--------RVGLLPEhawryphEFSGGQRQRICIARAL 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 1193 VRQPHILLLDEATSALDTE-SEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHG 1257
Cdd:PRK10261 479 ALNPKVIIADEAVSALDVSiRGQIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1044-1264 |
8.41e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 79.06 E-value: 8.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1044 FNYPT----RPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVS 1119
Cdd:PRK15112 14 FRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1120 QEPI-----------LFDCSIAENIAYGDNSRvvsHEEIMQAAKEANIhhfietLPEKYNTRvgdkGTQLSGGQKQRIAI 1188
Cdd:PRK15112 94 QDPStslnprqrisqILDFPLRLNTDLEPEQR---EKQIIETLRQVGL------LPDHASYY----PHMLAPGQKQRLGL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 1189 ARALVRQPHILLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQLLA 1264
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLA 239
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
394-606 |
8.69e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 81.79 E-value: 8.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLY--DPTDGMVCIDGQDIRTINVRHlREI 471
Cdd:TIGR02633 2 LEMKGIVKTFGG---VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRD-TER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 472 TGVV--SQEPVLFAT-TIAENIRYGRE----NVTMDEIEkAVKEANAYDFIMKLPNKFDTL-VGERGaqlsGGQKQRIAI 543
Cdd:TIGR02633 78 AGIViiHQELTLVPElSVAENIFLGNEitlpGGRMAYNA-MYLRAKNLLRELQLDADNVTRpVGDYG----GGQQQLVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 544 ARALVRNPKILLLDEATSAL-DTESEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDG 606
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1049-1263 |
9.17e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 82.40 E-value: 9.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1049 RPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLErFYDP----LAGSVLIDGKEIkhlNVQWLRAHLGIVSQEPIL 1124
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPkgvkGSGSVLLNGMPI---DAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1125 FDCSIA-ENIAYgdNSRVVSHEEIMQAAKEANIHHFIE--TLPEKYNTRVGDKGTQ--LSGGQKQRIAIARALVRQPHIL 1199
Cdd:TIGR00955 111 IPTLTVrEHLMF--QAHLRMPRRVTKKEKRERVDEVLQalGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1200 LLDEATSALDTES-EKVVQEALDKAREGRTCIVIAHRLST--IQNADLIVVFQNGKVKEHGTHQQLL 1263
Cdd:TIGR00955 189 FCDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
713-968 |
1.03e-15 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 79.38 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 713 FVVGIFCAIINGGLQpafsIIFSRIIGIFTRD-EDPETKRQNSNMFSVLFLVLGIISFITFFLQGFTFGKAGEILTKRLR 791
Cdd:cd18541 1 YLLGILFLILVDLLQ----LLIPRIIGRAIDAlTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 792 YMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIA 871
Cdd:cd18541 77 NDLFAHLLTLSPSFYQ--KNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 872 IAGVVEMKMLSGQALKDKKELegaGKIATEAIENF---RTVVSLTREQKFEYMYAQSLQVPYRNSLRKAHIFGVSFSITQ 948
Cdd:cd18541 155 LLVYRLGKKIHKRFRKVQEAF---SDLSDRVQESFsgiRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIG 231
|
250 260
....*....|....*....|
gi 925114634 949 AMMYFSYAGCFRFGAYLVAN 968
Cdd:cd18541 232 LLIGLSFLIVLWYGGRLVIR 251
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
411-617 |
1.26e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 78.60 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 411 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGM-----VCIDGQDIRTI-NVRHLREITGVVSQEPVLFAT 484
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 485 TIAENIRYG-RENVTMDEIE-KAVKEANAYDfiMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 562
Cdd:PRK14271 116 SIMDNVLAGvRAHKLVPRKEfRGVAQARLTE--VGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 563 LDTESEAVVQVALDKARKGRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKGNHDEL 617
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1051-1264 |
1.32e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 81.39 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1051 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPLAGSVlidgkeIKHLNVQWLRAHLGIVS--------- 1119
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRI------IYHVALCEKCGYVERPSkvgepcpvc 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1120 ------QEPILFDCS------IAENIA---------YGDNSRVV----SHEEIMQAAKEAnIHHFIETLPE-KYNTRVGD 1173
Cdd:TIGR03269 86 ggtlepEEVDFWNLSdklrrrIRKRIAimlqrtfalYGDDTVLDnvleALEEIGYEGKEA-VGRAVDLIEMvQLSHRITH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1174 KGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKA--REGRTCIVIAHRLSTIQN-ADLIVVFQN 1250
Cdd:TIGR03269 165 IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDKAIWLEN 244
|
250
....*....|....
gi 925114634 1251 GKVKEHGTHQQLLA 1264
Cdd:TIGR03269 245 GEIKEEGTPDEVVA 258
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
395-625 |
1.36e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 82.46 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 395 EFKNVHFSYPSRKEVK-ILKGLNLKVQSGQTVALVGNSGCGKSTtvqLMQRLYDPTDGMVCIDGqdIRTINVRHLRE--- 470
Cdd:TIGR00956 761 HWRNLTYEVKIKKEKRvILNNVDGWVKPGTLTALMGASGAGKTT---LLNVLAERVTTGVITGG--DRLVNGRPLDSsfq 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 471 -ITGVVSQEPVLFAT-TIAENIRYGRENVTMDEIEKavKEANAY-DFIMKL---PNKFDTLVGERGAQLSGGQKQRIAIA 544
Cdd:TIGR00956 836 rSIGYVQQQDLHLPTsTVRESLRFSAYLRQPKSVSK--SEKMEYvEEVIKLlemESYADAVVGVPGEGLNVEQRKRLTIG 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 545 RALVRNPKILL-LDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLStvrnADVIAGFDDGVIVEKGNhdelmkeKG 622
Cdd:TIGR00956 914 VELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKlADHGQAILCTIHQPS----AILFEEFDRLLLLQKGG-------QT 982
|
...
gi 925114634 623 IYF 625
Cdd:TIGR00956 983 VYF 985
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
394-594 |
1.40e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 77.22 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDI---RTINVRHLRE 470
Cdd:PRK10908 2 IRFEHVSKAYLGGRQA--LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 471 ITGVVSQE---------------PVLFATTIAENIRYgRENVTMDEIEKAVKEANaydfimkLPnkfdtlvgergAQLSG 535
Cdd:PRK10908 80 QIGMIFQDhhllmdrtvydnvaiPLIIAGASGDDIRR-RVSAALDKVGLLDKAKN-------FP-----------IQLSG 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 536 GQKQRIAIARALVRNPKILLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIAHRLSTV 594
Cdd:PRK10908 141 GEQQRVGIARAVVNKPAVLLADEPTGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLI 200
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
394-641 |
1.59e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 81.39 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRL--YDPTDGMV------CIDGQ--DIRTI 463
Cdd:TIGR03269 1 IEVKNLTKKF---DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalCEKCGyvERPSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 464 NVRHLREITGVVSQEPVLF---ATTIAENIR-------------YGRENV------TMDEIEKAVKEA--NAYDFI--MK 517
Cdd:TIGR03269 78 VGEPCPVCGGTLEPEEVDFwnlSDKLRRRIRkriaimlqrtfalYGDDTVldnvleALEEIGYEGKEAvgRAVDLIemVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 518 LPNKFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTVR 595
Cdd:TIGR03269 158 LSHRITHIARD----LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWPEVIE 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 925114634 596 N-ADVIAGFDDGVIVEKGNHDELMKekgIYFKLVTMQTRGNEIELEN 641
Cdd:TIGR03269 234 DlSDKAIWLENGEIKEEGTPDEVVA---VFMEGVSEVEKECEVEVGE 277
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1050-1252 |
1.70e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.82 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1050 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNV-QWLRAHLGIVSQEPILFD-C 1127
Cdd:PRK10762 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPkSSQEAGIGIIHQELNLIPqL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1128 SIAENIAYG----------DNSRVvsHEEIMQAAKEANIHHfietlpeKYNTRVGDkgtqLSGGQKQRIAIARALVRQPH 1197
Cdd:PRK10762 95 TIAENIFLGrefvnrfgriDWKKM--YAEADKLLARLNLRF-------SSDKLVGE----LSIGEQQMVEIAKVLSFESK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1198 ILLLDEATSAL-DTESE---KVVQEALDkarEGRTCIVIAHRLSTI-QNADLIVVFQNGK 1252
Cdd:PRK10762 162 VIIMDEPTDALtDTETEslfRVIRELKS---QGRGIVYISHRLKEIfEICDDVTVFRDGQ 218
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
769-949 |
1.73e-15 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 78.74 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 769 FITFFLQG-FTF------GKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSrlaVITQN 841
Cdd:cd18574 49 LGLYLLQSlLTFayisllSVVGERVAARLRNDLFSSLLRQDIAFFD--THRTGELVNRLTADVQEFKSSFKQ---CVSQG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 842 IANLG--TGIIISLIY-GWQLTLLLLAIVPIIAIAGVV---EMKMLSGQAlkdKKELEGAGKIATEAIENFRTVVSLTRE 915
Cdd:cd18574 124 LRSVTqtVGCVVSLYLiSPKLTLLLLVIVPVVVLVGTLygsFLRKLSRRA---QAQVAKATGVADEALGNIRTVRAFAME 200
|
170 180 190
....*....|....*....|....*....|....
gi 925114634 916 QKFEYMYAQSLQvpyrNSLRKAHIFGVSFSITQA 949
Cdd:cd18574 201 DRELELYEEEVE----KAAKLNEKLGLGIGIFQG 230
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
381-612 |
1.75e-15 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 77.19 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 381 SKSGHKPDNIKGNLEFKNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQdi 460
Cdd:cd03220 7 SKSYPTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 461 rtinvrhlreitgvVSqePVLFATTIAENIRYGRENVTM---------DEIEKavKEANAYDFiMKLPNKFDTLVGErga 531
Cdd:cd03220 85 --------------VS--SLLGLGGGFNPELTGRENIYLngrllglsrKEIDE--KIDEIIEF-SELGDFIDLPVKT--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 532 qLSGGQKQRIAIARALVRNPKILLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIV 609
Cdd:cd03220 143 -YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIR 221
|
...
gi 925114634 610 EKG 612
Cdd:cd03220 222 FDG 224
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
394-618 |
3.15e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 77.14 E-value: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVH--FSYPS----RKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDG---------- 457
Cdd:PRK15112 5 LEVRNLSktFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 458 --QDIRTI-----NVRHLREITGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFImklpnkfdtlvgerg 530
Cdd:PRK15112 85 rsQRIRMIfqdpsTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHM--------------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 531 aqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQVALD-KARKGRTTIVIAHRLSTVRN-ADVIAGFDDGV 607
Cdd:PRK15112 150 --LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSqLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGE 227
|
250
....*....|.
gi 925114634 608 IVEKGNHDELM 618
Cdd:PRK15112 228 VVERGSTADVL 238
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
736-950 |
3.38e-15 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 77.76 E-value: 3.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 736 RIIGIFTRDEDPetkrqNSNMFSVLFLvlGIISFITFFLQG-----FTFgkAGEILTKRLRYMVFRSMLRQDVSWFDdpK 810
Cdd:cd18590 21 RVIDILGGEYQH-----NAFTSAIGLM--CLFSLGSSLSAGlrgglFMC--TLSRLNLRLRHQLFSSLVQQDIGFFE--K 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 811 NTTGALTTRLANDAAQVKGAIGSRLAVITQN-IANLGT-GIIISLiyGWQLTLLLLAIVPIIAIAGVV----EMKMLsgQ 884
Cdd:cd18590 90 TKTGDLTSRLSTDTTLMSRSVALNANVLLRSlVKTLGMlGFMLSL--SWQLTLLTLIEMPLTAIAQKVyntyHQKLS--Q 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 885 ALKDKkeLEGAGKIATEAIENFRTVVSLTREQKFEYMYAQSLQVPYRNSLRKAHIFGVSFSITQAM 950
Cdd:cd18590 166 AVQDS--IAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVL 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1053-1253 |
3.59e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.07 E-value: 3.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1053 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERfyDPLAGSVLIDGKEIKHLNVQWLRAH-LGIVSQEP-----IL 1124
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPRERRRLgVAYIPEDRlgrglVP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1125 fDCSIAENIA--YGDNSRVVSHEEIMQAAkeanIHHFIETLPEKYNTRVGDKGT---QLSGGQKQRIAIARALVRQPHIL 1199
Cdd:COG3845 350 -DMSVAENLIlgRYRRPPFSRGGFLDRKA----IRAFAEELIEEFDVRTPGPDTparSLSGGNQQKVILARELSRDPKLL 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 1200 LLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQN-ADLIVVFQNGKV 1253
Cdd:COG3845 425 IAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEGRI 480
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1048-1262 |
4.26e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 77.11 E-value: 4.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1048 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWL---RAHLGIVSQEPIL 1124
Cdd:PRK11831 16 TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1125 F-DCSIAENIAYG--DNSRV---VSHEEIMQAAKEANIHHFIETLPekyntrvgdkgTQLSGGQKQRIAIARALVRQPHI 1198
Cdd:PRK11831 96 FtDMNVFDNVAYPlrEHTQLpapLLHSTVMMKLEAVGLRGAAKLMP-----------SELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1199 LLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQL 1262
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
405-569 |
6.50e-15 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 74.84 E-value: 6.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 405 SRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITGVVSQEPVLFAT 484
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 485 TIAENIRYGRENVTMDEIEKAVKEANAydfimklpNKFDTLVGergAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 564
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEALARVGL--------NGFEDRPV---AQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
....*
gi 925114634 565 TESEA 569
Cdd:cd03231 158 KAGVA 162
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1051-1258 |
6.74e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 75.83 E-value: 6.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1051 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPLAGSVLIDGKEIKHLNVQwLRAHLGI----------- 1117
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIflafqypieip 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1118 -VSQEPILfdcsiaeNIAYgdNSRVVSheeimQAAKEANIHHFIETLPEKYNTrVGDKGTQL--------SGGQKQRIAI 1188
Cdd:CHL00131 98 gVSNADFL-------RLAY--NSKRKF-----QGLPELDPLEFLEIINEKLKL-VGMDPSFLsrnvnegfSGGEKKRNEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 1189 ARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIV-IAH--RLSTIQNADLIVVFQNGKVKEHGT 1258
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
394-564 |
8.92e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 75.32 E-value: 8.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIR--TINVRHLREI 471
Cdd:PRK10895 4 LTAKNLAKAYKGRR---VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 472 tGVVSQEPVLFAT-TIAENIrygrenVTMDEIEKAVKEANAYDFIMKLPNKFDT--LVGERGAQLSGGQKQRIAIARALV 548
Cdd:PRK10895 81 -GYLPQEASIFRRlSVYDNL------MAVLQIRDDLSAEQREDRANELMEEFHIehLRDSMGQSLSGGERRRVEIARALA 153
|
170
....*....|....*.
gi 925114634 549 RNPKILLLDEATSALD 564
Cdd:PRK10895 154 ANPKFILLDEPFAGVD 169
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
398-617 |
9.30e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.13 E-value: 9.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 398 NVHFSYpSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQ----------DIRTINVRH 467
Cdd:PRK10261 19 NIAFMQ-EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 468 LREITG----VVSQEPV-----LFAT--TIAENIR----YGREnvtmdeieKAVKEANAYDFIMKLPNKfDTLVGERGAQ 532
Cdd:PRK10261 98 MRHVRGadmaMIFQEPMtslnpVFTVgeQIAESIRlhqgASRE--------EAMVEAKRMLDQVRIPEA-QTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 533 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA----VVQVALDKARKGrtTIVIAHRLSTVRN-ADVIAGFDDGV 607
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAqilqLIKVLQKEMSMG--VIFITHDMGVVAEiADRVLVMYQGE 246
|
250
....*....|
gi 925114634 608 IVEKGNHDEL 617
Cdd:PRK10261 247 AVETGSVEQI 256
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
415-620 |
9.50e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 75.35 E-value: 9.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 415 LNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYdPTDGMVCIDGQDIRTINVRHLREITGVVSQE-PVLFATTIAENI-RY 492
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVFQYLtLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 493 GRENVTMDEIEKAVKE-ANAydfiMKLPNKFDTLVGergaQLSGGQKQRIAIARALVR-----NP--KILLLDEATSALD 564
Cdd:PRK03695 94 QPDKTRTEAVASALNEvAEA----LGLDDKLGRSVN----QLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNSLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 565 TESeavvQVALDK-----ARKGRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKGNHDELMKE 620
Cdd:PRK03695 166 VAQ----QAALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTP 223
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
123-345 |
1.04e-14 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 76.33 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 123 IGAGVLVAAYIQVSFwclAAGRQIL----------KIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDdVSKINEGIGDKI 192
Cdd:cd18570 44 ISIGLILLYLFQSLL---SYIRSYLllklsqkldiRLILGYFKHLLKLPLSFFETRKTGEIISRFND-ANKIREAISSTT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 193 GMFFQSIATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQ 272
Cdd:cd18570 120 ISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAE 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 273 KKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTSLVLSSEYSIGQVLTvfFSVLIGAF 345
Cdd:cd18570 200 EQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQLSLGQLIA--FNALLGYF 270
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
394-617 |
1.16e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.59 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKEVK-ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYdPT------DGMVCIDGQDIRTINVR 466
Cdd:PRK15134 6 LAIENLSVAFRQQQTVRtVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 467 HLREITG----VVSQEPVlfattIAENirygrenvTMDEIEKAVKEANAYDFIM-KLPNKFDTL-----VGERGA----- 531
Cdd:PRK15134 85 TLRGVRGnkiaMIFQEPM-----VSLN--------PLHTLEKQLYEVLSLHRGMrREAARGEILncldrVGIRQAakrlt 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 532 ----QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTVRN-ADVIAGFD 604
Cdd:PRK15134 152 dyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQ 231
|
250
....*....|...
gi 925114634 605 DGVIVEKGNHDEL 617
Cdd:PRK15134 232 NGRCVEQNRAATL 244
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1055-1263 |
1.50e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 74.96 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1055 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWL----RAHL-----GIVSQEP--- 1122
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaeRRRLlrtewGFVHQHPrdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1123 ILFDCSIAENI-----AYGDNSrvvsHEEIMQAAKeanihHFIETLpEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPH 1197
Cdd:PRK11701 102 LRMQVSAGGNIgerlmAVGARH----YGDIRATAG-----DWLERV-EIDAARIDDLPTTFSGGMQQRLQIARNLVTHPR 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 1198 ILLLDEATSALDTEsekvVQ-EALDKARE-----GRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQLL 1263
Cdd:PRK11701 172 LVFMDEPTGGLDVS----VQaRLLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTDQVL 240
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
93-355 |
2.16e-14 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 75.13 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 93 IINESITNNTQHFINHLEEEMTTYAY--YYSGIGAGVLvAAYIQVSFwclaaGRQIlkiRKQFFHAIMRqeigwFDVHDV 170
Cdd:cd18548 25 IIDEGIANGDLSYILRTGLLMLLLALlgLIAGILAGYF-AAKASQGF-----GRDL---RKDLFEKIQS-----FSFAEI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 171 GE-----LNTRLTDDVSKINEGIGDKIGMFFQSIATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKE 245
Cdd:cd18548 91 DKfgtssLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 246 LLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTSLVLS 325
Cdd:cd18548 171 QKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINA 250
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 925114634 326 SEYSIGQV-------LTVFFSVLIGAF---SIGQASPSIE 355
Cdd:cd18548 251 GSLQVGDLvafinylMQILMSLMMLSMvfvMLPRASASAK 290
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
389-612 |
3.01e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.13 E-value: 3.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 389 NIKGNLEFKNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHL 468
Cdd:PRK09700 1 MATPYISMAGIGKSFGP---VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 469 REI-TGVVSQE-PVLFATTIAENIRYGRE------NVTMDEIEKAVKEANAYDFIMKLPNKFDTLVGErgaqLSGGQKQR 540
Cdd:PRK09700 78 AQLgIGIIYQElSVIDELTVLENLYIGRHltkkvcGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 925114634 541 IAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK-GRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKG 612
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKeGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1055-1251 |
3.25e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.13 E-value: 3.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1055 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQwLRAHLG--IVSQEPILFD-CSIAE 1131
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQLGigIIYQELSVIDeLTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1132 NIAYGD-------NSRVVSHEEIMQaakEANIHHFIETLPEKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEA 1204
Cdd:PRK09700 100 NLYIGRhltkkvcGVNIIDWREMRV---RAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 925114634 1205 TSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNG 1251
Cdd:PRK09700 173 TSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
398-619 |
4.10e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 74.09 E-value: 4.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 398 NVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQ-LMQRLYDPTD-------GMVCIDGQDIRTINVRHLR 469
Cdd:PRK13547 3 TADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKaLAGDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 470 EITGVVSQ--EPVlFATTIAENIRYGR----------ENVTMDEIEKAVKEANAydfimklpnkfDTLVGERGAQLSGGQ 537
Cdd:PRK13547 83 RLRAVLPQaaQPA-FAFSAREIVLLGRypharragalTHRDGEIAWQALALAGA-----------TALVGRDVTTLSGGE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 538 KQRIAIARAL---------VRNPKILLLDEATSALDTES-----EAVVQVALDkARKGRTTIVIAHRLSTvRNADVIAGF 603
Cdd:PRK13547 151 LARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHqhrllDTVRRLARD-WNLGVLAIVHDPNLAA-RHADRIAML 228
|
250
....*....|....*.
gi 925114634 604 DDGVIVEKGNHDELMK 619
Cdd:PRK13547 229 ADGAIVAHGAPADVLT 244
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1054-1268 |
5.09e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.00 E-value: 5.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQwLRAHLGI--VSQEPILFD-CSIA 1130
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLH-ARARRGIgyLPQEASIFRrLSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1131 ENIA--------YGDNSRVVSHEEIMQaakEANIHHFIETLpekyntrvgdkGTQLSGGQKQRIAIARALVRQPHILLLD 1202
Cdd:PRK10895 97 DNLMavlqirddLSAEQREDRANELME---EFHIEHLRDSM-----------GQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 1203 EATSALDTESEKVVQEALDKARE-GRTCIVIAHRL-STIQNADLIVVFQNGKVKEHGTHQQLLAQKGI 1268
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
405-588 |
5.95e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 72.01 E-value: 5.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 405 SRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITGVVSQEPVLFAT 484
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 485 TIAENIRYGRE--NVTMDEIEKAVKEANAYDFImklpnkfDTLVgergAQLSGGQKQRIAIARALVRNPKILLLDEATSA 562
Cdd:TIGR01189 89 SALENLHFWAAihGGAQRTIEDALAAVGLTGFE-------DLPA----AQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180
....*....|....*....|....*.
gi 925114634 563 LDTESEAVVQVALDkARKGRTTIVIA 588
Cdd:TIGR01189 158 LDKAGVALLAGLLR-AHLARGGIVLL 182
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
394-563 |
6.54e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.60 E-value: 6.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTI-NVRHLREIT 472
Cdd:PRK11614 6 LSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 473 GVVSQEPVLFA-TTIAENIRYGRENVTMDEIEKAVKEAnaYDFIMKLPNKfdtlVGERGAQLSGGQKQRIAIARALVRNP 551
Cdd:PRK11614 83 AIVPEGRRVFSrMTVEENLAMGGFFAERDQFQERIKWV--YELFPRLHER----RIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170
....*....|..
gi 925114634 552 KILLLDEATSAL 563
Cdd:PRK11614 157 RLLLLDEPSLGL 168
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
59-558 |
6.77e-14 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 75.99 E-value: 6.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 59 IIHGAALPLMMLVFGNMTDSFANAGISrnktfpVIINESITNNTqhfinhleEEMTTYAYYYSGIGAGVLVAAYI-QVSF 137
Cdd:COG4615 7 LLRESRWLLLLALLLGLLSGLANAGLI------ALINQALNATG--------AALARLLLLFAGLLVLLLLSRLAsQLLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 138 WCLAAgRQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVskinegigDKIGMFFQSIATFFTGFIVGFtrgwkLT 217
Cdd:COG4615 73 TRLGQ-HAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDV--------RTISQAFVRLPELLQSVALVL-----GC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 218 LVILA-ISPVLGLSAAIWAkILSSFTDKELLAYAKAG----AVAEEVL-AAIRTVIafGGQKkEL----ER----YNKNL 283
Cdd:COG4615 139 LAYLAwLSPPLFLLTLVLL-GLGVAGYRLLVRRARRHlrraREAEDRLfKHFRALL--EGFK-ELklnrRRrrafFDEDL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 284 E---EAKRIGIKKAITANISIGA-AFLLIYASYALAFWYGTSLVLSSEYSIGQ-VLTVFFsvLIGAfsIGQASPSIEAFA 358
Cdd:COG4615 215 QptaERYRDLRIRADTIFALANNwGNLLFFALIGLILFLLPALGWADPAVLSGfVLVLLF--LRGP--LSQLVGALPTLS 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 359 NARgAAYEifKIIDNKPSIDSYSKSGHKPDNIKGN-----LEFKNVHFSYPSRKEVK--ILKGLNLKVQSGQTVALVGNS 431
Cdd:COG4615 291 RAN-VALR--KIEELELALAAAEPAAADAAAPPAPadfqtLELRGVTYRYPGEDGDEgfTLGPIDLTIRRGELVFIVGGN 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 432 GCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITGVVSQEPVLFATTiaenirYGRENVTMDEiekavkEANA 511
Cdd:COG4615 368 GSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRL------LGLDGEADPA------RARE 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 925114634 512 YDFIMKLPNK-------FDTLvgergaQLSGGQKQRIAIARALVRNPKILLLDE 558
Cdd:COG4615 436 LLERLELDHKvsvedgrFSTT------DLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
394-609 |
7.87e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 74.38 E-value: 7.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKN--VHFSYPSrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTV-QLMQRLYDP--TDGMVCIDGQDIRTINVRHL 468
Cdd:PRK09473 13 LDVKDlrVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAfALMGLLAANgrIGGSATFNGREILNLPEKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 469 REI----TGVVSQEPVlfaTTIAENIRYG-------------------RENVTMDEiekAVKEANAYDFIMKLPNKFdtl 525
Cdd:PRK09473 92 NKLraeqISMIFQDPM---TSLNPYMRVGeqlmevlmlhkgmskaeafEESVRMLD---AVKMPEARKRMKMYPHEF--- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 526 vgergaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTT--IVIAHRLStvrnadVIAGF 603
Cdd:PRK09473 163 --------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaiIMITHDLG------VVAGI 228
|
....*.
gi 925114634 604 DDGVIV 609
Cdd:PRK09473 229 CDKVLV 234
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
394-612 |
1.11e-13 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 71.12 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKEVK-ILKGLNLKVQSGQTVALVGNSGCGKSTtvqLMQRLYDPTD-----GMVCIDGQDiRTINvrh 467
Cdd:cd03232 4 LTWKNLNYTVPVKGGKRqLLNNISGYVKPGTLTALMGESGAGKTT---LLDVLAGRKTagvitGEILINGRP-LDKN--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 468 LREITGVVSQEPVLFAT-TIAENIRygrenvtmdeiekavkeanaydFIMKLpnkfdtlvgeRGaqLSGGQKQRIAIARA 546
Cdd:cd03232 77 FQRSTGYVEQQDVHSPNlTVREALR----------------------FSALL----------RG--LSVEQRKRLTIGVE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 547 LVRNPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLStvrnADVIAGFDDGVIVEKG 612
Cdd:cd03232 123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPS----ASIFEKFDRLLLLKRG 185
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1047-1253 |
1.72e-13 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 71.59 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1047 PTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGkeikhlNVQW-----LRAHLGIV--S 1119
Cdd:cd03267 29 RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG------LVPWkrrkkFLRRIGVVfgQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1120 QEPILFDCSIAENIAYgdnsrvvsHEEIMQ---AAKEANIHHFIETLPEkynTRVGDKGT-QLSGGQKQRIAIARALVRQ 1195
Cdd:cd03267 103 KTQLWWDLPVIDSFYL--------LAAIYDlppARFKKRLDELSELLDL---EELLDTPVrQLSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 925114634 1196 PHILLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQN-ADLIVVFQNGKV 1253
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
384-617 |
1.82e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.11 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 384 GHKPDNIkgnLEFKNVHFSypsRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTI 463
Cdd:PRK11831 1 EQSVANL---VDMRGVSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 464 NVRHLREITGVVS---QEPVLFA-TTIAENIRYG-RENVTMDE--IEKAVkeanaydfIMKLpnkfdTLVGERGA----- 531
Cdd:PRK11831 75 SRSRLYTVRKRMSmlfQSGALFTdMNVFDNVAYPlREHTQLPAplLHSTV--------MMKL-----EAVGLRGAaklmp 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 532 -QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHR----LSTVRNADVIAgfd 604
Cdd:PRK11831 142 sELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDvpevLSIADHAYIVA--- 218
|
250
....*....|...
gi 925114634 605 DGVIVEKGNHDEL 617
Cdd:PRK11831 219 DKKIVAHGSAQAL 231
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
421-613 |
1.84e-13 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 68.94 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 421 SGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVC-IDGQDIRTINVRHLREItgvvsqepvlfattiaenirygrenvtm 499
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLLLI---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 500 deiekavkeanaydfimklpnkfdtLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALD--- 576
Cdd:smart00382 53 -------------------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 925114634 577 ----KARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGN 613
Cdd:smart00382 108 llllKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
404-675 |
2.39e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 72.81 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 404 PSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREItGVV----SQ-- 477
Cdd:COG4586 30 REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRI-GVVfgqrSQlw 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 478 --EPVLfattiaENIRYGRE--NVTMDEIEKAVKEanaYDFIMKLPNKFDTLVgeRgaQLSGGQKQRIAIARALVRNPKI 553
Cdd:COG4586 109 wdLPAI------DSFRLLKAiyRIPDAEYKKRLDE---LVELLDLGELLDTPV--R--QLSLGQRMRCELAAALLHRPKI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 554 LLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAHRLSTV----RNADVIagfDDGVIVEKGNHDELmKEKGIYFKL 627
Cdd:COG4586 176 LFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIealcDRVIVI---DHGRIIYDGSLEEL-KERFGPYKT 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 925114634 628 VTMQTRG--NEIELENATGESKSESDA--LEMSPKDSGSSLIKRRSTRRSIH 675
Cdd:COG4586 252 IVLELAEpvPPLELPRGGEVIEREGNRvrLEVDPRESLAEVLARLLARYPVR 303
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
412-606 |
2.44e-13 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 69.77 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 412 LKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREI-----------TGVVSQEPV 480
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgiayvpedrkrEGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 481 lfattiaenirygRENVTMdeiekavkeanaydfimklpnkfdtlvgerGAQLSGGQKQRIAIARALVRNPKILLLDEAT 560
Cdd:cd03215 96 -------------AENIAL------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPT 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 925114634 561 SALDTES-EAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDG 606
Cdd:cd03215 133 RGVDVGAkAEIYRLIRELADAGKAVLLISSELDELlGLCDRILVMYEG 180
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
415-564 |
3.64e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 72.60 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 415 LNLKVQ-----SGQTvALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQ---DI-RTINVR-HLREItGVVSQEPVLFA- 483
Cdd:PRK11144 13 LCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAeKGICLPpEKRRI-GYVFQDARLFPh 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 484 TTIAENIRYGrenvtMDEIEKAvkeanaydfimklpnKFDTLVGERG---------AQLSGGQKQRIAIARALVRNPKIL 554
Cdd:PRK11144 91 YKVRGNLRYG-----MAKSMVA---------------QFDKIVALLGieplldrypGSLSGGEKQRVAIGRALLTAPELL 150
|
170
....*....|
gi 925114634 555 LLDEATSALD 564
Cdd:PRK11144 151 LMDEPLASLD 160
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
410-621 |
5.52e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.43 E-value: 5.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 410 KILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLY--DPTDG--------MVCIDGQDIRtiNVRHLREITGVVSQEP 479
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGshiellgrTVQREGRLAR--DIRKSRANTGYIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 480 VLF-ATTIAENIRYGRENVT------MDEIEKAVKEaNAYDFIMKLpnKFDTLVGERGAQLSGGQKQRIAIARALVRNPK 552
Cdd:PRK09984 96 NLVnRLSVLENVLIGALGSTpfwrtcFSWFTREQKQ-RALQALTRV--GMVHFAHQRVSTLSGGQQQRVAIARALMQQAK 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 553 ILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKGNHDELMKEK 621
Cdd:PRK09984 173 VILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNER 244
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
405-621 |
5.94e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.60 E-value: 5.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 405 SRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIrtinvrhlreitgVVSQEpvlfaT 484
Cdd:COG2401 39 RVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDN-------------QFGRE-----A 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 485 TIAENIryGRENVTMDEIE--KAVKEANAYDFIMKLpnkfdtlvgergAQLSGGQKQRIAIARALVRNPKILLLDEATSA 562
Cdd:COG2401 101 SLIDAI--GRKGDFKDAVEllNAVGLSDAVLWLRRF------------KELSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 925114634 563 LDTESEAVVQVALDK-ARKGRTTIVIA-HRlstvrnADVIAGFDDGVIVEKGnHDELMKEK 621
Cdd:COG2401 167 LDRQTAKRVARNLQKlARRAGITLVVAtHH------YDVIDDLQPDLLIFVG-YGGVPEEK 220
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1050-1257 |
6.30e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 70.11 E-value: 6.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1050 PDIPVLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPLAGSVLIDGKEIKhlnVQWLRA-HLGIVSQEP-- 1122
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA---PCALRGrKIATIMQNPrs 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1123 ------ILFDCSIAENIAYGDNSRVVSHEEIMQAAKEANIHHFIETLPekyntrvgdkgTQLSGGQKQRIAIARALVRQP 1196
Cdd:PRK10418 91 afnplhTMHTHARETCLALGKPADDATLTAALEAVGLENAARVLKLYP-----------FEMSGGMLQRMMIALALLCEA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 925114634 1197 HILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHG 1257
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQG 223
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
394-614 |
9.01e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 69.82 E-value: 9.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKST-TVQLMQRL-YDPTDGMVCIDGQDIRTIN------- 464
Cdd:PRK09580 2 LSIKDLHVSV---EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTlSATLAGREdYEVTGGTVEFKGKDLLELSpedrage 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 465 -----VRHLREITGVVSQepvLFATTIAENIRYGRENVTMDEIEKAvkeanayDFI------MKLPNkfDTLVGERGAQL 533
Cdd:PRK09580 79 gifmaFQYPVEIPGVSNQ---FFLQTALNAVRSYRGQEPLDRFDFQ-------DLMeekialLKMPE--DLLTRSVNVGF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 534 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKG-RTTIVIAH--RLSTVRNADVIAGFDDGVIVE 610
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVK 226
|
....
gi 925114634 611 KGNH 614
Cdd:PRK09580 227 SGDF 230
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1049-1234 |
1.02e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.29 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1049 RPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIK------HLNVQWLRAHLGIVS--- 1119
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrqrdeyHQDLLYLGHQPGIKTelt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1120 -QEPILFDCSIAeniaygdnsRVVSHEEIMQAAKEANIHHFiETLPEKyntrvgdkgtQLSGGQKQRIAIARALVRQPHI 1198
Cdd:PRK13538 91 aLENLRFYQRLH---------GPGDDEALWEALAQVGLAGF-EDVPVR----------QLSAGQQRRVALARLWLTRAPL 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 925114634 1199 LLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAH 1234
Cdd:PRK13538 151 WILDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
146-343 |
1.05e-12 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 70.20 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 146 ILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSIATFFTGFIVGFTRGWKLTLVILAISP 225
Cdd:cd18550 71 MYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 226 VLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAA--IRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGA 303
Cdd:cd18550 151 LFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSVsgALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAA 230
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 925114634 304 AFLLIYASYALAFWYGTSLVLSSEYSIGQVltVFFSVLIG 343
Cdd:cd18550 231 LGLFTAIGPALVYWVGGLLVIGGGLTIGTL--VAFTALLG 268
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
113-337 |
1.23e-12 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 70.19 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 113 MTTYAYYYSGIGAGVLVAAYIQVSFWCLAAGRQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKI 192
Cdd:cd18545 39 LLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 193 GMFFQSIATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQ 272
Cdd:cd18545 119 INLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFARE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 273 KKELERYNKNLEEAKRIGIkKAITANISIGAAFLLIYA-SYALAFWYGTSLVLSSEYSIGqVLTVF 337
Cdd:cd18545 199 DENEEIFDELNRENRKANM-RAVRLNALFWPLVELISAlGTALVYWYGGKLVLGGAITVG-VLVAF 262
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1054-1237 |
1.66e-12 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 72.09 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPLAGSVLIDGKEIKhlnvqwlrahLGIVSQEPILFDCSIAENI 1133
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLTKPAKGK----------LFYVPQRPYMTLGTLRDQI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1134 AYGDNS-----RVVSHEEIMQAAKEANIHHFIETlpEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1208
Cdd:TIGR00954 536 IYPDSSedmkrRGLSDKDLEQILDNVQLTHILER--EGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
|
170 180
....*....|....*....|....*....
gi 925114634 1209 DTESEKVVQEALDKAreGRTCIVIAHRLS 1237
Cdd:TIGR00954 614 SVDVEGYMYRLCREF--GITLFSVSHRKS 640
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1055-1251 |
1.73e-12 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 67.65 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1055 LQGLSLEVKKGQTLALVGSSGCGKSTvvqLLerfyDPLA---------GSVLIDGKEIKhlnvQWLRAHLGIVSQEPILF 1125
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTT---LL----DVLAgrktagvitGEILINGRPLD----KNFQRSTGYVEQQDVHS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1126 DCS-IAENIAYGDNSRvvsheeimqaakeanihhfietlpekyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEA 1204
Cdd:cd03232 92 PNLtVREALRFSALLR------------------------------------GLSVEQRKRLTIGVELAAKPSILFLDEP 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 925114634 1205 TSALDTESEKVVQEALDK-AREGRTCIVIAHRLS--TIQNADLIVVFQNG 1251
Cdd:cd03232 136 TSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1037-1236 |
1.81e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.99 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKeikhlnvqwLRahLG 1116
Cdd:PRK09544 5 VSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1117 IVSQEpILFDCSIAENIaygdnSRV------VSHEEIMQAAKEANIHHFIETLPEKyntrvgdkgtqLSGGQKQRIAIAR 1190
Cdd:PRK09544 71 YVPQK-LYLDTTLPLTV-----NRFlrlrpgTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLAR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 925114634 1191 ALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIV--IAHRL 1236
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVlmVSHDL 181
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1058-1257 |
2.19e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.90 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1058 LSLEVK-----KGQTlALVGSSGCGKSTVVQLLERFYDP------LAGSVLIDGKEIKHLNVQwlRAHLGIVSQEPILF- 1125
Cdd:PRK11144 13 LCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPqkgrivLNGRVLFDAEKGICLPPE--KRRIGYVFQDARLFp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1126 DCSIAENIAYGdnsrvVSHEeiMQAakeanihHF--------IETLPEKYNTRvgdkgtqLSGGQKQRIAIARALVRQPH 1197
Cdd:PRK11144 90 HYKVRGNLRYG-----MAKS--MVA-------QFdkivallgIEPLLDRYPGS-------LSGGEKQRVAIGRALLTAPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 1198 ILLLDEATSALDTESEKVVQEALDK-AREGRTCIV-IAHRLSTI-QNADLIVVFQNGKVKEHG 1257
Cdd:PRK11144 149 LLLMDEPLASLDLPRKRELLPYLERlAREINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFG 211
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1053-1255 |
2.54e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.68 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1053 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDgkeikhlnvqwlrahlgiVSQEPILFDCSIAEN 1132
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------------------VPDNQFGREASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1133 IA-YGDNSRVVsheEIMQAAKEANIHHFIETLPEkyntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1211
Cdd:COG2401 106 IGrKGDFKDAV---ELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 925114634 1212 SEKVVQEALDKA--REGRTCIVIAHR---LSTIQnADLIVVFQNGKVKE 1255
Cdd:COG2401 171 TAKRVARNLQKLarRAGITLVVATHHydvIDDLQ-PDLLIFVGYGGVPE 218
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1029-1263 |
2.90e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 68.28 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1029 KPNTLEGNVTFNEVVFNYPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNV 1108
Cdd:PRK10575 4 YTNHSDTTFALRNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1109 QWLRAHLGIVSQE-PILFDCSIAENIAYG--------DNSRVVSHEEIMQAAKEANIHHFIETLPEkyntrvgdkgtQLS 1179
Cdd:PRK10575 81 KAFARKVAYLPQQlPAAEGMTVRELVAIGrypwhgalGRFGAADREKVEEAISLVGLKPLAHRLVD-----------SLS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1180 GGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAhRLSTIQNA----DLIVVFQNGKVKE 1255
Cdd:PRK10575 150 GGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGGEMIA 228
|
....*...
gi 925114634 1256 HGTHQQLL 1263
Cdd:PRK10575 229 QGTPAELM 236
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
394-609 |
3.10e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.44 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVhfSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREiTG 473
Cdd:COG3845 258 LEVENL--SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRR-LG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 V--VSQEPVLFAT----TIAENI---RYGRENVT------MDEIEKAVKEA-NAYDfiMKLPNKfDTLVGergaQLSGGQ 537
Cdd:COG3845 335 VayIPEDRLGRGLvpdmSVAENLilgRYRRPPFSrggfldRKAIRAFAEELiEEFD--VRTPGP-DTPAR----SLSGGN 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 925114634 538 KQRIAIARALVRNPKILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIV 609
Cdd:COG3845 408 QQKVILARELSRDPKLLIAAQPTRGLDVGAiEFIHQRLLELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1047-1264 |
4.07e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 70.24 E-value: 4.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1047 PTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-PLAGSVLIDGKEIKHLN-VQWLRAHLGIVSQEP-- 1122
Cdd:TIGR02633 268 VINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRkr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1123 --ILFDCSIAENIAYGDNSRVVSHEEIMQAAKEANIHHFIETLpeKYNTRVGDKG-TQLSGGQKQRIAIARALVRQPHIL 1199
Cdd:TIGR02633 348 hgIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRL--KVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 1200 LLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVK----EHG-THQQLLA 1264
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLKgdfvNHAlTQEQVLA 497
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
411-617 |
6.03e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 67.42 E-value: 6.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 411 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDP----TDGMVCIDGQDI-------RTI-----NVR-------- 466
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVapcalrgRKIatimqNPRsafnplht 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 467 ---HLREITGVVSQEPVlfATTIAENIrygrENVTMDEIEKAVKeanAYDFimklpnkfdtlvgergaQLSGGQKQRIAI 543
Cdd:PRK10418 98 mhtHARETCLALGKPAD--DATLTAAL----EAVGLENAARVLK---LYPF-----------------EMSGGMLQRMMI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 544 ARALVRNPKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDEL 617
Cdd:PRK10418 152 ALALLCEAPFIIADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETL 228
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1053-1253 |
6.42e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 69.76 E-value: 6.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1053 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLN-----------VQWLRAHLGIVSQE 1121
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfalVTEERRSTGIYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1122 PILFDCSIAENIAYGDNSRVVSHEEImqaakEANIHHFIETLPEK---YNTRVGdkgtQLSGGQKQRIAIARALVRQPHI 1198
Cdd:PRK10982 342 DIGFNSLISNIRNYKNKVGLLDNSRM-----KSDTQWVIDSMRVKtpgHRTQIG----SLSGGNQQKVIIGRWLLTQPEI 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1199 LLLDEATSALDTESE-KVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGKV 1253
Cdd:PRK10982 413 LMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
394-610 |
6.73e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 69.62 E-value: 6.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITG 473
Cdd:PRK10522 323 LELRNVTFAYQDNGFS--VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFATTIaeniryGRENvtmdeieKAVKEANAYDFI--MKLPNKFdTLVGERGA--QLSGGQKQRIAIARALVR 549
Cdd:PRK10522 401 AVFTDFHLFDQLL------GPEG-------KPANPALVEKWLerLKMAHKL-ELEDGRISnlKLSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 550 NPKILLLDEATSALDTESEAVV-QVALDKAR-KGRTTIVIAHRLSTVRNADVIAGFDDGVIVE 610
Cdd:PRK10522 467 ERDILLLDEWAADQDPHFRREFyQVLLPLLQeMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
759-1007 |
7.30e-12 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 67.81 E-value: 7.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 759 VLFLVLGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAI--GSRLA 836
Cdd:cd18548 43 LLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEID--KFGTSSLITRLTNDVTQVQNFVmmLLRML 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 837 VITqnIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGAGKIATEAIENFRTVVSLTRE- 915
Cdd:cd18548 121 VRA--PIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREd 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 916 ---QKFEymyAQSLQVpYRNSLRKAHIFGVSFSITQAMMYFSYAGCFRFGAYLVANEFMNFQDvLLVFSA----IVFGAM 988
Cdd:cd18548 199 yeeERFD---KANDDL-TDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGD-LVAFINylmqILMSLM 273
|
250
....*....|....*....
gi 925114634 989 AVGQVSSFAPdyaKAKVSA 1007
Cdd:cd18548 274 MLSMVFVMLP---RASASA 289
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
397-575 |
7.91e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.06 E-value: 7.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 397 KNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQdirtinvrhLReiTGVVS 476
Cdd:PRK09544 8 ENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 477 QEPVLFAT---TIAENIRYgRENVTMDEIEKAVKEANAYDFIMKLPNKfdtlvgergaqLSGGQKQRIAIARALVRNPKI 553
Cdd:PRK09544 74 QKLYLDTTlplTVNRFLRL-RPGTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQL 141
|
170 180
....*....|....*....|..
gi 925114634 554 LLLDEATSALDTESeavvQVAL 575
Cdd:PRK09544 142 LVLDEPTQGVDVNG----QVAL 159
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1064-1248 |
1.05e-11 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 63.93 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1064 KGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVlidgkeikhlnvqwlrahlgivsqepILFDCSIaeniaygdnsrvvs 1143
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------IYIDGED-------------- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1144 heeimqaakeanihHFIETLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALD-- 1221
Cdd:smart00382 41 --------------ILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106
|
170 180 190
....*....|....*....|....*....|..
gi 925114634 1222 -----KAREGRTCIVIAHRLSTIQNADLIVVF 1248
Cdd:smart00382 107 lllllKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
405-589 |
1.47e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.21 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 405 SRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREI------TGVvsqE 478
Cdd:PRK13538 10 ERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLlylghqPGI---K 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 479 PVLfatTIAENIRY---GRENVTMDEIEKAVKEANaydfimkLPNKFDTLVGergaQLSGGQKQRIAIARALVRNPKILL 555
Cdd:PRK13538 87 TEL---TALENLRFyqrLHGPGDDEALWEALAQVG-------LAGFEDVPVR----QLSAGQQRRVALARLWLTRAPLWI 152
|
170 180 190
....*....|....*....|....*....|....*
gi 925114634 556 LDEATSALDTESEAVVQVALDK-ARKGRTTIVIAH 589
Cdd:PRK13538 153 LDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
744-1003 |
2.58e-11 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 65.96 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 744 DEDPETKRQNSNMFSVLflvlGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLAND 823
Cdd:cd18589 29 KDAPEAFTAAITVMSLL----TIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFD--SNQTGDIVSRVTTD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 824 AAQVKGAIGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGAGKIATEAI 903
Cdd:cd18589 103 TEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETF 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 904 ENFRTVVSLTREQKFEYMYAQSLQVPYRNSLRKAHIFGVSFSITQAMMYFSYAGCFRFGAYLVANEFMNFQD-VLLVFSA 982
Cdd:cd18589 183 SAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQLVTAGTVSSGDlVTFVLYE 262
|
250 260
....*....|....*....|.
gi 925114634 983 IVFGAmAVGQVSSFAPDYAKA 1003
Cdd:cd18589 263 LQFTS-AVEVLLSYYPSVMKA 282
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
393-620 |
2.77e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 66.30 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 393 NLEFKNVHFSyPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD-PTDGM---VCIDGQDIRTINVRHL 468
Cdd:PRK11022 5 NVDKLSVHFG-DESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRVMaekLEFNGQDLQRISEKER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 469 REITG----VVSQEPVlfaTTIaeNIRYGRENVTMDEIE------KAVKEANAYDFImklpnkfdTLVG-----ER---- 529
Cdd:PRK11022 84 RNLVGaevaMIFQDPM---TSL--NPCYTVGFQIMEAIKvhqggnKKTRRQRAIDLL--------NQVGipdpaSRldvy 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 530 GAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQVALD-KARKGRTTIVIAHRLSTV-RNADVIAGFDDG 606
Cdd:PRK11022 151 PHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAqIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAG 230
|
250
....*....|....
gi 925114634 607 VIVEKGNHDELMKE 620
Cdd:PRK11022 231 QVVETGKAHDIFRA 244
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1051-1253 |
3.26e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.67 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1051 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydplAGSVLIDGKEI---KHLNVQWL-----RAHLGIVsqep 1122
Cdd:PRK11147 15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDGRIiyeQDLIVARLqqdppRNVEGTV---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1123 ilFDcSIAENIA--------YGDNSRVVSHEE----IMQAAK-------------EANIHHFIETL---PEKyntrvgdK 1174
Cdd:PRK11147 84 --YD-FVAEGIEeqaeylkrYHDISHLVETDPseknLNELAKlqeqldhhnlwqlENRINEVLAQLgldPDA-------A 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1175 GTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALdKAREGrTCIVIAHRLSTIQN-ADLIVVFQNGKV 1253
Cdd:PRK11147 154 LSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRIVDLDRGKL 231
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1051-1265 |
3.30e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 66.29 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1051 DIPVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP--LAGSVLIDGKEI-----KHLNVqwLRA-HLGIVSQE 1121
Cdd:PRK09473 28 DVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREIlnlpeKELNK--LRAeQISMIFQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1122 PIlfdCSIAENIAYGDNSRvvshEEIMQAAKEANIHHFIET--------LPEKyNTRVGDKGTQLSGGQKQRIAIARALV 1193
Cdd:PRK09473 106 PM---TSLNPYMRVGEQLM----EVLMLHKGMSKAEAFEESvrmldavkMPEA-RKRMKMYPHEFSGGMRQRVMIAMALL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 1194 RQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIV-IAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQLLAQ 1265
Cdd:PRK09473 178 CRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIImITHDLGVVAGiCDKVLVMYAGRTMEYGNARDVFYQ 252
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1051-1265 |
4.63e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 64.43 E-value: 4.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1051 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPLAGSVLIDGKEIKHLNVQwLRAHLGI--VSQEPILFD 1126
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPE-DRAGEGIfmAFQYPVEIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1127 CsiaeniaygdnsrvVSHEEIMQAAKEA-------------NIHHFIE------TLPEKYNTRVGDKGtqLSGGQKQRIA 1187
Cdd:PRK09580 92 G--------------VSNQFFLQTALNAvrsyrgqepldrfDFQDLMEekiallKMPEDLLTRSVNVG--FSGGEKKRND 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1188 IARALVRQPHILLLDEATSALDTESEKVVQEALDKAREG-RTCIVIAH--RLSTIQNADLIVVFQNGKVKEHGTH---QQ 1261
Cdd:PRK09580 156 ILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFtlvKQ 235
|
....
gi 925114634 1262 LLAQ 1265
Cdd:PRK09580 236 LEEQ 239
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
394-620 |
4.64e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 64.66 E-value: 4.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLM--QRLYDPTDGMVCIDGQDIRTINVR---HL 468
Cdd:CHL00131 8 LEIKNLHASV---NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPEeraHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 469 R---------EITGVVSQEpvlFATTIAENIRYGRENVTMDEIEkavkeanAYDFIM-KLPnkfdtLVGERGAQL----- 533
Cdd:CHL00131 85 GiflafqypiEIPGVSNAD---FLRLAYNSKRKFQGLPELDPLE-------FLEIINeKLK-----LVGMDPSFLsrnvn 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 534 ---SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAH--RLSTVRNADVIAGFDDGV 607
Cdd:CHL00131 150 egfSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGK 229
|
250
....*....|...
gi 925114634 608 IVEKGNhDELMKE 620
Cdd:CHL00131 230 IIKTGD-AELAKE 241
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
149-341 |
4.81e-11 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 65.20 E-value: 4.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 149 IRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGdKIGMFFQSIATFFTGFIVGFTRGWKLTLVILAISPVLG 228
Cdd:cd18543 74 LRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 229 LSAAIWAKILSSFTdkeLLAYAKAGAVA---EEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKA-ITANISigAA 304
Cdd:cd18543 153 LVARRFRRRYFPAS---RRAQDQAGDLAtvvEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAArLRARFW--PL 227
|
170 180 190
....*....|....*....|....*....|....*...
gi 925114634 305 FLLI-YASYALAFWYGTSLVLSSEYSIGQvLTVFFSVL 341
Cdd:cd18543 228 LEALpELGLAAVLALGGWLVANGSLTLGT-LVAFSAYL 264
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
419-592 |
4.91e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 64.70 E-value: 4.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 419 VQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCiDGQDIRTInvrhLREITGVVSQEpvLFATTIAENIRYGRENVT 498
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD-DPPDWDEI----LDEFRGSELQN--YFTKLLEGDVKVIVKPQY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 499 MDEIEKAVKeANAYDFIMKLP--NKFDTLVG--------ERG-AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 567
Cdd:cd03236 96 VDLIPKAVK-GKVGELLKKKDerGKLDELVDqlelrhvlDRNiDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180
....*....|....*....|....*.
gi 925114634 568 E-AVVQVALDKARKGRTTIVIAHRLS 592
Cdd:cd03236 175 RlNAARLIRELAEDDNYVLVVEHDLA 200
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
402-589 |
5.43e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.88 E-value: 5.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 402 SYPSRKEvkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDgqdiRTINVrhlreitGVVSQEPVL 481
Cdd:TIGR03719 13 VVPPKKE--ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ----PGIKV-------GYLPQEPQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 482 FAT-TIAENIRYGrenvtMDEIEKAVKEANAYDFIMKLPN-KFDTLVGERG----------------------------- 530
Cdd:TIGR03719 80 DPTkTVRENVEEG-----VAEIKDALDRFNEISAKYAEPDaDFDKLAAEQAelqeiidaadawdldsqleiamdalrcpp 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 925114634 531 -----AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALdKARKGrTTIVIAH 589
Cdd:TIGR03719 155 wdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL-QEYPG-TVVAVTH 216
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1041-1264 |
6.14e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.49 E-value: 6.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1041 EVVF---NY----PTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPLA--GSVLIDGKEIKHLN-VQW 1110
Cdd:PRK13549 257 EVILevrNLtawdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PGRweGEIFIDGKPVKIRNpQQA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1111 LRAHLGIVSQEP----ILFDCSIAENIAYGDNSRVVSHEEIMQAAKEANIHHFIETLPEKYNT---RVGdkgtQLSGGQK 1183
Cdd:PRK13549 336 IAQGIAMVPEDRkrdgIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASpelAIA----RLSGGNQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1184 QRIAIARALVRQPHILLLDEATSALDT----ESEKVVQEAldkAREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVK---- 1254
Cdd:PRK13549 412 QKAVLAKCLLLNPKILILDEPTRGIDVgakyEIYKLINQL---VQQGVAIIVISSELPEVLGlSDRVLVMHEGKLKgdli 488
|
250
....*....|.
gi 925114634 1255 -EHGTHQQLLA 1264
Cdd:PRK13549 489 nHNLTQEQVME 499
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
125-364 |
7.14e-11 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 64.87 E-value: 7.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 125 AGVLVAAYI-QVSFWCL-------AAGRQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFF 196
Cdd:cd18778 43 ALLLLGAYLlRALLNFLriylnhvAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 197 QSIATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKEL 276
Cdd:cd18778 123 TNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 277 ERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTSLVLSSEYSIGQVltVFFSVLIGAF--SIGQASPSI 354
Cdd:cd18778 203 KRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVLVLGFGGRLVLAGELTIGDL--VAFLLYLGLFyePITSLHGLN 280
|
250
....*....|
gi 925114634 355 EAFANARGAA 364
Cdd:cd18778 281 EMLQRALAGA 290
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1054-1276 |
9.56e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.06 E-value: 9.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE-RFY-DPLAGSVLIDGKEIKHlnvQWLRaHLGIVSQEPILF-DCSIA 1130
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQgNNFTGTILANNRKPTK---QILK-RTGFVTQDDILYpHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1131 ENIAYGDNSRV---VSHEEIMQAAkEANIHHFIETLPEkyNTRVGDKGTQ-LSGGQKQRIAIARALVRQPHILLLDEATS 1206
Cdd:PLN03211 159 ETLVFCSLLRLpksLTKQEKILVA-ESVISELGLTKCE--NTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 1207 ALD-TESEKVVQEALDKAREGRTCIVIAHRLST--IQNADLIVVFQNGKVKEHGTHQQLLAqkgiYFSMVSVQ 1276
Cdd:PLN03211 236 GLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA----YFESVGFS 304
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
396-588 |
1.33e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 62.28 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 396 FKNVHF-SYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTtvqLMQRL------YDPTDGMVCIDGQDIRTINVRHL 468
Cdd:cd03233 6 WRNISFtTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCST---LLKALanrtegNVSVEGDIHYNGIPYKEFAEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 469 REITgVVSQEPVLFAT-TIAEnirygrenvTMDeiekAVKEANAYDFImklpnkfdtlvgeRGaqLSGGQKQRIAIARAL 547
Cdd:cd03233 83 GEII-YVSEEDVHFPTlTVRE---------TLD----FALRCKGNEFV-------------RG--ISGGERKRVSIAEAL 133
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 925114634 548 VRNPKILLLDEATSALDTESE-AVVQVALDKARKGRTTIVIA 588
Cdd:cd03233 134 VSRASVLCWDNSTRGLDSSTAlEILKCIRTMADVLKTTTFVS 175
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
713-971 |
1.55e-10 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 63.66 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 713 FVVGIFCAIINGGLQPAFSIIFSRII--GIFTRDEDPETkrqnsnMFSVLFLVLGIISFITFFLQGFTFGKAGEILTKRL 790
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIdgPIAHGDRSALW------PLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 791 RYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIgSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPII 870
Cdd:cd18543 75 RTDLFAHLQRLDGAFHD--RWQSGQLLSRATSDLSLVQRFL-AFGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 871 AIAGVVEMKMLSGQALKDKkelEGAGKIATEAIEN---FRTVVSLTRE----QKFEYMyAQSLqvpYRNSLRKAHIFGVS 943
Cdd:cd18543 152 VLVARRFRRRYFPASRRAQ---DQAGDLATVVEESvtgIRVVKAFGRErrelDRFEAA-ARRL---RATRLRAARLRARF 224
|
250 260
....*....|....*....|....*...
gi 925114634 944 FSITQAMMYFSYAGCFRFGAYLVANEFM 971
Cdd:cd18543 225 WPLLEALPELGLAAVLALGGWLVANGSL 252
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
149-345 |
1.68e-10 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 63.62 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 149 IRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINE----GIGDkigmFFQSIATFFTGFIVGFTRGWKLTLVILAIS 224
Cdd:cd18549 77 MRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISElahhGPED----LFISIITIIGSFIILLTINVPLTLIVFALL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 225 PVLGLsAAIWA--KILSSFTDkellAYAKAG---AVAEEVLAAIRTVIAFGGQKKELERY---NKNLEEAKRIGIkKAIT 296
Cdd:cd18549 153 PLMII-FTIYFnkKMKKAFRR----VREKIGeinAQLEDSLSGIRVVKAFANEEYEIEKFdegNDRFLESKKKAY-KAMA 226
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 925114634 297 ANISIGAAFLLIYasYALAFWYGTSLVLSSEYSIGQVLTvfFSVLIGAF 345
Cdd:cd18549 227 YFFSGMNFFTNLL--NLVVLVAGGYFIIKGEITLGDLVA--FLLYVNVF 271
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
397-568 |
1.84e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.75 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 397 KNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREiTGV-- 474
Cdd:PRK10982 2 SNISKSFPG---VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALE-NGIsm 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 475 VSQE-PVLFATTIAENI---RYGRENVTMDEiEKAVKEANAYdfimklpnkFDTL-----VGERGAQLSGGQKQRIAIAR 545
Cdd:PRK10982 78 VHQElNLVLQRSVMDNMwlgRYPTKGMFVDQ-DKMYRDTKAI---------FDELdididPRAKVATLSVSQMQMIEIAK 147
|
170 180
....*....|....*....|...
gi 925114634 546 ALVRNPKILLLDEATSALdTESE 568
Cdd:PRK10982 148 AFSYNAKIVIMDEPTSSL-TEKE 169
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
422-612 |
2.40e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 62.64 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 422 GQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINV--------RHL-REITGVVSQEP-------VLFATT 485
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalseaerRRLlRTEWGFVHQHPrdglrmqVSAGGN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 486 IAENI------RYGRENVT----MDEIEKAVkeanayDFIMKLPNKFdtlvgergaqlSGGQKQRIAIARALVRNPKILL 555
Cdd:PRK11701 112 IGERLmavgarHYGDIRATagdwLERVEIDA------ARIDDLPTTF-----------SGGMQQRLQIARNLVTHPRLVF 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 556 LDEATSALDTESEAVVqvaLDKARK-----GRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKG 612
Cdd:PRK11701 175 MDEPTGGLDVSVQARL---LDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
414-594 |
2.49e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 62.31 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 414 GLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDI--------------RTI-NVRHLREITGV---- 474
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghqiarmgvvRTFqHVRLFREMTVIenll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 475 VSQE--------PVLFATTiaeniRYGREnvtmdEIEKAVKEANAYDFIMKLPnkfdtLVGERGAQLSGGQKQRIAIARA 546
Cdd:PRK11300 103 VAQHqqlktglfSGLLKTP-----AFRRA-----ESEALDRAATWLERVGLLE-----HANRQAGNLAYGQQRRLEIARC 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 925114634 547 LVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTV 594
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLV 217
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1058-1263 |
2.66e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.26 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1058 LSLEVKKGQTLALVGSSGCGKSTvvqLLERFYD--PLAGSVLIDGKEIKHLNVQWLRAHLGIVSQE---PILFDcsiaen 1132
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGllPGSGSIQFAGQPLEAWSAAELARHRAYLSQQqtpPFAMP------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1133 iaygdnsrVVSHEEIMQAAK--EANIHHFIETLPEKYNtrVGDK----GTQLSGGQKQRIAIArALVRQ------PH--I 1198
Cdd:PRK03695 86 --------VFQYLTLHQPDKtrTEAVASALNEVAEALG--LDDKlgrsVNQLSGGEWQRVRLA-AVVLQvwpdinPAgqL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 1199 LLLDEATSALDtesekVVQE-ALDK-----AREGRTCIVIAHRLS-TIQNADLIVVFQNGKVKEHGTHQQLL 1263
Cdd:PRK03695 155 LLLDEPMNSLD-----VAQQaALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1050-1252 |
3.41e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.98 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1050 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIK-HLNVQWLRAHLGIVSQE-PILFDC 1127
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1128 SIAENIAYGDNSR---VVSHEEIMQAAKEanihhFIETLPEKYNTRvgDKGTQLSGGQKQRIAIARALVRQPHILLLDEA 1204
Cdd:PRK10982 89 SVMDNMWLGRYPTkgmFVDQDKMYRDTKA-----IFDELDIDIDPR--AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 925114634 1205 TSALdteSEKVVQ---EALDKAREgRTC--IVIAHRLSTI-QNADLIVVFQNGK 1252
Cdd:PRK10982 162 TSSL---TEKEVNhlfTIIRKLKE-RGCgiVYISHKMEEIfQLCDEITILRDGQ 211
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
121-338 |
3.82e-10 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 62.51 E-value: 3.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 121 SGIGAGVLVAAYIQVSFWCLAAGR---QILK-IRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFF 196
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRtgeRLLYdLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 197 QSIATFFTGFIVGFTRGWKLTLVILAISPVLGLsAAIWAKILSSFtdkellAYAKA-GAVAE------EVLAAIRTVIAF 269
Cdd:cd18546 122 VSLLTLVGIAVVLLVLDPRLALVALAALPPLAL-ATRWFRRRSSR------AYRRArERIAAvnadlqETLAGIRVVQAF 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 270 GGQKKELERYnKNLEEAKRIGIKKAITAN-ISIGAAFLLIYASYALAFWYGTSLVLSSEYSIGqVLTVFF 338
Cdd:cd18546 195 RRERRNAERF-AELSDDYRDARLRAQRLVaIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVG-VLVAFL 262
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
407-593 |
5.86e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 63.75 E-value: 5.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 407 KEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQ-LMQRLYDPT-DGMVCIDGQDIrtinVRHLREITGVVSQEPVLFA- 483
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNaLAGRIQGNNfTGTILANNRKP----TKQILKRTGFVTQDDILYPh 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 484 TTIAENIRYGRENVTMDEIEKAVKEANAYDFI--MKLPNKFDTLVGE---RGaqLSGGQKQRIAIARALVRNPKILLLDE 558
Cdd:PLN03211 155 LTVRETLVFCSLLRLPKSLTKQEKILVAESVIseLGLTKCENTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190
....*....|....*....|....*....|....*.
gi 925114634 559 ATSALD-TESEAVVQVALDKARKGRTTIVIAHRLST 593
Cdd:PLN03211 233 PTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSS 268
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1031-1239 |
8.08e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.44 E-value: 8.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1031 NTLEGNVTFNEVVFNYptRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQW 1110
Cdd:PRK15056 1 MMQQAGIVVNDVTVTW--RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1111 LRAHLGIVSQEPILFDCSIAENIAYGDnsrvVSHEEIMQAAKEANIHHFIETLP-----EKYNTRVGdkgtQLSGGQKQR 1185
Cdd:PRK15056 79 LVAYVPQSEEVDWSFPVLVEDVVMMGR----YGHMGWLRRAKKRDRQIVTAALArvdmvEFRHRQIG----ELSGGQKKR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 1186 IAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTI 1239
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
394-598 |
9.69e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.58 E-value: 9.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREITG 473
Cdd:PRK13540 2 LDVIELDFDY---HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFATTIAEN----IRYGRENVTMDEIEKAVKEANAYDFIMKLpnkfdtlvgergaqLSGGQKQRIAIARALVR 549
Cdd:PRK13540 79 VGHRSGINPYLTLRENclydIHFSPGAVGITELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 925114634 550 NPKILLLDEATSALDTESEAVVQVALDKAR-KGRTTIVIAHRLSTVRNAD 598
Cdd:PRK13540 145 KAKLWLLDEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
713-875 |
1.01e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 61.40 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 713 FVVGIFCAIINGGLQPAFSIIFSRIIGIFTrdedpetkrQNSNMFSVLFLVLGIISFITFFLQGFTFG------KAGEIL 786
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVT---------IGSKSLGLLLGLALLLLGAYLLRALLNFLriylnhVAEQKV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 787 TKRLRYMVFRSMLRQDVSWFDDPKntTGALTTRLANDAAQVKGAIgsrLAVITQNIANLGT--GIIISLIY-GWQLTLLL 863
Cdd:cd18778 72 VADLRSDLYDKLQRLSLRYFDDRQ--TGDLMSRVINDVANVERLI---ADGIPQGITNVLTlvGVAIILFSiNPKLALLT 146
|
170
....*....|..
gi 925114634 864 LAIVPIIAIAGV 875
Cdd:cd18778 147 LIPIPFLALGAW 158
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
759-1007 |
1.10e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 61.37 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 759 VLFLVLGIISFitffLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVI 838
Cdd:cd18564 62 GIALLRGLASY----AGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHD--RRRTGDLLSRLTGDVGAIQDLLVSGVLPL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 839 TQNIANLG--TGIIISLiyGWQLTLLLLAIVPIIAIAGVV---EMKmlsgQALKDKKELEGA-GKIATEAIENFRTVVSL 912
Cdd:cd18564 136 LTNLLTLVgmLGVMFWL--DWQLALIALAVAPLLLLAARRfsrRIK----EASREQRRREGAlASVAQESLSAIRVVQAF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 913 TREQKFEYMYAQSLQVPYRNSLRKAHIFGVSFSITQAMMYFSYAGCFRFGAYLVANEFMNFQDvLLVFSAIVFGAMA-VG 991
Cdd:cd18564 210 GREEHEERRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGD-LLVFLAYLKNLYKpVR 288
|
250
....*....|....*.
gi 925114634 992 QVSSFAPDYAKAKVSA 1007
Cdd:cd18564 289 DLAKLTGRIAKASASA 304
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
717-1007 |
1.15e-09 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 60.92 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 717 IFCAIINGGLQPAFSIIFSRIIgiftrdeD---PETKRQNSNMFSVLFLVLGIISFITFFLQGFTFGKAGEILTKRLRYM 793
Cdd:cd18570 8 LLLSLLITLLGIAGSFFFQILI-------DdiiPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 794 VFRSMLRQDVSWFDdpKNTTGALTTRLaNDAAQVKGAIGSrlAVITQnIANLGTGIIISLI---YGWQLTLLLLAIVPII 870
Cdd:cd18570 81 YFKHLLKLPLSFFE--TRKTGEIISRF-NDANKIREAISS--TTISL-FLDLLMVIISGIIlffYNWKLFLITLLIIPLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 871 AIAGVVEMKMLSGqalKDKKELEGAGKIATEAIENFR---TVVSLTREQKFeymyAQSLQVPYRNSLRKAHIFG----VS 943
Cdd:cd18570 155 ILIILLFNKPFKK---KNREVMESNAELNSYLIESLKgieTIKSLNAEEQF----LKKIEKKFSKLLKKSFKLGklsnLQ 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 944 FSITQAMMYFSYAGCFRFGAYLVANEFMNFQDvLLVFSAIVFGAM-AVGQVSSFAPDYAKAKVSA 1007
Cdd:cd18570 228 SSIKGLISLIGSLLILWIGSYLVIKGQLSLGQ-LIAFNALLGYFLgPIENLINLQPKIQEAKVAA 291
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
412-600 |
1.39e-09 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 60.32 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 412 LKGLNLKVQSGQTVALVGNSGCGKSTTVQ------LMQRL---------YDPTDGMVCIDgqdiRTINV------RHLRE 470
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypaLARRLhlkkeqpgnHDRIEGLEHID----KVIVIdqspigRTPRS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 471 I----TGVVSQEPVLFATtIAENIRYGRE-------NVTMDEI-EKAVKEAnaYDF---IMKLPNKFDTLV--------- 526
Cdd:cd03271 87 NpatyTGVFDEIRELFCE-VCKGKRYNREtlevrykGKSIADVlDMTVEEA--LEFfenIPKIARKLQTLCdvglgyikl 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 527 GERGAQLSGGQKQRIAIARALVR---NPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLSTVRNADVI 600
Cdd:cd03271 164 GQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRlVDKGNTVVVIEHNLDVIKCADWI 241
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
758-876 |
1.52e-09 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 60.58 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 758 SVLFLVLGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAV 837
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHE--RETSGRIMTRMTSDIDALSELLQTGLVQ 119
|
90 100 110
....*....|....*....|....*....|....*....
gi 925114634 838 ITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVV 876
Cdd:cd18546 120 LVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRW 158
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
744-873 |
1.68e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 60.60 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 744 DEDPETKRQNSNMFSVLFLVLG-----IISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTT 818
Cdd:cd18563 27 DDVLIQLGPGGNTSLLLLLVLGlagayVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFD--KRQTGSLMS 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 819 RLANDAAQVKGAIGSRLAVITQNIANLgTGIIISLIY-GWQLTLLLLAIVPIIAIA 873
Cdd:cd18563 105 RVTSDTDRLQDFLSDGLPDFLTNILMI-IGIGVVLFSlNWKLALLVLIPVPLVVWG 159
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
412-594 |
1.79e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 60.28 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 412 LKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRtinvRHLRE-ITGVVSQE-------PVLFA 483
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKnLVAYVPQSeevdwsfPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 484 TTIAENiRYG-----RENVTMDE--IEKAVKEANAYDFIMKLpnkfdtlVGErgaqLSGGQKQRIAIARALVRNPKILLL 556
Cdd:PRK15056 99 DVVMMG-RYGhmgwlRRAKKRDRqiVTAALARVDMVEFRHRQ-------IGE----LSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 925114634 557 DEATSALDTESEAVVQVALDKAR-KGRTTIVIAHRLSTV 594
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
409-614 |
2.16e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 62.17 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 409 VKILKGLNLKVQSGQTVALVGNSGCGKSTtvqLMQRLYDPTDGMVcIDGqDIRTINVRHLRE----ITG----------- 473
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTT---LMDVLAGRKTGGY-IEG-DIRISGFPKKQEtfarISGyceqndihspq 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VVSQEPVLFATTIAENIRYGRENVTM--DEIEKAVKEANAYDFIMKLPnkfdtlvGERGaqLSGGQKQRIAIARALVRNP 551
Cdd:PLN03140 968 VTVRESLIYSAFLRLPKEVSKEEKMMfvDEVMELVELDNLKDAIVGLP-------GVTG--LSTEQRKRLTIAVELVANP 1038
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 925114634 552 KILLLDEATSALDTESEAVVQVAL-DKARKGRTTIVIAHRLSTvrnaDVIAGFDDGVIVEKGNH 614
Cdd:PLN03140 1039 SIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSI----DIFEAFDELLLMKRGGQ 1098
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
403-589 |
2.18e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 59.34 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 403 YPSRKEVKILKGLNLKVQSG-----QTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDirtinvrhlreitgvVSQ 477
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT---------------VSY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 478 EPVLFATTIAENIRYgrenvTMDEIEKAVKEANAYDF-IMKlPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLL 556
Cdd:cd03237 66 KPQYIKADYEGTVRD-----LLSSITKDFYTHPYFKTeIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLL 139
|
170 180 190
....*....|....*....|....*....|....*..
gi 925114634 557 DEATSALDTESEAVVQVAL----DKARKgrTTIVIAH 589
Cdd:cd03237 140 DEPSAYLDVEQRLMASKVIrrfaENNEK--TAFVVEH 174
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1041-1243 |
2.42e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.42 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1041 EVVFNYPtrpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHLGIVSQ 1120
Cdd:PRK13540 6 ELDFDYH---DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1121 EPILFDCSIAENIAYgDNSRVVSHEEIMQAAKEANIHHFIEtlpekYNTRVgdkgtqLSGGQKQRIAIARALVRQPHILL 1200
Cdd:PRK13540 83 SGINPYLTLRENCLY-DIHFSPGAVGITELCRLFSLEHLID-----YPCGL------LSSGQKRQVALLRLWMSKAKLWL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 925114634 1201 LDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNAD 1243
Cdd:PRK13540 151 LDEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1047-1265 |
2.56e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 60.49 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1047 PTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDG-----KEIKHLnvqwlrAHLGIV--- 1118
Cdd:COG4586 30 REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfkRRKEFA------RRIGVVfgq 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1119 -SQepILFDCSIAENIA-----YGdnsrvVSHEEImqaakEANIHHFIETL--PEKYNTRVgdkgTQLSGGQKQRIAIAR 1190
Cdd:COG4586 104 rSQ--LWWDLPAIDSFRllkaiYR-----IPDAEY-----KKRLDELVELLdlGELLDTPV----RQLSLGQRMRCELAA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 1191 ALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQLLAQ 1265
Cdd:COG4586 168 ALLHRPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1054-1258 |
2.95e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.46 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE-RFYDPLA-------GSVLIDGKEIKHLNVQWL---RAHLGIVSQEP 1122
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLarlRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1123 ILFdcSIAENIAYG-----DNSRVVSHEE---IMQAAKEANIhhfietlpekyNTRVGDKGTQLSGGQKQRIAIARAL-- 1192
Cdd:PRK13547 96 FAF--SAREIVLLGryphaRRAGALTHRDgeiAWQALALAGA-----------TALVGRDVTTLSGGELARVQFARVLaq 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 1193 -------VRQPHILLLDEATSALD-TESEKVVQEALDKAREGRT-CIVIAHRLS-TIQNADLIVVFQNGKVKEHGT 1258
Cdd:PRK13547 163 lwpphdaAQPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLgVLAIVHDPNlAARHADRIAMLADGAIVAHGA 238
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1058-1258 |
4.10e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 59.76 E-value: 4.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1058 LSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLR----AHLGIVSQEPIlfdcsI 1129
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRnlvgAEVAMIFQDPM-----T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1130 AENIAYgdnsrVVSHEeIMQA-------AKEANIHHFIETLpekynTRVG--DKGT-------QLSGGQKQRIAIARALV 1193
Cdd:PRK11022 101 SLNPCY-----TVGFQ-IMEAikvhqggNKKTRRQRAIDLL-----NQVGipDPASrldvyphQLSGGMSQRVMIAMAIA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 1194 RQPHILLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTI-QNADLIVVFQNGKVKEHGT 1258
Cdd:PRK11022 170 CRPKLLIADEPTTALDvTIQAQIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAGQVVETGK 237
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
129-347 |
4.48e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 59.50 E-value: 4.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 129 VAAYIQVSFWCLAAGRQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSIATFFTGFIV 208
Cdd:cd18565 69 LFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 209 GFTRGWKLTLVILAISPVLGLSAAIWAKILSSftdKELLAYAKAGAVA---EEVLAAIRTVIAFGGQKKELERynknLEE 285
Cdd:cd18565 149 LFYLNWQLALVALLPVPLIIAGTYWFQRRIEP---RYRAVREAVGDLNarlENNLSGIAVIKAFTAEDFERER----VAD 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 286 AKRIGIKKAITAnISIGAAF-----LLIYASYALAFWYGTSLVLSSEYSIGQVLTVffsvliGAFSI 347
Cdd:cd18565 222 ASEEYRDANWRA-IRLRAAFfpvirLVAGAGFVATFVVGGYWVLDGPPLFTGTLTV------GTLVT 281
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
374-566 |
4.54e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.73 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 374 KPSIDSYSKSGhkpdniKGNLEFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMV 453
Cdd:PRK11147 306 KMQVEEASRSG------KIVFEMENVNYQIDGKQ---LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 454 -CidGQDIRTINVRHLREITgvvsqEPvlfATTIAENIRYGRENVTMDEIEKAVKeanAY--DFIMKlPNKFDTLVgerg 530
Cdd:PRK11147 377 hC--GTKLEVAYFDQHRAEL-----DP---EKTVMDNLAEGKQEVMVNGRPRHVL---GYlqDFLFH-PKRAMTPV---- 438
|
170 180 190
....*....|....*....|....*....|....*.
gi 925114634 531 AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 566
Cdd:PRK11147 439 KALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1055-1258 |
5.20e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 58.57 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1055 LQGLSLEVKKG-----QTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHlNVQWLRAHL-GIVSQepILFDCS 1128
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY-KPQYIKADYeGTVRD--LLSSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1129 iaeNIAYGDNSRVVsheEIMQAAKeanihhfIETLpekYNTRVgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1208
Cdd:cd03237 87 ---KDFYTHPYFKT---EIAKPLQ-------IEQI---LDREV----PELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 1209 DTESE----KVVQEALDKARegRTCIVIAHRLSTIQN-ADLIVVFQnGKVKEHGT 1258
Cdd:cd03237 147 DVEQRlmasKVIRRFAENNE--KTAFVVEHDIIMIDYlADRLIVFE-GEPSVNGV 198
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
123-343 |
5.75e-09 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 58.76 E-value: 5.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 123 IGAGVLVAAYIQVSFWCL-------AAGRQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLtDDVSKINEGIGDKIGMF 195
Cdd:cd18782 44 IGVVMLVAALLEAVLTALrtylftdTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTGTALTT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 196 FQSIATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAfggQKKE 275
Cdd:cd18782 123 LLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKA---QNAE 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 276 L-------ERYNKNLEEAKRIGIKKAITANISigaaFLLIYASYALAFWYGTSLVLSSEYSIGQVLTvfFSVLIG 343
Cdd:cd18782 200 LkarwrwqNRYARSLGEGFKLTVLGTTSGSLS----QFLNKLSSLLVLWVGAYLVLRGELTLGQLIA--FRILSG 268
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
122-345 |
8.28e-09 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 58.29 E-value: 8.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 122 GIGAGVLVAAYIQVSFwclAAGRQILKIRKQFFHAIMRQEIG--------WFDVHDVGELNTRLtDDVSKINEGIGDKIG 193
Cdd:cd18555 45 GIGILILFLLYGLFSF---LRGYIIIKLQTKLDKSLMSDFFEhllklpysFFENRSSGDLLFRA-NSNVYIRQILSNQVI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 194 MFFQSIATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQK 273
Cdd:cd18555 121 SLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEK 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 274 KELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTSLVLSSEYSIGQVLTvfFSVLIGAF 345
Cdd:cd18555 201 NIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGELTLGELIA--FSSLAGSF 270
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1154-1246 |
9.61e-09 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 57.62 E-value: 9.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1154 ANIHHFIETLPE---KYnTRVGDKGTQLSGGQKQRIAIARALVRQ---PHILLLDEATSALDTESEKVVQEALDKARE-G 1226
Cdd:cd03271 144 PKIARKLQTLCDvglGY-IKLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkG 222
|
90 100
....*....|....*....|
gi 925114634 1227 RTCIVIAHRLSTIQNADLIV 1246
Cdd:cd03271 223 NTVVVIEHNLDVIKCADWII 242
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
403-567 |
9.96e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.36 E-value: 9.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 403 YPSRKevKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGmvcidgqdirtiNVRHLREIT-GVVSQEPVL 481
Cdd:PRK11819 16 VPPKK--QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG------------EARPAPGIKvGYLPQEPQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 482 FAT-TIAENIRYGrenvtMDEIEKAVKEANAYDFIMKLPN-KFDTLVGERG----------------------------- 530
Cdd:PRK11819 82 DPEkTVRENVEEG-----VAEVKAALDRFNEIYAAYAEPDaDFDALAAEQGelqeiidaadawdldsqleiamdalrcpp 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 925114634 531 -----AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 567
Cdd:PRK11819 157 wdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1051-1265 |
1.54e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.87 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1051 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQ---------WLRAHLGIVSQE 1121
Cdd:PRK10938 15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEqlqklvsdeWQRNNTDMLSPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1122 PILFDCSIAENIAYG--DNSRVvsheeiMQAAKEANIHHFIETlPEKYntrvgdkgtqLSGGQKQRIAIARALVRQPHIL 1199
Cdd:PRK10938 95 EDDTGRTTAEIIQDEvkDPARC------EQLAQQFGITALLDR-RFKY----------LSTGETRKTLLCQALMSEPDLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 1200 LLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQLLAQ 1265
Cdd:PRK10938 158 ILDEPFDGLDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
417-621 |
1.57e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 417 LKVQSGQTVALVGNSGCGKSTTVQLMQR--LYDptDGMVCIDgQDIRtinVRHL-----REITGVVsqepvlFATtIAEN 489
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGevLLD--DGRIIYE-QDLI---VARLqqdppRNVEGTV------YDF-VAEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 490 I--------RYGR--ENVTMDEIEKAVKE----------ANAYDF-------IMKLPNKFDTLVGErgaqLSGGQKQRIA 542
Cdd:PRK11147 91 IeeqaeylkRYHDisHLVETDPSEKNLNElaklqeqldhHNLWQLenrinevLAQLGLDPDAALSS----LSGGWLRKAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 543 IARALVRNPKILLLDEATSALDTESEAVVQVALdKARKGrTTIVIAHRLSTVRN-ADVIAGFDDGVIVE-KGNHDELMKE 620
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRIVDLDRGKLVSyPGNYDQYLLE 244
|
.
gi 925114634 621 K 621
Cdd:PRK11147 245 K 245
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1059-1263 |
1.70e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.77 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1059 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNV-QWLRAhlGIV------SQEPILFDCSIAE 1131
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPrDAIRA--GIMlcpedrKAEGIIPVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1132 NIAYGDNSRVVSHEEIMQAAKEA-NIHHFIETLPEKynTRVGD-KGTQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1209
Cdd:PRK11288 351 NINISARRHHLRAGCLINNRWEAeNADRFIRSLNIK--TPSREqLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 925114634 1210 TESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGKV-----KEHGTHQQLL 1263
Cdd:PRK11288 429 VGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIagelaREQATERQAL 489
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1062-1234 |
1.72e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.03 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1062 VKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGkeikhlnvQWlraHLGIVSQEPILFDCSIAENIAYGDNS-R 1140
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG--------NW---QLAWVNQETPALPQPALEYVIDGDREyR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1141 VVshEEIMQAAKEANIHHFIETLPEKYNT---------------RVGDKGTQL-------SGGQKQRIAIARALVRQPHI 1198
Cdd:PRK10636 93 QL--EAQLHDANERNDGHAIATIHGKLDAidawtirsraasllhGLGFSNEQLerpvsdfSGGWRMRLNLAQALICRSDL 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 925114634 1199 LLLDEATSALDTESEKVVQEALdKAREGrTCIVIAH 1234
Cdd:PRK10636 171 LLLDEPTNHLDLDAVIWLEKWL-KSYQG-TLILISH 204
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
717-872 |
2.09e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 57.11 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 717 IFCAIINGGLQPAFSIIFSRII--GIFTRDEDPETKrqnsnmFSVLFLVLGIISFITFFLQGFTFGKAGEILTKRLRYMV 794
Cdd:cd18550 5 LLLILLSALLGLLPPLLLREIIddALPQGDLGLLVL------LALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQL 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 795 FRSMLRQDVSWFDDPKntTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAI 872
Cdd:cd18550 79 YAHLQRMSLAFFTRTR--TGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVL 154
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
396-592 |
2.36e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 58.61 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 396 FKNVHFSYPSRKevKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQ--------RLYDPTDGMVCIdgqdirtinvrh 467
Cdd:TIGR00954 454 FENIPLVTPNGD--VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLFY------------ 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 468 lreitgvVSQEPVLFATTIAENIRYgrENVTMDEIEKAVKEAnayDFIMKLPN-KFDTLVGERGA---------QLSGGQ 537
Cdd:TIGR00954 520 -------VPQRPYMTLGTLRDQIIY--PDSSEDMKRRGLSDK---DLEQILDNvQLTHILEREGGwsavqdwmdVLSGGE 587
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 538 KQRIAIARALVRNPKILLLDEATSALDTESE-AVVQVAldkARKGRTTIVIAHRLS 592
Cdd:TIGR00954 588 KQRIAMARLFYHKPQFAILDECTSAVSVDVEgYMYRLC---REFGITLFSVSHRKS 640
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1048-1209 |
2.46e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.14 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1048 TRPDIPVLQ----------GLSLEVKKGQTLALVGSSGCGKStvvQLLERFY---DPLAGSVLIDGKEIKHLNVQwLRAH 1114
Cdd:PRK15439 262 QAAGAPVLTvedltgegfrNISLEVRAGEILGLAGVVGAGRT---ELAETLYglrPARGGRIMLNGKEINALSTA-QRLA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1115 LGIV-----SQEPILF-DCSIAENI---AYGDNSRvvsheeIMQAAKEANIHhfietlpEKYNTRVGDKGTQ-------L 1178
Cdd:PRK15439 338 RGLVylpedRQSSGLYlDAPLAWNVcalTHNRRGF------WIKPARENAVL-------ERYRRALNIKFNHaeqaartL 404
|
170 180 190
....*....|....*....|....*....|.
gi 925114634 1179 SGGQKQRIAIARALVRQPHILLLDEATSALD 1209
Cdd:PRK15439 405 SGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
713-996 |
2.85e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 56.81 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 713 FVVGIFCAIINgglqPAFSIIFSRIIG-----IFTRDED----------PETKRQnsnmfsvLFLVLGIISFITF----- 772
Cdd:cd18565 1 LVLGLLASILN----RLFDLAPPLLIGvaidaVFNGEASflplvpaslgPADPRG-------QLWLLGGLTVAAFllesl 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 773 --FLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDDpkNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGII 850
Cdd:cd18565 70 fqYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFED--RQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 851 ISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKkelEGAGKIATeAIEN----FRTVVSLTREQkFEY--MYAQ 924
Cdd:cd18565 148 ILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVR---EAVGDLNA-RLENnlsgIAVIKAFTAED-FERerVADA 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 925 SLQvpYRNSLRKAHIFGVSFS-ITQAMMYFSYAGCFRFGAYLVANEFMNFQdvllvfsaivfGAMAVGQVSSF 996
Cdd:cd18565 223 SEE--YRDANWRAIRLRAAFFpVIRLVAGAGFVATFVVGGYWVLDGPPLFT-----------GTLTVGTLVTF 282
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1061-1258 |
3.36e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.90 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1061 EVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDgkeikhLNV----QWLRA-HLGIVSQepilFDCSIAENIay 1135
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------LKIsykpQYIKPdYDGTVED----LLRSITDDL-- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1136 gDNSRVVSheEIMQAAKeanihhfIETLPEKYntrVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKV 1215
Cdd:PRK13409 429 -GSSYYKS--EIIKPLQ-------LERLLDKN---VKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 491
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 925114634 1216 VQEALDKAREGR--TCIVIAHRLSTIQN-ADLIVVFqNGKVKEHGT 1258
Cdd:PRK13409 492 VAKAIRRIAEEReaTALVVDHDIYMIDYiSDRLMVF-EGEPGKHGH 536
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1151-1246 |
3.44e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 58.10 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1151 AKEANIHHFIETLPE---KYnTRVGDKGTQLSGGQKQRIAIARALVRQ---PHILLLDEATSALDTESEK----VVQEAL 1220
Cdd:TIGR00630 801 EAVPSISRKLQTLCDvglGY-IRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKklleVLQRLV 879
|
90 100
....*....|....*....|....*.
gi 925114634 1221 DKareGRTCIVIAHRLSTIQNADLIV 1246
Cdd:TIGR00630 880 DK---GNTVVVIEHNLDVIKTADYII 902
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
127-343 |
4.07e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 56.41 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 127 VLVAAYIQVSFWCLAAG--RQILKIR----------KQFFHAIMRQEIGWFDVHDVGELNTRltddvskINEGigDKIGM 194
Cdd:cd18568 43 LILIGLLIVGIFQILLSavRQYLLDYfanridlsllSDFYKHLLSLPLSFFASRKVGDIITR-------FQEN--QKIRR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 195 FF-----QSIATFFTGFIVG---FTRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTV 266
Cdd:cd18568 114 FLtrsalTTILDLLMVFIYLglmFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 267 IAFGGQ----KKELERYNKNLEEAKRiGIKKAITANISIGAAFLLiyaSYALAFWYGTSLVLSSEYSIGQVltVFFSVLI 342
Cdd:cd18568 194 KALAAErpirWRWENKFAKALNTRFR-GQKLSIVLQLISSLINHL---GTIAVLWYGAYLVISGQLTIGQL--VAFNMLF 267
|
.
gi 925114634 343 G 343
Cdd:cd18568 268 G 268
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
102-339 |
4.42e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 56.33 E-value: 4.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 102 TQHFINHLEEEMTTYA-YYYSGIGAGVLVAAYIQVSFWCLAAGRQILK----IRKQFFHAIMRQEIGWFDVHDVGELNTR 176
Cdd:cd18540 25 TKYAIDHFITPGTLDGlTGFILLYLGLILIQALSVFLFIRLAGKIEMGvsydLRKKAFEHLQTLSFSYFDKTPVGWIMAR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 177 LTDDVSKINE----GIGDkigmFFQSIATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAIwakilssFTDKELLAYAKA 252
Cdd:cd18540 105 VTSDTQRLGEiiswGLVD----LVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIY-------FQKKILKAYRKV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 253 GAVAEEVLAA-------IRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTSLVLS 325
Cdd:cd18540 174 RKINSRITGAfnegitgAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLA 253
|
250
....*....|....
gi 925114634 326 SEYSIGQvLTVFFS 339
Cdd:cd18540 254 GAITIGT-LVAFIS 266
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
394-560 |
5.53e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.95 E-value: 5.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVhfsypSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHL----- 468
Cdd:COG1129 257 LEVEGL-----SVGGV--VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAiragi 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 469 ------REITGVVSQEPvlfattIAENI------RYGReNVTMDEiEKAVKEANAY--DFIMKLPNKfDTLVGergaQLS 534
Cdd:COG1129 330 ayvpedRKGEGLVLDLS------IRENItlasldRLSR-GGLLDR-RRERALAEEYikRLRIKTPSP-EQPVG----NLS 396
|
170 180
....*....|....*....|....*.
gi 925114634 535 GGQKQRIAIARALVRNPKILLLDEAT 560
Cdd:COG1129 397 GGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
713-980 |
5.65e-08 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 55.92 E-value: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 713 FVVGIFCAIINGGLqpafSIIFSRIIGIFTRDEDPEtkrQNSNMFSVLFLVLGIISFITFFLQgFTFGKAGEILTKR--- 789
Cdd:cd18549 4 FFLDLFCAVLIAAL----DLVFPLIVRYIIDDLLPS---KNLRLILIIGAILLALYILRTLLN-YFVTYWGHVMGARiet 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 790 -LRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVkgaigSRLA-------VITqnIANLGTGIIISLIYGWQLTL 861
Cdd:cd18549 76 dMRRDLFEHLQKLSFSFFD--NNKTGQLMSRITNDLFDI-----SELAhhgpedlFIS--IITIIGSFIILLTINVPLTL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 862 LLLAIVPIIAIAGVVEMKMLSGQALKDKKELegaGKIATEAIENF---RTVVSLTRE----QKFEYMYAQslqvpYRNSL 934
Cdd:cd18549 147 IVFALLPLMIIFTIYFNKKMKKAFRRVREKI---GEINAQLEDSLsgiRVVKAFANEeyeiEKFDEGNDR-----FLESK 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 925114634 935 RKAH-IFGVSFSITQAMMYFSYAGCFRFGAYLVANEFMNFQDvLLVF 980
Cdd:cd18549 219 KKAYkAMAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGD-LVAF 264
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1048-1211 |
5.78e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.85 E-value: 5.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1048 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNvqwlRA-HLGIVSQEPIL-F 1125
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD----RSrFMAYLGHLPGLkA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1126 DCSIAENIAY--GDNSRvvsHEEIMQAAKEAnihhfIETLPEKYNTRVgdkgTQLSGGQKQRIAIARALVRQPHILLLDE 1203
Cdd:PRK13543 96 DLSTLENLHFlcGLHGR---RAKQMPGSALA-----IVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWLLDE 163
|
....*...
gi 925114634 1204 ATSALDTE 1211
Cdd:PRK13543 164 PYANLDLE 171
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1054-1237 |
5.84e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 55.45 E-value: 5.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLeVKKGQTLALVGSSGCGKSTVVQLLE--------RFYDPLAGSVLID---GKEIKHLNVQWLRAHLGI----- 1117
Cdd:cd03236 16 KLHRLPV-PREGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVivkpq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1118 -VSQEPILFDCSIAENIAYGDNSRVVshEEIMqaaKEANIHHFIETlpekyntrvgdKGTQLSGGQKQRIAIARALVRQP 1196
Cdd:cd03236 95 yVDLIPKAVKGKVGELLKKKDERGKL--DELV---DQLELRHVLDR-----------NIDQLSGGELQRVAIAAALARDA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 925114634 1197 HILLLDEATSALDTESE----KVVQEAldkAREGRTCIVIAHRLS 1237
Cdd:cd03236 159 DFYFFDEPSSYLDIKQRlnaaRLIREL---AEDDNYVLVVEHDLA 200
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
405-566 |
6.29e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.47 E-value: 6.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 405 SRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTIN-VRHLREITGVVSQEPVLFA 483
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDrSRFMAYLGHLPGLKADLST 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 484 TtiaENIRY-----GRENVTMdeiekavkEANAYDfIMKLPNKFDTLVgergAQLSGGQKQRIAIARALVRNPKILLLDE 558
Cdd:PRK13543 100 L---ENLHFlcglhGRRAKQM--------PGSALA-IVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWLLDE 163
|
....*...
gi 925114634 559 ATSALDTE 566
Cdd:PRK13543 164 PYANLDLE 171
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1050-1221 |
7.13e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.88 E-value: 7.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1050 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGK-EIKHLNvQWlRAHLgivsqEPilfDCS 1128
Cdd:PRK11147 330 DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVAYFD-QH-RAEL-----DP---EKT 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1129 IAENIAYGDnsrvvshEEIMQAAKEANIHHFIETL---PEKYNTRVgdkgTQLSGGQKQRIAIARALVRQPHILLLDEAT 1205
Cdd:PRK11147 400 VMDNLAEGK-------QEVMVNGRPRHVLGYLQDFlfhPKRAMTPV----KALSGGERNRLLLARLFLKPSNLLILDEPT 468
|
170
....*....|....*.
gi 925114634 1206 SALDTESEKVVQEALD 1221
Cdd:PRK11147 469 NDLDVETLELLEELLD 484
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1035-1267 |
7.43e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 57.33 E-value: 7.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1035 GNVT----FNEVVFNYPTRPDiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKhLNVQW 1110
Cdd:TIGR01257 1932 GNKTdilrLNELTKVYSGTSS-PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TNISD 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1111 LRAHLGIVSQEPILFDCSIA-ENIAYGDNSRVVSHEEIMQAAKEAnihhfIETLP-EKYNTRVGdkGTqLSGGQKQRIAI 1188
Cdd:TIGR01257 2010 VHQNMGYCPQFDAIDDLLTGrEHLYLYARLRGVPAEEIEKVANWS-----IQSLGlSLYADRLA--GT-YSGGNKRKLST 2081
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1189 ARALVRQPHILLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGKVKEHGTHQQLLAQK 1266
Cdd:TIGR01257 2082 AIALIGCPPLVLLDEPTTGMDPQARRMLWNTIvSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKF 2161
|
.
gi 925114634 1267 G 1267
Cdd:TIGR01257 2162 G 2162
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
404-616 |
7.90e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.46 E-value: 7.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 404 PSRKEVKILKG------LNLKVQSGQTVALVGNSGCGKSttvQLMQRLY---DPTDGMVCIDGQDIRTINVRH-LReiTG 473
Cdd:PRK11288 255 EVRLRLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRS---ELMKLLYgatRRTAGQVYLDGKPIDIRSPRDaIR--AG 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 VV------SQEPVLFATTIAENIRYG--RENVTMDEIEKAVKEA-NAYDFIMKL----PNKfDTLVGergaQLSGGQKQR 540
Cdd:PRK11288 330 IMlcpedrKAEGIIPVHSVADNINISarRHHLRAGCLINNRWEAeNADRFIRSLniktPSR-EQLIM----NLSGGNQQK 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 541 IAIARALVRNPKILLLDEATSALD--TESEaVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDE 616
Cdd:PRK11288 405 AILGRWLSEDMKVILLDEPTRGIDvgAKHE-IYNVIYELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQ 482
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
753-971 |
9.03e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 55.28 E-value: 9.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 753 NSNMFSVLFLVLGIISFITF-----FLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLaNDAAQV 827
Cdd:cd18566 35 NESIPTLQVLVIGVVIAILLesllrLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFE--REPSGAHLERL-NSLEQI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 828 KGAIGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSgQALKDKKELEGA-GKIATEAIENF 906
Cdd:cd18566 112 REFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILR-RALKERSRADERrQNFLIETLTGI 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 907 RTVVSLTREQ----KFEYMYAQSLQVPYRNSLRKAHIFGVSFSITQAMMyfsyAGCFRFGAYLVANEFM 971
Cdd:cd18566 191 HTIKAMAMEPqmlrRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSM----VAVVAFGALLVINGDL 255
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
415-591 |
1.20e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 56.56 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 415 LNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTiNVRHLREITGVVSQEPVLfattiaENIRYGR 494
Cdd:TIGR01257 1958 LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAI------DDLLTGR 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 495 EN---------VTMDEIEKAvkeANAYDFIMKLPNKFDTLVGergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 565
Cdd:TIGR01257 2031 EHlylyarlrgVPAEEIEKV---ANWSIQSLGLSLYADRLAG----TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 2103
|
170 180
....*....|....*....|....*..
gi 925114634 566 ESEAVV-QVALDKARKGRTTIVIAHRL 591
Cdd:TIGR01257 2104 QARRMLwNTIVSIIREGRAVVLTSHSM 2130
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
710-872 |
1.51e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 54.41 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 710 WPYFVVGIFCAIINGGLQPAFSIIFSRIIGIFTRDEDPETKrqnsNMFSVLFLVLGIISFITFFLQGFTFGKAGEILTKR 789
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGL----TGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 790 LRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPI 869
Cdd:cd18540 77 LRKKAFEHLQTLSFSYFD--KTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPV 154
|
...
gi 925114634 870 IAI 872
Cdd:cd18540 155 LAV 157
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1053-1264 |
2.03e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.01 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1053 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAHlGIV------SQEPILFD 1126
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLAN-GIVyisedrKRDGLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1127 CSIAENI---AYGDNSRVVSHeeIMQAAKEANIHHFIETLPEKYNTRVGDKGTqLSGGQKQRIAIARALVRQPHILLLDE 1203
Cdd:PRK10762 345 MSVKENMsltALRYFSRAGGS--LKHADEQQAVSDFIRLFNIKTPSMEQAIGL-LSGGNQQKVAIARGLMTRPKVLILDE 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 1204 ATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQN-ADLIVVFQNGKV-----KEHGTHQQLLA 1264
Cdd:PRK10762 422 PTRGVDVGAKKEIYQLINQFKaEGLSIILVSSEMPEVLGmSDRILVMHEGRIsgeftREQATQEKLMA 489
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1061-1258 |
2.21e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.18 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1061 EVKKGQTLALVGSSGCGKSTVVQLLerfydplAGSVLIDGKEIkHLNVQwlrahlgiVSQEP----ILFDCSIAENIAYG 1136
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKIL-------AGVLKPDEGEV-DEDLK--------ISYKPqyisPDYDGTVEEFLRSA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1137 DNSRVVSH---EEIMQAAKeanihhfIETLPEKYntrVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTESE 1213
Cdd:COG1245 426 NTDDFGSSyykTEIIKPLG-------LEKLLDKN---VKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 491
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 925114634 1214 KVVQEALDKAREGR--TCIVIAHRLSTIQN-ADLIVVFqNGKVKEHGT 1258
Cdd:COG1245 492 LAVAKAIRRFAENRgkTAMVVDHDIYLIDYiSDRLMVF-EGEPGVHGH 538
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
490-617 |
2.25e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 55.40 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 490 IRYGRENVTmDEIEKAVKEAnaYDFIMKLPN---KFDTLV---------GERGAQLSGGQKQRIAIARALVR---NPKIL 554
Cdd:TIGR00630 778 VKYKGKNIA-DVLDMTVEEA--YEFFEAVPSisrKLQTLCdvglgyirlGQPATTLSGGEAQRIKLAKELSKrstGRTLY 854
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 555 LLDEATSALDTESEA----VVQVALDKarkGRTTIVIAHRLSTVRNADVI------AGFDDGVIVEKGNHDEL 617
Cdd:TIGR00630 855 ILDEPTTGLHFDDIKklleVLQRLVDK---GNTVVVIEHNLDVIKTADYIidlgpeGGDGGGTVVASGTPEEV 924
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1145-1212 |
2.38e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.12 E-value: 2.38e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 1145 EEIMQAAKEANIHHFIET------LPEkyntrvGD-KGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1212
Cdd:PRK11819 130 QEIIDAADAWDLDSQLEIamdalrCPP------WDaKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1048-1255 |
2.46e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.79 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1048 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKStvvQLLERFY--DPLA-GSVLIDGKEIKHLN-VQWLRAHLGIVSQ--- 1120
Cdd:PRK09700 272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFgvDKRAgGEIRLNGKDISPRSpLDAVKKGMAYITEsrr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1121 EPILF-DCSIAENIA---------YGDNSRVVSHEEIMQAAKEANihhfiETLPEKYNTrVGDKGTQLSGGQKQRIAIAR 1190
Cdd:PRK09700 349 DNGFFpNFSIAQNMAisrslkdggYKGAMGLFHEVDEQRTAENQR-----ELLALKCHS-VNQNITELSGGNQQKVLISK 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1191 ALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNA-DLIVVFQNGKVKE 1255
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1050-1212 |
2.51e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.94 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1050 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydplAGsvlIDgKEIkhLNVQWLR--AHLGIVSQEPILfDC 1127
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AG---VD-KDF--NGEARPQpgIKVGYLPQEPQL-DP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1128 S--IAENI-------------------AYGDNS--------RVVSHEEIMQAAKEANIHHFIETLPEKYNTRVGD-KGTQ 1177
Cdd:TIGR03719 82 TktVRENVeegvaeikdaldrfneisaKYAEPDadfdklaaEQAELQEIIDAADAWDLDSQLEIAMDALRCPPWDaDVTK 161
|
170 180 190
....*....|....*....|....*....|....*
gi 925114634 1178 LSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1212
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1051-1243 |
2.65e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1051 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL-----ERFYDPLA------GSvlidGKEIkhlnvqW-LRAHLGIV 1118
Cdd:PRK10938 272 DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpQGYSNDLTlfgrrrGS----GETI------WdIKKHIGYV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1119 SQEPIL---FDCSIAENIAYG--DN---SRVVSHEEIMQAAKEANIHHFietlpekyNTRVGDKGTQ-LSGGQkQRIA-I 1188
Cdd:PRK10938 342 SSSLHLdyrVSTSVRNVILSGffDSigiYQAVSDRQQKLAQQWLDILGI--------DKRTADAPFHsLSWGQ-QRLAlI 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1189 ARALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRT--------------CivIAHRLSTIQNAD 1243
Cdd:PRK10938 413 VRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETqllfvshhaedapaC--ITHRLEFVPDGD 480
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1037-1217 |
2.80e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.87 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1037 VTFNEVVFNYPTRPDIpvLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVL--------------IDGKE 1102
Cdd:PLN03073 509 ISFSDASFGYPGGPLL--FKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavfsqhhVDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1103 IKHLNV------------QWLRAHLGivsqepilfDCSIAENIAygdnsrvvsheeimqaakeanihhfietLPEKYNtr 1170
Cdd:PLN03073 587 LSSNPLlymmrcfpgvpeQKLRAHLG---------SFGVTGNLA----------------------------LQPMYT-- 627
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 925114634 1171 vgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTES-EKVVQ 1217
Cdd:PLN03073 628 -------LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
198-346 |
3.47e-07 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 53.27 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 198 SIATFFTG---------------FIVGFTRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAA 262
Cdd:cd18588 110 SIRQFLTGsaltlvldlvfsvvfLAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 263 IRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTSLVLSSEYSIGQVltVFFSVLI 342
Cdd:cd18588 190 IETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGELTIGQL--IAFNMLA 267
|
....
gi 925114634 343 GAFS 346
Cdd:cd18588 268 GQVS 271
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
385-609 |
3.81e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 54.45 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 385 HKPDNIKGN-LEFKNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPT-DGMVCIDGQ--DI 460
Cdd:TIGR02633 248 HEPHEIGDViLEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDI 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 461 RT---------INVRHLREITGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPNKFDTLvgergA 531
Cdd:TIGR02633 328 RNpaqairagiAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPI-----G 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 532 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQVALDKARKGRTTIVIAHRLSTVrnadviAGFDDGVIV 609
Cdd:TIGR02633 403 RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYeIYKLINQLAQEGVAIIVVSSELAEV------LGLSDRVLV 475
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
102-351 |
5.76e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 52.89 E-value: 5.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 102 TQHFINHLEEEMTTYAYYYSGIGAGVLVAAYIQVSFW----CLAAGRqilKIRKQFFHAIMRQEIGWFDVHDVGELNTRL 177
Cdd:cd18580 26 SSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLfvlaGLRASR---RLHDKLLRSVLRAPMSFFDTTPSGRILNRF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 178 TDDVSKINEGIGDKIGMFFQSIATFFTGFIV-GFTRGWkltlVILAISPVLGLSAAIW----------------AK--IL 238
Cdd:cd18580 103 SKDIGLIDEELPLALLDFLQSLFSVLGSLIViAIVSPY----FLIVLPPLLVVYYLLQryylrtsrqlrrleseSRspLY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 239 SSFTdkellayakagavaeEVLAAIRTVIAFGGQKKELERYNKNLeeakrigikkaitaNISIGAAFLLIYASYALAFWY 318
Cdd:cd18580 179 SHFS---------------ETLSGLSTIRAFGWQERFIEENLRLL--------------DASQRAFYLLLAVQRWLGLRL 229
|
250 260 270
....*....|....*....|....*....|...
gi 925114634 319 gtslvlsseysigQVLTVFFSVLIGAFSIGQAS 351
Cdd:cd18580 230 -------------DLLGALLALVVALLAVLLRS 249
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
712-872 |
6.65e-07 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 52.47 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 712 YFVVGIFCAIINGGLQPAFSIIFSRIIgiftrDEDPETKRQNS-NMFSVLFLVLGIISFITFFLQGFTFGKAGEILTKRL 790
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAI-----DEYIPNGDLSGlLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 791 RYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLgTGIIISLIY-GWQLTLLLLAIVPI 869
Cdd:cd18545 76 RQDLFSHLQKLSFSFFD--SRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTL-VGIVIIMFSlNVRLALVTLAVLPL 152
|
...
gi 925114634 870 IAI 872
Cdd:cd18545 153 LVL 155
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
394-623 |
6.98e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.36 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMV----------CidGQDirti 463
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenanigyY--AQD---- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 464 nvrHLREITGVVSqepvLFA-----TTIAEN---IR--YGRENVTMDEIEKAVKeanaydfimklpnkfdtlvgergaQL 533
Cdd:PRK15064 391 ---HAYDFENDLT----LFDwmsqwRQEGDDeqaVRgtLGRLLFSQDDIKKSVK------------------------VL 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 534 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKArKGrTTIVIAH------RLSTvrnaDVIAGFDDGV 607
Cdd:PRK15064 440 SGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdrefvsSLAT----RIIEITPDGV 513
|
250
....*....|....*.
gi 925114634 608 IVEKGNHDELMKEKGI 623
Cdd:PRK15064 514 VDFSGTYEEYLRSQGI 529
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
407-594 |
7.22e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.96 E-value: 7.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 407 KEVKILKGLNLKVQSGQTVALVGNSGCGKST-----TVQLMQRLYDpTDGMVCIDGQDIRTInVRHLREITGVVSQEPVL 481
Cdd:TIGR00956 72 KTFDILKPMDGLIKPGELTVVLGRPGSGCSTllktiASNTDGFHIG-VEGVITYDGITPEEI-KKHYRGDVVYNAETDVH 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 482 FAT-TIAE-----------NIRYgrENVtmDEIEKAVKEANAYDFIMKLPNKFDTLVGE---RGaqLSGGQKQRIAIARA 546
Cdd:TIGR00956 150 FPHlTVGEtldfaarcktpQNRP--DGV--SREEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEA 223
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 925114634 547 LVRNPKILLLDEATSALDTESeavvqvALDKARKGRTTIVIAHRLSTV 594
Cdd:TIGR00956 224 SLGGAKIQCWDNATRGLDSAT------ALEFIRALKTSANILDTTPLV 265
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
387-572 |
1.07e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 387 PDNIKGN--LEFKNVHFSYPSRKevKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVcidgqdIRTIN 464
Cdd:PLN03073 500 PDDRPGPpiISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV------FRSAK 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 465 VRhlreiTGVVSQEPVLFATTIAENIRYgrenvtMDEIEKAVKEanaydfiMKLPNKFDT--LVGERGAQ----LSGGQK 538
Cdd:PLN03073 572 VR-----MAVFSQHHVDGLDLSSNPLLY------MMRCFPGVPE-------QKLRAHLGSfgVTGNLALQpmytLSGGQK 633
|
170 180 190
....*....|....*....|....*....|....*
gi 925114634 539 QRIAIARALVRNPKILLLDEATSALDTES-EAVVQ 572
Cdd:PLN03073 634 SRVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1054-1220 |
1.09e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.86 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIdGKEIKhlnvqwlrahLGIVSQepilfdcsiaeni 1133
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIK----------LGYFAQ------------- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1134 aygdnsrvvsHEEIMQAAKEANIHHFIETLPEKYNTRV----------GDKGT----QLSGGQKQRIAIARALVRQPHIL 1199
Cdd:PRK10636 383 ----------HQLEFLRADESPLQHLARLAPQELEQKLrdylggfgfqGDKVTeetrRFSGGEKARLVLALIVWQRPNLL 452
|
170 180
....*....|....*....|.
gi 925114634 1200 LLDEATSALDTESEKVVQEAL 1220
Cdd:PRK10636 453 LLDEPTNHLDLDMRQALTEAL 473
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1072-1245 |
1.15e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 50.64 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1072 GSSGCGKSTVVQLLERFYDPLAGSVLIDGKEIKHLNVQWLRAhlgIVSQEPILFDCSIAENIAYGdnSRVVSHEEIMQAA 1151
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTY---IGHNLGLKLEMTVFENLKFW--SEIYNSAETLYAA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1152 keanIHHFietlpeKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALD-KAREGRTCI 1230
Cdd:PRK13541 108 ----IHYF------KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANSGGIVL 177
|
170
....*....|....*
gi 925114634 1231 VIAHRLSTIQNADLI 1245
Cdd:PRK13541 178 LSSHLESSIKSAQIL 192
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1177-1248 |
1.32e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.86 E-value: 1.32e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 1177 QLSGGQKQRIAIARALVRQPHILLLDEATSALD----TESEKVVQEAldkAREGRTCIVIAHRLSTIQN-ADLIVVF 1248
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrLNVARLIREL---AEEGKYVLVVEHDLAILDYlADYVHIL 285
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
532-593 |
1.77e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.48 E-value: 1.77e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 925114634 532 QLSGGQKQRIAIARALVRNPKILLLDEATSALD-TESEAVVQVALDKARKGRTTIVIAHRLST 593
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiYQRLNVARLIRELAEEGKYVLVVEHDLAI 274
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1178-1248 |
4.91e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.47 E-value: 4.91e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 925114634 1178 LSGGQKQRIAIARALVRQPH--ILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIVVF 1248
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1053-1268 |
5.20e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.66 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1053 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydplAGSVLIDGKEIKhlnvqWL-RAHLGIVSQEP--------I 1123
Cdd:PRK15064 333 PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL-------VGELEPDSGTVK-----WSeNANIGYYAQDHaydfendlT 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1124 LFDCsIAENIAYGDNSRVV---------SHEEIMQAAKeanihhfietlpekyntrvgdkgtQLSGGQKQRIAIARALVR 1194
Cdd:PRK15064 401 LFDW-MSQWRQEGDDEQAVrgtlgrllfSQDDIKKSVK------------------------VLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1195 QPHILLLDEATSALDTESEKVVQEALDKArEGrTCIVIAH------RLSTiqnaDLIVVFQNGKVKEHGTHQQLLAQKGI 1268
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdrefvsSLAT----RIIEITPDGVVDFSGTYEEYLRSQGI 529
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1051-1238 |
6.19e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 50.32 E-value: 6.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1051 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGSVLIdGKEIKHLNVQWLRAHLgivsqEPilfDCSIA 1130
Cdd:TIGR03719 334 DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVDQSRDAL-----DP---NKTVW 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1131 ENIAYGDNSRVVSHEEIMQAAkeanihhfietlpekYNTRVGDKGT-------QLSGGQKQRIAIARALVRQPHILLLDE 1203
Cdd:TIGR03719 405 EEISGGLDIIKLGKREIPSRA---------------YVGRFNFKGSdqqkkvgQLSGGERNRVHLAKTLKSGGNVLLLDE 469
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 925114634 1204 ATSALDTESEKVVQEALDKAreGRTCIVIAH------RLST 1238
Cdd:TIGR03719 470 PTNDLDVETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1062-1247 |
6.88e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.19 E-value: 6.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1062 VKKGQTLALVGSSGCGKSTVVQLL---------------------ERFydplAGSVLID------GKEIK-HLNVQWlra 1113
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILsgelipnlgdyeeepswdevlKRF----RGTELQNyfkklyNGEIKvVHKPQY--- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1114 hlgiVSQEPILFDCSIAENIAYGDNSRVVshEEImqaAKEANIHHFIetlpekyntrvgDKG-TQLSGGQKQRIAIARAL 1192
Cdd:PRK13409 169 ----VDLIPKVFKGKVRELLKKVDERGKL--DEV---VERLGLENIL------------DRDiSELSGGELQRVAIAAAL 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 1193 VRQPHILLLDEATSALDtesekvVQEALDKAR------EGRTCIVIAHRLSTIQN-ADLIVV 1247
Cdd:PRK13409 228 LRDADFYFFDEPTSYLD------IRQRLNVARlirelaEGKYVLVVEHDLAVLDYlADNVHI 283
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
490-600 |
1.29e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.83 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 490 IRYGRENVTmDEIEKAVKEANayDFIMKLP---NKFDTL---------VGERGAQLSGGQKQRIAIARAL---VRNPKIL 554
Cdd:PRK00635 758 VRYKGKNIA-DILEMTAYEAE--KFFLDEPsihEKIHALcslgldylpLGRPLSSLSGGEIQRLKLAYELlapSKKPTLY 834
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 925114634 555 LLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTVRNADVI 600
Cdd:PRK00635 835 VLDEPTTGLHTHDiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYV 881
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
513-564 |
1.33e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.23 E-value: 1.33e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 513 DFIM----KLPNKfDTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSALD 564
Cdd:PRK10762 377 DFIRlfniKTPSM-EQAIGL----LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1047-1209 |
1.35e-05 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 47.64 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1047 PTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKST----VVQLLERFYDPlAGSVLIDGKEIKHLNVQWlRAHLGIVSQEp 1122
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKEFAEKY-PGEIIYVSEE- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1123 ilfDCSIAEniaygdnsrvVSHEEIMQAAKEANIHHFIetlpekyntrvgdKGtqLSGGQKQRIAIARALVRQPHILLLD 1202
Cdd:cd03233 92 ---DVHFPT----------LTVRETLDFALRCKGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLCWD 143
|
....*..
gi 925114634 1203 EATSALD 1209
Cdd:cd03233 144 NSTRGLD 150
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
394-564 |
1.77e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.77 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD-PTDGMVCIDGQDIRTINVRHL---- 468
Cdd:PRK13549 260 LEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAiaqg 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 469 -------REITGVVSQEPVLFATTIAENIRYGRENVtmdeIEKAVKEANAYDFIMKLPNKFDTLVgERGAQLSGGQKQRI 541
Cdd:PRK13549 340 iamvpedRKRDGIVPVMGVGKNITLAALDRFTGGSR----IDDAAELKTILESIQRLKVKTASPE-LAIARLSGGNQQKA 414
|
170 180
....*....|....*....|...
gi 925114634 542 AIARALVRNPKILLLDEATSALD 564
Cdd:PRK13549 415 VLAKCLLLNPKILILDEPTRGID 437
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1178-1249 |
1.78e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.80 E-value: 1.78e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 1178 LSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQ 1249
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
117-233 |
1.85e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 48.23 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 117 AYY---YSGIGAGVLVAAYIQVSFWC---LAAGRqilKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGD 190
Cdd:cd18604 43 LYYlgiYALISLLSVLLGTLRYLLFFfgsLRASR---KLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELAD 119
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 925114634 191 KIGMFFQSIATFFTGFIvgftrgwkltlVILAISPVLGLSAAI 233
Cdd:cd18604 120 SLSSLLESTLSLLVILI-----------AIVVVSPAFLLPAVV 151
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
394-600 |
2.30e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.79 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYpsrkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTInvrhlreitg 473
Cdd:PRK13541 2 LSLHQLQFNI----EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 vvsQEPvlFATTIAENIRYGREnvtMDEIEKAVKEANAYDFIMKLPN-----KFDTLVGERGAQLSGGQKQRIAIARALV 548
Cdd:PRK13541 68 ---AKP--YCTYIGHNLGLKLE---MTVFENLKFWSEIYNSAETLYAaihyfKLHDLLDEKCYSLSSGMQKIVAIARLIA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 925114634 549 RNPKILLLDEATSALDTESEAVV-QVALDKARKGRTTIVIAHRLSTVRNADVI 600
Cdd:PRK13541 140 CQSDLWLLDEVETNLSKENRDLLnNLIVMKANSGGIVLLSSHLESSIKSAQIL 192
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
422-615 |
2.66e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.70 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 422 GQTVALVGNSGCGKSTTVQLM------------QRLY-------DPTDGMVCIDGQDIRtiNVRHLREITGVVSQEPVLF 482
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRYMamhaidgipkncQILHveqevvgDDTTALQCVLNTDIE--RTQLLEEEAQLVAQQRELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 483 ATTIAENIRyGRENVTMDE----------------IEKAVKEANAYDFIMKLPNKFDTLVgERGAQLSGGQKQRIAIARA 546
Cdd:PLN03073 281 FETETGKGK-GANKDGVDKdavsqrleeiykrlelIDAYTAEARAASILAGLSFTPEMQV-KATKTFSGGWRMRIALARA 358
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 547 LVRNPKILLLDEATSALDTESEAVVQVALDKARKgrTTIVIAHR---LSTVRnADVIAGFDDGVIVEKGNHD 615
Cdd:PLN03073 359 LFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK--TFIVVSHArefLNTVV-TDILHLHGQKLVTYKGDYD 427
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
419-591 |
3.26e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.27 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 419 VQSGQTVALVGNSGCGKSTTV-----QLMQRLYDPTDGmVCIDgqdirtiNVrhLREITGVVSQEpvLFATTIAENIRYG 493
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVkilsgELIPNLGDYEEE-PSWD-------EV--LKRFRGTELQN--YFKKLYNGEIKVV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 494 RENVTMDEIEKAVKeANAYDFIMKLP--NKFDTLVGERG---------AQLSGGQKQRIAIARALVRNPKILLLDEATSA 562
Cdd:PRK13409 164 HKPQYVDLIPKVFK-GKVRELLKKVDerGKLDEVVERLGlenildrdiSELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180
....*....|....*....|....*....
gi 925114634 563 LDTESEAVVQVALDKARKGRTTIVIAHRL 591
Cdd:PRK13409 243 LDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
412-647 |
4.00e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 46.73 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 412 LKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQ-DIRTINVRHLREITGVvsqepvlfattiaENI 490
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvSVIAISAGLSGQLTGI-------------ENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 491 RYGR--ENVTMDEIEKAVKEANAY----DFIMKLPNKFdtlvgergaqlSGGQKQRIAIARALVRNPKILLLDEATSALD 564
Cdd:PRK13546 107 EFKMlcMGFKRKEIKAMTPKIIEFselgEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 565 tesEAVVQVALDK----ARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQTRGNEIEL 639
Cdd:PRK13546 176 ---QTFAQKCLDKiyefKEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPKYEAFLNDFKKKSKAEQKEF 252
|
....*...
gi 925114634 640 ENATGESK 647
Cdd:PRK13546 253 RNKLDESR 260
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
532-603 |
4.02e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 45.43 E-value: 4.02e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 532 QLSGGQKQRIAIARAL----VRNPKILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGF 603
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDgQALAEAILEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
754-872 |
4.19e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 47.08 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 754 SNMFSVLFLVLGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpknTT--GALTTRLANDAAQVKGAI 831
Cdd:cd18606 34 QGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFD----TTplGRILNRFSKDTDVLDNEL 109
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 925114634 832 GSRLAVITQNIANLGTGIIISLIYgwqLTLLLLAIVPIIAI 872
Cdd:cd18606 110 PDSLRMFLYTLSSIIGTFILIIIY---LPWFAIALPPLLVL 147
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
717-968 |
4.43e-05 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 46.82 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 717 IFCAIINGGLQPAFSIIFSRIIG--IFTRDEDpetkrqNSNMFSVLFLVLGIISFITFFLQGFTFGKAGEILTKRLRYMV 794
Cdd:cd18782 8 LALSFVVQLLGLANPLLFQVIIDkvLVQQDLA------TLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 795 FRSMLRQDVSWFDdpKNTTGALTTRLaNDAAQVKG-AIGSRLAVITQNIANLGTgIIISLIYGWQLTLLLLAIVPIIAIA 873
Cdd:cd18782 82 IDHLLRLPLGFFD--KRPVGELSTRI-SELDTIRGfLTGTALTTLLDVLFSVIY-IAVLFSYSPLLTLVVLATVPLQLLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 874 GVVEMKMLsgQALKDKKELEGAGKIA--TEAIENFRTVVSLTRE----QKFEYMYAQSLQVPYRNSLRKAHIFGVSFSIT 947
Cdd:cd18782 158 TFLFGPIL--RRQIRRRAEASAKTQSylVESLTGIQTVKAQNAElkarWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLN 235
|
250 260
....*....|....*....|.
gi 925114634 948 QammyFSYAGCFRFGAYLVAN 968
Cdd:cd18782 236 K----LSSLLVLWVGAYLVLR 252
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
122-345 |
5.32e-05 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 46.77 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 122 GIGAGVLVAAYIQVSF---WCLAAGRQILKIR--KQFFHAIMRQEIGWFDVHDVGELNTRLTDdVSKINEGIGDkigmff 196
Cdd:cd18779 45 GLGLAALVLTQLLAGLlrsHLLLRLRTRLDTQltLGFLEHLLRLPYRFFQQRSTGDLLMRLSS-NATIRELLTS------ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 197 QSIATFFTG-FIVGFTrgwkltLVILAISP-----VLGLSAAIWAKILSSF------TDKELLAYAKAGAVAEEVLAAIR 264
Cdd:cd18779 118 QTLSALLDGtLVLGYL------ALLFAQSPllglvVLGLAALQVALLLATRrrvrelMARELAAQAEAQSYLVEALSGIE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 265 TVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTSLVLSSEYSIGQVLTvfFSVLIGA 344
Cdd:cd18779 192 TLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLVLLWVGAWQVLDGQLSLGTMLA--LNALAGA 269
|
.
gi 925114634 345 F 345
Cdd:cd18779 270 F 270
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
196-332 |
6.20e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 46.42 E-value: 6.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 196 FQSIATFFTG---------------FIVGFTRGWKLTLVILAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVL 260
Cdd:cd18566 108 LEQIREFLTGqallalldlpfvlifLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETL 187
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 925114634 261 AAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTSLVLSSEYSIGQ 332
Cdd:cd18566 188 TGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVINGDLTVGA 259
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1142-1252 |
6.97e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.41 E-value: 6.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1142 VSHEEimQAAKEANIHHFIETLPEKYNTRVGD---KGtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTESekvvqe 1218
Cdd:TIGR00956 175 VSREE--YAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT------ 244
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 925114634 1219 ALDKAREGRTCIVIAHRLSTI------QNA----DLIVVFQNGK 1252
Cdd:TIGR00956 245 ALEFIRALKTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGY 288
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
408-622 |
7.70e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 46.65 E-value: 7.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 408 EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVqLMQRLYDPTDGMvcidgQDIR----TINVRHLREITGVvsQEPVLFA 483
Cdd:NF000106 25 EVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGR-----RPWRf*twCANRRALRRTIG*--HRPVR*G 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 484 TTIAENiryGRENVTMD----EIEKAVKEANAYDFIMKLpnKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEA 559
Cdd:NF000106 97 RRESFS---GRENLYMIgr*lDLSRKDARARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 560 TSALD--TESEAVVQVAlDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELMKEKG 622
Cdd:NF000106 172 TTGLDprTRNEVWDEVR-SMVRDGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
141-338 |
7.72e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 46.12 E-value: 7.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 141 AAGRQILKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSIATFFTGFIVGFTRGWKLTLVI 220
Cdd:cd18561 63 AAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALIL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 221 LAISPVLGLSAAIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANIS 300
Cdd:cd18561 143 LVFALLIPLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLS 222
|
170 180 190
....*....|....*....|....*....|....*...
gi 925114634 301 IGAAFLLIYASYALAFWYGTSLVLSSEYSIGQVLTVFF 338
Cdd:cd18561 223 SGIMGLATALGTALALGVGALRVLGGQLTLSSLLLILF 260
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1177-1269 |
8.74e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 8.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1177 QLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARegRTCIVIAHRLStiqnadlivvFQNGKVKE- 1255
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSHARE----------FLNTVVTDi 411
|
90
....*....|....*
gi 925114634 1256 -HGTHQQLLAQKGIY 1269
Cdd:PLN03073 412 lHLHGQKLVTYKGDY 426
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
1170-1246 |
9.18e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.99 E-value: 9.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1170 RVGDKGTQLSGGQKQRIAIARALVRQPH---ILLLDEATSALDTES----EKVVQEALDKareGRTCIVIAHRLSTIQNA 1242
Cdd:PRK00349 823 KLGQPATTLSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDirklLEVLHRLVDK---GNTVVVIEHNLDVIKTA 899
|
....
gi 925114634 1243 DLIV 1246
Cdd:PRK00349 900 DWII 903
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
533-589 |
9.74e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 46.70 E-value: 9.74e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 925114634 533 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDK-AR-KGRTTIVIAH 589
Cdd:COG1245 456 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRfAEnRGKTAMVVDH 514
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
533-588 |
1.01e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 1.01e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 925114634 533 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESE-AVVQVALDKARKGRTTIVIA 588
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIIS 448
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1054-1237 |
1.04e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.76 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1054 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPLAGSVLIDGKEIKhlnvQWLRAHL-GIVSQEPILF-DCSI 1129
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGFPKK----QETFARIsGYCEQNDIHSpQVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1130 AENIAYGDNSRV---VSHEEIMQAAKEanIHHFIEtLPEKYNTRVGDKG-TQLSGGQKQRIAIARALVRQPHILLLDEAT 1205
Cdd:PLN03140 971 RESLIYSAFLRLpkeVSKEEKMMFVDE--VMELVE-LDNLKDAIVGLPGvTGLSTEQRKRLTIAVELVANPSIIFMDEPT 1047
|
170 180 190
....*....|....*....|....*....|...
gi 925114634 1206 SALDTESEKVVQEAL-DKAREGRTCIVIAHRLS 1237
Cdd:PLN03140 1048 SGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPS 1080
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
516-589 |
1.04e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.73 E-value: 1.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 516 MKLPNKFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAH 589
Cdd:PRK13409 441 LQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRiaEEREATALVVDH 512
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
419-591 |
1.19e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.10 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 419 VQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDgmvcidgqdirtinvrhlreitgvvsqepvlfattiaenirygrENVT 498
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNG--------------------------------------------DNDE 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 499 MDEIEKAVKeanaydfimklPNKFDtlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDK- 577
Cdd:cd03222 58 WDGITPVYK-----------PQYID---------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRl 117
|
170
....*....|....*
gi 925114634 578 -ARKGRTTIVIAHRL 591
Cdd:cd03222 118 sEEGKKTALVVEHDL 132
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
729-983 |
1.25e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 45.58 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 729 AFSIIFSRIIGIFTRDEDPETKRQNSNMFSVLFLVLGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDd 808
Cdd:cd18555 16 LLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFE- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 809 pKNTTGALTTRlANDAAQVKGAIGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGqalKD 888
Cdd:cd18555 95 -NRSSGDLLFR-ANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKK---LN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 889 KKELEGAGK---IATEAIENFRTVVSLTREQKF----EYMYAQSLQVpyrnSLRKAHIFGVSFSITQAMMYFSYAGCFRF 961
Cdd:cd18555 170 QEEIVAQTKvqsYLTETLYGIETIKSLGSEKNIykkwENLFKKQLKA----FKKKERLSNILNSISSSIQFIAPLLILWI 245
|
250 260
....*....|....*....|..
gi 925114634 962 GAYLVANEFMNFqDVLLVFSAI 983
Cdd:cd18555 246 GAYLVINGELTL-GELIAFSSL 266
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
416-620 |
1.87e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.78 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 416 NLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVRHLREI---------TGVVSQEPVLFATTI 486
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLvsdewqrnnTDMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 487 AENIRygrenvtmDEIEKAVKeanaydfIMKLPNKF--DTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 564
Cdd:PRK10938 103 AEIIQ--------DEVKDPAR-------CEQLAQQFgiTALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 565 TESEAVVQVALDK-ARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELMKE 620
Cdd:PRK10938 168 VASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
394-593 |
2.54e-04 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 45.31 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIdGQDIRTINVRHLREitg 473
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVDQSRD--- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 474 vvSQEPvlfATTIAENIRYGrenvtMDEIEKAVKEAN--AY--DFIMKLPNKfDTLVGergaQLSGGQKQRIAIARALVR 549
Cdd:TIGR03719 396 --ALDP---NKTVWEEISGG-----LDIIKLGKREIPsrAYvgRFNFKGSDQ-QKKVG----QLSGGERNRVHLAKTLKS 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 925114634 550 NPKILLLDEATSALDTESEAVVQVALDKArkGRTTIVIAH------RLST 593
Cdd:TIGR03719 461 GGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
153-339 |
2.81e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 44.37 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 153 FFHAIMRQEIGWFDVHDVGELNTRLtDDVSKINEGIGDK-IGMFFQSIATFFTgFIVGFTRGWKLTLVILAISPVLGLSA 231
Cdd:cd18567 81 LFRHLLRLPLSYFEKRHLGDIVSRF-GSLDEIQQTLTTGfVEALLDGLMAILT-LVMMFLYSPKLALIVLAAVALYALLR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 232 AIWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAItANISIGAAF-LLIYA 310
Cdd:cd18567 159 LALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQR-LQILFSAANgLLFGL 237
|
170 180
....*....|....*....|....*....
gi 925114634 311 SYALAFWYGTSLVLSSEYSIGqVLTVFFS 339
Cdd:cd18567 238 ENILVIYLGALLVLDGEFTVG-MLFAFLA 265
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1172-1258 |
3.22e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.34 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1172 GDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESE-KVVQEALDKAREGRTCIV----------IAHRLSTIQ 1240
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRnEVWDEVRSMVRDGATVLLttqymeeaeqLAHELTVID 218
|
90
....*....|....*...
gi 925114634 1241 NADLIVvfqNGKVKEHGT 1258
Cdd:NF000106 219 RGRVIA---DGKVDELKT 233
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1047-1232 |
3.34e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.78 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1047 PTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP-LAGSVLIDGKEIKHLNVQWL-----------RA 1113
Cdd:NF040905 268 PLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRnISGTVFKDGKEVDVSTVSDAidaglayvtedRK 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1114 HLGIVSQEPILFDCSIAENIAYGDNSRVVSHEEIMQAakeanihhfiETLPEKYNTR---VGDKGTQLSGGQKQRIAIAR 1190
Cdd:NF040905 348 GYGLNLIDDIKRNITLANLGKVSRRGVIDENEEIKVA----------EEYRKKMNIKtpsVFQKVGNLSGGNQQKVVLSK 417
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 925114634 1191 ALVRQPHILLLDEATSALDT----ESEKVVQEAldkAREGRTCIVI 1232
Cdd:NF040905 418 WLFTDPDVLILDEPTRGIDVgakyEIYTIINEL---AAEGKGVIVI 460
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
533-612 |
3.62e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 42.70 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 533 LSGGQKQRIAIARALVRNPK--ILLLDEATSALDTESEAVVQVALDKAR-KGRTTIVIAHRLSTVRNADVI------AGF 603
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIidfgpgSGK 167
|
....*....
gi 925114634 604 DDGVIVEKG 612
Cdd:cd03238 168 SGGKVVFSG 176
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1177-1264 |
3.88e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.02 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1177 QLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVFQNGKV 1253
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQT 237
|
90
....*....|.
gi 925114634 1254 KEHGTHQQLLA 1264
Cdd:PRK15093 238 VETAPSKELVT 248
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
415-608 |
4.75e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 44.27 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 415 LNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTDGMVCIDGQDIRTINVR--------HLRE---------------- 470
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAqrlarglvYLPEdrqssglyldaplawn 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 471 ITGVVSQEPVLFATTIAENI---RYGRE-NVTMDEIEKAVKeanaydfimklpnkfdtlvgergaQLSGGQKQRIAIARA 546
Cdd:PRK15439 362 VCALTHNRRGFWIKPARENAvleRYRRAlNIKFNHAEQAAR------------------------TLSGGNQQKVLIAKC 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 925114634 547 LVRNPKILLLDEATSALDTESEA-VVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVI 608
Cdd:PRK15439 418 LEASPQLLIVDEPTRGVDVSARNdIYQLIRSIAAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
378-621 |
8.53e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 43.62 E-value: 8.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 378 DSYSKSGHKPDNIKGN--LEFKNVhfsypSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSttvQLMQRLY--DP-TDGM 452
Cdd:PRK09700 248 NRFNAMKENVSNLAHEtvFEVRNV-----TSRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFgvDKrAGGE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 453 VCIDGQDIRTIN-----------VRHLREITGVVSQEPVLFATTIAENIRYGRENVTM----DEIEKAVKEANAYDFIMK 517
Cdd:PRK09700 320 IRLNGKDISPRSpldavkkgmayITESRRDNGFFPNFSIAQNMAISRSLKDGGYKGAMglfhEVDEQRTAENQRELLALK 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 518 LPNkfdtlVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLSTVRN 596
Cdd:PRK09700 400 CHS-----VNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIIT 474
|
250 260
....*....|....*....|....*..
gi 925114634 597 A-DVIAGFDDGVIVEK-GNHDELMKEK 621
Cdd:PRK09700 475 VcDRIAVFCEGRLTQIlTNRDDMSEEE 501
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
755-971 |
8.59e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 42.93 E-value: 8.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 755 NMFSVLFLVLGI----ISFITFFLQGFTFGKAGEILTKRLrymvFRSMLRQDVSWFDdpKNTTGALTTRLA-NDAAQ--- 826
Cdd:cd18568 42 NLILIGLLIVGIfqilLSAVRQYLLDYFANRIDLSLLSDF----YKHLLSLPLSFFA--SRKVGDIITRFQeNQKIRrfl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 827 VKGAIGSRLAVITqnianlgtgIIISLI----YGWQLTLLLLAIVPIIAIAGVV---EMKMLSGQALKDKKELEGAgkiA 899
Cdd:cd18568 116 TRSALTTILDLLM---------VFIYLGlmfyYNLQLTLIVLAFIPLYVLLTLLsspKLKRNSREIFQANAEQQSF---L 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 900 TEAIENFRTVVSLTREQKF----EYMYAQSLQVPYRNSlrKAHIfgVSFSITQAMMYFSYAGCFRFGAYLVANEFM 971
Cdd:cd18568 184 VEALTGIATIKALAAERPIrwrwENKFAKALNTRFRGQ--KLSI--VLQLISSLINHLGTIAVLWYGAYLVISGQL 255
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
1091-1275 |
1.03e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1091 PLAGSVLIDGKeikhlnvqwlraHLGIVSQEPIlfdcsiaENIAygdnsRVVSHEEIMQAAKEANIHHFIETLPekyntr 1170
Cdd:PRK00635 1643 PLAQEVVYEGK------------HFGQLLQTPI-------EEVA-----ETFPFLKKIQKPLQALIDNGLGYLP------ 1692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1171 VGDKGTQLSGGQKQRIAIARALV---RQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNADLIV 1246
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTlVSLGHSVIYIDHDPALLKQADYLI 1772
|
170 180 190
....*....|....*....|....*....|..
gi 925114634 1247 VFQNGKVKEHGthqQLL---AQKGIYFSMVSV 1275
Cdd:PRK00635 1773 EMGPGSGKTGG---KILfsgPPKDISASKDSL 1801
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
1176-1246 |
1.05e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.48 E-value: 1.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 1176 TQLSGGQKQRIAIARALVR---QPHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIV 1246
Cdd:COG0178 825 TTLSGGEAQRVKLASELSKrstGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDkGNTVVVIEHNLDVIKTADWII 899
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1177-1246 |
1.21e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.81 E-value: 1.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 925114634 1177 QLSGGQKQRIAIARALVRQPH----ILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIV 1246
Cdd:cd03227 77 QLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLI 151
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
375-598 |
1.47e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.69 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 375 PSIDSYSKSGHKPDNIKgNLEFKNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQ----------- 443
Cdd:PRK10938 243 PEPDEPSARHALPANEP-RIVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpqgysndl 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 444 RLYDPTDGmvciDGQDIRTINvRHLreitGVVSQEPVL---FATTIAENIRYGrenvTMDEI--EKAVKEANaydfiMKL 518
Cdd:PRK10938 319 TLFGRRRG----SGETIWDIK-KHI----GYVSSSLHLdyrVSTSVRNVILSG----FFDSIgiYQAVSDRQ-----QKL 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 519 PNKFDTLVGERGAQ-------LSGGQkQRIA-IARALVRNPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIV--- 586
Cdd:PRK10938 381 AQQWLDILGIDKRTadapfhsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfvs 459
|
250 260
....*....|....*....|.
gi 925114634 587 ---------IAHRLSTVRNAD 598
Cdd:PRK10938 460 hhaedapacITHRLEFVPDGD 480
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
511-600 |
2.09e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.37 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 511 AYDF---IMKLPNKFDTLV---------GERGAQLSGGQKQRIAIARALVRNP--KIL-LLDEATSALDTESEA----VV 571
Cdd:PRK00349 797 ALEFfeaIPKIARKLQTLVdvglgyiklGQPATTLSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFEDIRklleVL 876
|
90 100
....*....|....*....|....*....
gi 925114634 572 QVALDKarkGRTTIVIAHRLSTVRNADVI 600
Cdd:PRK00349 877 HRLVDK---GNTVVVIEHNLDVIKTADWI 902
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
393-600 |
2.28e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 40.67 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 393 NLEFKNVHfSYPSRKEVKILKGLNLkvqsgqtvaLVGNSGCGKSTTVQLMQrlydptdgMVCIDGQDIRTINVRHLREIT 472
Cdd:cd03240 3 KLSIRNIR-SFHERSEIEFFSPLTL---------IVGQNGAGKTTIIEALK--------YALTGELPPNSKGGAHDPKLI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 473 GVvsqepvlfATTIAEnIRYGRENVTMDEIeKAVKEANAYDFIMKLPN-KFDTLVGERGAQLSGGQKQ------RIAIAR 545
Cdd:cd03240 65 RE--------GEVRAQ-VKLAFENANGKKY-TITRSLAILENVIFCHQgESNWPLLDMRGRCSGGEKVlasliiRLALAE 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 925114634 546 ALVRNPKILLLDEATSALDTESEAVVQVALDKARKG---RTTIVIAHRLSTVRNADVI 600
Cdd:cd03240 135 TFGSNCGILALDEPTTNLDEENIEESLAEIIEERKSqknFQLIVITHDEELVDAADHI 192
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
1050-1085 |
2.42e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.84 E-value: 2.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 925114634 1050 PDIPV-----LQGLSLEV-----KKGQTLALVGSSGCGKSTVV-QLL 1085
Cdd:PRK01889 170 PGVPVlavsaLDGEGLDVlaawlSGGKTVALLGSSGVGKSTLVnALL 216
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
757-876 |
2.51e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 41.30 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 757 FSVLFLVLGIISFITFFLQGFtfgKAGEILTKRLRYMVFRSMLRqdvsWFDdpKNTTGALTTRLANDAaqvkGAIGSRLA 836
Cdd:cd18604 52 ISLLSVLLGTLRYLLFFFGSL---RASRKLHERLLHSVLRAPLR----WLD--TTPVGRILNRFSKDI----ETIDSELA 118
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 925114634 837 VITQNIANLGTGIIISLIygwqltlLLLAIVPIIAIAGVV 876
Cdd:cd18604 119 DSLSSLLESTLSLLVILI-------AIVVVSPAFLLPAVV 151
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
532-618 |
3.08e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 41.33 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 532 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTVRN-ADVIAGFDDGVI 608
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQwADKINVLYCGQT 237
|
90
....*....|
gi 925114634 609 VEKGNHDELM 618
Cdd:PRK15093 238 VETAPSKELV 247
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
536-618 |
3.43e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.42 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 536 GQKQRIAIARALVRNPKILLLDEATSALDTES----EAVVqvaldKARKGrTTIVIAH-R--LSTV--RNADViagfDDG 606
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTirwlEDVL-----NERNS-TMIIISHdRhfLNSVctHMADL----DYG 228
|
90
....*....|...
gi 925114634 607 VI-VEKGNHDELM 618
Cdd:PRK15064 229 ELrVYPGNYDEYM 241
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1176-1255 |
5.47e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.11 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 1176 TQLSGGQKQRIAIarALV-----RQPH-ILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLI--VV 1247
Cdd:pfam02463 1076 DLLSGGEKTLVAL--ALIfaiqkYKPApFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLvgVT 1153
|
....*...
gi 925114634 1248 FQNGKVKE 1255
Cdd:pfam02463 1154 MVENGVST 1161
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
1178-1246 |
7.27e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 39.55 E-value: 7.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925114634 1178 LSGGQKQRIAIARAL------VrqphILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIV 1246
Cdd:cd03270 138 LSGGEAQRIRLATQIgsgltgV----LYVLDEPSIGLHPRDNDRLIETLKRLRDlGNTVLVVEHDEDTIRAADHVI 209
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
394-564 |
7.95e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 394 LEFKN--VHfsYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKS-TTVQLMQRLYDP-TDGMVCIDGQDIRTINVRHL- 468
Cdd:NF040905 258 FEVKNwtVY--HPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRnISGTVFKDGKEVDVSTVSDAi 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925114634 469 ----------REITGVVSQEPVLFATTIAENIRYGRENVtMDEIEKaVKEANAY--DFIMKLPNkfdtlVGERGAQLSGG 536
Cdd:NF040905 336 daglayvtedRKGYGLNLIDDIKRNITLANLGKVSRRGV-IDENEE-IKVAEEYrkKMNIKTPS-----VFQKVGNLSGG 408
|
170 180
....*....|....*....|....*...
gi 925114634 537 QKQRIAIARALVRNPKILLLDEATSALD 564
Cdd:NF040905 409 NQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| |
