|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
13-1235 |
0e+00 |
|
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: 1327.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 13 FYQRVTEAQRCsPEKSASFFSKMTYSWFSRIIILGYKKPLEREDLFELNEGDSSYIVCPIFEKQWRKEVLRTQeRQKVKS 92
Cdd:TIGR00957 192 FSETNHDPNPC-PESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKECKKTR-KQPVSA 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 93 SFHKEAHT-------------------------RKPSLLRALWNTFKFALIQVALFKVLADVLSFTSPLIMKQMILFCEQ 147
Cdd:TIGR00957 270 VYGKKDPSkpkgssqldaneevealivksphkpRKPSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVND 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 148 RPDFGWSGYGYALALFVVVFLQTLILQQYQRFKMLTSAKIKTAVIGLIYKKALLLSNVSRKQFSTGEIINLMATDTQQLM 227
Cdd:TIGR00957 350 PMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFM 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 228 DLMTNINLLWSAPFQILMAVSLLWQELGPAVLAGVAVLVFVIPMNALVANRMKKLKKNQRKNKDKQIKLLNEILHGIKIL 307
Cdd:TIGR00957 430 DLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVL 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 308 KLYAWEPSYKKKIIEIREQELEVQKSAGYLAVFSMLTLTCIPFL------------------------------------ 351
Cdd:TIGR00957 510 KLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLvalitfavyvtvdennildaekafvslalfnilrfp 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 352 -------------TRISLVHLEDFLNTEELLPHSIEANYI---GDHAIGFINASFSWDKTGIPVLKDLNIKIPEGALVAV 415
Cdd:TIGR00957 590 lnilpmvissivqASVSLKRLRIFLSHEELEPDSIERRTIkpgEGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAV 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 416 VGQVGSGKSSVLSAILGEMEKLKGIVQRKGSVAYVSQQAWIQNCILQENILFGSVMQKQLYERVLEACALLPDLEQLPNG 495
Cdd:TIGR00957 670 VGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSG 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 496 DQTEIGEKGVNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQLFEKVIGSSGMLRNKTRILVTHNLTLLPQMD 575
Cdd:TIGR00957 750 DRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLKNKTRILVTHGISYLPQVD 829
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 576 LIVVMESGRVAQMGTYQEILAKTKNLTNLLQAFSEQETAHALKQVSVINSRTVLKDQILVQNDRPLLDQ-RKQFS----- 649
Cdd:TIGR00957 830 VIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQGHLEDSWTALVSGEGKEAKLIENGMLVTDVvGKQLQrqlsa 909
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 650 ------------------------------VRKEKIPVGGVKFSVILKYLHAFGWLWVWLNVATCLGQNLVGTGQNLWLS 699
Cdd:TIGR00957 910 sssdsgdqsrhhgssaelqkaeakeetwklMEADKAQTGQVELSVYWDYMKAIGLFITFLSIFLFVCNHVSALASNYWLS 989
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 700 TWAKEAkhMNDFTEwkQIRSKKLSIYGLLGLMQGLFVCSGAYVVTRGSLAASRVLHAQLLDNVLHLPLQFFETNPIGQVI 779
Cdd:TIGR00957 990 LWTDDP--MVNGTQ--NNTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLV 1065
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 780 NRFTKDMFIIDMRFHYYIRTWVNCTLDVIGTVLVIVGALPLFILGLIPLVFLYFTIQRYYMASSRQIRRLAGASHSPVIS 859
Cdd:TIGR00957 1066 NRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYS 1145
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 860 HFCETLLGVSTIRAFGHEQRFIQQNKEVVNENLVCFYNNVISNRWLSVRLEFLGNLMVFFTAVLTVLAGNSIDSAIVGLS 939
Cdd:TIGR00957 1146 HFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLS 1225
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 940 ISYALNITQTLNFWVRKACEIEANAVSIERVCEYETMDKEAPW-ITSKRPPSQWPSKGIVEFVDYRARYRDDLGLALQDI 1018
Cdd:TIGR00957 1226 VSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWqIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHI 1305
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1019 TFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLNIIPQDPVLFSGTLQMNLDPLDK 1098
Cdd:TIGR00957 1306 NVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQ 1385
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1099 YPDHELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVR 1178
Cdd:TIGR00957 1386 YSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIR 1465
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*..
gi 1387192242 1179 KEFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETPQNLIHKRGLFFDMLTEAGI 1235
Cdd:TIGR00957 1466 TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAKDAGL 1522
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
14-1243 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 927.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 14 YQRVTEAQRCSPEKSASFFSKMTYSWFSRIIILGYKKPLEREDLFELNEGDSSYIVCPIFEKQWRKEVLRTqerqkvkss 93
Cdd:PLN03130 217 YEELPGGEQICPERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKKP--------- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 94 fhkeahtrKPSLLRALWNTFKFALIQVALFKVLADVLSFTSPLIMKQMiLFCEQRPDFGWSGYGYALALFVVVFLQTLIL 173
Cdd:PLN03130 288 --------KPWLLRALNNSLGGRFWLGGFFKIGNDLSQFVGPLLLNLL-LESMQNGEPAWIGYIYAFSIFVGVVLGVLCE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 174 QQYQRFKMLTSAKIKTAVIGLIYKKALLLSNVSRKQFSTGEIINLMATDTQQLMDLMTNINLLWSAPFQILMAVSLLWQE 253
Cdd:PLN03130 359 AQYFQNVMRVGFRLRSTLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQ 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 254 LGPAVLAGVAVLVFVIPMNALVANRMKKLKKNQRKNKDKQIKLLNEILHGIKILKLYAWEPSYKKKIIEIREQELEVQKS 333
Cdd:PLN03130 439 LGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRK 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 334 AGYLAVFSMLTLTCIPFLT-----------------------------------------------RISLVHLEDFLNTE 366
Cdd:PLN03130 519 AQLLSAFNSFILNSIPVLVtvvsfgvftllggdltparaftslslfavlrfplfmlpnlitqavnaNVSLKRLEELLLAE 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 367 E--LLPH-SIEAnyiGDHAIGFINASFSWDKTG-IPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLK-GIV 441
Cdd:PLN03130 599 ErvLLPNpPLEP---GLPAISIKNGYFSWDSKAeRPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASV 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 442 QRKGSVAYVSQQAWIQNCILQENILFGSVMQKQLYERVLEACALLPDLEQLPNGDQTEIGEKGVNISGGQKHRVCLARAV 521
Cdd:PLN03130 676 VIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAV 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 522 YSGADIYLLDDPLSAVDVHVAKQLFEKVIgsSGMLRNKTRILVTHNLTLLPQMDLIVVMESGRVAQMGTYQEILAKTKNL 601
Cdd:PLN03130 756 YSNSDVYIFDDPLSALDAHVGRQVFDKCI--KDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLF 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 602 TNL------LQAFSEQETAHALKQVS---VINSRTVLKDQILVQNDRPllDQRKQFSVRKEKIPVGGVKFSVILKYLHAF 672
Cdd:PLN03130 834 QKLmenagkMEEYVEENGEEEDDQTSskpVANGNANNLKKDSSSKKKS--KEGKSVLIKQEERETGVVSWKVLERYKNAL 911
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 673 GWLWVWLNVATC-LGQNLVGTGQNLWLSTWAKeakhmndftewkQIRSKK------LSIYGLLGLMQGLFVCSGAYVVTR 745
Cdd:PLN03130 912 GGAWVVMILFLCyVLTEVFRVSSSTWLSEWTD------------QGTPKThgplfyNLIYALLSFGQVLVTLLNSYWLIM 979
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 746 GSLAASRVLHAQLLDNVLHLPLQFFETNPIGQVINRFTKDMFIIDMRFHYYIRTWVNCTLDVIGTVLVI--VGALPLFil 823
Cdd:PLN03130 980 SSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIgiVSTISLW-- 1057
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 824 GLIPLVFLYFTIQRYYMASSRQIRRLAGASHSPVISHFCETLLGVSTIRAFGHEQRFIQQNKEVVNENLVCFYNNVISNR 903
Cdd:PLN03130 1058 AIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNR 1137
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 904 WLSVRLEFLGNLMVFFTAVLTVLA-GNSIDSA----IVGLSISYALNITQTLNFWVRKACEIEANAVSIERVCEYETMDK 978
Cdd:PLN03130 1138 WLAIRLETLGGLMIWLTASFAVMQnGRAENQAafasTMGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLPS 1217
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 979 EAPW-ITSKRPPSQWPSKGIVEFVDYRARYRDDLGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKII 1057
Cdd:PLN03130 1218 EAPLvIENNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRIL 1297
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1058 IDGIDISTIGLHDLRGKLNIIPQDPVLFSGTLQMNLDPLDKYPDHELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSV 1137
Cdd:PLN03130 1298 IDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSV 1377
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1138 GQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVRKEFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETPQ 1217
Cdd:PLN03130 1378 GQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPE 1457
|
1290 1300
....*....|....*....|....*.
gi 1387192242 1218 NLIHKRGLFFdmlteAGITQDLGAKN 1243
Cdd:PLN03130 1458 NLLSNEGSAF-----SKMVQSTGAAN 1478
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
14-1234 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 871.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 14 YQRVTEAQRCSPEKSASFFSKMTYSWFSRIIILGYKKPLEREDLFELNEGDSSYIVCPIFEKQWRKEVLRTqerqkvkss 93
Cdd:PLN03232 217 YDALRGGENICPERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEESRRP--------- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 94 fhkeahtrKPSLLRALWNTFKFALIQVALFKVLADVLSFTSPLIMKQmILFCEQRPDFGWSGYGYALALFVVVFLQTLIL 173
Cdd:PLN03232 288 --------KPWLLRALNNSLGGRFWLGGIFKIGHDLSQFVGPVILSH-LLQSMQEGDPAWVGYVYAFLIFFGVTFGVLCE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 174 QQYQRFKMLTSAKIKTAVIGLIYKKALLLSNVSRKQFSTGEIINLMATDTQQLMDLMTNINLLWSAPFQILMAVSLLWQE 253
Cdd:PLN03232 359 SQYFQNVGRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQ 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 254 LGPAVLAGVAVLVFVIPMNALVANRMKKLKKNQRKNKDKQIKLLNEILHGIKILKLYAWEPSYKKKIIEIREQELEVQKS 333
Cdd:PLN03232 439 LGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRK 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 334 AGYLAVFSMLTLTCIPFL-----------------------------------------------TRISLVHLEDFLNTE 366
Cdd:PLN03232 519 AQLLSAFNSFILNSIPVVvtlvsfgvfvllggdltparaftslslfavlrsplnmlpnllsqvvnANVSLQRIEELLLSE 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 367 ELLPHSIEANYIGDHAIGFINASFSWD-KTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLK-GIVQRK 444
Cdd:PLN03232 599 ERILAQNPPLQPGAPAISIKNGYFSWDsKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtSSVVIR 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 445 GSVAYVSQQAWIQNCILQENILFGSVMQKQLYERVLEACALLPDLEQLPNGDQTEIGEKGVNISGGQKHRVCLARAVYSG 524
Cdd:PLN03232 679 GSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSN 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 525 ADIYLLDDPLSAVDVHVAKQLFEKVIGSSgmLRNKTRILVTHNLTLLPQMDLIVVMESGRVAQMGTYQEILAKTKNLTNL 604
Cdd:PLN03232 759 SDIYIFDDPLSALDAHVAHQVFDSCMKDE--LKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKL 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 605 LQAFSEQETAHALKQvsviNSRTVLKDQILVQND---RPLLD-----QRKQFSVRKEKIPVGGVKFSVILKYLHAFGWLW 676
Cdd:PLN03232 837 MENAGKMDATQEVNT----NDENILKLGPTVTIDvseRNLGStkqgkRGRSVLVKQEERETGIISWNVLMRYNKAVGGLW 912
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 677 VWLNVATC-LGQNLVGTGQNLWLSTWAKEAKHMNDFTEWKqirskkLSIYGLLGLMQGLFVCSGAYVVTRGSLAASRVLH 755
Cdd:PLN03232 913 VVMILLVCyLTTEVLRVSSSTWLSIWTDQSTPKSYSPGFY------IVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLH 986
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 756 AQLLDNVLHLPLQFFETNPIGQVINRFTKDMFIIDMRFHYYIRTWVNCTLDVIGTVLVIVGALPLFILGLIPLVFLYFTI 835
Cdd:PLN03232 987 DAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAA 1066
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 836 QRYYMASSRQIRRLAGASHSPVISHFCETLLGVSTIRAFGHEQRFIQQNKEVVNENLVCFYNNVISNRWLSVRLEFLGNL 915
Cdd:PLN03232 1067 YLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGV 1146
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 916 MVFFTAVLTVLA-GNSIDSA----IVGLSISYALNITQTLNFWVRKACEIEANAVSIERVCEYETMDKEAPWI-TSKRPP 989
Cdd:PLN03232 1147 MIWLTATFAVLRnGNAENQAgfasTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIiENNRPV 1226
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 990 SQWPSKGIVEFVDYRARYRDDLGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLH 1069
Cdd:PLN03232 1227 SGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLT 1306
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1070 DLRGKLNIIPQDPVLFSGTLQMNLDPLDKYPDHELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARAL 1149
Cdd:PLN03232 1307 DLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARAL 1386
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1150 LRKTKILILDEATASIDFETDNLVQTTVRKEFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETPQNLIHKRG-LFFD 1228
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFR 1466
|
....*.
gi 1387192242 1229 MLTEAG 1234
Cdd:PLN03232 1467 MVHSTG 1472
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
101-1234 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 658.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 101 RKPSLLRALWNTFKFALIQVALFKVLADVLSFTSPLIMKQMILFCEQRP-DFGWsGYGYALALFVVVFLQTLILQQYQRF 179
Cdd:PTZ00243 230 KRLSLLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFLDADNaTWGR-GLGLVLTLFLTQLIQSVCLHRFYYI 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 180 KMLTSAKIKTAVIGLIYKKALLLSN--VSRKQFSTGEIINLMATDTQQLMDLMTNINLLWSAPFQILMAVSLLWQELGPA 257
Cdd:PTZ00243 309 SIRCGLQYRSALNALIFEKCFTISSksLAQPDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWC 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 258 VLAGVAVLVFVIPMNALVANRMKKLKKNQRKNKDKQIKLLNEILHGIKILKLYAWEPSYKKKIIEIREQEL--------- 328
Cdd:PTZ00243 389 ALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELrylrdvqla 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 --------------------------------------------------------------------------------
Cdd:PTZ00243 469 rvatsfvnnatptlmiavvftvyyllgheltpevvfptiallgvlrmpffmipwvfttvlqflvsikristflecdnatc 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 329 -EVQKSAGYL-------------AVFSMLTLTC-----IPF--------LTRISL-----------------VHLEdflN 364
Cdd:PTZ00243 549 sTVQDMEEYWreqrehstacqlaAVLENVDVTAfvpvkLPRapkvktslLSRALRmlcceqcrptkrhpspsVVVE---D 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 365 TEELLPHSIEANYIGDHAIGFINASFSWDKT-GIP--------------VLKDLNIKIPEGALVAVVGQVGSGKSSVLSA 429
Cdd:PTZ00243 626 TDYGSPSSASRHIVEGGTGGGHEATPTSERSaKTPkmktddffelepkvLLRDVSVSVPRGKLTVVLGATGSGKSTLLQS 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 430 ILGEMEKLKGIVQRKGSVAYVSQQAWIQNCILQENILFGSVMQKQLYERVLEACALLPDLEQLPNGDQTEIGEKGVNISG 509
Cdd:PTZ00243 706 LLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSG 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 510 GQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQLFEKVIgsSGMLRNKTRILVTHNLTLLPQMDLIVVMESGRVAQMG 589
Cdd:PTZ00243 786 GQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECF--LGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSG 863
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 590 TYQEILAKT--KNLTNLLQ---------AFSEQETAHALKQVSVINSRTVLKDQILVQNDRPL-LD-QRKQFSVRKEKiP 656
Cdd:PTZ00243 864 SSADFMRTSlyATLAAELKenkdskegdADAEVAEVDAAPGGAVDHEPPVAKQEGNAEGGDGAaLDaAAGRLMTREEK-A 942
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 657 VGGVKFSVILKYLHAFGWLWVWLNV-ATCLGQNLVGTGQNLWLSTWAKEAKHMNDFTEwkqirskkLSIYGLLGLMQGL- 734
Cdd:PTZ00243 943 SGSVPWSTYVAYLRFCGGLHAAGFVlATFAVTELVTVSSGVWLSMWSTRSFKLSAATY--------LYVYLGIVLLGTFs 1014
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 735 --FVCSGAYVVTRgslAASRVLHAQLLDNVLHLPLQFFETNPIGQVINRFTKDMFIIDMRFHYYIRTWVNCTLDVIGTVL 812
Cdd:PTZ00243 1015 vpLRFFLSYEAMR---RGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSIL 1091
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 813 VIVGALPLFILGLIPLVFLYFTIQRYYMASSRQIRRLAGASHSPVISHFCETLLGVSTIRAFGHEQRFIQQNKEVVNENL 892
Cdd:PTZ00243 1092 VTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVVY 1171
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 893 VCFYNNVISNRWLSVRLEFLGNLMVFFTAVL----TVLAGNSIDSAIVGLSISYALNITQTLNFWVRKACEIEANAVSIE 968
Cdd:PTZ00243 1172 SCSYLENVANRWLGVRVEFLSNIVVTVIALIgvigTMLRATSQEIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVE 1251
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 969 RVCEY------ETM---DKE-----------AP-----WITSKRPPSQWP---SKGIVEFVDYRARYRDDLGLALQDITF 1020
Cdd:PTZ00243 1252 RLLYYtdevphEDMpelDEEvdalerrtgmaADvtgtvVIEPASPTSAAPhpvQAGSLVFEGVQMRYREGLPLVLRGVSF 1331
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1021 QTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLNIIPQDPVLFSGTLQMNLDPLDKYP 1100
Cdd:PTZ00243 1332 RIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEAS 1411
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1101 DHELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRKTKILIL-DEATASIDFETDNLVQTTVRK 1179
Cdd:PTZ00243 1412 SAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMS 1491
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*
gi 1387192242 1180 EFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETPQNLIHKRGLFFDMLTEAG 1234
Cdd:PTZ00243 1492 AFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVEAL 1546
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-1226 |
8.69e-155 |
|
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: 502.90 E-value: 8.69e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 21 QRcSPEKSASFFSKMTYSWFSRIIILGYKKPLEREDLFELNEGDSSYIVCPIFEKQWRKEVLRTQerqkvkssfhkeaht 100
Cdd:TIGR01271 2 QR-SPVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASAK--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 101 RKPSLLRALWNTFKFALIQVALFKVLADVLSFTSPLIMKQMIlfCEQRPDFGWS---GYGYALALFVVVFLQTLILQQ-- 175
Cdd:TIGR01271 66 KNPKLLNALRRCFFWRFVFYGILLYFGEATKAVQPLLLGRII--ASYDPFNAPEreiAYYLALGLCLLFIVRTLLLHPai 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 176 --YQRFKMltsaKIKTAVIGLIYKKALLLSNVSRKQFSTGEIINLMATDTQQLMDLMTNINLLWSAPFQILMAVSLLWQE 253
Cdd:TIGR01271 144 fgLHHLGM----QMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWEL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 254 LGPAVLAGVAVLVFVIPMNALVANRMKKLKKNQRKNKDKQIKLLNEILHGIKILKLYAWEPSYKKKIIEIREQELEVQKS 333
Cdd:TIGR01271 220 LEVNGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 334 AGYLAVFS----------MLTLTCIPF-------LTRI------------------------------SLVHLEDFLNTE 366
Cdd:TIGR01271 300 IAYLRYFYssafffsgffVVFLSVVPYalikgiiLRRIfttisycivlrmtvtrqfpgaiqtwydslgAITKIQDFLCKE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 367 ELlpHSIEANyIGDHAIGFINASFSWDK--------------------------------TGIPVLKDLNIKIPEGALVA 414
Cdd:TIGR01271 380 EY--KTLEYN-LTTTEVEMVNVTASWDEgigelfekikqnnkarkqpngddglffsnfslYVTPVLKNISFKLEKGQLLA 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 415 VVGQVGSGKSSVLSAILGEMEKLKGIVQRKGSVAYVSQQAWIQNCILQENILFGSVMQKQLYERVLEACALLPDLEQLPN 494
Cdd:TIGR01271 457 VAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPE 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 495 GDQTEIGEKGVNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQLFEKVIgsSGMLRNKTRILVTHNLTLLPQM 574
Cdd:TIGR01271 537 KDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCL--CKLMSNKTRILVTSKLEHLKKA 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 575 DLIVVMESGRVAQMGTYQEILAKTKNLTNLL-------------------------------QAFSEQETAHA------- 616
Cdd:TIGR01271 615 DKILLLHEGVCYFYGTFSELQAKRPDFSSLLlgleafdnfsaerrnsiltetlrrvsidgdsTVFSGPETIKQsfkqppp 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 617 -----LKQVSVINSRTVLKDQILVQN-------------DRPLLDQRkqFSVRKEK------IPVGGV-----------K 661
Cdd:TIGR01271 695 efaekRKQSIILNPIASARKFSFVQMgpqkaqattiedaVREPSERK--FSLVPEDeqgeesLPRGNQyhhglqhqaqrR 772
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 662 FSVILKYLHAFGWLWVWLNVATCLGQNLVGTGQNLWLST----------------------------WAKEAKHMNDFTE 713
Cdd:TIGR01271 773 QSVLQLMTHSNRGENRREQLQTSFRKKSSITQQNELASEldiysrrlskdsvyeiseeineedlkecFADERENVFETTT 852
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 714 W----KQIRSKKLSIYGLL-----------GLMQGLFVCSG----------------------AYVVTRGS--------- 747
Cdd:TIGR01271 853 WntylRYITTNRNLVFVLIfclviflaevaASLLGLWLITDnpsapnyvdqqhanasspdvqkPVIITPTSayyifyiyv 932
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 748 ---------------------LAASRVLHAQLLDNVLHLPLQFFETNPIGQVINRFTKDMFIIDMRFHYYIRTWVNCTLD 806
Cdd:TIGR01271 933 gtadsvlalgffrglplvhtlLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLI 1012
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 807 VIGTVLVIVGALPLFILGLIPLVFLYFTIQRYYMASSRQIRRLAGASHSPVISHFCETLLGVSTIRAFGHEQRFIQQNKE 886
Cdd:TIGR01271 1013 VLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHK 1092
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 887 VVNENLVCFYNNVISNRWLSVRLEFLgnLMVFFTAVLTV-LAGNSIDSAIVGLSISYALNITQTLNFWVRKACEIEANAV 965
Cdd:TIGR01271 1093 ALNLHTANWFLYLSTLRWFQMRIDII--FVFFFIAVTFIaIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMR 1170
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 966 SIERVCEYETMDKEAPWITSKRPPSQ---------------WPSKGIVEFVDYRARYRDDLGLALQDITFQTHGEEKIGI 1030
Cdd:TIGR01271 1171 SVSRVFKFIDLPQEEPRPSGGGGKYQlstvlvienphaqkcWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGL 1250
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1031 VGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDIStIGLHDLRGKLNIIPQDPVLFSGTLQMNLDPLDKYPDHELWEVLEL 1110
Cdd:TIGR01271 1251 LGRTGSGKSTLLSALLRLLSTEGEIQIDGVSWNS-VTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEE 1329
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1111 CHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVRKEFSDCTILTIA 1190
Cdd:TIGR01271 1330 VGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSE 1409
|
1450 1460 1470
....*....|....*....|....*....|....*.
gi 1387192242 1191 HRLHSIIDSDRVLVLDSGRITEFETPQNLIHKRGLF 1226
Cdd:TIGR01271 1410 HRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
681-973 |
9.29e-140 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 426.12 E-value: 9.29e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 681 VATCLGQNLVGTGQNLWLSTWAKEAKhmNDFTEWKQIRSKKLSIYGLLGLMQGLFVCSGAYVVTRGSLAASRVLHAQLLD 760
Cdd:cd18603 5 LLLYLLSQAFSVGSNIWLSEWSDDPA--LNGTQDTEQRDYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKLLH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 761 NVLHLPLQFFETNPIGQVINRFTKDMFIIDMRFHYYIRTWVNCTLDVIGTVLVIVGALPLFILGLIPLVFLYFTIQRYYM 840
Cdd:cd18603 83 NILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRFYV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 841 ASSRQIRRLAGASHSPVISHFCETLLGVSTIRAFGHEQRFIQQNKEVVNENLVCFYNNVISNRWLSVRLEFLGNLMVFFT 920
Cdd:cd18603 163 ATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVLFA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1387192242 921 AVLTVLAGNSIDSAIVGLSISYALNITQTLNFWVRKACEIEANAVSIERVCEY 973
Cdd:cd18603 243 ALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEY 295
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
996-1216 |
1.90e-118 |
|
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: 366.43 E-value: 1.90e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 996 GIVEFVDYRARYRDDLGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKL 1075
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1076 NIIPQDPVLFSGTLQMNLDPLDKYPDHELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRKTKI 1155
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387192242 1156 LILDEATASIDFETDNLVQTTVRKEFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETP 1216
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
383-584 |
2.24e-109 |
|
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: 341.37 E-value: 2.24e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 383 IGFINASFSWDK---TGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGSVAYVSQQAWIQNC 459
Cdd:cd03250 1 ISVEDASFTWDSgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 460 ILQENILFGSVMQKQLYERVLEACALLPDLEQLPNGDQTEIGEKGVNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDV 539
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1387192242 540 HVAKQLFEKVIGSSGMlRNKTRILVTHNLTLLPQMDLIVVMESGR 584
Cdd:cd03250 161 HVGRHIFENCILGLLL-NNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
121-357 |
1.20e-105 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350039 [Multi-domain] Cd Length: 290 Bit Score: 334.82 E-value: 1.20e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 121 ALFKVLADVLSFTSPLIMKQMILFCEQRPDFGWSGYGYALALFVVVFLQTLILQQYQRFKMLTSAKIKTAVIGLIYKKAL 200
Cdd:cd18595 3 ALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 201 LLSNVSRKQFSTGEIINLMATDTQQLMDLMTNINLLWSAPFQILMAVSLLWQELGPAVLAGVAVLVFVIPMNALVANRMK 280
Cdd:cd18595 83 RLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIK 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387192242 281 KLKKNQRKNKDKQIKLLNEILHGIKILKLYAWEPSYKKKIIEIREQELEVQKSAGYLAVFSMLTLTCIPFLtrISLV 357
Cdd:cd18595 163 KLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFL--VSLA 237
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
677-973 |
2.42e-93 |
|
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: 301.73 E-value: 2.42e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 677 VWLNVATCLGQNLVGTGQNLWLSTWAKEAKHMNDFTEWKQIrskkLSIYGLLGLMQGLFVCSGAYVVTRGSLAASRVLHA 756
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYL----GVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 757 QLLDNVLHLPLQFFETNPIGQVINRFTKDMFIIDMRFHYYIRTWVNCTLDVIGTVLVIVGALPLFILGLIPLVFLYFTIQ 836
Cdd:cd18580 77 KLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 837 RYYMASSRQIRRLAGASHSPVISHFCETLLGVSTIRAFGHEQRFIQQNKEVVNENLVCFYNNVISNRWLSVRLEFLGNLM 916
Cdd:cd18580 157 RYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1387192242 917 VFFTAVLTVLAGNSIDSAIVGLSISYALNITQTLNFWVRKACEIEANAVSIERVCEY 973
Cdd:cd18580 237 ALVVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEY 293
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
724-1229 |
1.03e-89 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 301.70 E-value: 1.03e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 724 IYGLLGLMQGLFVCSGAYVVTRGSLAASRVLHAQLLDNVLHLPLQFFETNPIGQVINRFTKDMFIIDMrfhyyirTWVNC 803
Cdd:COG1132 66 LLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQ-------FLAHG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 804 TLDVIGTVLVIVGALPLFI-----LGLIPLVF--LYFTIQRYYMASSRQIRRLAGASHSPVISHFCETLLGVSTIRAFGH 876
Cdd:COG1132 139 LPQLVRSVVTLIGALVVLFvidwrLALIVLLVlpLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGR 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 877 EQRFIQQNKEVVNENLVCFYNNVISNRWLSVRLEFLGNLMVFFTAVLT---VLAGnSIDSAIVGLSISYALNITQTL--- 950
Cdd:COG1132 219 EERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGgllVLSG-SLTVGDLVAFILYLLRLFGPLrql 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 951 -NFWVrkacEIEANAVSIERVceYETMDKEAPWITSKRPPSQWPSKGIVEFVDYRARYRDDlGLALQDITFQTHGEEKIG 1029
Cdd:COG1132 298 aNVLN----QLQRALASAERI--FELLDEPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1030 IVGRTGAGKSTLSNCLFRIVE-------------RSggkiiidgidistIGLHDLRGKLNIIPQDPVLFSGTLQMNL--- 1093
Cdd:COG1132 371 LVGPSGSGKSTLVNLLLRFYDptsgrilidgvdiRD-------------LTLESLRRQIGVVPQDTFLFSGTIRENIryg 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1094 DPldKYPDHELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLV 1173
Cdd:COG1132 438 RP--DATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALI 515
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387192242 1174 QTTVRKEFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETPQNLIHKRGLFFDM 1229
Cdd:COG1132 516 QEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARL 571
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
676-973 |
7.38e-89 |
|
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: 289.37 E-value: 7.38e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 676 WVWLnVATCLGQNLVGTGQNLWLSTWAKEAKHMNDFTEWKQIRSKKLSIYGLLGLMQGLFVCSGAYVVTRGSLAASRVLH 755
Cdd:cd18604 1 WALL-LLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEVSVLYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 756 AQLLDNVLHLPLQFFETNPIGQVINRFTKDMFIIDMRFHYYIRTWVNCTLDVIGTVLVIVGALPLFILGLIPLVFLYFTI 835
Cdd:cd18604 80 ERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 836 QRYYMASSRQIRRLAGASHSPVISHFCETLLGVSTIRAFGHEQRFIQQNKEVVNENLVCFYNNVISNRWLSVRLEFLGNL 915
Cdd:cd18604 160 GRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGAL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 916 MVFFTAVLtVLAGNSIDSAIVGLSISYALNITQTLNFWVRKACEIEANAVSIERVCEY 973
Cdd:cd18604 240 FSFATAAL-LVYGPGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEY 296
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
992-1216 |
2.48e-88 |
|
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: 284.30 E-value: 2.48e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 992 WPSKGIVEFVDYRARYRDDLGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDL 1071
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1072 RGKLNIIPQDPVLFSGTLQMNLDPLDKYPDHELWEVLelchlkefvqslpkkllhEISEGGENLSVGQRQLVCLARALLR 1151
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387192242 1152 KTKILILDEATASIDFETDNLVQTTVRKEFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETP 1216
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
693-973 |
2.40e-80 |
|
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: 265.49 E-value: 2.40e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 693 GQNLWLSTWakeakhmndfTEWKQIRSKK--LSIYGLLGLMQGLFVCSGAYVVTRGSLAASRVLHAQLLDNVLHLPLQFF 770
Cdd:cd18606 17 FTNLWLSFW----------TEDFFGLSQGfyIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 771 ETNPIGQVINRFTKDMFIIDMRFHYYIRTWVNCTLDVIGTVLVIVGALPLFILGLIPLVFLYFTIQRYYMASSRQIRRLA 850
Cdd:cd18606 87 DTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRASSRELKRLE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 851 GASHSPVISHFCETLLGVSTIRAFGHEQRFIQQNKEVVNENLVCFYNNVISNRWLSVRLEFLGNLMVFFTAVLTVLAGNS 930
Cdd:cd18606 167 SILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLLVLIVALLCVTRRFS 246
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1387192242 931 IDSAIVGLSISYALNITQTLNFWVRKACEIEANAVSIERVCEY 973
Cdd:cd18606 247 ISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHY 289
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
120-352 |
6.97e-77 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)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. ABC transporters typically consist 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: 350023 [Multi-domain] Cd Length: 289 Bit Score: 255.87 E-value: 6.97e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 120 VALFKVLADVLSFTSPLIMKQMILFCEQRPDFGWS-GYGYALALFVVVFLQTLILQQYQRFKMLTSAKIKTAVIGLIYKK 198
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPLSeGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 199 ALLLSNVSRKQFSTGEIINLMATDTQQLMDLMTNINLLWSAPFQILMAVSLLWQELGPAVLAGVAVLVFVIPMNALVANR 278
Cdd:cd18579 82 ALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387192242 279 MKKLKKNQRKNKDKQIKLLNEILHGIKILKLYAWEPSYKKKIIEIREQELEVQKSAGYLAVFSMLTLTCIPFLT 352
Cdd:cd18579 162 ISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLV 235
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
681-973 |
4.90e-76 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 254.07 E-value: 4.90e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 681 VATCLGQNLVGTGQNLWLSTW-------AKEAKHMNDFTEWKQIRSKKLSIYGLLGLMqGLFVCSGAYVVTR-GSLAASR 752
Cdd:cd18602 5 LALALLKQGLRVATDFWLADWteanhdvASVVFNITSSSLEDDEVSYYISVYAGLSLG-AVILSLVTNLAGElAGLRAAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 753 VLHAQLLDNVLHLPLQFFETNPIGQVINRFTKDMFIIDMRFHYYIRTWVNCTLDVIGTVLVIVGALPLFILGLIPLVFLY 832
Cdd:cd18602 84 RLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIIIVY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 833 FTIQRYYMASSRQIRRLAGASHSPVISHFCETLLGVSTIRAFGHEQRFIQQNKEVVNENLVCFYNNVISNRWLSVRLEFL 912
Cdd:cd18602 164 YFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRLDYL 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387192242 913 GNLMVFFTAVLTVLAG--NSIDSAIVGLSISYALNITQTLNFWVRKACEIEANAVSIERVCEY 973
Cdd:cd18602 244 GAVIVFLAALSSLTAAlaGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEY 306
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
726-1229 |
9.52e-75 |
|
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: 263.23 E-value: 9.52e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 726 GLLGLMQGLFVCSGAYVVTRGSLAASRVLHAQLLDNVLHLPLQFFETNPIGQVINRFtkdmfiidmRFHYYIR-----TW 800
Cdd:COG2274 203 LLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF---------RDVESIRefltgSL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 801 VNCTLDVIGTVLVIV------GALPLFILGLIPLVFLY-FTIQRYYMASSRQIRRLAGASHSpvisHFCETLLGVSTIRA 873
Cdd:COG2274 274 LTALLDLLFVLIFLIvlffysPPLALVVLLLIPLYVLLgLLFQPRLRRLSREESEASAKRQS----LLVETLRGIETIKA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 874 FGHEQRFIQQNKEVVNENLvcfyNNVISNRWLSVR-------LEFLGNLMVFFTAVLTVLAGN-SIDS--AIVGLsISYA 943
Cdd:COG2274 350 LGAESRFRRRWENLLAKYL----NARFKLRRLSNLlstlsglLQQLATVALLWLGAYLVIDGQlTLGQliAFNIL-SGRF 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 944 LN-ITQTLNFWVRkaceIEANAVSIERVCEYETMDKEAPWITSKRPPSQwpSKGIVEFVDYRARYRDDLGLALQDITFQT 1022
Cdd:COG2274 425 LApVAQLIGLLQR----FQDAKIALERLDDILDLPPEREEGRSKLSLPR--LKGDIELENVSFRYPGDSPPVLDNISLTI 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1023 HGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLNIIPQDPVLFSGTLQMNL---DPldKY 1099
Cdd:COG2274 499 KPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDP--DA 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1100 PDHELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVRK 1179
Cdd:COG2274 577 TDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRR 656
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1180 EFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETPQNLIHKRGLFFDM 1229
Cdd:COG2274 657 LLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
696-973 |
3.26e-74 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 248.60 E-value: 3.26e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 696 LWLSTWAKEAKhmNDFTEWKQIRSKK-LSIYGLLGLMQGLFVCSGAYVVTRGSLAASRVLHAQLLDNVLHLPLQFFETNP 774
Cdd:cd18605 20 FWLSYWVSHSN--NSFFNFINDSFNFfLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKTP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 775 IGQVINRFTKDMFIIDMRFHYYIRTWVNCTLDVIGTVLVIVGALPLFILGLIPLVFLYFTIQRYYMASSRQIRRLAGASH 854
Cdd:cd18605 98 VGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQRYYRATSRELKRLNSVNL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 855 SPVISHFCETLLGVSTIRAFGHEQRFIQQNKEVVNENLVCFYNNVISNRWLSVRLEFLGNLMVFF---TAVLTVLAGNSI 931
Cdd:cd18605 178 SPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVLIVTFvalTAVVQHFFGLSI 257
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1387192242 932 DSAIVGLSISYALNITQTLNFWVRKACEIEANAVSIERVCEY 973
Cdd:cd18605 258 DAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQY 299
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
996-1226 |
2.95e-68 |
|
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: 230.18 E-value: 2.95e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 996 GIVEFVDYRARYRDDLGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKL 1075
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1076 NIIPQDPVLFSGTLQMNLDPLDKYPDHELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRKTKI 1155
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387192242 1156 LILDEATASIDFETDNLVQTTVRKEFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETPQNLI-HKRGLF 1226
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVF 249
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
386-583 |
6.44e-64 |
|
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: 216.43 E-value: 6.44e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 386 INASFSWDkTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIV-----------------QRKGSVA 448
Cdd:cd03290 4 TNGYFSWG-SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRYSVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 449 YVSQQAWIQNCILQENILFGSVMQKQLYERVLEACALLPDLEQLPNGDQTEIGEKGVNISGGQKHRVCLARAVYSGADIY 528
Cdd:cd03290 83 YAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1387192242 529 LLDDPLSAVDVHVAKQLFEKviGSSGMLRN--KTRILVTHNLTLLPQMDLIVVMESG 583
Cdd:cd03290 163 FLDDPFSALDIHLSDHLMQE--GILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
101-597 |
3.58e-63 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 226.20 E-value: 3.58e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 101 RKPSLLRALWNTF---KFALIQVALFKVLADVLSFTSPLIMKQMILFCEQRPDFGwSGYGYALALFVVVFLQTLI--LQQ 175
Cdd:COG1132 4 SPRKLLRRLLRYLrpyRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLS-ALLLLLLLLLGLALLRALLsyLQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 176 YQRFKMltSAKIKTAVIGLIYKKALLLSNVSRKQFSTGEIINLMATDTQQLMDLMTN-INLLWSAPFQILMAVSLL---- 250
Cdd:COG1132 83 YLLARL--AQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHgLPQLVRSVVTLIGALVVLfvid 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 251 WQeLGPAVLAGVAVLVFVIpmnALVANRMKKLKKNQRKNKDKQIKLLNEILHGIKILKLYAWEPS----YKKKIIEIREQ 326
Cdd:COG1132 161 WR-LALIVLLVLPLLLLVL---RLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERelerFREANEELRRA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 327 ELEVQK---------------------------------SAGYLAVFSMLTLTCIPFLTRI------------SLVHLED 361
Cdd:COG1132 237 NLRAARlsalffplmellgnlglalvllvggllvlsgslTVGDLVAFILYLLRLFGPLRQLanvlnqlqralaSAERIFE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 362 FLNTEELLPHSIEANYI--GDHAIGFINASFSWDKtGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEME---- 435
Cdd:COG1132 317 LLDEPPEIPDPPGAVPLppVRGEIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDptsg 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 436 --KLKGIVQRK-------GSVAYVSQQAWIQNCILQENILFG--SVMQKQLyERVLEACALLPDLEQLPNGDQTEIGEKG 504
Cdd:COG1132 396 riLIDGVDIRDltleslrRQIGVVPQDTFLFSGTIRENIRYGrpDATDEEV-EEAAKAAQAHEFIEALPDGYDTVVGERG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 505 VNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQLFEKVigsSGMLRNKTRILVTHNLTLLPQMDLIVVMESGR 584
Cdd:COG1132 475 VNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEAL---ERLMKGRTTIVIAHRLSTIRNADRILVLDDGR 551
|
570
....*....|...
gi 1387192242 585 VAQMGTYQEILAK 597
Cdd:COG1132 552 IVEQGTHEELLAR 564
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
122-352 |
1.85e-61 |
|
Six-transmembrane helical domain 1 (TMD1) 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: 350041 [Multi-domain] Cd Length: 293 Bit Score: 211.93 E-value: 1.85e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 122 LFKVLADVLSFTSPLIMKQMILFCEQRPDFG-----WSGYGYALALFVVVFLQTLILQQYQRFKMLTSAKIKTAVIGLIY 196
Cdd:cd18597 4 LLKLLADVLQVLSPLLLKYLINFVEDAYLGGpppsiGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTKAIY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 197 KKALLLSNVSRKQFSTGEIINLMATDTQQLMDLMTNINLLWSAPFQILMAVSLLWQELGPAVLAGVAVLVFVIPMNALVA 276
Cdd:cd18597 84 RKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGFLM 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387192242 277 NRMKKLKKNQRKNKDKQIKLLNEILHGIKILKLYAWEPSYKKKIIEIREQELEVQKSAGYLAVFSMLTLTCIPFLT 352
Cdd:cd18597 164 KKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLA 239
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
695-973 |
3.11e-61 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 212.04 E-value: 3.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 695 NLWLSTWAKEAKHMNDFTEWKQIRSK-----------KLSIYGLLGLMQGLFVCSGAYVVTRGSLAASRVLHAQLLDNVL 763
Cdd:cd18599 23 DWWLSYWLKQGSGNTTNNVDNSTVDSgnisdnpdlnfYQLVYGGSILVILLLSLIRGFVFVKVTLRASSRLHNKLFQKIL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 764 HLPLQFFETNPIGQVINRFTKDMFIIDMRFHYYIRTWVNCTLDVIGTVLVIVGALPLFILGLIPLVFLYFTIQRYYMASS 843
Cdd:cd18599 103 RSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWFLIALIPLAIIFVFLSKIFRRAI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 844 RQIRRLAGASHSPVISHFCETLLGVSTIRAFGHEQRFIQQNKEVVNENLVCFYNNVISNRWLSVRLEFLGNLMVFFTAVL 923
Cdd:cd18599 183 RELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCAMRWLAVRLDILAVLITLITALL 262
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1387192242 924 TVLAGNSIDSAIVGLSISYALNITQTLNFWVRKACEIEANAVSIERVCEY 973
Cdd:cd18599 263 VVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEY 312
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
73-606 |
2.30e-58 |
|
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: 215.08 E-value: 2.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 73 FEKQWRKEVLRtqerqkVKSSFHKEAHTRKPSLLRALWNTF---KFALIQVALFKVLADVLSFTSPLIMKQMIlfceqrp 149
Cdd:COG2274 117 FAESWTGVALL------LEPTPEFDKRGEKPFGLRWFLRLLrryRRLLLQVLLASLLINLLALATPLFTQVVI------- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 150 DFGWSG------YGYALALFVVVFLQTLI--LQQYqrFKMLTSAKIKTAVIGLIYKKALLLSNVSRKQFSTGEIINLMaT 221
Cdd:COG2274 184 DRVLPNqdlstlWVLAIGLLLALLFEGLLrlLRSY--LLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-R 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 222 DTQQLMDLMTN--INLLWSAPFQILMAVSLLWQ--ELGPAVLAGVAVLVFVIpmnALVANRMKKLKKNQRKNKDKQIKLL 297
Cdd:COG2274 261 DVESIREFLTGslLTALLDLLFVLIFLIVLFFYspPLALVVLLLIPLYVLLG---LLFQPRLRRLSREESEASAKRQSLL 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 298 NEILHGIKILKLYAWEPSYKKKIIEIREQELEVQKSAGYLA--------VFSMLTLTCI--------------------- 348
Cdd:COG2274 338 VETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSnllstlsgLLQQLATVALlwlgaylvidgqltlgqliaf 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 349 ---------PFL-----------TRISLVHLEDFLNTE---ELLPHSIEANYIGDHaIGFINASFSWDKTGIPVLKDLNI 405
Cdd:COG2274 418 nilsgrflaPVAqligllqrfqdAKIALERLDDILDLPperEEGRSKLSLPRLKGD-IELENVSFRYPGDSPPVLDNISL 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 406 KIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQ--------------RKgSVAYVSQQAWIQNCILQENILFGSvm 471
Cdd:COG2274 497 TIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgidlrqidpaslRR-QIGVVLQDVFLFSGTIRENITLGD-- 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 472 qKQL-YERVLEAC---ALLPDLEQLPNGDQTEIGEKGVNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQLFE 547
Cdd:COG2274 574 -PDAtDEEIIEAArlaGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILE 652
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1387192242 548 KVigsSGMLRNKTRILVTHNLTLLPQMDLIVVMESGRVAQMGTYQEILAKTKNLTNLLQ 606
Cdd:COG2274 653 NL---RRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
723-1224 |
1.12e-57 |
|
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: 209.61 E-value: 1.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 723 SIYGLLGLMQGLFVCSGA------YVVTRGSLAASRVLHAQLLDNVLHLPLQFFETNPIGQVINRFTKDMFIIDMrfhYY 796
Cdd:COG4988 56 ALLPLLGLLLAVLLLRALlawlreRAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDG---YF 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 797 IRTWVNCTLDVIGTVLVIVGALPL-FILGLIPLVFLYFTI----------QRyymASSRQIRRLAGAShspviSHFCETL 865
Cdd:COG4988 133 ARYLPQLFLAALVPLLILVAVFPLdWLSGLILLVTAPLIPlfmilvgkgaAK---ASRRQWRALARLS-----GHFLDRL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 866 LGVSTIRAFGHEQRfiqQNKEV--VNENLvcfynnviSNRWLSV-RLEFLGNL-MVFFTAVltvlagnSIdsAIVGLSIS 941
Cdd:COG4988 205 RGLTTLKLFGRAKA---EAERIaeASEDF--------RKRTMKVlRVAFLSSAvLEFFASL-------SI--ALVAVYIG 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 942 YALnITQTLNFW---------------VR--------KACEIEAnAVSIERVceyetMDKEAPWITSKRPPSQWPSKGIV 998
Cdd:COG4988 265 FRL-LGGSLTLFaalfvlllapefflpLRdlgsfyhaRANGIAA-AEKIFAL-----LDAPEPAAPAGTAPLPAAGPPSI 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 999 EFVDYRARYRDDlGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLNII 1078
Cdd:COG4988 338 ELEDVSFSYPGG-RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1079 PQDPVLFSGTLQMNL---DPldKYPDHELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRKTKI 1155
Cdd:COG4988 417 PQNPYLFAGTIRENLrlgRP--DASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPL 494
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387192242 1156 LILDEATASIDFETDNLVQTTVRKEFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETPQNLIHKRG 1224
Cdd:COG4988 495 LLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1014-1224 |
2.60e-57 |
|
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: 197.83 E-value: 2.60e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLNIIPQDPVLFSGTLQMNL 1093
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSGTIMENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1094 DPLDKYPDHELW-EVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRKTKILILDEATASIDFETDNL 1172
Cdd:cd03254 98 RLGRPNATDEEViEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1387192242 1173 VQTTVRKEFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETPQNLIHKRG 1224
Cdd:cd03254 178 IQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
675-973 |
1.21e-56 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 199.08 E-value: 1.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 675 LWVWLNVAtclgQNLVGTGQNLWLSTWAKEAKHMNDFTEWKQI------------RSKKLSIYGLLGLMQGLFVCSGAYV 742
Cdd:cd18601 7 LLVLLNIA----AQVLYVLSDWWLSYWANLEEKLNDTTDRVQGenstnvdiedldRDFNLGIYAGLTAATFVFGFLRSLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 743 VTRGSLAASRVLHAQLLDNVLHLPLQFFETNPIGQVINRFTKDMFIIDMRFHYYIRTWVNCTLDVIGTVLVIVGALPLFI 822
Cdd:cd18601 83 FFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPWVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 823 LGLIPLVFLYFTIQRYYMASSRQIRRLAGASHSPVISHFCETLLGVSTIRAFGHEQRFIQQNKEVVNENLVCFYNNVISN 902
Cdd:cd18601 163 IPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLATS 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387192242 903 RWLSVRLEFLGNLMVFFTAVLTVLAGNSIDSAIVGLSISYALNITQTLNFWVRKACEIEANAVSIERVCEY 973
Cdd:cd18601 243 RWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEY 313
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
121-328 |
2.61e-55 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350042 [Multi-domain] Cd Length: 288 Bit Score: 194.31 E-value: 2.61e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 121 ALFKVLADVLSFTSPLIMKQMILFCEQRPDFGWSGYGYALALFVVVFLQTLILQQYQRFKMLTSAKIKTAVIGLIYKKAL 200
Cdd:cd18598 3 GLLKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYRKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 201 LLSNVSRKQFSTGEIINLMATDTQQLMDLMTNINLLWSAPFQILMAVSLLWQELGPAVLAGVAVLVFVIPMNALVANRMK 280
Cdd:cd18598 83 RVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRIG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1387192242 281 KLKKNQRKNKDKQIKLLNEILHGIKILKLYAWEPSYKKKIIEIREQEL 328
Cdd:cd18598 163 ALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKEL 210
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
367-623 |
7.54e-54 |
|
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: 190.07 E-value: 7.54e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 367 ELLPHSIEANYIGDHAIGFINASFS-WDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKG 445
Cdd:cd03291 19 ELLEKAKQENNDRKHSSDDNNLFFSnLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 446 SVAYVSQQAWIQNCILQENILFGSVMQKQLYERVLEACALLPDLEQLPNGDQTEIGEKGVNISGGQKHRVCLARAVYSGA 525
Cdd:cd03291 99 RISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 526 DIYLLDDPLSAVDVHVAKQLFEKVIgsSGMLRNKTRILVTHNLTLLPQMDLIVVMESGRVAQMGTYQEILAKTKNLTNLL 605
Cdd:cd03291 179 DLYLLDSPFGYLDVFTEKEIFESCV--CKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
250
....*....|....*...
gi 1387192242 606 QAFSEQETAHALKQVSVI 623
Cdd:cd03291 257 MGYDTFDQFSAERRNSIL 274
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
726-1226 |
4.82e-52 |
|
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: 193.39 E-value: 4.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 726 GLLGLM--QGLFVCSGAYVVTRGSLAASRVLHAQLLDNVLHLPLQFFETNPIGQVINRFTKDmfiIDMRFHY---YIRTW 800
Cdd:TIGR02203 59 VVIGLAvlRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFD---SEQVASAatdAFIVL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 801 VNCTLDVIGTVLVIV---GALPLFILGLIPLVFLyftIQRYYMASSRQIRRLAGASHSPVISHFCETLLGVSTIRAFGHE 877
Cdd:TIGR02203 136 VRETLTVIGLFIVLLyysWQLTLIVVVMLPVLSI---LMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 878 ----QRFIQqnkevVNENLVCFYNNVISNRWLSVRL-EFLGNL---MVFFTAVLTVLAGNSIDSAIVGLsISYALNITQT 949
Cdd:TIGR02203 213 ayetRRFDA-----VSNRNRRLAMKMTSAGSISSPItQLIASLalaVVLFIALFQAQAGSLTAGDFTAF-ITAMIALIRP 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 950 LNFWVRKACEIEANAVSIERVCEYetMDKEAPWITSKRPPSQwpSKGIVEFVDYRARYRDDLGLALQDITFQTHGEEKIG 1029
Cdd:TIGR02203 287 LKSLTNVNAPMQRGLAAAESLFTL--LDSPPEKDTGTRAIER--ARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVA 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1030 IVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLNIIPQDPVLFSGTLQMNL--DPLDKYPDHELWEV 1107
Cdd:TIGR02203 363 LVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIayGRTEQADRAEIERA 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1108 LELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVRKEFSDCTIL 1187
Cdd:TIGR02203 443 LAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTL 522
|
490 500 510
....*....|....*....|....*....|....*....
gi 1387192242 1188 TIAHRLHSIIDSDRVLVLDSGRITEFETPQNLIHKRGLF 1226
Cdd:TIGR02203 523 VIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLY 561
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
754-1241 |
9.79e-52 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 193.01 E-value: 9.79e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 754 LHAQLLDNVLHLPLQFFETNPIGQVINRFTKDMFII-DMrfhyyirtWVNctldVIGTVL---VIVGA-----------L 818
Cdd:PRK10790 100 LRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIrDL--------YVT----VVATVLrsaALIGAmlvamfsldwrM 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 819 PLFILGLIPLVFLYFTI-QRYYMASSRQIRR-LAGASHSpvishFCETLLGVSTIRAFGHEQRFiqqnKEVVNENLVCFY 896
Cdd:PRK10790 168 ALVAIMIFPAVLVVMVIyQRYSTPIVRRVRAyLADINDG-----FNEVINGMSVIQQFRQQARF----GERMGEASRSHY 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 897 NNvisnRWLSVRLE--FLGNLMVFFTAV----LTVLAGNSIDSAI-VGL---SISYALNITQTLNFWVRKACEIEANAVS 966
Cdd:PRK10790 239 MA----RMQTLRLDgfLLRPLLSLFSALilcgLLMLFGFSASGTIeVGVlyaFISYLGRLNEPLIELTTQQSMLQQAVVA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 967 IERVceYETMDKEA-PWITSKRPPSQwpskGIVEFVDYRARYRDDlGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCL 1045
Cdd:PRK10790 315 GERV--FELMDGPRqQYGNDDRPLQS----GRIDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1046 FRIVERSGGKIIIDGIDISTIGLHDLRGKLNIIPQDPVLFSGTLQMNLDPLDKYPDHELWEVLELCHLKEFVQSLPKKLL 1125
Cdd:PRK10790 388 MGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLY 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1126 HEISEGGENLSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVRKEFSDCTILTIAHRLHSIIDSDRVLVL 1205
Cdd:PRK10790 468 TPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVL 547
|
490 500 510
....*....|....*....|....*....|....*...
gi 1387192242 1206 DSGRITEFETPQNLIHKRGLFFDM--LTEAGitQDLGA 1241
Cdd:PRK10790 548 HRGQAVEQGTHQQLLAAQGRYWQMyqLQLAG--EELAA 583
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
776-1230 |
1.09e-49 |
|
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: 186.13 E-value: 1.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 776 GQVINRFTKDmfiIDMRFHYYIRT----WVNCTLDVIGTVLV---------IVGALPLFILGLIPLVFLyftiqRYYMAS 842
Cdd:COG4987 112 GDLLNRLVAD---VDALDNLYLRVllplLVALLVILAAVAFLaffspalalVLALGLLLAGLLLPLLAA-----RLGRRA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 843 SRQIRRLAGASHSPVIshfcETLLGVSTIRAFGHEQRFIQQNKEVVNEnlvcfynnVISNRWLSVRLEFLGNLMVFFTAV 922
Cdd:COG4987 184 GRRLAAARAALRARLT----DLLQGAAELAAYGALDRALARLDAAEAR--------LAAAQRRLARLSALAQALLQLAAG 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 923 LTVLA----------GNSIDS---AIVGLSISYALNITQTLnfwVRKACEIEANAVSIERVCEyetMDKEAPWITSKRPP 989
Cdd:COG4987 252 LAVVAvlwlaaplvaAGALSGpllALLVLAALALFEALAPL---PAAAQHLGRVRAAARRLNE---LLDAPPAVTEPAEP 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 990 SQWPSKGIVEFVDYRARYRDDLGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLH 1069
Cdd:COG4987 326 APAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDED 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1070 DLRGKLNIIPQDPVLFSGTLQMNL---DP-LDkypDHELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCL 1145
Cdd:COG4987 406 DLRRRIAVVPQRPHLFDTTLRENLrlaRPdAT---DEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLAL 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1146 ARALLRKTKILILDEATASIDFETDNLVQTTVRKEFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETPQNLIHKRGL 1225
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGR 562
|
....*
gi 1387192242 1226 FFDML 1230
Cdd:COG4987 563 YRQLY 567
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
121-352 |
1.36e-49 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) 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: 350040 [Multi-domain] Cd Length: 309 Bit Score: 178.46 E-value: 1.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 121 ALFKVLADVLSFTSPLIMKQMILFCEQRPDF-GWSGYGYALALFVVVFLQTLILQQYQRFKMLTSAKIKTAVIGLIYKKA 199
Cdd:cd18596 3 ALLAVLSSVLSFAPPFFLNRLLRYLEDPGEDaTVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 200 LLLSNVS-------------------RKQFSTGEIINLMATDTQQLMDLMTNINLLWSAPFQILMAVSLLWQELGPAVLA 260
Cdd:cd18596 83 LRRRDKSgssksseskkkdkeededeKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 261 GVAVLVFVIPMNALVANRMKKLKKNQRKNKDKQIKLLNEILHGIKILKLYAWEPSYKKKIIEIREQELEVQKSAGYLAVF 340
Cdd:cd18596 163 GLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLL 242
|
250
....*....|..
gi 1387192242 341 SMLTLTCIPFLT 352
Cdd:cd18596 243 LSLLWFLIPILV 254
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
998-1229 |
5.06e-49 |
|
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: 174.34 E-value: 5.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 998 VEFVDYRARYRDDLGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLNI 1077
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1078 IPQDPVLFSGTLQMNLdpldKY-----PDHELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRK 1152
Cdd:cd03251 81 VSQDVFLFNDTVAENI----AYgrpgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387192242 1153 TKILILDEATASIDFETDNLVQTTVRKEFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETPQNLIHKRGLFFDM 1229
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
122-359 |
2.22e-47 |
|
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 1 (TMD1) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and they belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350035 [Multi-domain] Cd Length: 309 Bit Score: 172.03 E-value: 2.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 122 LFKVLADVLSFTSPLIMKQMILFCEQR------------------PDFGWSGYGYALALFVVVFLQTLILQQYQRFKMLT 183
Cdd:cd18591 4 ILKLLGDLLGFVGPLCISGIVDYVEENtysssnstdklsvsyvtvEEFFSNGYVLAVILFLALLLQATFSQASYHIVIRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 184 SAKIKTAVIGLIYKKALLLS--NVSRKQFSTGEIINLMATDTQQLMDLMTNINLLWSAPFQILMAVSLLWQELGPAVLAG 261
Cdd:cd18591 84 GIRLKTALQAMIYEKALRLSswNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 262 VAVLVFVIPMNALVANRMKKLKKNQRKNKDKQIKLLNEILHGIKILKLYAWEPSYKKKIIEIREQELEVQKSAGYLAVFS 341
Cdd:cd18591 164 AALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWSLM 243
|
250
....*....|....*...
gi 1387192242 342 MltltcipFLTRISLVHL 359
Cdd:cd18591 244 T-------FLTQASPILV 254
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
98-597 |
3.71e-47 |
|
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: 178.80 E-value: 3.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 98 AHTRKPSLLRALWNTFKFALIqVALFKVLADVLSftsPLIMKQMILFceqrpdfgwSGYGYALALFVVVFLQTLILQQYQ 177
Cdd:COG4988 13 RGARRWLALAVLLGLLSGLLI-IAQAWLLASLLA---GLIIGGAPLS---------ALLPLLGLLLAVLLLRALLAWLRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 178 RFKMLTSAKIKTAVIGLIYKKALLLSNVSRKQFSTGEIINLM-----ATDT------QQLMDLMTninllwsAPFQILMA 246
Cdd:COG4988 80 RAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLtegveALDGyfarylPQLFLAAL-------VPLLILVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 247 VSLL-WqelgpavLAGVAVLVFV--IPM-NALVanrMKKLKKNQRKNKDKQIKL---LNEILHGIKILKLYAWEPSYKKK 319
Cdd:COG4988 153 VFPLdW-------LSGLILLVTAplIPLfMILV---GKGAAKASRRQWRALARLsghFLDRLRGLTTLKLFGRAKAEAER 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 320 IIEI----REQELEVQK----SAGYLAVFSMLTLTCIPFLTRISLVH--------------------------------- 358
Cdd:COG4988 223 IAEAsedfRKRTMKVLRvaflSSAVLEFFASLSIALVAVYIGFRLLGgsltlfaalfvlllapefflplrdlgsfyhara 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 359 --------LEDFLNTEE--LLPHSIEANYIGDHAIGFINASFSWDKtGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLS 428
Cdd:COG4988 303 ngiaaaekIFALLDAPEpaAPAGTAPLPAAGPPSIELEDVSFSYPG-GRPALDGLSLTIPPGERVALVGPSGAGKSTLLN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 429 AILGEMEKLKGIV-------------QRKGSVAYVSQQAWIQNCILQENILFGS--VMQKQLyERVLEACALLPDLEQLP 493
Cdd:COG4988 382 LLLGFLPPYSGSIlingvdlsdldpaSWRRQIAWVPQNPYLFAGTIRENLRLGRpdASDEEL-EAALEAAGLDEFVAALP 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 494 NGDQTEIGEKGVNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQLFEKVigsSGMLRNKTRILVTHNLTLLPQ 573
Cdd:COG4988 461 DGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQAL---RRLAKGRTVILITHRLALLAQ 537
|
570 580
....*....|....*....|....
gi 1387192242 574 MDLIVVMESGRVAQMGTYQEILAK 597
Cdd:COG4988 538 ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
122-355 |
1.40e-46 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain 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.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 169.32 E-value: 1.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 122 LFKVLADVLSFTSPLIMKQMILFCEQRPDFGWSGYGYALALFVVVFLQTLILQQYQRFKMLTSAKIKTAVIGLIYKKALL 201
Cdd:cd18559 4 LIKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 202 LSNVSRKQFSTGEIINLMATDTQQLMDLMTNINLLWSAPFQILMAVSLLWQELGPAVLAGVAVLVFVIPMNALVANRMKK 281
Cdd:cd18559 84 SPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387192242 282 LKKNQRKNKDKQIKLLNEILHGIKILKLYAWEPSYKKKIIEIREQELEVQKSAGYLAVFSMLTLTCIPFLTRIS 355
Cdd:cd18559 164 LKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFA 237
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
195-597 |
3.00e-46 |
|
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: 176.11 E-value: 3.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 195 IYKKALLLSNVSRKQFSTGEIINLMATDTQQLMDLMtnINLLwsAPFQILMAVSL--------LWQELGPAVLAGVAVLV 266
Cdd:COG4987 94 LYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLY--LRVL--LPLLVALLVILaavaflafFSPALALVLALGLLLAG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 267 FVIPmnALVANRMKKLKKNQRKNKDKQIKLLNEILHGIKILKLYAWEPSYKKKIIEIREQELEVQK-------------- 332
Cdd:COG4987 170 LLLP--LLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRrlarlsalaqallq 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 333 -----------------------SAGYLAVFSMLTLTCI-PFL-----------TRISLVHLEDFLNTEELLPHSIEANY 377
Cdd:COG4987 248 laaglavvavlwlaaplvaagalSGPLLALLVLAALALFeALAplpaaaqhlgrVRAAARRLNELLDAPPAVTEPAEPAP 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 378 I-GDHAIGFINASFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIV-------------QR 443
Cdd:COG4987 328 ApGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSItlggvdlrdldedDL 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 444 KGSVAYVSQQAWIQNCILQENILFG--SVMQKQLYErVLEACALLPDLEQLPNGDQTEIGEKGVNISGGQKHRVCLARAV 521
Cdd:COG4987 408 RRRIAVVPQRPHLFDTTLRENLRLArpDATDEELWA-ALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARAL 486
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387192242 522 YSGADIYLLDDPLSAVDVHVAKQLFEKVIGSsgmLRNKTRILVTHNLTLLPQMDLIVVMESGRVAQMGTYQEILAK 597
Cdd:COG4987 487 LRDAPILLLDEPTEGLDAATEQALLADLLEA---LAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQ 559
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
998-1209 |
3.47e-46 |
|
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: 163.71 E-value: 3.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 998 VEFVDYRARYRDDLGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLNI 1077
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1078 IPQDPVLFSGTLQMNLdpldkypdhelwevlelchlkefvqslpkkllheiseggenLSVGQRQLVCLARALLRKTKILI 1157
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1387192242 1158 LDEATASIDFETDNLVQTTVRKEFSDCTILTIAHRLHSIIDSDRVLVLDSGR 1209
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
996-1226 |
7.46e-46 |
|
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: 166.57 E-value: 7.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 996 GIVEFVDYRARYRDDLGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVErSGGKIIIDGIDISTIGLHDLRGKL 1075
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1076 NIIPQDPVLFSGTLQMNLDPLDKYPDHELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRKTKI 1155
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387192242 1156 LILDEATASIDFETDNLVQTTVRKEFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETPQNLIHKRGLF 1226
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
119-357 |
4.12e-45 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 165.11 E-value: 4.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 119 QVALFKVLADVLSFTSPLIMKQMI-LFCEQRPDFGWSGYGYALALFVVVFLQTLILQQY----QRFKMltsaKIKTAVIG 193
Cdd:cd18594 1 LLGILLFLEESLKIVQPLLLGRLVaYFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYffglHRYGM----QLRIALSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 194 LIYKKALLLSNVSRKQFSTGEIINLMATDTQQLMDLMTNINLLWSAPFQILMAVSLLWQELGPAVLAGVAVLVFVIPMNA 273
Cdd:cd18594 77 LIYKKTLKLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 274 LVANRMKKLKKNQRKNKDKQIKLLNEILHGIKILKLYAWEPSYKKKIIEIREQELEVQKSAGYL-AVFSMLTLTCIPFLT 352
Cdd:cd18594 157 YLGKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIrAFNMAFFFFSPTLVS 236
|
....*
gi 1387192242 353 RISLV 357
Cdd:cd18594 237 FATFV 241
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
998-1229 |
7.88e-45 |
|
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: 162.01 E-value: 7.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 998 VEFVDYRARYrDDLGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLNI 1077
Cdd:cd03253 1 IEFENVTFAY-DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1078 IPQDPVLFSGTLQMNLdpldKY-----PDHELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRK 1152
Cdd:cd03253 80 VPQDTVLFNDTIGYNI----RYgrpdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387192242 1153 TKILILDEATASIDFETDNLVQTTVRKEFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETPQNLIHKRGLFFDM 1229
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
996-1210 |
1.20e-44 |
|
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: 161.22 E-value: 1.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 996 GIVEFVDYRARYRDDLGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKL 1075
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1076 NIIPQDPVLFSGTLQMNL---DPLDKypDHELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRK 1152
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNItlgAPLAD--DERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1387192242 1153 TKILILDEATASIDFETDNLVQTTVRKEFSDCTILTIAHRLhSIID-SDRVLVLDSGRI 1210
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP-SLLDlVDRIIVMDSGRI 216
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
749-1230 |
3.30e-42 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 166.05 E-value: 3.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 749 AASRV---LHAQLLDNVLHLPLQFFETNPIGQVINRFTKDMFIIDMRFHYYIRTWV-NCTLDVIGTVLVIVGALPLFILG 824
Cdd:TIGR00958 228 TMARInlrIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLrNLVMLLGLLGFMLWLSPRLTMVT 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 825 LI--PLVFLYFTI-QRYYMASSRQIRRLAGASHSPVIshfcETLLGVSTIRAFGHEQRFIQQNKEVVNENLVCFYNNVIS 901
Cdd:TIGR00958 308 LInlPLVFLAEKVfGKRYQLLSEELQEAVAKANQVAE----EALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 902 NRWLSVRLEFLGNLM---VFFTAVLTVLAGNSIDSAIVGLSIsYALNITQTLNFWVRKACEIEANAVSIERVCEYetMDK 978
Cdd:TIGR00958 384 YAGYLWTTSVLGMLIqvlVLYYGGQLVLTGKVSSGNLVSFLL-YQEQLGEAVRVLSYVYSGMMQAVGASEKVFEY--LDR 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 979 E--APWITSKRPPsqwPSKGIVEFVDYRARY--RDDLgLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGG 1054
Cdd:TIGR00958 461 KpnIPLTGTLAPL---NLEGLIEFQDVSFSYpnRPDV-PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGG 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1055 KIIIDGIDISTIGLHDLRGKLNIIPQDPVLFSGTLQMNLD-PLDKYPDHELWEVLELCHLKEFVQSLPKKLLHEISEGGE 1133
Cdd:TIGR00958 537 QVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGS 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1134 NLSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTvrKEFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEF 1213
Cdd:TIGR00958 617 QLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEM 694
|
490
....*....|....*..
gi 1387192242 1214 ETPQNLIHKRGLFFDML 1230
Cdd:TIGR00958 695 GTHKQLMEDQGCYKHLV 711
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
998-1226 |
8.23e-42 |
|
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: 153.41 E-value: 8.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 998 VEFVDYRARYRDDLGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLNI 1077
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1078 IPQDPVLFSGTLQMNLDPLDKYPD-HELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRKTKIL 1156
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSmERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1157 ILDEATASIDFETDNLVQTTVRKEFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETPQNLIHKRGLF 1226
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLY 230
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
998-1233 |
9.97e-42 |
|
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: 153.46 E-value: 9.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 998 VEFVDYRARY--RDDLgLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKL 1075
Cdd:cd03249 1 IEFKNVSFRYpsRPDV-PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1076 NIIPQDPVLFSGTLQMNLdpldKY-----PDHELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALL 1150
Cdd:cd03249 80 GLVSQEPVLFDGTIAENI----RYgkpdaTDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1151 RKTKILILDEATASIDFETDNLVQTTVRKEFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETPQNLIHKRGLFFDML 1230
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLV 235
|
...
gi 1387192242 1231 TEA 1233
Cdd:cd03249 236 KAQ 238
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
153-366 |
9.68e-41 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350037 [Multi-domain] Cd Length: 291 Bit Score: 152.37 E-value: 9.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 153 WSGYGYALALFVVVFLQTLILQQY----QRFKMltsaKIKTAVIGLIYKKALLLSNVSRKQFSTGEIINLMATDTQQLMD 228
Cdd:cd18593 37 TEAYLYAGGVSLCSFLFIITHHPYffgmQRIGM----RLRVACSSLIYRKALRLSQAALGKTTVGQIVNLLSNDVNRFDQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 229 LMTNINLLWSAPFQILMAVSLLWQELGPAVLAGVAVLVFVIPMNALVANRMKKLKKNQRKNKDKQIKLLNEILHGIKILK 308
Cdd:cd18593 113 AVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIK 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387192242 309 LYAWEPSYKKKIIEIREQELEVQKSAGYLAVFSMLTLTC----IPFLTRISLVHLEDFLNTE 366
Cdd:cd18593 193 MYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVssklILFLTFLAYILLGNILTAE 254
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
685-973 |
1.00e-40 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain 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.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 152.37 E-value: 1.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 685 LGQNLVGTG-QNLWLSTWAKEAKHMndfTEWK-QIRskkLSIYGLLGLMQGLFVCSGAYVVTRGSLAASRVLHAQLLDNV 762
Cdd:cd18559 8 VLCNHVFSGpSNLWLLLWFDDPVNG---PQEHgQVY---LSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 763 LHLPLQFFETNPIGQVINRFTKDMFIIDMRFHYYIRTWVNCTLDVIGTVLVIVGALPLFILGlIPLVFLYFTIQRYYMAS 842
Cdd:cd18559 82 LRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVG-IPLGLLYVPVNRVYAAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 843 SRQIRRLAGASHSPVISHFCETLLGVSTIRAFGHEQRFIQQNKEVVNENLVcFYNNVISNRWLSVRLEFLGNLMVFFTAV 922
Cdd:cd18559 161 SRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELA-YLPSIVYLRALAVRLWCVGPCIVLFASF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1387192242 923 LTVLAGNSIdSAIVGLSISYALNITQTLNFWVRKACEIEANAVSIERVCEY 973
Cdd:cd18559 240 FAYVSRHSL-AGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLER 289
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
722-1205 |
1.25e-40 |
|
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: 158.22 E-value: 1.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 722 LSIYGLLGLMQGLFVCSGAYVVTRGSLAASRVLHAQLLDNVLHLPLQFFETNPIGQVINRFTKDMFIIDMRFHYYIRTWV 801
Cdd:TIGR02857 47 LGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 802 NCtldVIGTVLVIVGALP------LFILGLIPLVFLyFTIQRYYMASSRQIRRLAGAShspVIS-HFCETLLGVSTIRAF 874
Cdd:TIGR02857 127 LA---VIVPLAILAAVFPqdwisgLILLLTAPLIPI-FMILIGWAAQAAARKQWAALS---RLSgHFLDRLRGLPTLKLF 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 875 GHEQRFIQQNKEVVNENlvcfynnviSNRWLSV-RLEFLGnlmvffTAVLTVLAgnSIDSAIVGLSISYAL---NITQTL 950
Cdd:TIGR02857 200 GRAKAQAAAIRRSSEEY---------RERTMRVlRIAFLS------SAVLELFA--TLSVALVAVYIGFRLlagDLDLAT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 951 NFWV-----------RK-------ACEIEANAVSIERVCEyetmdkEAPWITSKRPPSQWPSKGIVEFVDYRARYRDDlG 1012
Cdd:TIGR02857 263 GLFVlllapefylplRQlgaqyhaRADGVAAAEALFAVLD------AAPRPLAGKAPVTAAPASSLEFSGVSVAYPGR-R 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1013 LALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLNIIPQDPVLFSGTLQMN 1092
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAEN 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1093 LDPLDKY-PDHELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRKTKILILDEATASIDFETDN 1171
Cdd:TIGR02857 416 IRLARPDaSDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEA 495
|
490 500 510
....*....|....*....|....*....|....
gi 1387192242 1172 LVQTTVRKEFSDCTILTIAHRLHSIIDSDRVLVL 1205
Cdd:TIGR02857 496 EVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
942-1229 |
9.07e-40 |
|
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: 157.29 E-value: 9.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 942 YALNITQTLNF--WV-RkacEIEANAVSIERVceYETMDKEaPWITSK--RPPSQwPSKGIVEFVDYRARYRDDLGLaLQ 1016
Cdd:COG5265 304 YLIQLYIPLNFlgFVyR---EIRQALADMERM--FDLLDQP-PEVADApdAPPLV-VGGGEVRFENVSFGYDPERPI-LK 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1017 DITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLNIIPQDPVLFSGTLQMNLdpl 1096
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNI--- 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1097 dKY--PD---HELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRKTKILILDEATASIDFETDN 1171
Cdd:COG5265 453 -AYgrPDaseEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTER 531
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 1172 LVQTTVRKEFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETPQNLIHKRGLFFDM 1229
Cdd:COG5265 532 AIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
383-597 |
1.57e-38 |
|
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: 143.91 E-value: 1.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 383 IGFINASFSWDkTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVL-----------SAILGEMEKLKGIVQ---RKgSVA 448
Cdd:cd03253 1 IEFENVTFAYD-PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILrllfrfydvssGSILIDGQDIREVTLdslRR-AIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 449 YVSQQAWIQNCILQENILFG--SVMQKQLYErVLEACALLPDLEQLPNGDQTEIGEKGVNISGGQKHRVCLARAVYSGAD 526
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGrpDATDEEVIE-AAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387192242 527 IYLLDDPLSAVDVHVAKQLFEKVigsSGMLRNKTRILVTHNLTLLPQMDLIVVMESGRVAQMGTYQEILAK 597
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAAL---RDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAK 225
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
383-597 |
4.14e-38 |
|
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: 142.75 E-value: 4.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 383 IGFINASFSWDKtGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILG--------------EMEKLKGIVQRKgSVA 448
Cdd:cd03254 3 IEFENVNFSYDE-KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRfydpqkgqilidgiDIRDISRKSLRS-MIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 449 YVSQQAWIQNCILQENILFGSVMQKQlyERVLEACALL---PDLEQLPNGDQTEIGEKGVNISGGQKHRVCLARAVYSGA 525
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATD--EEVIEAAKEAgahDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387192242 526 DIYLLDDPLSAVDVHVakqlfEKVIgSSGMLR---NKTRILVTHNLTLLPQMDLIVVMESGRVAQMGTYQEILAK 597
Cdd:cd03254 159 KILILDEATSNIDTET-----EKLI-QEALEKlmkGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
383-597 |
1.72e-37 |
|
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: 140.83 E-value: 1.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 383 IGFINASFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAIL-------GEMEkLKGIVQR-------KGSVA 448
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPrfydvdsGRIL-IDGHDVRdytlaslRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 449 YVSQQAWIQNCILQENILFGS--VMQKQLyERVLEACALLPDLEQLPNGDQTEIGEKGVNISGGQKHRVCLARAVYSGAD 526
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRpgATREEV-EEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387192242 527 IYLLDDPLSAVDVHVakqlfEKVIGSS--GMLRNKTRILVTHNLTLLPQMDLIVVMESGRVAQMGTYQEILAK 597
Cdd:cd03251 159 ILILDEATSALDTES-----ERLVQAAleRLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
762-1231 |
2.31e-37 |
|
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: 151.05 E-value: 2.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 762 VLHLPLQFFETNPIGQVINRFTKDMFIIDMRFHYYIRTWVNCTLDVI-GTVLVIVGALpLFILGLIPlVFLYFTIQRYYM 840
Cdd:TIGR01193 239 LFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIvGLFLVRQNML-LFLLSLLS-IPVYAVIIILFK 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 841 ASSRQIRRLAGASHSPVISHFCETLLGVSTIRAFGHEQ-RFIQQNKEVV---NENLVCFYNNVISNRwLSVRLEFLGNLM 916
Cdd:TIGR01193 317 RTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAeRYSKIDSEFGdylNKSFKYQKADQGQQA-IKAVTKLILNVV 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 917 VFFTAVLTVLAGNSIDSAIVGLS--ISYALN-ITQTLNFWVRkaceIEANAVSIERVCEYETMDKEapWITSKRPPSQWP 993
Cdd:TIGR01193 396 ILWTGAYLVMRGKLTLGQLITFNalLSYFLTpLENIINLQPK----LQAARVANNRLNEVYLVDSE--FINKKKRTELNN 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 994 SKGIVEF--VDYRARYRDDlglALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDL 1071
Cdd:TIGR01193 470 LNGDIVIndVSYSYGYGSN---ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTL 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1072 RGKLNIIPQDPVLFSGTLQMNL--DPLDKYPDHELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARAL 1149
Cdd:TIGR01193 547 RQFINYLPQEPYIFSGSILENLllGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARAL 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1150 LRKTKILILDEATASIDFET-----DNLVQTTvrkefsDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETPQNLIHKRG 1224
Cdd:TIGR01193 627 LTDSKVLILDESTSNLDTITekkivNNLLNLQ------DKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNG 700
|
....*..
gi 1387192242 1225 LFFDMLT 1231
Cdd:TIGR01193 701 FYASLIH 707
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
383-597 |
3.80e-37 |
|
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: 139.98 E-value: 3.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 383 IGFINASFSWD-KTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAIL-------------GEMEKLKGIVQRKGSVA 448
Cdd:cd03249 1 IEFKNVSFRYPsRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLErfydptsgeilldGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 449 YVSQQAWIQNCILQENILFGSVMQKQlyERVLEAC--ALLPD-LEQLPNGDQTEIGEKGVNISGGQKHRVCLARAVYSGA 525
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAkkANIHDfIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387192242 526 DIYLLDDPLSAVDVHVAKQLFEKVigsSGMLRNKTRILVTHNLTLLPQMDLIVVMESGRVAQMGTYQEILAK 597
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEAL---DRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1018-1232 |
1.84e-36 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 146.91 E-value: 1.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1018 ITFQTHGEEKIGIVGRTGAGKSTLSNCL--FRIVERSGGKiiidgidiSTIGLHDL-----RGKLNIIPQDPVLFSGTLQ 1090
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALlgFLPYQGSLKI--------NGIELRELdpeswRKHLSWVGQNPQLPHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1091 MNL---DPldKYPDHELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRKTKILILDEATASIDF 1167
Cdd:PRK11174 441 DNVllgNP--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387192242 1168 ETDNLVQTTVRKEFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETPQNLIHKRGLFFDMLTE 1232
Cdd:PRK11174 519 HSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAH 583
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
383-584 |
4.87e-36 |
|
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: 134.43 E-value: 4.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 383 IGFINASFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQ--------------RKgSVA 448
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILidgvdlrdldleslRK-NIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 449 YVSQQAWIQNCILQENILfgsvmqkqlyervleacallpdleqlpngdqteigekgvniSGGQKHRVCLARAVYSGADIY 528
Cdd:cd03228 80 YVPQDPFLFSGTIRENIL-----------------------------------------SGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387192242 529 LLDDPLSAVDVHVAKQLFEKVigsSGMLRNKTRILVTHNLTLLPQMDLIVVMESGR 584
Cdd:cd03228 119 ILDEATSALDPETEALILEAL---RALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
995-1210 |
9.58e-36 |
|
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: 135.68 E-value: 9.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 995 KGIVEF--VDYRARYRDDLgLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLR 1072
Cdd:cd03248 9 KGIVKFqnVTFAYPTRPDT-LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1073 GKLNIIPQDPVLFSGTLQMNLD-PLDKYPDHELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLR 1151
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1387192242 1152 KTKILILDEATASIDFETDNLVQTTVRKEFSDCTILTIAHRLHSIIDSDRVLVLDSGRI 1210
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
381-585 |
1.77e-35 |
|
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: 134.64 E-value: 1.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 381 HAIGFINASFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILG--------------EMEKLKGIVQRKGs 446
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGlykptsgsvlldgtDIRQLDPADLRRN- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 447 VAYVSQQAWIQNCILQENILFGSVMQKQlyERVLEAcALLPDLEQL----PNGDQTEIGEKGVNISGGQKHRVCLARAVY 522
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADD--ERILRA-AELAGVTDFvnkhPNGLDLQIGERGRGLSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387192242 523 SGADIYLLDDPLSAVDVHVAKQLFEKVigsSGMLRNKTRILVTHNLTLLPQMDLIVVMESGRV 585
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERL---RQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
995-1238 |
2.45e-35 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 143.56 E-value: 2.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 995 KGIVEFVDYRARYrDDLGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGK 1074
Cdd:PRK13657 332 KGAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1075 LNIIPQDPVLFSGTLQMNLDpLDKyPD---HELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLR 1151
Cdd:PRK13657 411 IAVVFQDAGLFNRSIEDNIR-VGR-PDatdEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLK 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1152 KTKILILDEATASIDFETDNLVQT---TVRKefsDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETPQNLIHKRGLFFD 1228
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAaldELMK---GRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAA 565
|
250
....*....|
gi 1387192242 1229 MLTEAGITQD 1238
Cdd:PRK13657 566 LLRAQGMLQE 575
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
730-1229 |
5.09e-35 |
|
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: 143.56 E-value: 5.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 730 LMQGLFVCSGAYVVTRGSLAASRVLHAQLLDNVLHLPLQFFETNPIGQVINRFtkdMFIIDMR----------------- 792
Cdd:TIGR03797 187 VGAAAFQLAQSLAVLRLETRMDASLQAAVWDRLLRLPVSFFRQYSTGDLASRA---MGISQIRrilsgstlttllsgifa 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 793 -FHYYIRTWVNCTLDVIGTVLVIVGALPLFILGLIplvflyftiQRYYmasSRQIRRLAGASHSPVIshfcETLLGVSTI 871
Cdd:TIGR03797 264 lLNLGLMFYYSWKLALVAVALALVAIAVTLVLGLL---------QVRK---ERRLLELSGKISGLTV----QLINGISKL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 872 RAFGHEQRFiqqnkevvnenlvcFY---NNVISNRWLSVRLEFLGNLMVFFTAVLTVLAGNSIDSAIVGLSISYALNITQ 948
Cdd:TIGR03797 328 RVAGAENRA--------------FArwaKLFSRQRKLELSAQRIENLLTVFNAVLPVLTSAALFAAAISLLGGAGLSLGS 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 949 TLNFW---------VRKACE--IEANAVsierVCEYETMD---KEAPWITSKRPPSQWPSKGI-VEFVDYRarYRDDLGL 1013
Cdd:TIGR03797 394 FLAFNtafgsfsgaVTQLSNtlISILAV----IPLWERAKpilEALPEVDEAKTDPGKLSGAIeVDRVTFR--YRPDGPL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLsnclFRIV---ERSGGKIIIDG-IDISTIGLHDLRGKLNIIPQDPVLFSGTL 1089
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTL----LRLLlgfETPESGSVFYDgQDLAGLDVQAVRRQLGVVLQNGRLMSGSI 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1090 QMNLDPLDKYPDHELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRKTKILILDEATASIDFET 1169
Cdd:TIGR03797 544 FENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRT 623
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387192242 1170 dnlvQTTVRKEFS--DCTILTIAHRLHSIIDSDRVLVLDSGRITEFETPQNLIHKRGLFFDM 1229
Cdd:TIGR03797 624 ----QAIVSESLErlKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQL 681
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
132-359 |
1.71e-34 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350036 [Multi-domain] Cd Length: 287 Bit Score: 134.23 E-value: 1.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 132 FTSPLIMKQMILFCE-QRPDFgWSGYGYALALFVVVFLQTLILQQYQRFKMLTSAKIKTAVIGLIYKKALLLSNVSRKqf 210
Cdd:cd18592 15 IGPTILIRKLLEYLEdSDSSV-WYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYKKILRLRSLGDK-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 211 STGEIINLMATDTQQLMDLMTNINLLWSAPFQILMAVSLLWQELGPAVLAGVAVLVFVIPMNALVANRMKKLKKNQRKNK 290
Cdd:cd18592 92 SVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVIT 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387192242 291 DKQIKLLNEILHGIKILKLYAWEPSYKKKIIEIREQELEVQKSAGYLAVFSMLTLTCIPFLTRIS--LVHL 359
Cdd:cd18592 172 DKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVtfLAHV 242
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
382-580 |
5.02e-32 |
|
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: 132.41 E-value: 5.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 382 AIGFINASFSWDKTGiPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQ-------------RKGSVA 448
Cdd:TIGR02857 321 SLEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAvngvpladadadsWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 449 YVSQQAWIQNCILQENILFG-SVMQKQLYERVLEACALLPDLEQLPNGDQTEIGEKGVNISGGQKHRVCLARAVYSGADI 527
Cdd:TIGR02857 400 WVPQHPFLFAGTIAENIRLArPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1387192242 528 YLLDDPLSAVDVHVAKQLFEKVigsSGMLRNKTRILVTHNLTLLPQMDLIVVM 580
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEAL---RALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
993-1226 |
9.67e-32 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 132.45 E-value: 9.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 993 PSKGIVEFVDYRARYRDDLGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLR 1072
Cdd:PRK11176 337 RAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1073 GKLNIIPQDPVLFSGTLQMNL--DPLDKYPDHELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALL 1150
Cdd:PRK11176 417 NQVALVSQNVHLFNDTIANNIayARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387192242 1151 RKTKILILDEATASIDFETDNLVQTTVRKEFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETPQNLIHKRGLF 1226
Cdd:PRK11176 497 RDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVY 572
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
359-611 |
1.70e-31 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 131.51 E-value: 1.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 359 LEDFLNTEELLPHSIEANYIGDHAIGfINAS----FSWDktGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEM 434
Cdd:PRK11174 324 LVTFLETPLAHPQQGEKELASNDPVT-IEAEdleiLSPD--GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 435 E-----KLKGIVQRKGSVAYVSQQ-AWI-QNCIL-----QENILFGSV-MQKQLYERVLEACALLPDLEQLPNGDQTEIG 501
Cdd:PRK11174 401 PyqgslKINGIELRELDPESWRKHlSWVgQNPQLphgtlRDNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIG 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 502 EKGVNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQLFEKVIGSSgmlRNKTRILVTHNLTLLPQMDLIVVME 581
Cdd:PRK11174 481 DQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS---RRQTTLMVTHQLEDLAQWDQIWVMQ 557
|
250 260 270
....*....|....*....|....*....|
gi 1387192242 582 SGRVAQMGTYQEILAKTKNLTNLLQAFSEQ 611
Cdd:PRK11174 558 DGQIVQQGDYAELSQAGGLFATLLAHRQEE 587
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
383-606 |
3.43e-30 |
|
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: 119.90 E-value: 3.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 383 IGFINASFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGSVAYVSQQAWIQ---NC 459
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRrqvGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 460 ILQENILFGSVMQKQL--------YERVLEACALLPDLE---QLPNGDQTEIGEKGVNISGGQKHRVCLARAVYSGADIY 528
Cdd:cd03252 81 VLQENVLFNRSIRDNIaladpgmsMERVIEAAKLAGAHDfisELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 529 LLDDPLSAVDVHVakqlfEKVIGSS--GMLRNKTRILVTHNLTLLPQMDLIVVMESGRVAQMGTYQEILAKTKNLTNLLQ 606
Cdd:cd03252 161 IFDEATSALDYES-----EHAIMRNmhDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
383-590 |
1.14e-28 |
|
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: 115.28 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 383 IGFINASFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKG-SVAYVSQQAWIQN--C 459
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvDISKIGLHDLRSRisI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 460 ILQENILFGSVMQKQL-----YE-----RVLEACALLPDLEQLPNGDQTEIGEKGVNISGGQKHRVCLARAVYSGADIYL 529
Cdd:cd03244 83 IPQDPVLFSGTIRSNLdpfgeYSdeelwQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387192242 530 LDDPLSAVDVHVAKQLfEKVIGSsgMLRNKTRILVTHNLTLLPQMDLIVVMESGRVAQMGT 590
Cdd:cd03244 163 LDEATASVDPETDALI-QKTIRE--AFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
179-568 |
2.36e-28 |
|
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: 121.31 E-value: 2.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 179 FKMLTSAKIKTavigliYKKALLLSNVSRKQFSTGEIINLMATDTQQLMDLMTN-INLLWSAPFQILMAVS----LLWqE 253
Cdd:TIGR02868 82 LRSLGALRVRV------YERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRvIVPAGVALVVGAAAVAaiavLSV-P 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 254 LGPAVLAGVAVLVFVIPMNALVANRMK-KLKKNQRKNKDKQiklLNEILHGIKILKLYAWEPSYKKKIIEIREQELEVQK 332
Cdd:TIGR02868 155 AALILAAGLLLAGFVAPLVSLRAARAAeQALARLRGELAAQ---LTDALDGAAELVASGALPAALAQVEEADRELTRAER 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 333 SAGY--------------LAVFSML---------------TLTCIPFLT--------------------RISLVHLEDFL 363
Cdd:TIGR02868 232 RAAAatalgaaltllaagLAVLGALwaggpavadgrlapvTLAVLVLLPlaafeafaalpaaaqqltrvRAAAERIVEVL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 364 NTEELLP----HSIEANYIGDHAIGFINASFSWDkTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKG 439
Cdd:TIGR02868 312 DAAGPVAegsaPAAGAVGLGKPTLELRDLSAGYP-GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQG 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 440 IVQRKGS-------------VAYVSQQAWIQNCILQENILFG--SVMQKQLYeRVLEACALLPDLEQLPNGDQTEIGEKG 504
Cdd:TIGR02868 391 EVTLDGVpvssldqdevrrrVSVCAQDAHLFDTTVRENLRLArpDATDEELW-AALERVGLADWLRALPDGLDTVLGEGG 469
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387192242 505 VNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQLFEKVIGSsgmLRNKTRILVTHNL 568
Cdd:TIGR02868 470 ARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAA---LSGRTVVLITHHL 530
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
677-941 |
3.34e-28 |
|
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: 115.43 E-value: 3.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 677 VWLNVATCLGQNLVGTGQNLWLSTWAKeakHMNDFTEWKQIRSKKLSI-YGLLGLMQGLFVCSGAYVVTRGSLAASRVLH 755
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILD---VLLPDGDPETQALNVYSLaLLLLGLAQFILSFLQSYLLNHTGERLSRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 756 AQLLDNVLHLPLQFFETNPIGQVINRFTKDMFIIDMRFHYYIRTWVNCTLDVIGTVLVIVGALPLFILGLIPLVFLYFTI 835
Cdd:pfam00664 78 RKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 836 QRYYMASSRQIRRLAGASHSPVISHFCETLLGVSTIRAFGHEQRFIQQNKEVVNENLVCFYNNVISNRWLSVRLEFLGNL 915
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYL 237
|
250 260 270
....*....|....*....|....*....|
gi 1387192242 916 M---VFFTAVLTVLAGN-SIDSAIVGLSIS 941
Cdd:pfam00664 238 SyalALWFGAYLVISGElSVGDLVAFLSLF 267
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
380-608 |
6.71e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 113.65 E-value: 6.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 380 DHAIGFINASFSWDKTgiPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIV--------QRKGSVAYVS 451
Cdd:COG1121 4 MPAIELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrlfgkpprRARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 452 QQAWIQ-------------NCILQENILFGsvMQKQLYERVLEACALLpDLEQLpnGDQTeIGEkgvnISGGQKHRVCLA 518
Cdd:COG1121 82 QRAEVDwdfpitvrdvvlmGRYGRRGLFRR--PSRADREAVDEALERV-GLEDL--ADRP-IGE----LSGGQQQRVLLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 519 RAVYSGADIYLLDDPLSAVDVHVAKQLFEkvigssgMLR-----NKTRILVTHNLTLLPQM-DLIVVMESGRVAQmGTYQ 592
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYE-------LLRelrreGKTILVVTHDLGAVREYfDRVLLLNRGLVAH-GPPE 223
|
250
....*....|....*.
gi 1387192242 593 EILAKtknlTNLLQAF 608
Cdd:COG1121 224 EVLTP----ENLSRAY 235
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
776-1193 |
8.44e-27 |
|
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: 116.31 E-value: 8.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 776 GQVINRFTKDmfiIDMRFHYYIRTWV---NCTLDVIGTVLVI----VGALPLFILGLIPLVFLYFTIQRYYMASSRQIRR 848
Cdd:TIGR02868 110 GDLLGRLGAD---VDALQDLYVRVIVpagVALVVGAAAVAAIavlsVPAALILAAGLLLAGFVAPLVSLRAARAAEQALA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 849 lagASHSPVISHFCETLLGVSTIRAFGHEQRFIQQNKEVvnenlvcfynnviSNRWL-----SVRLEFLGNLMVFFTAVL 923
Cdd:TIGR02868 187 ---RLRGELAAQLTDALDGAAELVASGALPAALAQVEEA-------------DRELTraerrAAAATALGAALTLLAAGL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 924 TVL----------AGNSIDSAIVGLSISYALNITQTLNFWVRKACEIEANAVSIERVCEYETMDKEAPWITSKRPPSQWP 993
Cdd:TIGR02868 251 AVLgalwaggpavADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGL 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 994 SKGIVEFVDYRARYRDDlGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRG 1073
Cdd:TIGR02868 331 GKPTLELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRR 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1074 KLNIIPQDPVLFSGTLQMNL-----DPldkyPDHELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARA 1148
Cdd:TIGR02868 410 RVSVCAQDAHLFDTTVRENLrlarpDA----TDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARA 485
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1387192242 1149 LLRKTKILILDEATASIDFETDNLVQTTVRKEFSDCTILTIAHRL 1193
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
747-970 |
1.10e-26 |
|
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; 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: 350044 [Multi-domain] Cd Length: 324 Bit Score: 112.20 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 747 SLAASRVLHAQLLDNVLHLPLQFFETNPIGQVINRFTKDMFIIDMRFHYYIRTWVNCTLDVIGTVLVIVGALPLFILGLI 826
Cdd:cd18600 98 LITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVVSILQPYIFLATV 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 827 PLVFLYFTIQRYYMASSRQIRRLAGASHSPVISHFCETLLGVSTIRAFGHEQRFIQQNKEVVNENLVCFYNNVISNRWLS 906
Cdd:cd18600 178 PVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQ 257
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387192242 907 VRLEFLgnLMVFFTAVLTVLAGNSIDS-AIVGLSISYALNITQTLNFWVRKACEIEANAVSIERV 970
Cdd:cd18600 258 MRIEMI--FVIFFTAVTFISIGTTGDGeGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRI 320
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
389-598 |
1.94e-26 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 115.97 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 389 SFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQR-------------KGSVAYVSQQAW 455
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFhdipltklqldswRSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 456 IQNCILQENILFG--SVMQKQLyERVLEACALLPDLEQLPNGDQTEIGEKGVNISGGQKHRVCLARAVYSGADIYLLDDP 533
Cdd:PRK10789 400 LFSDTVANNIALGrpDATQQEI-EHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDA 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387192242 534 LSAVDVHVAKQLFEKVigsSGMLRNKTRILVTHNLTLLPQMDLIVVMESGRVAQMGTYQEILAKT 598
Cdd:PRK10789 479 LSAVDGRTEHQILHNL---RQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1014-1209 |
3.61e-26 |
|
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: 107.17 E-value: 3.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLfriversggkiiidgidistIG-LHDLRGKLNI------IPQDPVLFS 1086
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--------------------LGeLEKLSGSVSVpgsiayVSQEPWIQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1087 GTLQMNL---DPLDKYpdhELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRKTKILILDEATA 1163
Cdd:cd03250 80 GTIRENIlfgKPFDEE---RYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1387192242 1164 SIDFET-DNLVQTTVRKEFSDC-TILTIAHRLHSIIDSDRVLVLDSGR 1209
Cdd:cd03250 157 AVDAHVgRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
339-1207 |
4.46e-26 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 116.67 E-value: 4.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 339 VFSMLTLTCI-PFLTRI-----SLVHLEDFLNTEELLPHSIEANYIGD-HAIGFINASFSWD-KTGIPVLKDLNIKIPEG 410
Cdd:PTZ00265 332 LISMFMLTIIlPNITEYmksleATNSLYEIINRKPLVENNDDGKKLKDiKKIQFKNVRFHYDtRKDVEIYKDLNFTLTEG 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 411 ALVAVVGQVGSGKSSVLS------------AILGEMEKLKGIVQR--KGSVAYVSQQAWIQNCILQENILF--------- 467
Cdd:PTZ00265 412 KTYAFVGESGCGKSTILKlierlydptegdIIINDSHNLKDINLKwwRSKIGVVSQDPLLFSNSIKNNIKYslyslkdle 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 468 ---------GSVMQKQLYERVLEACALLPDL----------------------------------------EQLPNGDQT 498
Cdd:PTZ00265 492 alsnyynedGNDSQENKNKRNSCRAKCAGDLndmsnttdsneliemrknyqtikdsevvdvskkvlihdfvSALPDKYET 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 499 EIGEKGVNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDvHVAKQLFEKVIGSSGMLRNKTRILVTHNLTLLPQMDLIV 578
Cdd:PTZ00265 572 LVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIF 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 579 VM---ESGRVAQMGTYQEILAKTKN---------------------LTNLLQAFSEQETAHALKQ------VSVINSRTV 628
Cdd:PTZ00265 651 VLsnrERGSTVDVDIIGEDPTKDNKennnknnkddnnnnnnnnnnkINNAGSYIIEQGTHDALMKnkngiyYTMINNQKV 730
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 629 ---------------LKDQILVQNDR------------------------PLLDQRKQFSVRKEKIPVGGVKF------- 662
Cdd:PTZ00265 731 sskkssnndndkdsdMKSSAYKDSERgydpdemngnskhenesasnkkscKMSDENASENNAGGKLPFLRNLFkrkpkap 810
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 663 -SVILKYLHAFGWLwvwLNVATCLGQNLVGTG-QNLWLSTWAKEAKHMNDFTEWkQIRSKKLSIYGLLgLMQGLFVCSGA 740
Cdd:PTZ00265 811 nNLRIVYREIFSYK---KDVTIIALSILVAGGlYPVFALLYAKYVSTLFDFANL-EANSNKYSLYILV-IAIAMFISETL 885
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 741 --YVVTRGSLAASRVLHAQLLDNVLHLPLQFFE--TNPIGQVINRFTKDMFIIDMrfhyyirtwvnctlDVIGTVLVIVG 816
Cdd:PTZ00265 886 knYYNNVIGEKVEKTMKRRLFENILYQEISFFDqdKHAPGLLSAHINRDVHLLKT--------------GLVNNIVIFTH 951
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 817 ALPLFILGLI------PLV-----FLYFTIQRYY-----MASSRQIRRLAGASHSPVISH-------------FCETLLG 867
Cdd:PTZ00265 952 FIVLFLVSMVmsfyfcPIVaavltGTYFIFMRVFairarLTANKDVEKKEINQPGTVFAYnsddeifkdpsflIQEAFYN 1031
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 868 VSTIRAFGHEQRFI-------------QQNKEVVNENLVCFYNNV---ISN--RWLSVRL---------EFLGNLMVF-- 918
Cdd:PTZ00265 1032 MNTVIIYGLEDYFCnliekaidysnkgQKRKTLVNSMLWGFSQSAqlfINSfaYWFGSFLirrgtilvdDFMKSLFTFlf 1111
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 919 ---FTAVLTVLAGNSiDSAIVGLSISYALnITQTLNFWVRKACEIE-ANAVSIervceyetmdkeapwitskrppsqwps 994
Cdd:PTZ00265 1112 tgsYAGKLMSLKGDS-ENAKLSFEKYYPL-IIRKSNIDVRDNGGIRiKNKNDI--------------------------- 1162
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 995 KGIVEFVDYRARYRDDLGLAL-QDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRI------------------------- 1048
Cdd:PTZ00265 1163 KGKIEIMDVNFRYISRPNVPIyKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneqdy 1242
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1049 ------------VERSGGKIIIDGIDISTI-----------------GLHDLRGKLNIIPQDPVLFSGTLQMNLdpldKY 1099
Cdd:PTZ00265 1243 qgdeeqnvgmknVNEFSLTKEGGSGEDSTVfknsgkilldgvdicdyNLKDLRNLFSIVSQEPMLFNMSIYENI----KF 1318
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1100 --PDHELWEVLELCH---LKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQ 1174
Cdd:PTZ00265 1319 gkEDATREDVKRACKfaaIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE 1398
|
1130 1140 1150
....*....|....*....|....*....|....*
gi 1387192242 1175 TTVR--KEFSDCTILTIAHRLHSIIDSDRVLVLDS 1207
Cdd:PTZ00265 1399 KTIVdiKDKADKTIITIAHRIASIKRSDKIVVFNN 1433
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
382-597 |
4.11e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 111.84 E-value: 4.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 382 AIGFINASFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKG-------------SVA 448
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqpiadyseaalrqAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 449 YVSQQAWIQNCILQENILFGS--VMQKQLYErVLEACallpDLEQLPNGDQ---TEIGEKGVNISGGQKHRVCLARAVYS 523
Cdd:PRK11160 418 VVSQRVHLFSATLRDNLLLAApnASDEALIE-VLQQV----GLEKLLEDDKglnAWLGEGGRQLSGGEQRRLGIARALLH 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 524 GADIYLLDDPLSAVDV----HVAKQLFEkvigssgMLRNKTRILVTHNLTLLPQMDLIVVMESGRVAQMGTYQEILAK 597
Cdd:PRK11160 493 DAPLLLLDEPTEGLDAeterQILELLAE-------HAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQ 563
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
383-597 |
4.75e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 111.65 E-value: 4.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 383 IGFINASFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAIL-------GEMEkLKGIVQR-------KGSVA 448
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTrfydideGEIL-LDGHDLRdytlaslRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 449 YVSQQAWIQNCILQENILFGSvmqKQLYERV-LEACALLPD----LEQLPNGDQTEIGEKGVNISGGQKHRVCLARAVYS 523
Cdd:PRK11176 421 LVSQNVHLFNDTIANNIAYAR---TEQYSREqIEEAARMAYamdfINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLR 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387192242 524 GADIYLLDDPLSAVDVHVakqlfEKVIGSS--GMLRNKTRILVTHNLTLLPQMDLIVVMESGRVAQMGTYQEILAK 597
Cdd:PRK11176 498 DSPILILDEATSALDTES-----ERAIQAAldELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQ 568
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
385-585 |
5.05e-25 |
|
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: 104.86 E-value: 5.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 385 FINASFSW-DKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGS-------------VAYV 450
Cdd:cd03248 14 FQNVTFAYpTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhskVSLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 451 SQQAWIQNCILQENILFGsvMQKQLYERVLEAC------ALLPDLEQlpnGDQTEIGEKGVNISGGQKHRVCLARAVYSG 524
Cdd:cd03248 94 GQEPVLFARSLQDNIAYG--LQSCSFECVKEAAqkahahSFISELAS---GYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387192242 525 ADIYLLDDPLSAVDVHVAKQLFEKVigsSGMLRNKTRILVTHNLTLLPQMDLIVVMESGRV 585
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQAL---YDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
387-572 |
5.16e-25 |
|
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: 104.15 E-value: 5.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 387 NASFSWDKTgiPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKG--------SVAYVSQQAWIQN 458
Cdd:cd03235 4 DLTVSYGGH--PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQRRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 459 C------------ILQENILFGSVMQKQlYERVLEACALLpDLEQLPNgdqTEIGEkgvnISGGQKHRVCLARAVYSGAD 526
Cdd:cd03235 82 DfpisvrdvvlmgLYGHKGLFRRLSKAD-KAKVDEALERV-GLSELAD---RQIGE----LSGGQQQRVLLARALVQDPD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1387192242 527 IYLLDDPLSAVDVHVAKQLFEKVIGssgmLR--NKTRILVTHNLTLLP 572
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRE----LRreGMTILVVTHDLGLVL 196
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
361-605 |
5.73e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 112.12 E-value: 5.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 361 DFLNTEELLPHSIEANYIGDHA-IGFINASFSW-DKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLK 438
Cdd:TIGR00958 456 EYLDRKPNIPLTGTLAPLNLEGlIEFQDVSFSYpNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTG 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 439 GIVQRKG-------------SVAYVSQQAWIQNCILQENILFG--SVMQKQLYERVLEACALlPDLEQLPNGDQTEIGEK 503
Cdd:TIGR00958 536 GQVLLDGvplvqydhhylhrQVALVGQEPVLFSGSVRENIAYGltDTPDEEIMAAAKAANAH-DFIMEFPNGYDTEVGEK 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 504 GVNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVakqlfEKVIGSSGMLRNKTRILVTHNLTLLPQMDLIVVMESG 583
Cdd:TIGR00958 615 GSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC-----EQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKG 689
|
250 260
....*....|....*....|..
gi 1387192242 584 RVAQMGTYQEILAKTKNLTNLL 605
Cdd:TIGR00958 690 SVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
117-351 |
8.80e-25 |
|
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: 105.42 E-value: 8.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 117 LIQVALFKVLADVLSFTSPLIMKQMI--LFCEQRPDFgWSGYGYALALFVVVFLQTLILQQYQRFKMLTSAKIKTAVIGL 194
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILdvLLPDGDPET-QALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 195 IYKKALLLSNVSRKQFSTGEIINLMATDTQQLMDLMTNINLLWSAPFQILMAVSLLWQELGPAV-LAGVAVLVFVIPMNA 273
Cdd:pfam00664 80 LFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLtLVLLAVLPLYILVSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 274 LVANRMKKLKKNQRKNKDKQIKLLNEILHGIKILKLYAWEPSYKKKIIEIREQELEVQKSAGYLAVFSMLTLTCIPFL 351
Cdd:pfam00664 160 VFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYL 237
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1001-1229 |
9.54e-25 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 110.57 E-value: 9.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1001 VDYRA-RYRDDLGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLNIIP 1079
Cdd:PRK10789 316 VNIRQfTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1080 QDPVLFSGTLQMNLdPLDKyPD---HELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRKTKIL 1156
Cdd:PRK10789 396 QTPFLFSDTVANNI-ALGR-PDatqQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387192242 1157 ILDEATASIDFETDNLVQTTVRKEFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETPQNLIHKRGLFFDM 1229
Cdd:PRK10789 474 ILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDM 546
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
396-589 |
1.28e-24 |
|
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: 102.98 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIV-----------QRKGSVAYVSQQ-AWIQNCILQE 463
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgrdvtgvpPERRNIGMVFQDyALFPHLTVAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 464 NILFGSVMQK----QLYERVLEACALL---PDLEQLPNGdqteigekgvnISGGQKHRVCLARAVYSGADIYLLDDPLSA 536
Cdd:cd03259 92 NIAFGLKLRGvpkaEIRARVRELLELVgleGLLNRYPHE-----------LSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387192242 537 VDVHVAKQLFEKVigsSGMLRN--KTRILVTHNLT-LLPQMDLIVVMESGRVAQMG 589
Cdd:cd03259 161 LDAKLREELREEL---KELQRElgITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
387-585 |
1.62e-24 |
|
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: 101.52 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 387 NASFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGsvAYVSQQAWIQ-----NCIL 461
Cdd:cd03246 5 NVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG--ADISQWDPNElgdhvGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 462 QENILF-GSVMQkqlyervleacallpdleqlpngdqteigekgvNI-SGGQKHRVCLARAVYSGADIYLLDDPLSAVDV 539
Cdd:cd03246 83 QDDELFsGSIAE---------------------------------NIlSGGQRQRLGLARALYGNPRILVLDEPNSHLDV 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1387192242 540 HVAKQLFEKVIGSSgmLRNKTRILVTHNLTLLPQMDLIVVMESGRV 585
Cdd:cd03246 130 EGERALNQAIAALK--AAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
983-1227 |
3.63e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 108.76 E-value: 3.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 983 ITSKRPPSQWP-------SKGIVEFVDYRARYRDDLGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGK 1055
Cdd:PRK11160 317 ITEQKPEVTFPttstaaaDQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1056 IIIDGIDISTIGLHDLRGKLNIIPQDPVLFSGTLQMNLD-PLDKYPDHELWEVLELCHLKEFVQSlPKKLLHEISEGGEN 1134
Cdd:PRK11160 397 ILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLlAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1135 LSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVRKEFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEFE 1214
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQG 555
|
250
....*....|...
gi 1387192242 1215 TPQNLIHKRGLFF 1227
Cdd:PRK11160 556 THQELLAQQGRYY 568
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1007-1212 |
5.22e-24 |
|
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: 100.47 E-value: 5.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1007 YRDDLGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGlHDLRGKLNIIPQDPVLFS 1086
Cdd:cd03247 10 YPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISVLNQRPYLFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1087 GTLQMNLdpldkypdhelwevlelchlkefvqslpkkllheisegGENLSVGQRQLVCLARALLRKTKILILDEATASID 1166
Cdd:cd03247 89 TTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1387192242 1167 FETDNLVQTTVRKEFSDCTILTIAHRLHSIIDSDRVLVLDSGRITE 1212
Cdd:cd03247 131 PITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
997-1213 |
5.45e-24 |
|
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: 101.81 E-value: 5.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 997 IVEFVDYRARYRDDLGL--ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVER---SGGKIIIDGIDISTIGLHDL 1071
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPtsgSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1072 RGKLNIIPQDPVLfsgtlqmNLDPLDKYPDHeLWEVLELcHLKEFVQSLPKKLLHEISEGGEN-----------LSVGQR 1140
Cdd:cd03257 81 RKEIQMVFQDPMS-------SLNPRMTIGEQ-IAEPLRI-HGKLSKKEARKEAVLLLLVGVGLpeevlnrypheLSGGQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1141 QLVCLARALLRKTKILILDEATASIDFetdnLVQTTV-------RKEFsDCTILTIAH--RLHSIIdSDRVLVLDSGRIT 1211
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDV----SVQAQIldllkklQEEL-GLTLLFITHdlGVVAKI-ADRVAVMYAGKIV 225
|
..
gi 1387192242 1212 EF 1213
Cdd:cd03257 226 EE 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1001-1225 |
1.11e-23 |
|
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: 106.53 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1001 VDYRARYRDDLgLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSG---GKIIIDGIDISTIGLHDLRGKLNI 1077
Cdd:COG1123 268 KRYPVRGKGGV-RAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSgsiLFDGKDLTKLSRRSLRELRRRVQM 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1078 IPQDPvlFSgtlQMN---------LDPLD---KYPDHELW----EVLELCHL-KEFVQSLPkkllHEiseggenLSVGQR 1140
Cdd:COG1123 347 VFQDP--YS---SLNprmtvgdiiAEPLRlhgLLSRAERRervaELLERVGLpPDLADRYP----HE-------LSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1141 QLVCLARALLRKTKILILDEATASIDFetdnLVQTTV-------RKEFsDCTILTIAHRLHSIID-SDRVLVLDSGRITE 1212
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDV----SVQAQIlnllrdlQREL-GLTYLFISHDLAVVRYiADRVAVMYDGRIVE 485
|
250 260
....*....|....*....|
gi 1387192242 1213 -------FETPQNLIHKRGL 1225
Cdd:COG1123 486 dgpteevFANPQHPYTRALL 505
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
387-584 |
1.33e-23 |
|
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: 100.23 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 387 NASFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKG-------------IVQRKGSVAYVSQQ 453
Cdd:cd03225 4 NLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGevlvdgkdltklsLKELRRKVGLVFQN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 454 AWIQ--NCILQENILFG----SVMQKQLYERV---LEACALLPDLEQLPNgdqteigekgvNISGGQKHRVCLARAVYSG 524
Cdd:cd03225 84 PDDQffGPTVEEEVAFGlenlGLPEEEIEERVeeaLELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387192242 525 ADIYLLDDPLSAVDVHVAKQLFEKVIGSSGmlRNKTRILVTHNL-TLLPQMDLIVVMESGR 584
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKA--EGKTIIIVTHDLdLLLELADRVIVLEDGK 211
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
398-689 |
1.60e-23 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 103.69 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 398 PVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGeMEK-------LKGIV--------QRKgsVAYVSQQ--------- 453
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAG-LETpdsgrivLNGRDlftnlpprERR--VGFVFQHyalfphmtv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 454 AwiqncilqENILFG-SVM---QKQLYERVLEACAL--LPDLEQ-LPNgdqteigekgvNISGGQKHRVCLARAVYSGAD 526
Cdd:COG1118 93 A--------ENIAFGlRVRppsKAEIRARVEELLELvqLEGLADrYPS-----------QLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 527 IYLLDDPLSAVDVHVAKQLfEKVigssgmLR------NKTRILVTHNLTL-LPQMDLIVVMESGRVAQMGTYQEILAKTK 599
Cdd:COG1118 154 VLLLDEPFGALDAKVRKEL-RRW------LRrlhdelGGTTVFVTHDQEEaLELADRVVVMNQGRIEQVGTPDEVYDRPA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 600 NL--------TNLLQAFSEQETAHAlkqvsvinsrtvlkDQILVQNDRPLLDQRKQFSVRKEKI-----PVGGVKFSVIL 666
Cdd:COG1118 227 TPfvarflgcVNVLRGRVIGGQLEA--------------DGLTLPVAEPLPDGPAVAGVRPHDIevsrePEGENTFPATV 292
|
330 340
....*....|....*....|....
gi 1387192242 667 KYLHAFGWLW-VWLNVATCLGQNL 689
Cdd:COG1118 293 ARVSELGPEVrVELKLEDGEGQPL 316
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
999-1209 |
1.66e-23 |
|
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: 99.85 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 999 EFVDYRARYRDDLGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLNII 1078
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1079 PQDP------------VLFsGTLQMNLDPLDKypDHELWEVLELCHLKEFVQSLPkkllheiseggENLSVGQRQLVCLA 1146
Cdd:cd03225 81 FQNPddqffgptveeeVAF-GLENLGLPEEEI--EERVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387192242 1147 RALLRKTKILILDEATASIDFETDNLVQTTVrKEFSDC--TILTIAHRLHSIID-SDRVLVLDSGR 1209
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELL-KKLKAEgkTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1006-1210 |
6.86e-23 |
|
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: 96.90 E-value: 6.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1006 RYRDDLGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLNIIPQDPVLF 1085
Cdd:cd03246 9 RYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDELF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1086 SGTLQMNLdpldkypdhelwevlelchlkefvqslpkkllheiseggenLSVGQRQLVCLARALLRKTKILILDEATASI 1165
Cdd:cd03246 89 SGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1387192242 1166 DFETDNLVQTTVRK-EFSDCTILTIAHRLHSIIDSDRVLVLDSGRI 1210
Cdd:cd03246 128 DVEGERALNQAIAAlKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
385-584 |
7.16e-23 |
|
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: 96.16 E-value: 7.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 385 FINASFSWDktGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQrkgsvayvsqqawiqncilqen 464
Cdd:cd00267 2 IENLSFRYG--GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL---------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 465 iLFGSVMQKQLYERVLEACALLPDLeqlpngdqteigekgvniSGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQ 544
Cdd:cd00267 58 -IDGKDIAKLPLEELRRRIGYVPQL------------------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRER 118
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1387192242 545 LFEKVIGSSgmLRNKTRILVTHNLTLL-PQMDLIVVMESGR 584
Cdd:cd00267 119 LLELLRELA--EEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
386-607 |
1.06e-22 |
|
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: 98.72 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 386 INASFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILG-----------EMEKLKGIVQRK--GSVAYVSQ 452
Cdd:COG1124 7 LSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGlerpwsgevtfDGRPVTRRRRKAfrRRVQMVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 453 QA-------WIQNCILQE--NILFGSVMQKQLyERVLEACALLPDL-----EQLpngdqteigekgvniSGGQKHRVCLA 518
Cdd:COG1124 87 DPyaslhprHTVDRILAEplRIHGLPDREERI-AELLEQVGLPPSFldrypHQL---------------SGGQRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 519 RAVYSGADIYLLDDPLSAVDVHVAKQ---LFEKVIGSSGMlrnkTRILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEI 594
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEilnLLKDLREERGL----TYLFVSHDLAVVAHLcDRVAVMQNGRIVEELTVADL 226
|
250
....*....|....*
gi 1387192242 595 LAKTKNLT--NLLQA 607
Cdd:COG1124 227 LAGPKHPYtrELLAA 241
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
998-1223 |
2.35e-22 |
|
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: 97.02 E-value: 2.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 998 VEFVDYRARYRDDlGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLNI 1077
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1078 IPQDPV--LFSGTLQ-------MNLdpldKYPDHELW----EVLELCHLKEFVQSLPkkllHEiseggenLSVGQRQLVC 1144
Cdd:COG1122 80 VFQNPDdqLFAPTVEedvafgpENL----GLPREEIRerveEALELVGLEHLADRPP----HE-------LSGGQKQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1145 LARALLRKTKILILDEATASIDFETDNLVQTTVRK-EFSDCTILTIAHRLHSIID-SDRVLVLDSGRITEFETPQNLIHK 1222
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSD 224
|
.
gi 1387192242 1223 R 1223
Cdd:COG1122 225 Y 225
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
398-597 |
4.20e-22 |
|
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: 102.13 E-value: 4.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 398 PVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIV-------------QRKGSVAYVSQQawIQncilqen 464
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsqwdreELGRHIGYLPQD--VE------- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 465 iLF-GSV------MQKQLYERVLEACAL--LPDL-EQLPNGDQTEIGEKGVNISGGQKHRVCLARAVYSGADIYLLDDPL 534
Cdd:COG4618 417 -LFdGTIaeniarFGDADPEKVVAAAKLagVHEMiLRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPN 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387192242 535 SAVD----------VHVAKQlfekvigssgmlRNKTRILVTHNLTLLPQMDLIVVMESGRVAQMGTYQEILAK 597
Cdd:COG4618 496 SNLDdegeaalaaaIRALKA------------RGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1015-1163 |
5.23e-22 |
|
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: 93.48 E-value: 5.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLNIIPQDPVLFSG-TLQMNL 1093
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387192242 1094 -------DPLDKYPDHELWEVLELCHLKEFVQSLpkkllheISEGGENLSVGQRQLVCLARALLRKTKILILDEATA 1163
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKLGLGDLADRP-------VGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
387-589 |
5.85e-22 |
|
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: 94.42 E-value: 5.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 387 NASFSWDKTgiPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIV-------------QRKGSVAYVSQq 453
Cdd:cd03214 4 NLSVGYGGR--TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIlldgkdlaslspkELARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 454 awiqncilqenilfgsvmqkqlyerVLEACallpDLEQLpngdqteiGEKGVN-ISGGQKHRVCLARAVYSGADIYLLDD 532
Cdd:cd03214 81 -------------------------ALELL----GLAHL--------ADRPFNeLSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 533 PLSAVDVHVAKQLFEKVIGSSGMlRNKTRILVTHNLTLLPQM-DLIVVMESGRVAQMG 589
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARE-RGKTVVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
400-535 |
2.51e-21 |
|
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: 91.56 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 400 LKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKG-------------SVAYVSQQAWIQNCI-LQENI 465
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslrkEIGYVFQDPQLFPRLtVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387192242 466 LFGSVMQKQLY----ERVLEAcallpdLEQLPNGDQ--TEIGEKGVNISGGQKHRVCLARAVYSGADIYLLDDPLS 535
Cdd:pfam00005 81 RLGLLLKGLSKrekdARAEEA------LEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
383-589 |
2.88e-21 |
|
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: 92.38 E-value: 2.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 383 IGFINASFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGSVAYVSQqawiqnCILQ 462
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE------KALS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 463 ENIlfgSVMQKQLYervLEACALLPDLeqlpngdqteigekGVNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVA 542
Cdd:cd03247 75 SLI---SVLNQRPY---LFDTTLRNNL--------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITE 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1387192242 543 KQLFEKVIgssGMLRNKTRILVTHNLTLLPQMDLIVVMESGRVAQMG 589
Cdd:cd03247 135 RQLLSLIF---EVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1014-1209 |
3.14e-21 |
|
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: 91.54 E-value: 3.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSggkiiidgidistiglhdlrgklniipqdpvlfSGTLQMNL 1093
Cdd:cd00267 14 ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT---------------------------------SGEILIDG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1094 DPLDKYPDHELwevlelchlKEFVQSLPKkllheiseggenLSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLV 1173
Cdd:cd00267 61 KDIAKLPLEEL---------RRRIGYVPQ------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERL 119
|
170 180 190
....*....|....*....|....*....|....*...
gi 1387192242 1174 QTTVRKEFSD-CTILTIAHRLHSIID-SDRVLVLDSGR 1209
Cdd:cd00267 120 LELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
387-601 |
3.53e-21 |
|
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: 98.82 E-value: 3.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 387 NASFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILG---EMEKLKGIV-------------QRKGSVAYV 450
Cdd:COG1123 9 DLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVlldgrdllelseaLRGRRIGMV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 451 SQQAWIQNCILQ------ENILFGSVMQKQLYERVLEACALLpDLEQLPNGDQTEIgekgvniSGGQKHRVCLARAVYSG 524
Cdd:COG1123 89 FQDPMTQLNPVTvgdqiaEALENLGLSRAEARARVLELLEAV-GLERRLDRYPHQL-------SGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 525 ADIYLLDDPLSAVDVHVAKQLFEkVIGSSGMLRNKTRILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEILAKTKNL 601
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILD-LLRELQRERGTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEILAAPQAL 237
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1015-1213 |
4.03e-21 |
|
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: 98.96 E-value: 4.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIidgidistIGLHDLR-------GK-LNIIPQDPVLFS 1086
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVR--------LDGADLKqwdretfGKhIGYLPQDVELFP 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1087 GTLQMNLDPLDKYPDHE-LWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRKTKILILDEATASI 1165
Cdd:TIGR01842 406 GTVAENIARFGENADPEkIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNL 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1387192242 1166 DFETDN-LVQTTVRKEFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEF 1213
Cdd:TIGR01842 486 DEEGEQaLANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARF 534
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
359-607 |
8.52e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 98.11 E-value: 8.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 359 LEDFLNTEELLPHSIE-------ANYIGDhaIGFINASFSWDKTGiPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAI- 430
Cdd:PRK13657 306 LEEFFEVEDAVPDVRDppgaidlGRVKGA--VEFDDVSFSYDNSR-QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLq 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 431 ------LGEMeKLKGI----VQRKG---SVAYVSQQAWIQNCILQENILFG--SVMQKQLYErVLEACALLPDLEQLPNG 495
Cdd:PRK13657 383 rvfdpqSGRI-LIDGTdirtVTRASlrrNIAVVFQDAGLFNRSIEDNIRVGrpDATDEEMRA-AAERAQAHDFIERKPDG 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 496 DQTEIGEKGVNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQLFEKVigsSGMLRNKTRILVTHNLTLLPQMD 575
Cdd:PRK13657 461 YDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAAL---DELMKGRTTFIIAHRLSTVRNAD 537
|
250 260 270
....*....|....*....|....*....|..
gi 1387192242 576 LIVVMESGRVAQMGTYQEILAKTKNLTNLLQA 607
Cdd:PRK13657 538 RILVFDNGRVVESGSFDELVARGGRFAALLRA 569
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
382-597 |
1.31e-20 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 97.48 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 382 AIGFINASFSWDKtGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILG--------------EMEKLKGIVQRKGsV 447
Cdd:PRK10790 340 RIDIDNVSFAYRD-DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGyypltegeirldgrPLSSLSHSVLRQG-V 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 448 AYVSQQAWIQNCILQENILFGSVMQKQLYERVLEACALLPDLEQLPNGDQTEIGEKGVNISGGQKHRVCLARAVYSGADI 527
Cdd:PRK10790 418 AMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQI 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387192242 528 YLLDDPLSAVDVHvAKQLFEKVIgssGMLRNKTRILV-THNLTLLPQMDLIVVMESGRVAQMGTYQEILAK 597
Cdd:PRK10790 498 LILDEATANIDSG-TEQAIQQAL---AAVREHTTLVViAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
398-587 |
2.01e-20 |
|
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: 91.38 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 398 PVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKG--------SVAYVSQQA----WIQnciLQENI 465
Cdd:cd03293 18 TALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepvtgpgpDRGYVFQQDallpWLT---VLDNV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 466 LFGSVMQ----KQLYERVLEACAL--LPDLE-----QLpngdqteigekgvniSGGQKHRVCLARAVYSGADIYLLDDPL 534
Cdd:cd03293 95 ALGLELQgvpkAEARERAEELLELvgLSGFEnayphQL---------------SGGMRQRVALARALAVDPDVLLLDEPF 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 535 SAVDVHVAKQLFEKVIgssGMLR--NKTRILVTHNLT---LLPqmDLIVVMES--GRVAQ 587
Cdd:cd03293 160 SALDALTREQLQEELL---DIWRetGKTVLLVTHDIDeavFLA--DRVVVLSArpGRIVA 214
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
998-1235 |
2.81e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 92.39 E-value: 2.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 998 VEFVDYRarYRDDLGLALQDITFQTHGEEKIGIVGRTGAGKSTLS---NCLFRiVERSGGKIIIDGIDISTIglHDLRGK 1074
Cdd:PRK13635 8 VEHISFR--YPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAkllNGLLL-PEAGTITVGGMVLSEETV--WDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1075 LNIIPQDP-VLFSGT---------LQMNLDPLDKYPDhELWEVLELCHLKEFVQSLPKKllheiseggenLSVGQRQLVC 1144
Cdd:PRK13635 83 VGMVFQNPdNQFVGAtvqddvafgLENIGVPREEMVE-RVDQALRQVGMEDFLNREPHR-----------LSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1145 LARALLRKTKILILDEATASIDFETDNLVQTTVR--KEFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETPQNlIHK 1222
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEE-IFK 229
|
250
....*....|...
gi 1387192242 1223 RGlffDMLTEAGI 1235
Cdd:PRK13635 230 SG---HMLQEIGL 239
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1015-1213 |
2.91e-20 |
|
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: 96.36 E-value: 2.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVE------RsggkiiidgidistIGLHDLR-----------GKLni 1077
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPptagsvR--------------LDGADLSqwdreelgrhiGYL-- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1078 iPQDPVLFSGTLQMNLDPLDKYPDHELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRKTKILI 1157
Cdd:COG4618 412 -PQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVV 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 1158 LDEATASIDFETDNLVQTTVR--KEfSDCTILTIAHRLHSIIDSDRVLVLDSGRITEF 1213
Cdd:COG4618 491 LDEPNSNLDDEGEAALAAAIRalKA-RGATVVVITHRPSLLAAVDKLLVLRDGRVQAF 547
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
997-1221 |
3.05e-20 |
|
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: 96.13 E-value: 3.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 997 IVEFVDYRARYRDDLGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKI---IIDGIDISTIGLHDLRG 1073
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISgevLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1074 KLNIIPQDPvlfsgtlQMNLDPL------------DKYPDHELW----EVLELCHLKEFVQSLPkkllHEiseggenLSV 1137
Cdd:COG1123 84 RIGMVFQDP-------MTQLNPVtvgdqiaealenLGLSRAEARarvlELLEAVGLERRLDRYP----HQ-------LSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1138 GQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVRK--EFSDCTILTIAHRLHSIID-SDRVLVLDSGRITEFE 1214
Cdd:COG1123 146 GQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDG 225
|
....*..
gi 1387192242 1215 TPQNLIH 1221
Cdd:COG1123 226 PPEEILA 232
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
387-595 |
1.02e-19 |
|
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: 90.10 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 387 NASFSWDKTgiPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKG-------------SVAYVSQQ 453
Cdd:COG1120 6 NLSVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAYVPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 454 AwiqncILQENI------LFG--------SVMQKQLYERVLEACALLpDLEQLpngdqteiGEKGVN-ISGGQKHRVCLA 518
Cdd:COG1120 84 P-----PAPFGLtvrelvALGryphlglfGRPSAEDREAVEEALERT-GLEHL--------ADRPVDeLSGGERQRVLIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 519 RAVYSGADIYLLDDPLSAVDVH-------VAKQLFEKvigssgmlRNKTRILVTHNLTLLPQM-DLIVVMESGRVAQMGT 590
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLAhqlevleLLRRLARE--------RGRTVVMVLHDLNLAARYaDRLVLLKDGRIVAQGP 221
|
....*
gi 1387192242 591 YQEIL 595
Cdd:COG1120 222 PEEVL 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1001-1219 |
1.02e-19 |
|
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: 89.86 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1001 VDYRARYRDDLglALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLNIIPQ 1080
Cdd:COG1124 9 VSYGQGGRRVP--VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1081 DPvlfSGTL--QMNLD-----PLD--KYPDHE--LWEVLELCHL-KEFVQSLPkkllHEiseggenLSVGQRQLVCLARA 1148
Cdd:COG1124 87 DP---YASLhpRHTVDrilaePLRihGLPDREerIAELLEQVGLpPSFLDRYP----HQ-------LSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387192242 1149 LLRKTKILILDEATASID----FETDNLVQtTVRKEFsDCTILTIAHRLhSIID--SDRVLVLDSGRITEFETPQNL 1219
Cdd:COG1124 153 LILEPELLLLDEPTSALDvsvqAEILNLLK-DLREER-GLTYLFVSHDL-AVVAhlCDRVAVMQNGRIVEELTVADL 226
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
378-597 |
1.18e-19 |
|
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: 94.50 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 378 IGDHAIGFINASFSWDkTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSvLS------------AILGEMEKLKGIVQR-- 443
Cdd:COG5265 353 VGGGEVRFENVSFGYD-PERPILKGVSFEVPAGKTVAIVGPSGAGKST-LArllfrfydvtsgRILIDGQDIRDVTQAsl 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 444 KGSVAYVSQQAWIQNCILQENILFG--SVMQKQLyERVLEACALLPDLEQLPNGDQTEIGEKGVNISGGQKHRVCLARAV 521
Cdd:COG5265 431 RAAIGIVPQDTVLFNDTIAYNIAYGrpDASEEEV-EAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTL 509
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 522 YSGADIYLLDDPLSAVDVHVakqlfEKVIGSS--GMLRNKTRILVTHNLTLLPQMDLIVVMESGRVAQMGTYQEILAK 597
Cdd:COG5265 510 LKNPPILIFDEATSALDSRT-----ERAIQAAlrEVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQ 582
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
387-601 |
1.32e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 92.06 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 387 NASFSWDKTgiPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGeMEKLKG--IV------------QRKgsVAYVSQ 452
Cdd:COG3839 8 NVSKSYGGV--EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG-LEDPTSgeILiggrdvtdlppkDRN--IAMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 453 qawiqNCIL------QENILFGSVMQK----QLYERVLEACALLpDLEQL----PNgdqteigekgvNISGGQKHRVCLA 518
Cdd:COG3839 83 -----SYALyphmtvYENIAFPLKLRKvpkaEIDRRVREAAELL-GLEDLldrkPK-----------QLSGGQRQRVALG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 519 RAVYSGADIYLLDDPLSAVDvhvAKqlfekvigssgmLRNKTR--------------ILVTHN----LTLlpqMDLIVVM 580
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLD---AK------------LRVEMRaeikrlhrrlgtttIYVTHDqveaMTL---ADRIAVM 207
|
250 260
....*....|....*....|.
gi 1387192242 581 ESGRVAQMGTYQEILAKTKNL 601
Cdd:COG3839 208 NDGRIQQVGTPEELYDRPANL 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
382-594 |
2.50e-19 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 90.93 E-value: 2.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 382 AIGFINASFSWDKTgiPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGeMEK-------LKGIV-------QRKgsV 447
Cdd:COG3842 5 ALELENVSKRYGDV--TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAG-FETpdsgrilLDGRDvtglppeKRN--V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 448 AYVSQQ---------AwiqncilqENILFGSVMQK----QLYERVLEACAL--LPDLE-----QLpngdqteigekgvni 507
Cdd:COG3842 80 GMVFQDyalfphltvA--------ENVAFGLRMRGvpkaEIRARVAELLELvgLEGLAdryphQL--------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 508 SGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQL-FEkvigssgmLR------NKTRILVTHN----LTLlpqMDL 576
Cdd:COG3842 137 SGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMrEE--------LRrlqrelGITFIYVTHDqeeaLAL---ADR 205
|
250
....*....|....*...
gi 1387192242 577 IVVMESGRVAQMGTYQEI 594
Cdd:COG3842 206 IAVMNDGRIEQVGTPEEI 223
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
997-1217 |
3.24e-19 |
|
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: 88.02 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 997 IVEFVDYRARYRDDLGL--ALQDITFQTHGEEKIGIVGRTGAGKSTL---SNCLFRIVERSGGKIIIDGIDISTIGLHDL 1071
Cdd:cd03258 1 MIELKNVSKVFGDTGGKvtALKDVSLSVPKGEIFGIIGRSGAGKSTLircINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1072 RGKLNIIPQDPVLFSG-TLQMNLD-PL--DKYPDHEL----WEVLELCHLKEFVQSLPkkllheiseggENLSVGQRQLV 1143
Cdd:cd03258 81 RRRIGMIFQHFNLLSSrTVFENVAlPLeiAGVPKAEIeervLELLELVGLEDKADAYP-----------AQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1144 CLARALLRKTKILILDEATASIDFE-TDNLVQ--TTVRKEFsDCTILTIAHRLHSIID-SDRVLVLDSGRITE------- 1212
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPEtTQSILAllRDINREL-GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEegtveev 228
|
....*
gi 1387192242 1213 FETPQ 1217
Cdd:cd03258 229 FANPQ 233
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
386-585 |
3.40e-19 |
|
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: 87.95 E-value: 3.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 386 INASFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILG--------------EMEKLKGIVQ--RKGSVAY 449
Cdd:cd03257 7 LSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGllkptsgsiifdgkDLLKLSRRLRkiRRKEIQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 450 VSQQAW--------IQNcILQE--NILFGSVMQKQLYERVLEACALLPD----LEQLPNGdqteigekgvnISGGQKHRV 515
Cdd:cd03257 87 VFQDPMsslnprmtIGE-QIAEplRIHGKLSKKEARKEAVLLLLVGVGLpeevLNRYPHE-----------LSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387192242 516 CLARAVYSGADIYLLDDPLSAVDVHVAKQ---LFEKVIGSSGMlrnkTRILVTHNLTLLPQM-DLIVVMESGRV 585
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQildLLKKLQEELGL----TLLFITHDLGVVAKIaDRVAVMYAGKI 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
399-589 |
3.53e-19 |
|
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: 87.31 E-value: 3.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 399 VLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKG-----------SVAYVSQQ-AWIQNCILQENIL 466
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppkdrDIAMVFQNyALYPHMTVYDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 467 FGSVMQKQ----LYERVLEACALLpDLEQLpngdqteIGEKGVNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVA 542
Cdd:cd03301 95 FGLKLRKVpkdeIDERVREVAELL-QIEHL-------LDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1387192242 543 KQLFEKvIGSSGMLRNKTRILVTHNLTLLPQM-DLIVVMESGRVAQMG 589
Cdd:cd03301 167 VQMRAE-LKRLQQRLGTTTIYVTHDQVEAMTMaDRIAVMNDGQIQQIG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
398-601 |
3.81e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 90.78 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 398 PVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKG-SVAYVSQQAWIQNCILQ-----------ENI 465
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqDITHVPAENRHVNTVFQsyalfphmtvfENV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 466 LFGSVMQK----QLYERVLEACALLpDLEQLPNgdqteigEKGVNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHV 541
Cdd:PRK09452 108 AFGLRMQKtpaaEITPRVMEALRMV-QLEEFAQ-------RKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387192242 542 AKQLFEKVigssGMLRNK---TRILVTHN----LTLlpqMDLIVVMESGRVAQMGTYQEILAKTKNL 601
Cdd:PRK09452 180 RKQMQNEL----KALQRKlgiTFVFVTHDqeeaLTM---SDRIVVMRDGRIEQDGTPREIYEEPKNL 239
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
399-600 |
4.01e-19 |
|
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: 87.78 E-value: 4.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 399 VLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGS-----------VAYVSQQ-AWIQNCILQENIL 466
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNyALFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 467 FG----SVMQKQLYERVLEACALLpDLEQLPNgdqteigEKGVNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVA 542
Cdd:cd03299 94 YGlkkrKVDKKEIERKVLEIAEML-GIDHLLN-------RKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387192242 543 KQLFE--KVIGSSgmlRNKTRILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEILAKTKN 600
Cdd:cd03299 166 EKLREelKKIRKE---FGVTVLHVTHDFEEAWALaDKVAIMLNGKLIQVGKPEEVFKKPKN 223
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
383-600 |
4.25e-19 |
|
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: 88.13 E-value: 4.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 383 IGFINASFSWdKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKG-------------SVAY 449
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 450 VSQQAWI-QNCILQENI-----LFGsVMQKQLYERVLEACALLpDLEqlpngDQTEIGEKGVNISGGQKHRVCLARAVYS 523
Cdd:cd03295 80 VIQQIGLfPHMTVEENIalvpkLLK-WPKEKIRERADELLALV-GLD-----PAEFADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 524 GADIYLLDDPLSAVDVHVAKQLFEKVIGSSGMLrNKTRILVTHNL-TLLPQMDLIVVMESGRVAQMGTYQEILAKTKN 600
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQEL-GKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSPAN 229
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
398-594 |
4.97e-19 |
|
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: 87.78 E-value: 4.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 398 PVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIV-----------QRKGSVAYVSQQ-AWIQNCILQENI 465
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggedatdvpVQERNVGFVFQHyALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 466 LFGSVMQK--------QLYERVLEacalLPDLEQL-------PNgdqteigekgvNISGGQKHRVCLARAVYSGADIYLL 530
Cdd:cd03296 96 AFGLRVKPrserppeaEIRAKVHE----LLKLVQLdwladryPA-----------QLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387192242 531 DDPLSAVDVHVAKQLfekvigsSGMLR------NKTRILVTHNLT-LLPQMDLIVVMESGRVAQMGTYQEI 594
Cdd:cd03296 161 DEPFGALDAKVRKEL-------RRWLRrlhdelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1004-1217 |
5.24e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 92.56 E-value: 5.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1004 RARYRDDLGLALQDITFQT-HGE-------------EKIGIVGRTGAGKSTLsnclFRiversggkiiidgidiS----- 1064
Cdd:COG4178 354 RIETSEDGALALEDLTLRTpDGRplledlslslkpgERLLITGPSGSGKSTL----LR----------------Aiaglw 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1065 -----TIGLHDLRGKLnIIPQDPVLFSGTLQMNL---DPLDKYPDHELWEVLELCHLKEFVQSLpkkllHEISEGGENLS 1136
Cdd:COG4178 414 pygsgRIARPAGARVL-FLPQRPYLPLGTLREALlypATAEAFSDAELREALEAVGLGHLAERL-----DEEADWDQVLS 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1137 VGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVRKEFSDCTILTIAHR-----LHsiidsDRVLVLD---SG 1208
Cdd:COG4178 488 LGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRstlaaFH-----DRVLELTgdgSW 562
|
....*....
gi 1387192242 1209 RITEFETPQ 1217
Cdd:COG4178 563 QLLPAEAPA 571
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
389-586 |
7.46e-19 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 87.84 E-value: 7.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 389 SFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKG--------SVAYVSQQA----Wi 456
Cdd:COG1116 16 RFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvtgpgpDRGVVFQEPallpW- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 457 qnciL--QENILFGSVMQ----KQLYERVLEACAL--LPDLEQ-LPNgdqteigekgvNISGGQKHRVCLARAVYSGADI 527
Cdd:COG1116 95 ----LtvLDNVALGLELRgvpkAERRERARELLELvgLAGFEDaYPH-----------QLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387192242 528 YLLDDPLSAVDVHVAKQL---FEKVIGSSGmlrnKTRILVTHNLT---LLPqmDLIVVMES--GRVA 586
Cdd:COG1116 160 LLMDEPFGALDALTRERLqdeLLRLWQETG----KTVLFVTHDVDeavFLA--DRVVVLSArpGRIV 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1015-1211 |
1.12e-18 |
|
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: 84.79 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSggkiiidgidistiglhdlrgklniipqdpvlfSGTLQMNLD 1094
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS---------------------------------SGEILLDGK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1095 PLDKYPDHE-------LWEVLELCHLKEFVQslpkKLLHEiseggenLSVGQRQLVCLARALLRKTKILILDEATASIDF 1167
Cdd:cd03214 62 DLASLSPKElarkiayVPQALELLGLAHLAD----RPFNE-------LSGGERQRVLLARALAQEPPILLLDEPTSHLDI 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1387192242 1168 ----ETDNLVQTTVRKEfsDCTILTIAHRL-HSIIDSDRVLVLDSGRIT 1211
Cdd:cd03214 131 ahqiELLELLRRLARER--GKTVVMVLHDLnLAARYADRVILLKDGRIV 177
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
394-585 |
3.20e-18 |
|
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: 84.85 E-value: 3.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 394 KTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSaILGEMEKL-KGIVQ-----------------RKGSVAYVSQQ-A 454
Cdd:cd03255 14 GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVRvdgtdisklsekelaafRRRHIGFVFQSfN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 455 WIQNCILQENILFGSVMQKQLY----ERVLEACALLpDLEQLPNgdqteigEKGVNISGGQKHRVCLARAVYSGADIYLL 530
Cdd:cd03255 93 LLPDLTALENVELPLLLAGVPKkerrERAEELLERV-GLGDRLN-------HYPSELSGGQQQRVAIARALANDPKIILA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1387192242 531 DDPLSAVDVHVAKQLFEkVIGSSGMLRNKTRILVTHNLTLLPQMDLIVVMESGRV 585
Cdd:cd03255 165 DEPTGNLDSETGKEVME-LLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
394-645 |
3.55e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 86.09 E-value: 3.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 394 KTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKG---IVQ-------RKGSVAYVSQQA---WIQNCI 460
Cdd:PRK15056 17 RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGkisILGqptrqalQKNLVAYVPQSEevdWSFPVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 461 LQENILFGS--------VMQKQLYERVLEACALLPDLEQlpngDQTEIGEkgvnISGGQKHRVCLARAVYSGADIYLLDD 532
Cdd:PRK15056 97 VEDVVMMGRyghmgwlrRAKKRDRQIVTAALARVDMVEF----RHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 533 PLSAVDVhvakQLFEKVIGSSGMLRN--KTRILVTHNLTLLPQMDLIVVMESGRVAQMGTYQeilaKTKNLTNLLQAFSe 610
Cdd:PRK15056 169 PFTGVDV----KTEARIISLLRELRDegKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE----TTFTAENLELAFS- 239
|
250 260 270
....*....|....*....|....*....|....*
gi 1387192242 611 qetaHALKQVSVINSrtvlKDQILVQNDRPLLDQR 645
Cdd:PRK15056 240 ----GVLRHVALNGS----EESIITDDERPFISHR 266
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
400-589 |
4.25e-18 |
|
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: 84.27 E-value: 4.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 400 LKDLNIKIP---EGALVAVVGQVGSGKSSVLSAILGeMEKL-KGIV-------------------QRKgsVAYVSQQ-AW 455
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAG-LEKPdGGTIvlngtvlfdsrkkinlppqQRK--IGLVFQQyAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 456 IQNCILQENILFG-----SVMQKQLYERVLEACALLPDLEQLPNGdqteigekgvnISGGQKHRVCLARAVYSGADIYLL 530
Cdd:cd03297 87 FPHLNVRENLAFGlkrkrNREDRISVDELLDLLGLDHLLNRYPAQ-----------LSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 531 DDPLSAVDVHVAKQLfEKVIGSSGMLRNKTRILVTHNLTLLPQM-DLIVVMESGRVAQMG 589
Cdd:cd03297 156 DEPFSALDRALRLQL-LPELKQIKKNLNIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
398-585 |
4.46e-18 |
|
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: 83.22 E-value: 4.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 398 PVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVqrkgsvayvsqqawiqncilqenILFGSVMQKQlYE 477
Cdd:cd03230 14 TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEI-----------------------KVLGKDIKKE-PE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 478 RVLEACALLPDLEQLPngdQTEIGEKGVNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQLFEKVIGSSGmlR 557
Cdd:cd03230 70 EVKRRIGYLPEEPSLY---ENLTVRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKK--E 144
|
170 180
....*....|....*....|....*....
gi 1387192242 558 NKTRILVTHNLTLLPQM-DLIVVMESGRV 585
Cdd:cd03230 145 GKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
396-600 |
5.94e-18 |
|
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: 84.52 E-value: 5.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQ------RKGSVAYVSQQAWI-QNCIL------Q 462
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILidgedvRKEPREARRQIGVLpDERGLydrltvR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 463 ENI-LFGSVMQKQLYERVLEACALLPDLEQLPNGDQteigeKGVNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVhV 541
Cdd:COG4555 93 ENIrYFAELYGLFDEELKKRIEELIELLGLEEFLDR-----RVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV-M 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387192242 542 AKQLFEKVIGSsgmLRN--KTRILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEILAKTKN 600
Cdd:COG4555 167 ARRLLREILRA---LKKegKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
394-596 |
6.09e-18 |
|
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: 88.81 E-value: 6.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 394 KTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILG--------------EMEKLKG--IVQRKGSVAYVSQQAWIQ 457
Cdd:COG1123 275 KGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGllrptsgsilfdgkDLTKLSRrsLRELRRRVQMVFQDPYSS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 458 -NC------ILQENI-LFGSVMQKQLYERV---LEACALLPD-LEQLPNGdqteigekgvnISGGQKHRVCLARAVYSGA 525
Cdd:COG1123 355 lNPrmtvgdIIAEPLrLHGLLSRAERRERVaelLERVGLPPDlADRYPHE-----------LSGGQRQRVAIARALALEP 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 526 DIYLLDDPLSAVDVHVAKQLFEkvigssgMLR------NKTRILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEILA 596
Cdd:COG1123 424 KLLILDEPTSALDVSVQAQILN-------LLRdlqrelGLTYLFISHDLAVVRYIaDRVAVMYDGRIVEDGPTEEVFA 494
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
399-594 |
7.46e-18 |
|
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: 84.15 E-value: 7.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 399 VLKDLNIKIPEGALVAVVGQVGSGKSSVLSAI-----LGEMEKLKGIVQRKGS---------------VAYVSQQAWIQN 458
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKdiydldvdvlelrrrVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 459 CILQENI-----LFGSVMQKQLYERVLEAC--ALLPDLEqlpnGDQTeigeKGVNISGGQKHRVCLARAVYSGADIYLLD 531
Cdd:cd03260 95 GSIYDNVayglrLHGIKLKEELDERVEEALrkAALWDEV----KDRL----HALGLSGGQQQRLCLARALANEPEVLLLD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 532 DPLSAVDVhVAKQLFEKVIGSsgmLRNKTRIL-VTHNltlLPQM----DLIVVMESGRVAQMGTYQEI 594
Cdd:cd03260 167 EPTSALDP-ISTAKIEELIAE---LKKEYTIViVTHN---MQQAarvaDRTAFLLNGRLVEFGPTEQI 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
997-1235 |
9.18e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 84.80 E-value: 9.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 997 IVEFVDYRARYRDDLGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLN 1076
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1077 IIPQDP------------VLFSgtLQMNLDPLDKYpDHELWEVLELCHLKEFVQSLPkkllheiseggENLSVGQRQLVC 1144
Cdd:PRK13648 87 IVFQNPdnqfvgsivkydVAFG--LENHAVPYDEM-HRRVSEALKQVDMLERADYEP-----------NALSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1145 LARALLRKTKILILDEATASIDFETDNLVQTTVR--KEFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETPQNLIHK 1222
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDH 232
|
250
....*....|...
gi 1387192242 1223 RglffDMLTEAGI 1235
Cdd:PRK13648 233 A----EELTRIGL 241
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
380-604 |
1.29e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 84.42 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 380 DHAIGFINASFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGeMEKLKgivqrKGSVAYVSQQAWIQN- 458
Cdd:PRK13648 5 NSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIG-IEKVK-----SGEIFYNNQAITDDNf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 459 --------------------CILQENILFG----SVMQKQLYERVLEAcalLPDLEQLPNGDqteigEKGVNISGGQKHR 514
Cdd:PRK13648 79 eklrkhigivfqnpdnqfvgSIVKYDVAFGlenhAVPYDEMHRRVSEA---LKQVDMLERAD-----YEPNALSGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 515 VCLARAVYSGADIYLLDDPLSAVDVHVAKQLFEkVIGSSGMLRNKTRILVTHNLTLLPQMDLIVVMESGRVAQMGTYQEI 594
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNLLD-LVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
250
....*....|
gi 1387192242 595 LAKTKNLTNL 604
Cdd:PRK13648 230 FDHAEELTRI 239
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
398-598 |
1.36e-17 |
|
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: 83.32 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 398 PVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKG----SVAYVSQQAWIQNC--ILQENILFGS-- 469
Cdd:cd03261 14 TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisGLSEAELYRLRRRMgmLFQSGALFDSlt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 470 ----VM----------QKQLYERV---LEACALLPDLEQLPngdqteiGEkgvnISGGQKHRVCLARAVYSGADIYLLDD 532
Cdd:cd03261 94 vfenVAfplrehtrlsEEEIREIVlekLEAVGLRGAEDLYP-------AE----LSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387192242 533 PLSAVDvHVAKQLFEKVIGSSGMLRNKTRILVTHNL-TLLPQMDLIVVMESGRVAQMGTYQEILAKT 598
Cdd:cd03261 163 PTAGLD-PIASGVIDDLIRSLKKELGLTSIMVTHDLdTAFAIADRIAVLYDGKIVAEGTPEELRASD 228
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
928-1205 |
2.57e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 88.16 E-value: 2.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 928 GNSIDSAIVGLSISYAL------NITQTLnfwvrKACEIEANAvsiervceYETMDKEaPWITSKRPPSQWPSKGIVEFV 1001
Cdd:PTZ00265 321 GGSVISILLGVLISMFMltiilpNITEYM-----KSLEATNSL--------YEIINRK-PLVENNDDGKKLKDIKKIQFK 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1002 DYRARY--RDDLGLaLQDITFQTHGEEKIGIVGRTGAGKSTLsnclFRIVERSGGKIIIDGIDISTIGLHDL-----RGK 1074
Cdd:PTZ00265 387 NVRFHYdtRKDVEI-YKDLNFTLTEGKTYAFVGESGCGKSTI----LKLIERLYDPTEGDIIINDSHNLKDInlkwwRSK 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1075 LNIIPQDPVLFSGTLQMN----------LDPLDKY--------------------------------------------- 1099
Cdd:PTZ00265 462 IGVVSQDPLLFSNSIKNNikyslyslkdLEALSNYynedgndsqenknkrnscrakcagdlndmsnttdsneliemrkny 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1100 ---PDHELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTT 1176
Cdd:PTZ00265 542 qtiKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
|
330 340 350
....*....|....*....|....*....|.
gi 1387192242 1177 VR--KEFSDCTILTIAHRLHSIIDSDRVLVL 1205
Cdd:PTZ00265 622 INnlKGNENRITIIIAHRLSTIRYANTIFVL 652
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
396-601 |
4.49e-17 |
|
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: 81.90 E-value: 4.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILG-----------EMEKLKGIVQRKGSVAYVSQQ-AWIQNCILQE 463
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGfetptsgeillDGKDITNLPPHKRPVNTVFQNyALFPHLTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 464 NILFGSVMQK----QLYERVLEACALLpDLEQLPNGDQTEIgekgvniSGGQKHRVCLARAVYSGADIYLLDDPLSAVDV 539
Cdd:cd03300 92 NIAFGLRLKKlpkaEIKERVAEALDLV-QLEGYANRKPSQL-------SGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387192242 540 HVAKQL------FEKVIGSsgmlrnkTRILVTHN----LTLlpqMDLIVVMESGRVAQMGTYQEILAKTKNL 601
Cdd:cd03300 164 KLRKDMqlelkrLQKELGI-------TFVFVTHDqeeaLTM---SDRIAVMNKGKIQQIGTPEEIYEEPANR 225
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
997-1233 |
4.57e-17 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 82.06 E-value: 4.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 997 IVEFVDYRARYRDDLglALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSggkiiidgidiS---TIGLHDLRG 1073
Cdd:COG1121 6 AIELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPT-----------SgtvRLFGKPPRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1074 KLNII---PQ----DP--------VLFSGTL-QMNLDPLDKYPDHEL-WEVLELCHLKEFVQSLpkkllheISEggenLS 1136
Cdd:COG1121 73 ARRRIgyvPQraevDWdfpitvrdVVLMGRYgRRGLFRRPSRADREAvDEALERVGLEDLADRP-------IGE----LS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1137 VGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTV---RKEfsDCTILTIAHRLHSIID-SDRVLVLDSGRIT- 1211
Cdd:COG1121 142 GGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLrelRRE--GKTILVVTHDLGAVREyFDRVLLLNRGLVAh 219
|
250 260
....*....|....*....|....*.
gi 1387192242 1212 ----EFETPQNLIHKRGLFFDMLTEA 1233
Cdd:COG1121 220 gppeEVLTPENLSRAYGGPVALLAHG 245
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1014-1224 |
5.71e-17 |
|
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: 81.83 E-value: 5.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRiVERSGGKIIIDGIDISTIGLHDLRGKLNIIPQDPVLFSG-TLQMN 1092
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAG-LLKPDSGSILIDGEDVRKEPREARRQIGVLPDERGLYDRlTVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1093 LD---PLDKYPDHELWEVLE-LCHLKEFVQSLPKKLlheiseggENLSVGQRQLVCLARALLRKTKILILDEATASIDFE 1168
Cdd:COG4555 95 IRyfaELYGLFDEELKKRIEeLIELLGLEEFLDRRV--------GELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387192242 1169 TdnlvQTTVRKEF-----SDCTILTIAHRLHSIID-SDRVLVLDSGRITEFETPQNLIHKRG 1224
Cdd:COG4555 167 A----RRLLREILralkkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
389-585 |
7.02e-17 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 81.24 E-value: 7.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 389 SFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSaILG---------------EMEKLKGIVQ---RKGSVAYV 450
Cdd:COG1136 13 SYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILGgldrptsgevlidgqDISSLSERELarlRRRHIGFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 451 SQQ--------AWiqncilqENI----LFGSVMQKQLYERVLEACAL--LPD-LEQLPNgdqteigekgvNISGGQKHRV 515
Cdd:COG1136 92 FQFfnllpeltAL-------ENValplLLAGVSRKERRERARELLERvgLGDrLDHRPS-----------QLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387192242 516 CLARAVYSGADIYLLDDPLSAVDVHVAKQLFEkvigssgMLR------NKTRILVTHNLTLLPQMDLIVVMESGRV 585
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLE-------LLRelnrelGTTIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
390-584 |
1.36e-16 |
|
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: 78.77 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 390 FSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKG-------IVQRKGSVAYVSQQAWiqNCILQ 462
Cdd:cd03229 6 VSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGsilidgeDLTDLEDELPPLRRRI--GMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 463 ENILFgSVMQkqlyerVLEACALLpdleqlpngdqteigekgvnISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVA 542
Cdd:cd03229 84 DFALF-PHLT------VLENIALG--------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITR 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1387192242 543 K---QLFEKVIGSSGMlrnkTRILVTHNLTLLPQM-DLIVVMESGR 584
Cdd:cd03229 137 RevrALLKSLQAQLGI----TVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1014-1209 |
1.50e-16 |
|
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: 78.77 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLH--DLRGKLNIIPQDPVLFSgtlqm 1091
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRIGMVFQDFALFP----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1092 NLDPLDKypdhelwevlelchlkefvqslpkkllheISEGgenLSVGQRQLVCLARALLRKTKILILDEATASIDFETDN 1171
Cdd:cd03229 90 HLTVLEN-----------------------------IALG---LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1387192242 1172 LVQTTVR--KEFSDCTILTIAHRLHSIID-SDRVLVLDSGR 1209
Cdd:cd03229 138 EVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
383-594 |
2.10e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 82.44 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 383 IGFINASFSWDKtgipVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGS-----------VAYVS 451
Cdd:PRK10851 5 IANIKKSFGRTQ----VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 452 QQ-AWIQNCILQENILFG-SVMQ----------KQLYERVLEACALLPDLEQLPNgdqteigekgvNISGGQKHRVCLAR 519
Cdd:PRK10851 81 QHyALFRHMTVFDNIAFGlTVLPrrerpnaaaiKAKVTQLLEMVQLAHLADRYPA-----------QLSGGQKQRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 520 AVYSGADIYLLDDPLSAVDVHVAKQLfekvigsSGMLRNK------TRILVTHNLT-LLPQMDLIVVMESGRVAQMGTYQ 592
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALDAQVRKEL-------RRWLRQLheelkfTSVFVTHDQEeAMEVADRVVVMSQGNIEQAGTPD 222
|
..
gi 1387192242 593 EI 594
Cdd:PRK10851 223 QV 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
394-600 |
4.18e-16 |
|
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: 80.00 E-value: 4.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 394 KTGIPV-LKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQ-----------------RKGSVAYVSQQ-A 454
Cdd:cd03294 33 KTGQTVgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLidgqdiaamsrkelrelRRKKISMVFQSfA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 455 WIQNCILQENILFG----SVMQKQLYER---VLEACALLPDLEQLPNgdqteigekgvNISGGQKHRVCLARAVYSGADI 527
Cdd:cd03294 113 LLPHRTVLENVAFGlevqGVPRAEREERaaeALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDI 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387192242 528 YLLDDPLSAVDVHVAKQLFEKVIGSSGMLRnKTRILVTHNLT-LLPQMDLIVVMESGRVAQMGTYQEILAKTKN 600
Cdd:cd03294 182 LLMDEAFSALDPLIRREMQDELLRLQAELQ-KTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTNPAN 254
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1006-1222 |
4.79e-16 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 78.95 E-value: 4.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1006 RYRDdlGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCL---------------FRIVERSggkiiidgidistiglHD 1070
Cdd:COG1131 9 RYGD--KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLlgllrptsgevrvlgEDVARDP----------------AE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1071 LRGKLNIIPQDPVLFSG-TLQMNLD------PLDKYPDHELW-EVLELCHLKEFVQSLPKkllheiseggeNLSVGQRQL 1142
Cdd:COG1131 71 VRRRIGYVPQEPALYPDlTVRENLRffarlyGLPRKEARERIdELLELFGLTDAADRKVG-----------TLSGGMKQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1143 VCLARALLRKTKILILDEATASIDFETDNLVQTTVRKEFSD-CTILTIAHRLHSIID-SDRVLVLDSGRITEFETPQNLI 1220
Cdd:COG1131 140 LGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELK 219
|
..
gi 1387192242 1221 HK 1222
Cdd:COG1131 220 AR 221
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
399-594 |
4.85e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 81.30 E-value: 4.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 399 VLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGSvaYVSQQAwIQN---CI------------LQE 463
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE--DVTHRS-IQQrdiCMvfqsyalfphmsLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 464 NILFGSVMQK----QLYERVLEACALLpDLEQLPNG--DQteigekgvnISGGQKHRVCLARAVYSGADIYLLDDPLSAV 537
Cdd:PRK11432 98 NVGYGLKMLGvpkeERKQRVKEALELV-DLAGFEDRyvDQ---------ISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 538 DVHVAKQLFEKVIGSSGMLrNKTRILVTHNLT-LLPQMDLIVVMESGRVAQMGTYQEI 594
Cdd:PRK11432 168 DANLRRSMREKIRELQQQF-NITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
398-590 |
5.19e-16 |
|
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: 78.22 E-value: 5.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 398 PVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKG-SVAYVSQQAWIQN--CILQENILF-GSVM-- 471
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGiDISTIPLEDLRSSltIIPQDPTLFsGTIRsn 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 472 --------QKQLYErvleacALlpdleqlpngdqtEIGEKGVNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHvAK 543
Cdd:cd03369 102 ldpfdeysDEEIYG------AL-------------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYA-TD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1387192242 544 QLFEKVIGSSgmLRNKTRILVTHNLTLLPQMDLIVVMESGRVAQMGT 590
Cdd:cd03369 162 ALIQKTIREE--FTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
998-1217 |
6.68e-16 |
|
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: 78.38 E-value: 6.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 998 VEFVDYRARYRDDLglALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVErsggkIIIDGIDISTIGLHD------- 1070
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLND-----LIPGAPDEGEVLLDGkdiydld 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1071 -----LRGKLNIIPQDPVLFSGTLQMNLD--------PLDKYPDHELWEVLELCHLKEFVqslpKKLLHEISeggenLSV 1137
Cdd:cd03260 74 vdvleLRRRVGMVFQKPNPFPGSIYDNVAyglrlhgiKLKEELDERVEEALRKAALWDEV----KDRLHALG-----LSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1138 GQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVRKEFSDCTILTIAHRLHSIID-SDRVLVLDSGRITEFETP 1216
Cdd:cd03260 145 GQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPT 224
|
.
gi 1387192242 1217 Q 1217
Cdd:cd03260 225 E 225
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1014-1211 |
8.15e-16 |
|
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: 76.31 E-value: 8.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSggkiiidgidistiglhdlRGKlniipqdpVLFSGTLQMNL 1093
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPD-------------------SGE--------ILVDGKEVSFA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1094 DPLDKypdhelwevlelchlkefvQSLPKKLLHEiseggenLSVGQRQLVCLARALLRKTKILILDEATASI-DFETDNL 1172
Cdd:cd03216 68 SPRDA-------------------RRAGIAMVYQ-------LSVGERQMVEIARALARNARLLILDEPTAALtPAEVERL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1387192242 1173 VQTTVRKEFSDCTILTIAHRLHSIID-SDRVLVLDSGRIT 1211
Cdd:cd03216 122 FKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1015-1220 |
8.53e-16 |
|
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: 78.55 E-value: 8.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLNIIPQDPVL-FSGTL---- 1089
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPPApFGLTVrelv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1090 -------QMNLDPLDKYpDHEL-WEVLELCHLKEFVQslpkKLLHEISeGGEnlsvgqRQLVCLARALLRKTKILILDEA 1161
Cdd:COG1120 97 algryphLGLFGRPSAE-DREAvEEALERTGLEHLAD----RPVDELS-GGE------RQRVLIARALAQEPPLLLLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387192242 1162 TASIDF----ETDNLVQTTVRKEfsDCTILTIAHRL-HSIIDSDRVLVLDSGRITEFETPQNLI 1220
Cdd:COG1120 165 TSHLDLahqlEVLELLRRLARER--GRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
396-598 |
1.25e-15 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 77.80 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIV------------QRKGSVAYVSQQAWI-QNCILQ 462
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrvlgedvardpaEVRRRIGYVPQEPALyPDLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 463 ENI-LFGSVM------QKQLYERVLEACALLPDLEQLPNgdqteigekgvNISGGQKHRVCLARAVYSGADIYLLDDPLS 535
Cdd:COG1131 92 ENLrFFARLYglprkeARERIDELLELFGLTDAADRKVG-----------TLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387192242 536 AVDVHVAKQLFEKVIGSSGmlRNKTRILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEILAKT 598
Cdd:COG1131 161 GLDPEARRELWELLRELAA--EGKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKARL 222
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
382-595 |
1.42e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 78.49 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 382 AIGFINASFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSS---VLSAIL----GEMeKLKGIVQRKGSVAYVSQQA 454
Cdd:PRK13632 7 MIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTiskILTGLLkpqsGEI-KIDGITISKENLKEIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 455 WI--QN-------CILQENILFG--------SVMQKQLYErVLEACALLPDLEQLPNgdqteigekgvNISGGQKHRVCL 517
Cdd:PRK13632 86 GIifQNpdnqfigATVEDDIAFGlenkkvppKKMKDIIDD-LAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 518 ARAVYSGADIYLLDDPLSAVDVHvAKQLFEKVIGSSGMLRNKTRILVTHNLTLLPQMDLIVVMESGRVAQMGTYQEIL 595
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPK-GKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
396-614 |
1.70e-15 |
|
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: 82.27 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILgEMEKLKGIVQRKG-SVAYVSQQAWIQ--NCILQENILFGSVMQ 472
Cdd:TIGR01271 1231 GRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGvSWNSVTLQTWRKafGVIPQKVFIFSGTFR 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 473 KQL--YE--------RVLEACALLPDLEQLPNGDQTEIGEKGVNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDvHVA 542
Cdd:TIGR01271 1310 KNLdpYEqwsdeeiwKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLD-PVT 1388
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387192242 543 KQLFEKVIGSSgmLRNKTRILVTHNLTLLPQMDLIVVMESGRVAQMGTYQEILAKTknlTNLLQAFSEQETA 614
Cdd:TIGR01271 1389 LQIIRKTLKQS--FSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNET---SLFKQAMSAADRL 1455
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
396-580 |
1.98e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 76.12 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKG--SVAYVSQQ------------------AW 455
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRsevpdslpltvrdlvamgRW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 456 iqncilQENILFG--SVMQKQLYERVLEACALLpDLEQLPngdqteIGEkgvnISGGQKHRVCLARAVYSGADIYLLDDP 533
Cdd:NF040873 84 ------ARRGLWRrlTRDDRAAVDDALERVGLA-DLAGRQ------LGE----LSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1387192242 534 LSAVDVHvAKQLFEKVIGSSgMLRNKTRILVTHNLTLLPQMDLIVVM 580
Cdd:NF040873 147 TTGLDAE-SRERIIALLAEE-HARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
387-612 |
2.06e-15 |
|
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: 77.97 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 387 NASFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILgEMEKLKGIVQRKG-SVAYVSQQAWIQ--NCILQE 463
Cdd:cd03289 7 DLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvSWNSVPLQKWRKafGVIPQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 464 NILFGSVMQKQL--YE--------RVLEACALLPDLEQLPNGDQTEIGEKGVNISGGQKHRVCLARAVYSGADIYLLDDP 533
Cdd:cd03289 86 VFIFSGTFRKNLdpYGkwsdeeiwKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEP 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387192242 534 LSAVDvHVAKQLFEKVIGSSgmLRNKTRILVTHNLTLLPQMDLIVVMESGRVAQMGTYQEILAKTknlTNLLQAFSEQE 612
Cdd:cd03289 166 SAHLD-PITYQVIRKTLKQA--FADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEK---SHFKQAISPSD 238
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1006-1210 |
2.65e-15 |
|
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: 75.13 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1006 RYRDdlGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGlHDLRGKLNIIPQDPVLf 1085
Cdd:cd03230 9 RYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGYLPEEPSL- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1086 sgtlqmnldpldkYPDHELWEVLELchlkefvqslpkkllheiseggenlSVGQRQLVCLARALLRKTKILILDEATASI 1165
Cdd:cd03230 85 -------------YENLTVRENLKL-------------------------SGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1387192242 1166 DFETDNLVQTTVRKE-FSDCTILTIAHRLHSIID-SDRVLVLDSGRI 1210
Cdd:cd03230 127 DPESRREFWELLRELkKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
722-929 |
2.83e-15 |
|
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: 77.98 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 722 LSIYGLLGLMQGLFVCSGAYVVTRgslAASRVLHA---QLLDNVLHLPLQFFETNPIGQVINRFTKDMFIIDMRFHYYIR 798
Cdd:cd07346 42 ALLLLLLALLRALLSYLRRYLAAR---LGQRVVFDlrrDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 799 TWVNCTLdvigTVLVIVGAL-----PLFILGLIPLVFLYFTIqRYYMASSRQIRRLAGASHSPVISHFCETLLGVSTIRA 873
Cdd:cd07346 119 QLLSDVL----TLIGALVILfylnwKLTLVALLLLPLYVLIL-RYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKA 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1387192242 874 FGHEQRFIQQNKEVVNENLVCFYNNVISNRWLSVRLEFLGNL---MVFFTAVLTVLAGN 929
Cdd:cd07346 194 FAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALgtaLVLLYGGYLVLQGS 252
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
396-596 |
3.83e-15 |
|
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: 75.93 E-value: 3.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQ---------------RKGsVAYVSQ-QAWIQNC 459
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRfdgrditglppheraRAG-IGYVPEgRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 460 ILQENILFGSVMQ-----KQLYERVLEacaLLPDLEQLPNgdqteigEKGVNISGGQKHRVCLARAVYSGADIYLLDDP- 533
Cdd:cd03224 91 TVEENLLLGAYARrrakrKARLERVYE---LFPRLKERRK-------QLAGTLSGGEQQMLAIARALMSRPKLLLLDEPs 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 534 --LSAVdvhVAKQLFEKV--IGSSGMlrnkTRILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEILA 596
Cdd:cd03224 161 egLAPK---IVEEIFEAIreLRDEGV----TILLVEQNARFALEIaDRAYVLERGRVVLEGTAAELLA 221
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1015-1208 |
4.05e-15 |
|
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: 75.83 E-value: 4.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDL----RGKLNIIPQDPVLFSGTLQ 1090
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1091 MNLDPLDKYPDHELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRKTKILILDEATASIDFE-T 1169
Cdd:cd03290 97 ENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1387192242 1170 DNLVQTTVRKEFSD--CTILTIAHRLHSIIDSDRVLVLDSG 1208
Cdd:cd03290 177 DHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
402-596 |
7.93e-15 |
|
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: 77.45 E-value: 7.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 402 DLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQ-----------------RKGSVAYVSQQAwiqncIL--- 461
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevlqdsargiflppHRRRIGYVFQEA-----RLfph 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 462 ---QENILFG-----SVMQKQLYERVLEACALLPDLEQLPNgdqteigekgvNISGGQKHRVCLARAVYSGADIYLLDDP 533
Cdd:COG4148 92 lsvRGNLLYGrkrapRAERRISFDEVVELLGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387192242 534 LSAVDVHvAKQ----LFEKvigssgmLRNKTRI---LVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEILA 596
Cdd:COG4148 161 LAALDLA-RKAeilpYLER-------LRDELDIpilYVSHSLDEVARLaDHVVLLEQGRVVASGPLAEVLS 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
396-594 |
1.44e-14 |
|
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: 74.53 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILG--------------EMEKLKGIVQRK--GSVAYVSQQawiQNC 459
Cdd:cd03256 13 GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGlveptsgsvlidgtDINKLKGKALRQlrRQIGMIFQQ---FNL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 460 ILQ----ENILFGSVMQKQLY---------ERVLEACALLpdleqlpngDQTEIGEKGV----NISGGQKHRVCLARAVY 522
Cdd:cd03256 90 IERlsvlENVLSGRLGRRSTWrslfglfpkEEKQRALAAL---------ERVGLLDKAYqradQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387192242 523 SGADIYLLDDPLSAVDVHVAKQLFEkVIGSSGMLRNKTRILVTHNLTL-LPQMDLIVVMESGRVAQMGTYQEI 594
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMD-LLKRINREEGITVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
387-589 |
2.13e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 76.22 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 387 NASFSWDKTGIPvlKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIV----QR-------KGSVAYVSQQ-A 454
Cdd:PRK11000 8 NVTKAYGDVVIS--KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLfigeKRmndvppaERGVGMVFQSyA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 455 WIQNCILQENILFG----SVMQKQLYERVLEACALLpDLEQLpngdqteIGEKGVNISGGQKHRVCLARAVYSGADIYLL 530
Cdd:PRK11000 86 LYPHLSVAENMSFGlklaGAKKEEINQRVNQVAEVL-QLAHL-------LDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387192242 531 DDPLSAVDVHVAKQL------FEKVIGSsgmlrnkTRILVTHN----LTLlpqMDLIVVMESGRVAQMG 589
Cdd:PRK11000 158 DEPLSNLDAALRVQMrieisrLHKRLGR-------TMIYVTHDqveaMTL---ADKIVVLDAGRVAQVG 216
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
349-596 |
2.93e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 78.15 E-value: 2.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 349 PFLTRISLVHLED-----FLNTEELlphsieanyigDHAIGFINASFSW-DKTGIPVLKDLNIKIPEGALVAVVGQVGSG 422
Cdd:PTZ00265 1138 PLIIRKSNIDVRDnggirIKNKNDI-----------KGKIEIMDVNFRYiSRPNVPIYKDLTFSCDSKKTTAIVGETGSG 1206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 423 KSSVLSAIL------------------GEMEKLK------------------------------GIVQRKGSV------- 447
Cdd:PTZ00265 1207 KSTVMSLLMrfydlkndhhivfknehtNDMTNEQdyqgdeeqnvgmknvnefsltkeggsgedsTVFKNSGKIlldgvdi 1286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 448 ------------AYVSQQAWIQNCILQENILFGSvmQKQLYERVLEAC---ALLPDLEQLPNGDQTEIGEKGVNISGGQK 512
Cdd:PTZ00265 1287 cdynlkdlrnlfSIVSQEPMLFNMSIYENIKFGK--EDATREDVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQK 1364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 513 HRVCLARAVYSGADIYLLDDPLSAVDVHvAKQLFEKVIGSSGMLRNKTRILVTHNLTLLPQMDLIVVM----ESGRVAQM 588
Cdd:PTZ00265 1365 QRIAIARALLREPKILLLDEATSSLDSN-SEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQA 1443
|
....*....
gi 1387192242 589 -GTYQEILA 596
Cdd:PTZ00265 1444 hGTHEELLS 1452
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1014-1206 |
3.40e-14 |
|
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: 72.95 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLfriversggkiiidgidistIGLHDL-RGKLNI--------------I 1078
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAI--------------------LGLLKPtSGSIRVfgkplekerkrigyV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1079 PQD-------PVLFSGTLQMNLDP---LDKYPDHELW----EVLELCHLKEFVQslpkkllHEISEggenLSVGQRQLVC 1144
Cdd:cd03235 74 PQRrsidrdfPISVRDVVLMGLYGhkgLFRRLSKADKakvdEALERVGLSELAD-------RQIGE----LSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387192242 1145 LARALLRKTKILILDEATASIDFETDNLVQTTVRK-EFSDCTILTIAHRLHSIIDS-DRVLVLD 1206
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYfDRVLLLN 206
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
398-579 |
4.36e-14 |
|
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: 72.51 E-value: 4.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 398 PVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKG------------SVAYVSQQ-AWIQNCILQEN 464
Cdd:COG4133 16 LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLAYLGHAdGLKPELTVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 465 ILFGSVMQKQLY--ERVLEACAL--LPDLEQLPNGdqteigekgvNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVH 540
Cdd:COG4133 96 LRFWAALYGLRAdrEAIDEALEAvgLAGLADLPVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1387192242 541 vAKQLFEKVI----GSSGMLrnktrILVTHNLTLLPQMDLIVV 579
Cdd:COG4133 166 -GVALLAELIaahlARGGAV-----LLTTHQPLELAAARVLDL 202
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
383-585 |
7.07e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 72.39 E-value: 7.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 383 IGFINASFSWDKtGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEmEKL-KGIVQ---------RKGSVAYVSQ 452
Cdd:COG2884 2 IRFENVSKRYPG-GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGE-ERPtSGQVLvngqdlsrlKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 453 QawI----QNCIL------QENILFgsVMQ------KQLYERVLEACAL--LPDLE-QLPNgdqteigekgvNISGGQKH 513
Cdd:COG2884 80 R--IgvvfQDFRLlpdrtvYENVAL--PLRvtgksrKEIRRRVREVLDLvgLSDKAkALPH-----------ELSGGEQQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387192242 514 RVCLARAVYSGADIYLLDDPLSAVDVHVAK---QLFEKvIGSSGmlrnKTRILVTHNLTLLPQMDL-IVVMESGRV 585
Cdd:COG2884 145 RVAIARALVNRPELLLADEPTGNLDPETSWeimELLEE-INRRG----TTVLIATHDLELVDRMPKrVLELEDGRL 215
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1014-1210 |
7.51e-14 |
|
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: 72.14 E-value: 7.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSN---CLFRIVERSGGKIIIDGIDISTIGLHDLRGK-LNIIPQD-------- 1081
Cdd:cd03255 19 ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNilgGLDRPTSGEVRVDGTDISKLSEKELAAFRRRhIGFVFQSfnllpdlt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1082 -------PVLFSGTlqmnldpldKYPDHELW--EVLELCHLKEfvqslpkKLLHEISEggenLSVGQRQLVCLARALLRK 1152
Cdd:cd03255 99 alenvelPLLLAGV---------PKKERRERaeELLERVGLGD-------RLNHYPSE----LSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387192242 1153 TKILILDEATASIDFETDNLVQTTVRK--EFSDCTILTIAH--RLHSIidSDRVLVLDSGRI 1210
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHdpELAEY--ADRIIELRDGKI 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1015-1221 |
7.84e-14 |
|
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: 72.53 E-value: 7.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSG---GKIIIDGIDISTIGLHDLRGKLNIIPQDPVLFSG-TLQ 1090
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSgevLIDGEDISGLSEAELYRLRRRMGMLFQSGALFDSlTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1091 MNLD-PL---DKYPDHELWEV----LELCHLKEFVQSLPkkllheiSEggenLSVGQRQLVCLARALLRKTKILILDEAT 1162
Cdd:cd03261 96 ENVAfPLrehTRLSEEEIREIvlekLEAVGLRGAEDLYP-------AE----LSGGMKKRVALARALALDPELLLYDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387192242 1163 ASID----FETDNLVQtTVRKEFsDCTILTIAHRLHSIID-SDRVLVLDSGRITEFETPQNLIH 1221
Cdd:cd03261 165 AGLDpiasGVIDDLIR-SLKKEL-GLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
400-604 |
9.14e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 73.52 E-value: 9.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 400 LKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQ------------------RKgSVAYVSQQAWIQ--NC 459
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTigervitagkknkklkplRK-KVGIVFQFPEHQlfEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 460 ILQENILFG----SVMQKQLYERVLEACAL--LPD--LEQLPngdqteigekgVNISGGQKHRVCLARAVYSGADIYLLD 531
Cdd:PRK13634 102 TVEKDICFGpmnfGVSEEDAKQKAREMIELvgLPEelLARSP-----------FELSGGQMRRVAIAGVLAMEPEVLVLD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387192242 532 DPLSAVDVHVAK---QLFEKVIGSSGMlrnkTRILVTHNLTLLPQ-MDLIVVMESGRVAQMGTYQEILAKTKNLTNL 604
Cdd:PRK13634 171 EPTAGLDPKGRKemmEMFYKLHKEKGL----TTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFADPDELEAI 243
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
398-594 |
1.29e-13 |
|
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: 71.38 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 398 PVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKG-SVayVSQQAWIQNCI---LQENILFG--SVM 471
Cdd:cd03263 16 PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGySI--RTDRKAARQSLgycPQFDALFDelTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 472 QkqlyerVLEACALLPDLEQLPNGDQTEIGEKGVNI-----------SGGQKHRVCLARAVYSGADIYLLDDPLSAVDVH 540
Cdd:cd03263 94 E------HLRFYARLKGLPKSEIKEEVELLLRVLGLtdkankrartlSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387192242 541 VAKQLFEKVigsSGMLRNKTRILVTHNltllpqMDL-------IVVMESGRVAQMGTYQEI 594
Cdd:cd03263 168 SRRAIWDLI---LEVRKGRSIILTTHS------MDEaealcdrIAIMSDGKLRCIGSPQEL 219
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
387-571 |
1.33e-13 |
|
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: 69.40 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 387 NASFSWDKTgiPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQR--KGSVAYVSQQawiqncilqen 464
Cdd:cd03221 5 NLSKTYGGK--LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWgsTVKIGYFEQL----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 465 ilfgsvmqkqlyervleacallpdleqlpngdqteigekgvniSGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHvAKQ 544
Cdd:cd03221 72 -------------------------------------------SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE-SIE 107
|
170 180
....*....|....*....|....*....
gi 1387192242 545 LFEkvigssGMLRN--KTRILVTHNLTLL 571
Cdd:cd03221 108 ALE------EALKEypGTVILVSHDRYFL 130
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
387-635 |
1.37e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 72.74 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 387 NASFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEME------KLKGIVQRKGSVAYVSQQAWI--QN 458
Cdd:PRK13635 10 HISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLpeagtiTVGGMVLSEETVWDVRRQVGMvfQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 459 -------CILQENILFG----SVMQKQLYERVLEAcallpdLEQLpnGDQTEIGEKGVNISGGQKHRVCLARAVYSGADI 527
Cdd:PRK13635 90 pdnqfvgATVQDDVAFGleniGVPREEMVERVDQA------LRQV--GMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 528 YLLDDPLSAVDvhvaKQLFEKVIGSSGMLRNKTRILV---THNLTLLPQMDLIVVMESGRVAQMGTYQEILAKTKNLTN- 603
Cdd:PRK13635 162 IILDEATSMLD----PRGRREVLETVRQLKEQKGITVlsiTHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHMLQEi 237
|
250 260 270
....*....|....*....|....*....|...
gi 1387192242 604 -LLQAFSEQETAhALKQVSVINSRTVLKDQILV 635
Cdd:PRK13635 238 gLDVPFSVKLKE-LLKRNGILLPNTYLTMESLV 269
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
382-595 |
1.45e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 72.38 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 382 AIGFINASFSWDKTGIpvLKDLNIKIPEGALVAVVGQVGSGKSSVLSAiLGEMEKLKGIVQRKGSVAYVSQQAW-----I 456
Cdd:PRK14258 7 AIKVNNLSFYYDTQKI--LEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQNIYerrvnL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 457 QNCILQENILFG--SVMQKQLYERVLEACALL---PDLE------------QLPNGDQTEIGEKGVNISGGQKHRVCLAR 519
Cdd:PRK14258 84 NRLRRQVSMVHPkpNLFPMSVYDNVAYGVKIVgwrPKLEiddivesalkdaDLWDEIKHKIHKSALDLSGGQQQRLCIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 520 AVYSGADIYLLDDPLSAVDvHVAKQLFEKVIGSSGMLRNKTRILVTHNLTLLPQM-DLIVVMES--GRVAQM---GTYQE 593
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLD-PIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLsDFTAFFKGneNRIGQLvefGLTKK 242
|
..
gi 1387192242 594 IL 595
Cdd:PRK14258 243 IF 244
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
863-1243 |
1.78e-13 |
|
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: 75.75 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 863 ETLLGVSTIRAFGHEQRFIQQNKEVVNENL-----VCFYNNVISNRWLSVrlEFLGNLMVFFTAVlTVLAGNSIDS--AI 935
Cdd:TIGR00957 501 EILNGIKVLKLYAWELAFLDKVEGIRQEELkvlkkSAYLHAVGTFTWVCT--PFLVALITFAVYV-TVDENNILDAekAF 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 936 VGLSIsyaLNITQ-TLNFWVRKACEIEANAVSIERVCEYETMDKEAPWITSKRPPSQWPSKGIVeFVDYRARYRDDLGLA 1014
Cdd:TIGR00957 578 VSLAL---FNILRfPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEGNSIT-VHNATFTWARDLPPT 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGgkiiidgidistiGLHDLRGKLNIIPQDPVLFSGTLQMNLD 1094
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVE-------------GHVHMKGSVAYVPQQAWIQNDSLRENIL 720
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1095 PLDKYPDHELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQ 1174
Cdd:TIGR00957 721 FGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIF 800
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387192242 1175 TTV---RKEFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETPQNLIHKRGLFFDML-TEAGITQDLGAKN 1243
Cdd:TIGR00957 801 EHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLrTYAPDEQQGHLED 873
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
397-597 |
2.08e-13 |
|
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: 71.07 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 397 IPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILG--------------EMEKLKGIVQRKGS--VAYVSQQ-AWIQNC 459
Cdd:cd03258 18 VTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGlerptsgsvlvdgtDLTLLSGKELRKARrrIGMIFQHfNLLSSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 460 ILQENILF----GSVMQKQLYERVLEACALLpDLEQL----PNgdqteigekgvNISGGQKHRVCLARAVYSGADIYLLD 531
Cdd:cd03258 98 TVFENVALpleiAGVPKAEIEERVLELLELV-GLEDKadayPA-----------QLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387192242 532 DPLSAVDVHVAKQLFEkvigssgMLR--NK----TRILVTHnltllpQMDLI-------VVMESGRVAQMGTYQEILAK 597
Cdd:cd03258 166 EATSALDPETTQSILA-------LLRdiNRelglTIVLITH------EMEVVkricdrvAVMEKGEVVEEGTVEEVFAN 231
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1014-1210 |
2.28e-13 |
|
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: 71.06 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRG----------KLNIIPQDPV 1083
Cdd:cd03256 16 ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrqigmifqQFNLIERLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1084 L---FSGTL-QMNLDP--LDKYPDHELWEVLELchLKEFvqslpkKLLHEISEGGENLSVGQRQLVCLARALLRKTKILI 1157
Cdd:cd03256 96 LenvLSGRLgRRSTWRslFGLFPKEEKQRALAA--LERV------GLLDKAYQRADQLSGGQQQRVAIARALMQQPKLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1387192242 1158 LDEATASIDFETDNLVQTTVR---KEFSDCTILTIaHRLHSIID-SDRVLVLDSGRI 1210
Cdd:cd03256 168 ADEPVASLDPASSRQVMDLLKrinREEGITVIVSL-HQVDLAREyADRIVGLKDGRI 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1010-1211 |
2.68e-13 |
|
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: 69.98 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1010 DLGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSggkiiidgidISTIGLH-------DLRGKLNIIPQDP 1082
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKES----------SGSILLNgkpikakERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1083 --VLFSGT----LQMNLDPLDKYPDhELWEVLELCHLKEFvqslpkKLLHEISeggenLSVGQRQLVCLARALLRKTKIL 1156
Cdd:cd03226 81 dyQLFTDSvreeLLLGLKELDAGNE-QAETVLKDLDLYAL------KERHPLS-----LSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1387192242 1157 ILDEATASIDFETDNLVQTTVRKEFS-DCTILTIAHRLHSIID-SDRVLVLDSGRIT 1211
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
387-601 |
3.34e-13 |
|
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: 71.09 E-value: 3.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 387 NASFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKG-IVQRKGSVAYVSQQAWIQ--NCILQE 463
Cdd:cd03288 24 DLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGkIVIDGIDISKLPLHTLRSrlSIILQD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 464 NILF-GSV----------MQKQLYErVLEACALLPDLEQLPNGDQTEIGEKGVNISGGQKHRVCLARAVYSGADIYLLDD 532
Cdd:cd03288 104 PILFsGSIrfnldpeckcTDDRLWE-ALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387192242 533 PLSAVDVhVAKQLFEKVIGSSgmLRNKTRILVTHNLTLLPQMDLIVVMESGRVAQMGTYQEILAKTKNL 601
Cdd:cd03288 183 ATASIDM-ATENILQKVVMTA--FADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGV 248
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1013-1211 |
5.34e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 73.14 E-value: 5.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1013 LALQDITFQTH-GEekI-GIVGRTGAGKSTLSNCLFriversggkiiidgidistiGLHD-------LRGK--------- 1074
Cdd:COG3845 19 VANDDVSLTVRpGE--IhALLGENGAGKSTLMKILY--------------------GLYQpdsgeilIDGKpvrirsprd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1075 ---LNI--IPQDPVLFsgtlqmnldpldkyPDHELWE--VLELCHLKEFVQSLPK--KLLHEISEG-G---------ENL 1135
Cdd:COG3845 77 aiaLGIgmVHQHFMLV--------------PNLTVAEniVLGLEPTKGGRLDRKAarARIRELSERyGldvdpdakvEDL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1136 SVGQRQLVCLARALLRKTKILILDEATASI-DFETDNLVQT--TVRKEfsDCTILTIAHRLHSIID-SDRVLVLDSGRIT 1211
Cdd:COG3845 143 SVGEQQRVEILKALYRGARILILDEPTAVLtPQEADELFEIlrRLAAE--GKSIIFITHKLREVMAiADRVTVLRRGKVV 220
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
383-606 |
5.72e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 70.12 E-value: 5.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 383 IGFINASFSWDKTgiPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAI------------------LGEMEKLKGIVQRK 444
Cdd:PRK09493 2 IEFKNVSKHFGPT--QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitsgdlivdglkvNDPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 445 GsvaYVSQQAWI--QNCILqENILFGSV----MQKQLYERVleACALLPD--LEQLPNGDQTEIgekgvniSGGQKHRVC 516
Cdd:PRK09493 80 G---MVFQQFYLfpHLTAL-ENVMFGPLrvrgASKEEAEKQ--ARELLAKvgLAERAHHYPSEL-------SGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 517 LARAVYSGADIYLLDDPLSAVD-------VHVAKQLFEKvigssGMlrnkTRILVTHNLTLLPQM-DLIVVMESGRVAQM 588
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDpelrhevLKVMQDLAEE-----GM----TMVIVTHEIGFAEKVaSRLIFIDKGRIAED 217
|
250 260
....*....|....*....|
gi 1387192242 589 GTYQEILAKTKN--LTNLLQ 606
Cdd:PRK09493 218 GDPQVLIKNPPSqrLQEFLQ 237
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1014-1210 |
6.14e-13 |
|
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: 69.77 E-value: 6.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSggkiiidgidISTIGLH---------DLRGKLNIIP--QDP 1082
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPT----------SGSVLFDgeditglppHEIARLGIGRtfQIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1083 VLFSG-TLQMNL-------------DPLDKYPDHELWE----VLELCHLKEfvqslpkkLLHEISeggENLSVGQRQLVC 1144
Cdd:cd03219 85 RLFPElTVLENVmvaaqartgsgllLARARREEREAREraeeLLERVGLAD--------LADRPA---GELSYGQQRRLE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 1145 LARALLRKTKILILDEATASIDF-ETDNLVQTTVRKEFSDCTILTIAHRLHSIID-SDRVLVLDSGRI 1210
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPeETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRV 221
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1030-1206 |
6.69e-13 |
|
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: 67.95 E-value: 6.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1030 IVGRTGAGKSTLsnclFRIVE-----RSggkiiidgidiSTIGLHDLRGKLnIIPQDPVLFSGTL--QMNldpldkYPdh 1102
Cdd:cd03223 32 ITGPSGTGKSSL----FRALAglwpwGS-----------GRIGMPEGEDLL-FLPQRPYLPLGTLreQLI------YP-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1103 elWevlelchlkefvqslpkkllheisegGENLSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVRKEFs 1182
Cdd:cd03223 88 --W--------------------------DDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG- 138
|
170 180
....*....|....*....|....*....
gi 1387192242 1183 dCTILTIAHR-----LHsiidsDRVLVLD 1206
Cdd:cd03223 139 -ITVISVGHRpslwkFH-----DRVLDLD 161
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1014-1219 |
7.42e-13 |
|
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: 69.39 E-value: 7.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSggkiiidgidISTIGL--HDLRGK---------LNIIPQDP 1082
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPR----------SGSIRFdgRDITGLppheraragIGYVPEGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1083 VLFSG-----TLQMNLDPLDKYPDHELWE-VLELC-HLKEFVQSLpkkllheisegGENLSVGQRQLVCLARALLRKTKI 1155
Cdd:cd03224 85 RIFPEltveeNLLLGAYARRRAKRKARLErVYELFpRLKERRKQL-----------AGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387192242 1156 LILDEATASIdfetdnlvQTTVRKEFSDC---------TILTIAHRLHSIID-SDRVLVLDSGRITEFETPQNL 1219
Cdd:cd03224 154 LLLDEPSEGL--------APKIVEEIFEAirelrdegvTILLVEQNARFALEiADRAYVLERGRVVLEGTAAEL 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1014-1217 |
7.56e-13 |
|
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: 70.85 E-value: 7.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGkiiidgidisTIG----------------LHDLRGK-LN 1076
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGI----------TSGeilfdgedllklsekeLRKIRGReIQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1077 IIPQDPvlfsgtlqMN-LDPL--------------DKYPDHELW----EVLELCHL---KEFVQSLPkkllHEiseggen 1134
Cdd:COG0444 90 MIFQDP--------MTsLNPVmtvgdqiaeplrihGGLSKAEAReraiELLERVGLpdpERRLDRYP----HE------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1135 LSVGQRQLVCLARALLRKTKILILDEATASIDFetdnLVQTTV-------RKEFsDCTILTIAHRLhSIID--SDRVLVL 1205
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQAQIlnllkdlQREL-GLAILFITHDL-GVVAeiADRVAVM 224
|
250
....*....|....*....
gi 1387192242 1206 DSGRITE-------FETPQ 1217
Cdd:COG0444 225 YAGRIVEegpveelFENPR 243
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
380-604 |
7.89e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 70.60 E-value: 7.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 380 DHAIGFINASFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILG-----EMEKLK----GIVQRKGSVAYV 450
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpdDNPNSKitvdGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 451 SQQAWI--QN-------CILQENILFG--------SVMQKqLYERVLEACALLPDLEQLPNgdqteigekgvNISGGQKH 513
Cdd:PRK13640 83 REKVGIvfQNpdnqfvgATVGDDVAFGlenravprPEMIK-IVRDVLADVGMLDYIDSEPA-----------NLSGGQKQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 514 RVCLARAVYSGADIYLLDDPLSAVDVHVAKQLFeKVIGSSGMLRNKTRILVTHNLTLLPQMDLIVVMESGRVAQMGTYQE 593
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGKEQIL-KLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVE 229
|
250
....*....|.
gi 1387192242 594 ILAKTKNLTNL 604
Cdd:PRK13640 230 IFSKVEMLKEI 240
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
995-1219 |
8.03e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 70.15 E-value: 8.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 995 KGIVEFVDYRARYRDDL-GLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRG 1073
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1074 KLNIIPQDP-VLFSGT-----LQMNLDplDKYPDHELW-----EVLELCHLKEFVQSLPKKLlheiseggenlSVGQRQL 1142
Cdd:PRK13650 82 KIGMVFQNPdNQFVGAtveddVAFGLE--NKGIPHEEMkervnEALELVGMQDFKEREPARL-----------SGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1143 VCLARALLRKTKILILDEATASIDFETD-NLVQT--TVRKEFsDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETPQNL 1219
Cdd:PRK13650 149 VAIAGAVAMRPKIIILDEATSMLDPEGRlELIKTikGIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1006-1212 |
9.97e-13 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 68.93 E-value: 9.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1006 RYRDDlGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTI---GLHDLRGKLNIIPQD- 1081
Cdd:COG2884 10 RYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRRIGVVFQDf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1082 PVLFSGTLQMNLD-PLD--KYPDHELW----EVLELCHLKEFVQSLPkkllHEiseggenLSVGQRQLVCLARALLRKTK 1154
Cdd:COG2884 89 RLLPDRTVYENVAlPLRvtGKSRKEIRrrvrEVLDLVGLSDKAKALP----HE-------LSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387192242 1155 ILILDEATASIDFET-DNLVQttVRKEFSD--CTILtIA-HRLHsIIDS--DRVLVLDSGRITE 1212
Cdd:COG2884 158 LLLADEPTGNLDPETsWEIME--LLEEINRrgTTVL-IAtHDLE-LVDRmpKRVLELEDGRLVR 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1014-1210 |
1.02e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.97 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFriversggkiiidgidistiGLHD-------LRGK------------ 1074
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILS--------------------GVYQpdsgeilLDGEpvrfrsprdaqa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1075 --LNIIPQDPVL----------FSGTLQMNLDPLDkypdhelW-----EVLELchLKEFVQSL-PKKLLheiseggENLS 1136
Cdd:COG1129 79 agIAIIHQELNLvpnlsvaeniFLGREPRRGGLID-------WramrrRAREL--LARLGLDIdPDTPV-------GDLS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 1137 VGQRQLVCLARALLRKTKILILDEATASIDF-ETDNLVQtTVR--KEfSDCTILTIAHRLHSIID-SDRVLVLDSGRI 1210
Cdd:COG1129 143 VAQQQLVEIARALSRDARVLILDEPTASLTErEVERLFR-IIRrlKA-QGVAIIYISHRLDEVFEiADRVTVLRDGRL 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
994-1210 |
1.28e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 69.63 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 994 SKGIVEFVDYRARYRDDLGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRG 1073
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1074 KLNIIPQDP------------VLFSgtLQMNldpldKYPDHELWEVLElcHLKEFVQsLPKKLLHEisegGENLSVGQRQ 1141
Cdd:PRK13632 84 KIGIIFQNPdnqfigatveddIAFG--LENK-----KVPPKKMKDIID--DLAKKVG-MEDYLDKE----PQNLSGGQKQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387192242 1142 LVCLARALLRKTKILILDEATASIDFETDNLVQTTVR--KEFSDCTILTIAHRLHSIIDSDRVLVLDSGRI 1210
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKL 220
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
998-1210 |
1.44e-12 |
|
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: 68.20 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 998 VEFVDYRARYRDDLgLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDIStiGLHD-----LR 1072
Cdd:cd03292 1 IEFINVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS--DLRGraipyLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1073 GKLNIIPQDPVLFSgtlqmNLDPLDK--------YPDHELW-----EVLELCHLKEFVQSLPkkllheiseggENLSVGQ 1139
Cdd:cd03292 78 RKIGVVFQDFRLLP-----DRNVYENvafalevtGVPPREIrkrvpAALELVGLSHKHRALP-----------AELSGGE 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387192242 1140 RQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVRKEFSDCTILTIAHRLHSIID--SDRVLVLDSGRI 1210
Cdd:cd03292 142 QQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDttRHRVIALERGKL 214
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
393-600 |
1.76e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 70.83 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 393 DKTGIPV-LKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQ-----------------RKGSVAYVSQQ- 453
Cdd:PRK10070 36 EKTGLSLgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLidgvdiakisdaelrevRRKKIAMVFQSf 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 454 AWIQNCILQENILFG----SVMQKQLYERVLEACALLpDLEQLPNGDQTEIgekgvniSGGQKHRVCLARAVYSGADIYL 529
Cdd:PRK10070 116 ALMPHMTVLDNTAFGmelaGINAEERREKALDALRQV-GLENYAHSYPDEL-------SGGMRQRVGLARALAINPDILL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387192242 530 LDDPLSAVDVHVAKQLFEKVIGSSGMlRNKTRILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEILAKTKN 600
Cdd:PRK10070 188 MDEAFSALDPLIRTEMQDELVKLQAK-HQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNNPAN 258
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
998-1210 |
2.03e-12 |
|
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: 67.88 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 998 VEFVDYRARYRDDLG--LALQDITFQTHGEEKIGIVGRTGAGKSTLsnclFRIVErsggkiiidgidistiGLHD----- 1070
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTL----LRIIA----------------GLERptsge 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1071 --LRGK--------LNIIPQDPVLFS----------GtLQMNLDPlDKYPDHELWEVLELCHLKEFVQSLPkkllHEise 1130
Cdd:cd03293 61 vlVDGEpvtgpgpdRGYVFQQDALLPwltvldnvalG-LELQGVP-KAEARERAEELLELVGLSGFENAYP----HQ--- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1131 ggenLSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVRK--EFSDCTILTIAHRLH-SIIDSDRVLVLDS 1207
Cdd:cd03293 132 ----LSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSA 207
|
....*
gi 1387192242 1208 --GRI 1210
Cdd:cd03293 208 rpGRI 212
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
993-1235 |
2.58e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 69.06 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 993 PSKGIVEFVDYRARYRDDLGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIV-----ERSGGKIIIDGIDISTIg 1067
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpddnPNSKITVDGITLTAKTV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1068 lHDLRGKLNIIPQDP------VLFSGTLQMNLDPlDKYPDHELW----EVLELCHLKEFVQSLPkkllheiseggENLSV 1137
Cdd:PRK13640 80 -WDIREKVGIVFQNPdnqfvgATVGDDVAFGLEN-RAVPRPEMIkivrDVLADVGMLDYIDSEP-----------ANLSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1138 GQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVRK--EFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEFET 1215
Cdd:PRK13640 147 GQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKlkKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
250 260
....*....|....*....|
gi 1387192242 1216 PQNLIHKRglffDMLTEAGI 1235
Cdd:PRK13640 227 PVEIFSKV----EMLKEIGL 242
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
398-596 |
3.45e-12 |
|
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: 67.70 E-value: 3.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 398 PVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKG-SVAYVSQQAWIQnciLQENI--------LFG 468
Cdd:COG1127 19 VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqDITGLSEKELYE---LRRRIgmlfqggaLFD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 469 S------VM----------QKQLYERVLEACAL--LPDLEQL-PngdqteiGEkgvnISGGQKHRVCLARAVYSGADIYL 529
Cdd:COG1127 96 SltvfenVAfplrehtdlsEAEIRELVLEKLELvgLPGAADKmP-------SE----LSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387192242 530 LD------DPLSAVDVHvakQLFEKVIGSSGMlrnkTRILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEILA 596
Cdd:COG1127 165 YDeptaglDPITSAVID---ELIRELRDELGL----TSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTPEELLA 231
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1014-1220 |
4.15e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 68.09 E-value: 4.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLS---NCLFRIVERSGGKIIIDGIDISTigLHDLRGKLNIIPQDPV------- 1083
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLAlhlNGLLRPQKGKVLVSGIDTGDFSK--LQGIRKLVGIVFQNPEtqfvgrt 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1084 ----LFSGTLQMNLDPLD--KYPDHELWEVlelcHLKEFVQSLPKkllheiseggeNLSVGQRQLVCLARALLRKTKILI 1157
Cdd:PRK13644 95 veedLAFGPENLCLPPIEirKRVDRALAEI----GLEKYRHRSPK-----------TLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387192242 1158 LDEATASIDFETDNLVQTTVRKEFSDC-TILTIAHRLHSIIDSDRVLVLDSGRITEFETPQNLI 1220
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
402-589 |
4.19e-12 |
|
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: 66.75 E-value: 4.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 402 DLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKG-SVAYVSQQAWIQNCILQENILFG--SVMQKQlyer 478
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvDVTAAPPADRPVSMLFQENNLFAhlTVEQNV---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 479 vleACALLPDLeQLPNGDQTEI----GEKGVN---------ISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQL 545
Cdd:cd03298 92 ---GLGLSPGL-KLTAEDRQAIevalARVGLAglekrlpgeLSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1387192242 546 FEKVIGSSGMlRNKTRILVTHNLTLLPQM-DLIVVMESGRVAQMG 589
Cdd:cd03298 168 LDLVLDLHAE-TKMTVLMVTHQPEDAKRLaQRVVFLDNGRIAAQG 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1014-1210 |
5.02e-12 |
|
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: 66.77 E-value: 5.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHdlRGKLNIIPQDPVLF-------- 1085
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFphltvaen 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1086 --SGtLQMNLDPLDKYPDHELwEVLELCHLKEFVQSLPkkllHEiseggenLSVGQRQLVCLARALLRKTKILILDEATA 1163
Cdd:cd03259 93 iaFG-LKLRGVPKAEIRARVR-ELLELVGLEGLLNRYP----HE-------LSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1387192242 1164 SIDFETDNLVQTTVRKEFSDCTILTIAHRlHSIID----SDRVLVLDSGRI 1210
Cdd:cd03259 160 ALDAKLREELREELKELQRELGITTIYVT-HDQEEalalADRIAVMNEGRI 209
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
387-604 |
5.62e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 68.11 E-value: 5.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 387 NASFSWDKTG---IPVLKDLNIKIPEGALVAVVGQVGSGKSSVLS------------------AILGEMEKLKGIVQRKG 445
Cdd:PRK13645 11 NVSYTYAKKTpfeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQltngliisetgqtivgdyAIPANLKKIKEVKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 446 SVAYVSQQAWIQ--NCILQENILFGSVM----QKQLYERVLEacalLPDLEQLPngdQTEIGEKGVNISGGQKHRVCLAR 519
Cdd:PRK13645 91 EIGLVFQFPEYQlfQETIEKDIAFGPVNlgenKQEAYKKVPE----LLKLVQLP---EDYVKRSPFELSGGQKRRVALAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 520 AVYSGADIYLLDDPLSAVDVHVAK---QLFEKVIGSSGmlrnKTRILVTHNL-TLLPQMDLIVVMESGRVAQMGTYQEIL 595
Cdd:PRK13645 164 IIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNKEYK----KRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
....*....
gi 1387192242 596 AKTKNLTNL 604
Cdd:PRK13645 240 SNQELLTKI 248
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
391-589 |
6.10e-12 |
|
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: 66.04 E-value: 6.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 391 SWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILG--EMEKLKGIV----------QRKGSVAYVsqqawiqn 458
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVlingrpldkrSFRKIIGYV-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 459 ciLQENILFGsvmQKQLYERVLEACALlpdleqlpngdqteigeKGvnISGGQKHRVCLARAVYSGADIYLLDDPLSAVD 538
Cdd:cd03213 88 --PQDDILHP---TLTVRETLMFAAKL-----------------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 539 VHVAKQLFEkvigssgMLR-----NKTRILVTHNLT--LLPQMDLIVVMESGRVAQMG 589
Cdd:cd03213 144 SSSALQVMS-------LLRrladtGRTIICSIHQPSseIFELFDKLLLLSQGRVIYFG 194
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
399-587 |
6.87e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 66.76 E-value: 6.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 399 VLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKG---SVAYVSQQAWIQN----CILQ--------- 462
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmSKLSSAAKAELRNqklgFIYQfhhllpdft 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 463 --ENI----LFGSVMQKQLYERVLEACALLpDLEQLPNGDQTEigekgvnISGGQKHRVCLARAVYSGADIYLLDDPLSA 536
Cdd:PRK11629 104 alENVamplLIGKKKPAEINSRALEMLAAV-GLEHRANHRPSE-------LSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1387192242 537 VDVHVAKQLFEkVIGSSGMLRNKTRILVTHNLTLLPQMDLIVVMESGRVAQ 587
Cdd:PRK11629 176 LDARNADSIFQ-LLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTA 225
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1014-1217 |
7.09e-12 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 68.22 E-value: 7.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRG---KLNIIPQDPvlfsgtlQ 1090
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQMVFQDP-------Y 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1091 MNLDP-----------LDkypDHELW----------EVLELCHLK-EFVQSLPkkllHEiseggenLSVGQRQLVCLARA 1148
Cdd:COG4608 106 ASLNPrmtvgdiiaepLR---IHGLAskaerrervaELLELVGLRpEHADRYP----HE-------FSGGQRQRIGIARA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1149 LLRKTKILILDEATASIDFEtdnlVQTTV-------RKEFsDCTILTIAHRLhSIID--SDRVLVLDSGRITE------- 1212
Cdd:COG4608 172 LALNPKLIVCDEPVSALDVS----IQAQVlnlledlQDEL-GLTYLFISHDL-SVVRhiSDRVAVMYLGKIVEiaprdel 245
|
....*
gi 1387192242 1213 FETPQ 1217
Cdd:COG4608 246 YARPL 250
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
397-589 |
1.06e-11 |
|
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: 66.02 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 397 IPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGSVAYV-SQQAWIQNCIL-QENILF-GSVM-- 471
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLlGLGGGFNPELTgRENIYLnGRLLgl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 472 -QKQLYERVleacallPDLEQLpngdqTEIGEKG----VNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQLF 546
Cdd:cd03220 115 sRKEIDEKI-------DEIIEF-----SELGDFIdlpvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQ 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1387192242 547 EKVigsSGMLRN-KTRILVTHNLTLLPQM-DLIVVMESGRVAQMG 589
Cdd:cd03220 183 RRL---RELLKQgKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1015-1208 |
1.24e-11 |
|
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: 66.80 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGgkiiidgidistiGLHDLRGKLNIIPQDPVLFSGTLQMNLD 1094
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSE-------------GKIKHSGRISFSSQFSWIMPGTIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1095 PLDKYPDHELWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLV- 1173
Cdd:cd03291 120 FGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIf 199
|
170 180 190
....*....|....*....|....*....|....*
gi 1387192242 1174 QTTVRKEFSDCTILTIAHRLHSIIDSDRVLVLDSG 1208
Cdd:cd03291 200 ESCVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1014-1212 |
1.25e-11 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 65.84 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCL----------FRIVERSGGKIiidgidiSTIGLHDLRGKlNI--IPQD 1081
Cdd:COG1136 23 ALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILggldrptsgeVLIDGQDISSL-------SERELARLRRR-HIgfVFQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1082 PVLFSG-------TLQMNLDPLDKYPDHE-LWEVLELCHLKEFVQSLPKKLlheiseggenlSVGQRQLVCLARALLRKT 1153
Cdd:COG1136 95 FNLLPEltalenvALPLLLAGVSRKERRErARELLERVGLGDRLDHRPSQL-----------SGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387192242 1154 KILILDEATASIDFET-DNLVQ--TTVRKEFsDCTILTIAHRLHSIIDSDRVLVLDSGRITE 1212
Cdd:COG1136 164 KLILADEPTGNLDSKTgEEVLEllRELNREL-GTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
396-596 |
1.35e-11 |
|
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: 65.77 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKG----------------IVqRKGsVAYVSQqawIQNC 459
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGsirfdgeditglpphrIA-RLG-IGYVPE---GRRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 460 ILQ----ENILFGSVM------QKQLYERVLEacaLLPDLEQLpngdqteIGEKGVNISGGQKHRVCLARAVYSGADIYL 529
Cdd:COG0410 90 FPSltveENLLLGAYArrdraeVRADLERVYE---LFPRLKER-------RRQRAGTLSGGEQQMLAIGRALMSRPKLLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387192242 530 LDDP---LSAVdvhVAKQLFEKV--IGSSGMlrnkTRILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEILA 596
Cdd:COG0410 160 LDEPslgLAPL---IVEEIFEIIrrLNREGV----TILLVEQNARFALEIaDRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1006-1219 |
1.36e-11 |
|
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: 65.60 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1006 RYRDDLGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTiGLHDLRGKLNIIPQDPVLF 1085
Cdd:cd03263 9 TYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1086 SgtlqmNLDPldkypdhelWEVLELCHLkefVQSLPKKLLHEISEGGE--------------NLSVGQRQLVCLARALLR 1151
Cdd:cd03263 88 D-----ELTV---------REHLRFYAR---LKGLPKSEIKEEVELLLrvlgltdkankrarTLSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387192242 1152 KTKILILDEATASIDFETDNLVQTTVRKEFSDCTILTIAHRLHSI-IDSDRVLVLDSGRITEFETPQNL 1219
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
400-568 |
1.36e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 66.34 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 400 LKDLNIKIPEGALVAVVGQVGSGKSSVLSAIlGEMEKLKGIVQRKGSVAY---------------------VSQQAWIQN 458
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRMNDLNPEVTITGSIVYnghniysprtdtvdlrkeigmVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 459 CILQENILFG----SVMQKQLYERVLEAcallpDLEQLPNGDQTE--IGEKGVNISGGQKHRVCLARAVYSGADIYLLDD 532
Cdd:PRK14239 100 MSIYENVVYGlrlkGIKDKQVLDEAVEK-----SLKGASIWDEVKdrLHDSALGLSGGQQQRVCIARVLATSPKIILLDE 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1387192242 533 PLSAVDVHVAKQLFEKVIGssgmLRNK-TRILVTHNL 568
Cdd:PRK14239 175 PTSALDPISAGKIEETLLG----LKDDyTMLLVTRSM 207
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1006-1212 |
1.54e-11 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 66.27 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1006 RYRDDLG--LALQDITFQTHGEEKIGIVGRTGAGKSTLsnclFRIVersggkiiidgidistIGLHD-------LRGK-- 1074
Cdd:COG1116 16 RFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKSTL----LRLI----------------AGLEKptsgevlVDGKpv 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1075 ------LNIIPQDPVLF----------SGtLQMNLDPLDKYPDHELwEVLELCHLKEFVQSLPkkllHEiseggenLSVG 1138
Cdd:COG1116 76 tgpgpdRGVVFQEPALLpwltvldnvaLG-LELRGVPKAERRERAR-ELLELVGLAGFEDAYP----HQ-------LSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1139 QRQLVCLARALLRKTKILILDEATASIDFET----DNLVQTTVRKEfsDCTILTIAH------RLhsiidSDRVLVLDS- 1207
Cdd:COG1116 143 MRQRVAIARALANDPEVLLMDEPFGALDALTrerlQDELLRLWQET--GKTVLFVTHdvdeavFL-----ADRVVVLSAr 215
|
....*.
gi 1387192242 1208 -GRITE 1212
Cdd:COG1116 216 pGRIVE 221
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
396-595 |
1.76e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 67.56 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKG-------------SVAYVSQQAWIQ-NCIL 461
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVASVPQDTSLSfEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 462 QENILFGSVMQKQLYERVLEACALLPDlEQLPNGDQTEIGEKGV-NISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVH 540
Cdd:PRK09536 95 RQVVEMGRTPHRSRFDTWTETDRAAVE-RAMERTGVAQFADRPVtSLSGGERQRVLLARALAQATPVLLLDEPTASLDIN 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 541 VAKQLFEKV--IGSSGmlrnKTRILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEIL 595
Cdd:PRK09536 174 HQVRTLELVrrLVDDG----KTAVAAIHDLDLAARYcDELVLLADGRVRAAGPPADVL 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1014-1221 |
1.79e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 67.04 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKII---IDGIDISTIGLHDLRGKLNIIPQDPvLFSGTLQ 1090
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwlgKDLLGMKDDEWRAVRSDIQMIFQDP-LASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1091 MNL-----DPLDKY-PDHELWEVlelchlKEFVQSLPKK--LL--------HEISEggenlsvGQRQLVCLARALLRKTK 1154
Cdd:PRK15079 115 MTIgeiiaEPLRTYhPKLSRQEV------KDRVKAMMLKvgLLpnlinrypHEFSG-------GQCQRIGIARALILEPK 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387192242 1155 ILILDEATA----SIDFETDNLVQtTVRKEFsDCTILTIAHRLhSIID--SDRVLVLDSGRITEFETPQNLIH 1221
Cdd:PRK15079 182 LIICDEPVSaldvSIQAQVVNLLQ-QLQREM-GLSLIFIAHDL-AVVKhiSDRVLVMYLGHAVELGTYDEVYH 251
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
392-589 |
1.90e-11 |
|
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: 65.37 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 392 WDKTGIpVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLK---GIV----------QRKGSVAYVSQQ-AWIQ 457
Cdd:cd03234 16 WNKYAR-ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQIlfngqprkpdQFQKCVAYVRQDdILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 458 NCILQENILFGSVM-----QKQLYERVLEACALLPDLeqlpnGDQTEIGEKGVNISGGQKHRVCLARAVYSGADIYLLDD 532
Cdd:cd03234 95 GLTVRETLTYTAILrlprkSSDAIRKKRVEDVLLRDL-----ALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387192242 533 PLSAVDVHVAKQLFEkvigssgML-----RNKTRILVTHNLT--LLPQMDLIVVMESGRVAQMG 589
Cdd:cd03234 170 PTSGLDSFTALNLVS-------TLsqlarRNRIVILTIHQPRsdLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
386-585 |
2.33e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 68.21 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 386 INASFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSaILGEMEK-LKGIVQRKGS-VAYVSQQAWIQncILQE 463
Cdd:PRK10535 10 IRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDKpTSGTYRVAGQdVATLDADALAQ--LRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 464 NilFGSVMQK----------------QLY------ERVLEACALLPDLeqlpnGDQTEIGEKGVNISGGQKHRVCLARAV 521
Cdd:PRK10535 87 H--FGFIFQRyhllshltaaqnvevpAVYaglerkQRLLRAQELLQRL-----GLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387192242 522 YSGADIYLLDDPLSAVDVHVAkqlfEKVIGSSGMLRNK--TRILVTHNLTLLPQMDLIVVMESGRV 585
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSG----EEVMAILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
396-567 |
3.24e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.12 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKG----------SVAYVSQQ-AWIQNCILQEN 464
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddpdvaeACHYLGHRnAMKPALTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 465 ILFGSVMQKQLYERVLEA-CAL-LPDLEQLPNGdqteigekgvNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHvA 542
Cdd:PRK13539 94 LEFWAAFLGGEELDIAAAlEAVgLAPLAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-A 162
|
170 180
....*....|....*....|....*....
gi 1387192242 543 KQLFEKVI----GSSGMLrnktrILVTHN 567
Cdd:PRK13539 163 VALFAELIrahlAQGGIV-----IAATHI 186
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
117-357 |
3.25e-11 |
|
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: 65.65 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 117 LIQVALFKVLADVLSFTSPLIMKQMILFCEQRPDFGWSGYgYALALFVVVFLQTLILQQYQRFKMLTSAKIKTAVIGLIY 196
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLW-IALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 197 KKALLLSNVSRKQFSTGEIINLMATDTQQLMDLMT-NINLLWSAPFQILMAVSLL----WQelgpAVLAGVAVLVFVIPM 271
Cdd:cd07346 80 RHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSsGLLQLLSDVLTLIGALVILfylnWK----LTLVALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 272 NALVANRMKKLKKNQRKNKDKQIKLLNEILHGIKILKLYAWEPSYKKKIIEIREQELEVQKSAGYL-AVFSMLtltcIPF 350
Cdd:cd07346 156 LRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLsALFSPL----IGL 231
|
....*..
gi 1387192242 351 LTRISLV 357
Cdd:cd07346 232 LTALGTA 238
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1015-1222 |
3.36e-11 |
|
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: 64.66 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGgkiiidgidistiGLHDLRGK-----------LNIIPQDPV 1083
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDS-------------GKILLNGKditnlppekrdISYVPQNYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1084 LFsgtlqmnldpldkyPDHELWEVLE--LCHLKEFVQSLPKKLlHEISE----------GGENLSVGQRQLVCLARALLR 1151
Cdd:cd03299 82 LF--------------PHMTVYKNIAygLKKRKVDKKEIERKV-LEIAEmlgidhllnrKPETLSGGEQQRVAIARALVV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 1152 KTKILILDEATASIDFET-DNLVQ--TTVRKEFSdctiLTIAHRLHSIID----SDRVLVLDSGRITEFETPQNLIHK 1222
Cdd:cd03299 147 NPKILLLDEPFSALDVRTkEKLREelKKIRKEFG----VTVLHVTHDFEEawalADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
386-538 |
3.37e-11 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 65.27 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 386 INASFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGSV--------AYVSQQ---- 453
Cdd:COG4525 9 VSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVVFQKdall 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 454 AWiQNCIlqENILFGSVMQK----QLYERVLEACAL--LPDLEQLPngdqteIGEkgvnISGGQKHRVCLARAVYSGADI 527
Cdd:COG4525 89 PW-LNVL--DNVAFGLRLRGvpkaERRARAEELLALvgLADFARRR------IWQ----LSGGMRQRVGIARALAADPRF 155
|
170
....*....|.
gi 1387192242 528 YLLDDPLSAVD 538
Cdd:COG4525 156 LLMDEPFGALD 166
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
399-600 |
3.43e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 65.07 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 399 VLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGSVAYVSQQAWIQNCI------------------ 460
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAIklrkevgmvfqqpnpfph 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 461 --LQENILF----GSVMQKQLYERVLEAC----ALLPDLEQLPNGDQTEIgekgvniSGGQKHRVCLARAVYSGADIYLL 530
Cdd:PRK14246 105 lsIYDNIAYplksHGIKEKREIKKIVEEClrkvGLWKEVYDRLNSPASQL-------SGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387192242 531 DDPLSAVDVhVAKQLFEKVIgsSGMLRNKTRILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEILAKTKN 600
Cdd:PRK14246 178 DEPTSMIDI-VNSQAIEKLI--TELKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGSSNEIFTSPKN 245
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1015-1244 |
3.74e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 67.84 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTL-SNCLFRIVERSGGKIIidgidistiglhdLRGKLNIIPQDPVLFSGTLQMNL 1093
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLiSAMLGELPPRSDASVV-------------IRGTVAYVPQVSWIFNATVRDNI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1094 ------DPlDKYpdhelWEVLELCHLKEFVQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRKTKILILDEATASIDF 1167
Cdd:PLN03130 700 lfgspfDP-ERY-----ERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 1168 ETDNLV-QTTVRKEFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETPQNLIHKRGLFFDMLTEAGITQDLGAKNK 1244
Cdd:PLN03130 774 HVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENAGKMEEYVEENG 851
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
387-596 |
3.85e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 65.39 E-value: 3.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 387 NASFSWdKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSV---LSAIL--------------GEMEKLKGIVQRKGSVAY 449
Cdd:PRK13644 6 NVSYSY-PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLalhLNGLLrpqkgkvlvsgidtGDFSKLQGIRKLVGIVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 450 VSQQAWIQNCIlQENILFGSvmqkqlyervlEACALLP-DLEQLPNGDQTEIG-EK-----GVNISGGQKHRVCLARAVY 522
Cdd:PRK13644 85 NPETQFVGRTV-EEDLAFGP-----------ENLCLPPiEIRKRVDRALAEIGlEKyrhrsPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387192242 523 SGADIYLLDDPLSAVDVHVAKQLFEKVigSSGMLRNKTRILVTHNLTLLPQMDLIVVMESGRVAQMGTYQEILA 596
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERI--KKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
398-566 |
4.16e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.21 E-value: 4.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 398 PVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGivqrKGSVAyVSQQAWIQNCILQENIL-FGSVMQKQly 476
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPV----AGCVD-VPDNQFGREASLIDAIGrKGDFKDAV-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 477 eRVLEACALlpdleqlpnGDQTEIGEKGVNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQLFEKVigsSGML 556
Cdd:COG2401 117 -ELLNAVGL---------SDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNL---QKLA 183
|
170
....*....|..
gi 1387192242 557 R--NKTRILVTH 566
Cdd:COG2401 184 RraGITLVVATH 195
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
380-589 |
4.25e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 65.14 E-value: 4.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 380 DHAIGFINASFSWdKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGSVAYVSQQAWIQNC 459
Cdd:PRK13647 2 DNIIEVEDLHFRY-KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 460 I---------------LQENILFGSV----MQKQLYERVLEACALLpdleqlpngDQTEIGEKG-VNISGGQKHRVCLAR 519
Cdd:PRK13647 81 VglvfqdpddqvfsstVWDDVAFGPVnmglDKDEVERRVEEALKAV---------RMWDFRDKPpYHLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387192242 520 AVYSGADIYLLDDPLSAVDVHVAKQLFEKVIGSSGmlRNKTRILVTHNLTLLPQ-MDLIVVMESGRVAQMG 589
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHN--QGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEG 220
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
379-619 |
4.85e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 65.11 E-value: 4.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 379 GDHAIGFINASFSWDKTG----IPVLKDLNIKIPEGALVAVVGQVGSGKSSV---LSAIL--------------GEMEKL 437
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALLipsegkvyvdgldtSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 438 KGIVQRKGSVaYVSQQAWIQNCILQENILFG----SVMQKQLYERVLEACallpdleqlpngdqteigeKGVN------- 506
Cdd:PRK13633 81 WDIRNKAGMV-FQNPDNQIVATIVEEDVAFGpenlGIPPEEIRERVDESL-------------------KKVGmyeyrrh 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 507 ----ISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQLF---EKVIGSSGMlrnkTRILVTHNLTLLPQMDLIVV 579
Cdd:PRK13633 141 aphlLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVntiKELNKKYGI----TIILITHYMEEAVEADRIIV 216
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1387192242 580 MESGRVAQMGTYQEILAKTKNLTNL-LQAFSEQETAHALKQ 619
Cdd:PRK13633 217 MDSGKVVMEGTPKEIFKEVEMMKKIgLDVPQVTELAYELKK 257
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
399-585 |
6.03e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 64.31 E-value: 6.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 399 VLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGeMEKLKGIVQRKGSVAYVS---------QQA----W---IQNCILQ 462
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG-LETPSAGELLAGTAPLAEaredtrlmfQDArllpWkkvIDNVGLG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 463 eniLFGSVMQKQLyeRVLEACALLPDLEQLPNGdqteigekgvnISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHV- 541
Cdd:PRK11247 106 ---LKGQWRDAAL--QALAAVGLADRANEWPAA-----------LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTr 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1387192242 542 --AKQLFEKVIGSSGMlrnkTRILVTHNLTLLPQM-DLIVVMESGRV 585
Cdd:PRK11247 170 ieMQDLIESLWQQHGF----TVLLVTHDVSEAVAMaDRVLLIEEGKI 212
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
396-586 |
6.34e-11 |
|
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: 62.06 E-value: 6.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGS-VAYVSQQAWIQNCIlqenilfGSVMQkq 474
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKeVSFASPRDARRAGI-------AMVYQ-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 475 lyervleacallpdleqlpngdqteigekgvnISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQLFeKVIgssG 554
Cdd:cd03216 83 --------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLF-KVI---R 126
|
170 180 190
....*....|....*....|....*....|....*
gi 1387192242 555 MLRN--KTRILVTHNLTLLPQM-DLIVVMESGRVA 586
Cdd:cd03216 127 RLRAqgVAVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1013-1220 |
1.05e-10 |
|
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: 63.82 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1013 LALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIG---LHDLRGK--------LNIIPQD 1081
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKkismvfqsFALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1082 PVLFSGTLQMNLDPLDKYPDHEL-WEVLELCHLKEFVQSLPKKllheiseggenLSVGQRQLVCLARALLRKTKILILDE 1160
Cdd:cd03294 118 TVLENVAFGLEVQGVPRAEREERaAEALELVGLEGWEHKYPDE-----------LSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387192242 1161 ATASIDfetdnlvqTTVRKEFSDC----------TILTIAHRLHSIID-SDRVLVLDSGRITEFETPQNLI 1220
Cdd:cd03294 187 AFSALD--------PLIRREMQDEllrlqaelqkTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
724-935 |
1.06e-10 |
|
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: 63.95 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 724 IYGLLGLMQGLFVCSGAYVVTRGSLAASRVLHAQLLDNVLHLPLQFFETNPIGQVINRFTKDM-FIIDMrfhyyirtWVN 802
Cdd:cd18544 46 LYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTeALNEL--------FTS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 803 CTLDVIGTVLVIVGA----------LPLFILGLIPLVFL---YFtiQRYYMASSRQIRRLAGAshspVISHFCETLLGVS 869
Cdd:cd18544 118 GLVTLIGDLLLLIGIliamfllnwrLALISLLVLPLLLLatyLF--RKKSRKAYREVREKLSR----LNAFLQESISGMS 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387192242 870 TIRAFGHEQRFIQQNKEVVNENLVCFYNNVISNRWLSVRLEFLGNLMVffTAVLTVLAGNSIDSAI 935
Cdd:cd18544 192 VIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLAL--ALVLWYGGGQVLSGAV 255
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
400-601 |
1.14e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 63.91 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 400 LKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEME------------------KLKGIVQRKGSV-AYVSQQAWIQNci 460
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKptsgkiiidgvditdkkvKLSDIRKKVGLVfQYPEYQLFEET-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 461 LQENILFG----SVMQKQLYERVLEACALLP-DLEQLPNGDQTEIgekgvniSGGQKHRVCLARAVYSGADIYLLDDPLS 535
Cdd:PRK13637 101 IEKDIAFGpinlGLSEEEIENRVKRAMNIVGlDYEDYKDKSPFEL-------SGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387192242 536 AVDVHVAKQLFEKvIGSSGMLRNKTRILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEILAKTKNL 601
Cdd:PRK13637 174 GLDPKGRDEILNK-IKELHKEYNMTIILVSHSMEDVAKLaDRIIVMNKGKCELQGTPREVFKEVETL 239
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1105-1210 |
1.16e-10 |
|
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: 63.52 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1105 WEVLELCHLKEFVQSLPKkllheiseggeNLSVGQRQLVCLARALLRKTKILILDEATA--SIDfETDNLVQT--TVRKE 1180
Cdd:COG0411 134 EELLERVGLADRADEPAG-----------NLSYGQQRRLEIARALATEPKLLLLDEPAAglNPE-ETEELAELirRLRDE 201
|
90 100 110
....*....|....*....|....*....|.
gi 1387192242 1181 FsDCTILTIAHRLHSIID-SDRVLVLDSGRI 1210
Cdd:COG0411 202 R-GITILLIEHDMDLVMGlADRIVVLDFGRV 231
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
396-621 |
1.19e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 66.34 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIP-VLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGS--VAYVSQQAWIQ-NCILQENILF-GSV 470
Cdd:PTZ00243 1321 GLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGReiGAYGLRELRRQfSMIPQDPVLFdGTV 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 471 MQK--QLYE-------RVLEACALLPDLEQLPNGDQTEIGEKGVNISGGQKHRVCLARAVYS-GADIYLLDDPLSAVDVH 540
Cdd:PTZ00243 1401 RQNvdPFLEassaevwAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEATANIDPA 1480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 541 VAKQLFEKVIGSsgmLRNKTRILVTHNLTLLPQMDLIVVMESGRVAQMGTYQEILAKTKNL-TNLLQAFSEQETAHALKQ 619
Cdd:PTZ00243 1481 LDRQIQATVMSA---FSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIfHSMVEALGRSEAKRFLQL 1557
|
..
gi 1387192242 620 VS 621
Cdd:PTZ00243 1558 VG 1559
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1014-1214 |
1.36e-10 |
|
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: 62.55 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLH-----DLRGKLNIIpqdpvlFSGT 1088
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGggfnpELTGRENIY------LNGR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1089 LqMNLDPldKYPDHELWEVLELCHLKEFVQsLPKKllheiseggeNLSVGQRQLVCLARALLRKTKILILDEATASIDFE 1168
Cdd:cd03220 111 L-LGLSR--KEIDEKIDEIIEFSELGDFID-LPVK----------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1387192242 1169 TDNLVQTTVRKEFSDCTILTIA-HRLHSIID-SDRVLVLDSGRITEFE 1214
Cdd:cd03220 177 FQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
379-533 |
1.44e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.47 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 379 GDHAIGFINASFSWDktGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRkGS---VAYVSQQaw 455
Cdd:COG0488 312 GKKVLELEGLSKSYG--DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GEtvkIGYFDQH-- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 456 iqncilqenilfgsvmQKQLYE--RVLEAcallpdLEQL-PNGDQTEI----------GEK-----GVnISGGQKHRVCL 517
Cdd:COG0488 387 ----------------QEELDPdkTVLDE------LRDGaPGGTEQEVrgylgrflfsGDDafkpvGV-LSGGEKARLAL 443
|
170
....*....|....*.
gi 1387192242 518 ARAVYSGADIYLLDDP 533
Cdd:COG0488 444 AKLLLSPPNVLLLDEP 459
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
399-600 |
1.50e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 63.01 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 399 VLKDLNIKIPEGALVAVVGQVGSGKSSVLSaILGEMEKLKGIVQRKGSVAYVSQQAW--------------------IQN 458
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLR-VFNRLIELYPEARVSGEVYLDGQDIFkmdvielrrrvqmvfqipnpIPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 459 CILQENILFGSVM------QKQLYERVLEAcallpdLE--QLPNGDQTEIGEKGVNISGGQKHRVCLARAVYSGADIYLL 530
Cdd:PRK14247 97 LSIFENVALGLKLnrlvksKKELQERVRWA------LEkaQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 531 DDPLSAVD-VHVAK--QLFEKvigssgMLRNKTRILVTHnltlLPQM-----DLIVVMESGRVAQMGTYQEILAKTKN 600
Cdd:PRK14247 171 DEPTANLDpENTAKieSLFLE------LKKDMTIVLVTH----FPQQaarisDYVAFLYKGQIVEWGPTREVFTNPRH 238
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
396-568 |
1.56e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 63.18 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGSV--------AYVSQQ----AWiQNciLQE 463
Cdd:PRK11248 13 GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPvegpgaerGVVFQNegllPW-RN--VQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 464 NILFG----SVMQKQLYERVLEACALLpDLEqlpngdqtEIGEKGV-NISGGQKHRVCLARAVYSGADIYLLDDPLSAVD 538
Cdd:PRK11248 90 NVAFGlqlaGVEKMQRLEIAHQMLKKV-GLE--------GAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190
....*....|....*....|....*....|...
gi 1387192242 539 VHVAKQLFE---KVIGSSGmlrnKTRILVTHNL 568
Cdd:PRK11248 161 AFTREQMQTlllKLWQETG----KQVLLITHDI 189
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
396-585 |
1.59e-10 |
|
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: 62.43 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQ---------RKGSVAYVSQQAWIqncILQENIL 466
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRvngqdvsdlRGRAIPYLRRKIGV---VFQDFRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 467 ------FGSVM---------QKQLYERVLEACALLpDLE----QLPNGdqteigekgvnISGGQKHRVCLARAVYSGADI 527
Cdd:cd03292 90 lpdrnvYENVAfalevtgvpPREIRKRVPAALELV-GLShkhrALPAE-----------LSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387192242 528 YLLDDPLSAVDVHVAKQ---LFEKVigssgMLRNKTRILVTHNLTLLPQMD-LIVVMESGRV 585
Cdd:cd03292 158 LIADEPTGNLDPDTTWEimnLLKKI-----NKAGTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
398-533 |
2.23e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 64.70 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 398 PVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKG--SVAYVSQQAWI-QNCILQENILFGSVMQKQ 474
Cdd:COG0488 12 PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLdDDLTVLDTVLDGDAELRA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 475 LYERVLEACALLPDLEQLPN--GD-QTEIGEKGV--------------------------NISGGQKHRVCLARAVYSGA 525
Cdd:COG0488 92 LEAELEELEAKLAEPDEDLErlAElQEEFEALGGweaearaeeilsglgfpeedldrpvsELSGGWRRRVALARALLSEP 171
|
....*...
gi 1387192242 526 DIYLLDDP 533
Cdd:COG0488 172 DLLLLDEP 179
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1006-1213 |
2.58e-10 |
|
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: 61.44 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1006 RYRDdlGLALQDITFqTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSggkiiidgidISTIGLHD---------LRGKLN 1076
Cdd:cd03264 9 RYGK--KRALDGVSL-TLGPGMYGLLGPNGAGKTTLMRILATLTPPS----------SGTIRIDGqdvlkqpqkLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1077 IIPQDPVLFSG-TLQMNLDPL-------DKYPDHELWEVLELCHLKEFVQSLPKKllheiseggenLSVGQRQLVCLARA 1148
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYIawlkgipSKEVKARVDEVLELVNLGDRAKKKIGS-----------LSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387192242 1149 LLRKTKILILDEATASIDFETDNLVQTTVRKEFSDCTILTIAHRLHSIIDS-DRVLVLDSGRITEF 1213
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFE 210
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
396-589 |
2.79e-10 |
|
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: 61.00 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEM--EKLKGIVQRKGsvayvsqqawiqncilqENILFGSVmqk 473
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKG-----------------EDITDLPP--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 474 qlYERVLEACALL----PDLEQLPNGDQteIGEKGVNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVhVAKQLFEKV 549
Cdd:cd03217 72 --EERARLGIFLAfqypPEIPGVKNADF--LRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI-DALRLVAEV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1387192242 550 IGSsgmLRNKTR--ILVTHNLTLLPQM--DLIVVMESGRVAQMG 589
Cdd:cd03217 147 INK---LREEGKsvLIITHYQRLLDYIkpDRVHVLYDGRIVKSG 187
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1014-1242 |
2.81e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 63.56 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTH-GEekI-GIVGRTGAGKSTLSNCLFRIvER----SGGKIIIDGIDISTIGLHDLRGKLNIIPQDPVLFSG 1087
Cdd:COG1135 20 ALDDVSLTIEkGE--IfGIIGYSGAGKSTLIRCINLL-ERptsgSVLVDGVDLTALSERELRAARRKIGMIFQHFNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1088 -TLQMNLD-PLdkypdhELW------------EVLELCHLKEFVQSLPKkllheiseggeNLSVGQRQLVCLARALLRKT 1153
Cdd:COG1135 97 rTVAENVAlPL------EIAgvpkaeirkrvaELLELVGLSDKADAYPS-----------QLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1154 KILILDEATASIDFET-----DNLVQttVRKEFsDCTILTIAHRLHSI--IdSDRVLVLDSGRITE-------FETPQNL 1219
Cdd:COG1135 160 KVLLCDEATSALDPETtrsilDLLKD--INREL-GLTIVLITHEMDVVrrI-CDRVAVLENGRIVEqgpvldvFANPQSE 235
|
250 260
....*....|....*....|...
gi 1387192242 1220 IHKRglFFDMLTEAGITQDLGAK 1242
Cdd:COG1135 236 LTRR--FLPTVLNDELPEELLAR 256
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1014-1220 |
2.81e-10 |
|
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: 61.93 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLNIIPQDPVLFSG-TLQMN 1092
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQIGLFPHmTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1093 --LDP-LDKYPDHEL----WEVLELCHL--KEFVQSLPkkllHEiseggenLSVGQRQLVCLARALLRKTKILILDEATA 1163
Cdd:cd03295 96 iaLVPkLLKWPKEKIreraDELLALVGLdpAEFADRYP----HE-------LSGGQQQRVGVARALAADPPLLLMDEPFG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387192242 1164 SIdfetDNLVQTTVRKEFSDC------TILTIAHRL-HSIIDSDRVLVLDSGRITEFETPQNLI 1220
Cdd:cd03295 165 AL----DPITRDQLQEEFKRLqqelgkTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
389-596 |
2.95e-10 |
|
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: 63.15 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 389 SFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGeMEKLKGIVqrKGSVAY-------VSQQAW------ 455
Cdd:COG0444 10 YFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILG-LLPPPGIT--SGEILFdgedllkLSEKELrkirgr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 456 -IQnCILQE-----N-------------ILFGSVMQKQLYERVLEACAL--LPD----LEQLPNgdqteigekgvNISGG 510
Cdd:COG0444 87 eIQ-MIFQDpmtslNpvmtvgdqiaeplRIHGGLSKAEARERAIELLERvgLPDperrLDRYPH-----------ELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 511 QKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQ---LFEKVIGSSGMlrnkTRILVTHNLTLLPQM-DLIVVMESGRVA 586
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQilnLLKDLQRELGL----AILFITHDLGVVAEIaDRVAVMYAGRIV 230
|
250
....*....|
gi 1387192242 587 QMGTYQEILA 596
Cdd:COG0444 231 EEGPVEELFE 240
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
380-604 |
3.00e-10 |
|
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: 62.02 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 380 DHAIGFINASFSWDKTgiPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIV-----QRKGSV------- 447
Cdd:COG1119 1 DPLLELRNVTVRRGGK--TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrlfgERRGGEdvwelrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 448 --AYVSQ--QAWIQNCILQENI----LFGSV--------MQKQLYERVLEACALLpDLEQLPNGDqteigekgvnISGGQ 511
Cdd:COG1119 79 riGLVSPalQLRFPRDETVLDVvlsgFFDSIglyreptdEQRERARELLELLGLA-HLADRPFGT----------LSQGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 512 KHRVCLARAVYSGADIYLLDDPLSAVDVHvAKQLFEKVIGSSGMLRNKTRILVTHNLT-LLPQMDLIVVMESGRVAQMGT 590
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLG-ARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGITHVLLLKDGRVVAAGP 226
|
250
....*....|....
gi 1387192242 591 YQEILaKTKNLTNL 604
Cdd:COG1119 227 KEEVL-TSENLSEA 239
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1015-1210 |
3.58e-10 |
|
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: 62.02 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTL-----------SNCLFRIVERsggkiiidgidisTIG---LHDLRGKL----- 1075
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLlslitgdlpptYGNDVRLFGE-------------RRGgedVWELRKRIglvsp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1076 ----NIIPQDPVL------FSGT--LQMNLDPLDKYPDHELWEVLELCHLKEfvqslpkKLLHEiseggenLSVGQRQLV 1143
Cdd:COG1119 86 alqlRFPRDETVLdvvlsgFFDSigLYREPTDEQRERARELLELLGLAHLAD-------RPFGT-------LSQGEQRRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1144 CLARALLRKTKILILDEATASIDFETDNLVQTTVRK--EFSDCTILTIAHRLHSIIDS-DRVLVLDSGRI 1210
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRV 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1013-1219 |
3.76e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 62.41 E-value: 3.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1013 LALQDITFQTHGEEKIGIVGRTGAGKSTLS---NCLFriVERSGGKIIIDGIDISTIGLHDLRGKLNIIPQDP------- 1082
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAkhmNALL--IPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNPdnqivat 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1083 -----VLFsGTLQMNLDPLD--KYPDhelwEVLELCHLKEFVQSLPKKLlheiseggenlSVGQRQLVCLARALLRKTKI 1155
Cdd:PRK13633 102 iveedVAF-GPENLGIPPEEirERVD----ESLKKVGMYEYRRHAPHLL-----------SGGQKQRVAIAGILAMRPEC 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387192242 1156 LILDEATASIDFETDNLVQTTVRK--EFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETPQNL 1219
Cdd:PRK13633 166 IIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
399-597 |
4.43e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 61.64 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 399 VLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGSVAyvsqqawiqnCILQ------------ENIL 466
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVS----------ALLElgagfhpeltgrENIY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 467 F-GSV--MQKQLYERVLEACAllpdleqlpngDQTEIGE------KgvNISGGQKHRVCLARAVYSGADIYLLDDPLSAV 537
Cdd:COG1134 111 LnGRLlgLSRKEIDEKFDEIV-----------EFAELGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVG 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387192242 538 DVHV---AKQLFEKVIGssgmlRNKTRILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEILAK 597
Cdd:COG1134 178 DAAFqkkCLARIRELRE-----SGRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1015-1196 |
4.47e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.98 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVE-------RSGGKIIIDGIDISTIGLHDLRGKLNIIPQDPVLFSG 1087
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevrvEGRVEFFNQNIYERRVNLNRLRRQVSMVHPKPNLFPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1088 TLQMNLDPLDK----YPDHELWEVLElCHLKEfvQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRKTKILILDEATA 1163
Cdd:PRK14258 103 SVYDNVAYGVKivgwRPKLEIDDIVE-SALKD--ADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCF 179
|
170 180 190
....*....|....*....|....*....|....*..
gi 1387192242 1164 SID----FETDNLVQTTVRKefSDCTILTIAHRLHSI 1196
Cdd:PRK14258 180 GLDpiasMKVESLIQSLRLR--SELTMVIVSHNLHQV 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1013-1220 |
4.62e-10 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 61.31 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1013 LALQDITFQTHGE-----------EKIGIVGRTGAGKSTLSNCL--FriversggkiiidgidistigLHDLRGKLNIIP 1079
Cdd:COG3840 2 LRLDDLTYRYGDFplrfdltiaagERVAILGPSGAGKSTLLNLIagF---------------------LPPDSGRILWNG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1080 QD---------PV--------LFSG-TLQ----------MNLDPLDKypdHELWEVLELCHLKEFVQSLPkkllheiseg 1131
Cdd:COG3840 61 QDltalppaerPVsmlfqennLFPHlTVAqniglglrpgLKLTAEQR---AQVEQALERVGLAGLLDRLP---------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1132 gENLSVGQRQLVCLARALLRKTKILILDEATASID----FETDNLVQtTVRKEFsDCTILTIAHRLHSIID-SDRVLVLD 1206
Cdd:COG3840 128 -GQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVD-ELCRER-GLTVLMVTHDPEDAARiADRVLLVA 204
|
250
....*....|....
gi 1387192242 1207 SGRITEFETPQNLI 1220
Cdd:COG3840 205 DGRIAADGPTAALL 218
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
399-616 |
5.85e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 61.39 E-value: 5.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 399 VLKDLNIKIPEGALVAVVGQVGSGKSSvLSAILGEMEK-------LKGIVQRKGSVAYVSQQawI----QNC-------- 459
Cdd:COG4167 28 AVKPVSFTLEAGQTLAIIGENGSGKST-LAKMLAGIIEptsgeilINGHKLEYGDYKYRCKH--IrmifQDPntslnprl 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 460 ----ILQENILFGSVM----QKQLYERVLEACALLPD-LEQLPNgdqteigekgvNISGGQKHRVCLARAVYSGADIYLL 530
Cdd:COG4167 105 nigqILEEPLRLNTDLtaeeREERIFATLRLVGLLPEhANFYPH-----------MLSSGQKQRVALARALILQPKIIIA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 531 DDPLSAVDVHVAKQLFEKvigssgMLRNKTR-----ILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEILAKTKN-LT- 602
Cdd:COG4167 174 DEALAALDMSVRSQIINL------MLELQEKlgisyIYVSQHLGIVKHIsDKVLVMHQGEVVEYGKTAEVFANPQHeVTk 247
|
250
....*....|....*
gi 1387192242 603 NLLQA-FSEQETAHA 616
Cdd:COG4167 248 RLIEShFGEALTADA 262
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
399-585 |
6.19e-10 |
|
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: 60.62 E-value: 6.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 399 VLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGSVAYVSQQAWIQnciLQENIlfGSVMQK-QLYE 477
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINE---LRQKV--GMVFQQfNLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 478 R--VLEACALLP-DLEQLPNGDQTEIGEK-----GV---------NISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVH 540
Cdd:cd03262 90 HltVLENITLAPiKVKGMSKAEAEERALEllekvGLadkadaypaQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1387192242 541 VAKQLFE--KVIGSSGMlrnkTRILVTHnltllpQM-------DLIVVMESGRV 585
Cdd:cd03262 170 LVGEVLDvmKDLAEEGM----TMVVVTH------EMgfarevaDRVIFMDDGRI 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1006-1210 |
6.38e-10 |
|
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: 60.46 E-value: 6.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1006 RYRDDLG--LALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLhDLRGKLNIIPQDPV 1083
Cdd:cd03266 10 RFRDVKKtvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPA-EARRRLGFVSDSTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1084 LfsgtlqmnldpldkYPDHELWEVLE-------------LCHLKEFVQSLPKKLLHEISEGGenLSVGQRQLVCLARALL 1150
Cdd:cd03266 89 L--------------YDRLTARENLEyfaglyglkgdelTARLEELADRLGMEELLDRRVGG--FSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387192242 1151 RKTKILILDEATASID-FETDNLVQTTVRKEFSDCTILTIAHRLHSIID-SDRVLVLDSGRI 1210
Cdd:cd03266 153 HDPPVLLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRV 214
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
383-604 |
7.07e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 61.72 E-value: 7.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 383 IGFINASFSWDKtGIP----VLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIV----------------- 441
Cdd:PRK13646 3 IRFDNVSYTYQK-GTPyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVtvdditithktkdkyir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 442 ---QRKGSVAYVSQQAWIQNCILQEnILFGSVMQKQLYERVLE-ACALLPDLeqlpnGDQTEIGEKG-VNISGGQKHRVC 516
Cdd:PRK13646 82 pvrKRIGMVFQFPESQLFEDTVERE-IIFGPKNFKMNLDEVKNyAHRLLMDL-----GFSRDVMSQSpFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 517 LARAVYSGADIYLLDDPLSAVDVHVAKQLFeKVIGSSGMLRNKTRILVTHNLTLLPQ-MDLIVVMESGRVAQMGTYQEIL 595
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVM-RLLKSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELF 234
|
....*....
gi 1387192242 596 AKTKNLTNL 604
Cdd:PRK13646 235 KDKKKLADW 243
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1015-1210 |
8.01e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.76 E-value: 8.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGgkiiidgidiSTIGLHDLR---------GKLNI--IPQDPV 1083
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDS----------GTLEIGGNPcarltpakaHQLGIylVPQEPL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1084 LFSG-TLQMNLdpLDKYPDHELwevlELCHLKEFVQSLPKKLLHEISEGgeNLSVGQRQLVCLARALLRKTKILILDEAT 1162
Cdd:PRK15439 97 LFPNlSVKENI--LFGLPKRQA----SMQKMKQLLAALGCQLDLDSSAG--SLEVADRQIVEILRGLMRDSRILILDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1163 ASID-FETDNLVQTTVRKEFSDCTILTIAHRLHSIID-SDRVLVLDSGRI 1210
Cdd:PRK15439 169 ASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTI 218
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
396-599 |
8.51e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 60.92 E-value: 8.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAI------------LGEME--KLKGIVQRKGSVAYVSQQAWI--QNC 459
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirVGDITidTARSLSQQKGLIRQLRQHVGFvfQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 460 IL------QENILFGSVMQKQlyERVLEACALLPDLeqlpngdQTEIGEKGVN------ISGGQKHRVCLARAVYSGADI 527
Cdd:PRK11264 95 NLfphrtvLENIIEGPVIVKG--EPKEEATARAREL-------LAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387192242 528 YLLDDPLSAVDvhvaKQLFEKVIGSSGML--RNKTRILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEILAKTK 599
Cdd:PRK11264 166 ILFDEPTSALD----PELVGEVLNTIRQLaqEKRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKALFADPQ 236
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
387-604 |
9.65e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 60.88 E-value: 9.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 387 NASFSWDK-TGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGSvAYVSQQAW---------I 456
Cdd:PRK13642 9 NLVFKYEKeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-LLTAENVWnlrrkigmvF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 457 QN-------CILQENILFG----SVMQKQLYERVLEACALLPDLEQLPngdqteigEKGVNISGGQKHRVCLARAVYSGA 525
Cdd:PRK13642 88 QNpdnqfvgATVEDDVAFGmenqGIPREEMIKRVDEALLAVNMLDFKT--------REPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387192242 526 DIYLLDDPLSAVDvHVAKQLFEKVIGSSGMLRNKTRILVTHNLTLLPQMDLIVVMESGRVAQMGTYQEILAKTKNLTNL 604
Cdd:PRK13642 160 EIIILDESTSMLD-PTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMVEI 237
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
997-1220 |
9.87e-10 |
|
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: 62.51 E-value: 9.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 997 IVEFVDYRARYRD-DLGL--ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDG----IDISTIGLh 1069
Cdd:TIGR03269 279 IIKVRNVSKRYISvDRGVvkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVgdewVDMTKPGP- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1070 DLRGK----LNIIPQDPVLFsgTLQMNLDPLDK-----YPDhELWEVLELCHLK------EFVQSLPKKLLHEISEGgen 1134
Cdd:TIGR03269 358 DGRGRakryIGILHQEYDLY--PHRTVLDNLTEaigleLPD-ELARMKAVITLKmvgfdeEKAEEILDKYPDELSEG--- 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1135 lsvgQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTV---RKEFSDcTILTIAHRLHSIID-SDRVLVLDSGRI 1210
Cdd:TIGR03269 432 ----ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkaREEMEQ-TFIIVSHDMDFVLDvCDRAALMRDGKI 506
|
250
....*....|
gi 1387192242 1211 TEFETPQNLI 1220
Cdd:TIGR03269 507 VKIGDPEEIV 516
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
400-596 |
1.02e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 61.00 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 400 LKDLNIKIPEGALVAVVGQVGSGKSSVL---SAIL----GEME-------------KLKGIVQRKGSVAYVSQQAWIQNC 459
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMqhfNALLkpssGTITiagyhitpetgnkNLKKLRKKVSLVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 460 ILqENILFG----SVMQKQLYERVLEACALLPDLEQLPNGDQTEIgekgvniSGGQKHRVCLARAVYSGADIYLLDDPLS 535
Cdd:PRK13641 103 VL-KDVEFGpknfGFSEDEAKEKALKWLKKVGLSEDLISKSPFEL-------SGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387192242 536 AVDVHVAKQLFEkvIGSSGMLRNKTRILVTHNLTLLPQ-MDLIVVMESGRVAQMGTYQEILA 596
Cdd:PRK13641 175 GLDPEGRKEMMQ--LFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFS 234
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1014-1211 |
1.02e-09 |
|
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: 60.42 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIiidgidiSTIGLHDLRGKLNIIPQDPVLFS--GTLQM 1091
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV-------RVAGLVPWKRRKKFLRRIGVVFGqkTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1092 NLDPLDKY---------PDHELWEVLElcHLKEFVQslpkkLLHEISEGGENLSVGQRQLVCLARALLRKTKILILDEAT 1162
Cdd:cd03267 109 DLPVIDSFyllaaiydlPPARFKKRLD--ELSELLD-----LEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1387192242 1163 ASIDFETDNLVQTTVRKEFSD--CTILTIAHRLHSIID-SDRVLVLDSGRIT 1211
Cdd:cd03267 182 IGLDVVAQENIRNFLKEYNRErgTTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
726-929 |
1.05e-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: 60.99 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 726 GLLGLMQGLFVCSGAYVVTRGSLAASRVLHAQLLDNVLHLPLQFFETNPIGQVINRFTKDMFIIDMRFHYYIRTWVNCTL 805
Cdd:cd18555 49 LILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLFRANSNVYIRQILSNQVISLIIDLLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 806 DVIGTVLVIVGALPL----FILGLIPLVFLYFTIQRYYMASSRQIrrlagASHSPVISHFCETLLGVSTIRAFGHEQRFI 881
Cdd:cd18555 129 LVIYLIYMLYYSPLLtlivLLLGLLIVLLLLLTRKKIKKLNQEEI-----VAQTKVQSYLTETLYGIETIKSLGSEKNIY 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1387192242 882 QQNKEVVNENLVCF-----YNNVISNrwLSVRLEFLGNLMVFFTAVLTVLAGN 929
Cdd:cd18555 204 KKWENLFKKQLKAFkkkerLSNILNS--ISSSIQFIAPLLILWIGAYLVINGE 254
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
387-605 |
1.15e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 61.26 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 387 NASFSWDK---TGIPVLKDLNIKIPEGALVAVVGQVGSGKSSV---LSAIL----GEME--------------------- 435
Cdd:PRK13651 7 NIVKIFNKklpTELKALDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALLlpdtGTIEwifkdeknkkktkekekvlek 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 436 ---------KLKGIVQRKGSVAYVSQQAWIQ--NCILQENILFGS----VMQKQLYERVLEACAL--LPD--LEQLPngd 496
Cdd:PRK13651 87 lviqktrfkKIKKIKEIRRRVGVVFQFAEYQlfEQTIEKDIIFGPvsmgVSKEEAKKRAAKYIELvgLDEsyLQRSP--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 497 qteigekgVNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQLFE--KVIGSSGmlrnKTRILVTHNL-TLLPQ 573
Cdd:PRK13651 164 --------FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEifDNLNKQG----KTIILVTHDLdNVLEW 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 1387192242 574 MDLIVVMESGRVAQMGTYQEILAKTKNL-------TNLL 605
Cdd:PRK13651 232 TKRTIFFKDGKIIKDGDTYDILSDNKFLiennmepPKLL 270
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
399-590 |
1.25e-09 |
|
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: 59.75 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 399 VLKDLNIKIPEGALVAVVGQVGSGKSSVLSAI--------------------LGEMEKLKGivqRKGSVAYVsQQAW--I 456
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLagldrptsgtvrlagqdlfaLDEDARARL---RARHVGFV-FQSFqlL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 457 QNCILQENI-----LFGSVMQKQLYERVLEACALLPDLEQLPNGdqteigekgvnISGGQKHRVCLARAVYSGADIYLLD 531
Cdd:COG4181 103 PTLTALENVmlpleLAGRRDARARARALLERVGLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAILFAD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387192242 532 DPLSAVD----VHVAKQLFEkvigssgmlRNKTR----ILVTHNLTLLPQMDLIVVMESGRVAQMGT 590
Cdd:COG4181 172 EPTGNLDaatgEQIIDLLFE---------LNRERgttlVLVTHDPALAARCDRVLRLRAGRLVEDTA 229
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1019-1210 |
1.28e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 59.98 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1019 TFQTHGEEKIGIVGRTGAGKSTLSNCL--FRIVERSGGKIIIDGIDISTIGlhdlRGKLNIIPQDPVLFSG-TLQMN--- 1092
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIagFLTPASGSLTLNGQDHTTTPPS----RRPVSMLFQENNLFSHlTVAQNigl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1093 -LDP---LDKYPDHELWEVLELCHLKEFVQSLPKKLlheiseggenlSVGQRQLVCLARALLRKTKILILDEATASID-- 1166
Cdd:PRK10771 95 gLNPglkLNAAQREKLHAIARQMGIEDLLARLPGQL-----------SGGQRQRVALARCLVREQPILLLDEPFSALDpa 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1387192242 1167 --FETDNLVQTTVRKEfsDCTILTIAHRL---HSIidSDRVLVLDSGRI 1210
Cdd:PRK10771 164 lrQEMLTLVSQVCQER--QLTLLMVSHSLedaARI--APRSLVVADGRI 208
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
396-596 |
1.31e-09 |
|
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: 59.76 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQ---------------RKGsVAYVSQQAWI---- 456
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdgeditglppheiaRLG-IGRTFQIPRLfpel 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 457 ---QNCIL------QENILFGSVMQ--KQLYERVLEACAL--LPDLEQLPNGdqteigekgvNISGGQKHRVCLARAVYS 523
Cdd:cd03219 91 tvlENVMVaaqartGSGLLLARARReeREARERAEELLERvgLADLADRPAG----------ELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387192242 524 GADIYLLDDP---LSAVDVHVAKQLFEKvIGSSGMlrnkTRILVTHNLTLLpqMDL---IVVMESGRVAQMGTYQEILA 596
Cdd:cd03219 161 DPKLLLLDEPaagLNPEETEELAELIRE-LRERGI----TVLLVEHDMDVV--MSLadrVTVLDQGRVIAEGTPDEVRN 232
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1015-1212 |
1.42e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 60.47 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIvER----SGGKIIIDGIDISTIGLHDLRGKLNIIPQDPV------- 1083
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL-ESpsqgNVSWRGEPLAKLNRAQRKAFRRDIQMVFQDSIsavnprk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1084 ----LFSGTLQ--MNLDPLDKypDHELWEVLELCHLK-EFVQSLPKKLlheiseggenlSVGQRQLVCLARALLRKTKIL 1156
Cdd:PRK10419 107 tvreIIREPLRhlLSLDKAER--LARASEMLRAVDLDdSVLDKRPPQL-----------SGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1157 ILDEATASID--FETDNLVQTTVRKEFSDCTILTIAHRLhSIID--SDRVLVLDSGRITE 1212
Cdd:PRK10419 174 ILDEAVSNLDlvLQAGVIRLLKKLQQQFGTACLFITHDL-RLVErfCQRVMVMDNGQIVE 232
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
997-1223 |
1.47e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 60.63 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 997 IVEFVDYRARYRDDLGlALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDI--STIGLHDLRGK 1074
Cdd:PRK13636 5 ILKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1075 LNIIPQDP--VLFSGTL--QMNLDPLD-KYPDHELWEVLELCHLKEFVQSLPKKLLHEiseggenLSVGQRQLVCLARAL 1149
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVyqDVSFGAVNlKLPEDEVRKRVDNALKRTGIEHLKDKPTHC-------LSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387192242 1150 LRKTKILILDEATASID----FETDNLVQTTVrKEFsDCTILTIAHRLHSI-IDSDRVLVLDSGRITEFETPQNLIHKR 1223
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQ-KEL-GLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
394-602 |
1.92e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.20 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 394 KTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGS-------------VAYVSQQA--WIQN 458
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfVGLVFQNPddQIFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 459 CILQENILFGSVM----QKQLYERVLEACALLpDLEQL----PNgdqteigekgvNISGGQKHRVCLARAVYSGADIYLL 530
Cdd:PRK13652 94 PTVEQDIAFGPINlgldEETVAHRVSSALHML-GLEELrdrvPH-----------HLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387192242 531 DDPLSAVDVHVAKQLFE---KVIGSSGMlrnkTRILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEILAKTKNLT 602
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDflnDLPETYGM----TVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEIFLQPDLLA 233
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
396-601 |
2.01e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 60.25 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGSVAYVSQQAWIQnciLQENIlfGSVMQ--- 472
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMK---LRESV--GMVFQdpd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 473 KQLYE-RVLEACALLPDLEQLPNGDQTE-----IGEKGVN---------ISGGQKHRVCLARAVYSGADIYLLDDPLSAV 537
Cdd:PRK13636 93 NQLFSaSVYQDVSFGAVNLKLPEDEVRKrvdnaLKRTGIEhlkdkpthcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387192242 538 DVHVAKQLFEKVIGSSGMLrNKTRILVTHNLTLLP-QMDLIVVMESGRVAQMGTYQEILAKTKNL 601
Cdd:PRK13636 173 DPMGVSEIMKLLVEMQKEL-GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEKEML 236
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
400-568 |
2.14e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 59.80 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 400 LKDLNIKIPEGALVAVVGQVGSGKSSVLSAiLGEMEKLKGIVQRKGSVAYVSQQAWIQNC-----------ILQ------ 462
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRC-FNRLNDLIPGFRVEGKVTFHGKNLYAPDVdpvevrrrigmVFQkpnpfp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 463 ----ENILFGSVMQ------KQLYERVLEACALLPDLEQlpngdqtEIGEKGVNISGGQKHRVCLARAVYSGADIYLLDD 532
Cdd:PRK14243 105 ksiyDNIAYGARINgykgdmDELVERSLRQAALWDEVKD-------KLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 1387192242 533 PLSAVDvHVAKQLFEKVIGSSGmlRNKTRILVTHNL 568
Cdd:PRK14243 178 PCSALD-PISTLRIEELMHELK--EQYTIIIVTHNM 210
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
727-927 |
2.26e-09 |
|
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: 60.13 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 727 LLGLMQGLFVCSGAYVVTRGSLAASRVLHAQLLDNVLHLPLQFFETNPIGQVINRFTKDmfiIDMrfhyyIRTWVNCTLD 806
Cdd:cd18552 47 GLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITND---VNQ-----VQNALTSALT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 807 VIG----TVLVIVGA-------LPLFILGLIPLVFLYFT-IQRYYMASSRQIRRLAGAshspVISHFCETLLGVSTIRAF 874
Cdd:cd18552 119 VLVrdplTVIGLLGVlfyldwkLTLIALVVLPLAALPIRrIGKRLRKISRRSQESMGD----LTSVLQETLSGIRVVKAF 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1387192242 875 GHEQRFIQQNKEVVNEnlvcfynnvisNRWLSVRLEFLGNLMVFFTAVLTVLA 927
Cdd:cd18552 195 GAEDYEIKRFRKANER-----------LRRLSMKIARARALSSPLMELLGAIA 236
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
402-547 |
3.07e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 59.26 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 402 DLNIKipEGALVAVVGQVGSGKSSVLSAILG----------EMEKLKGIVQRKGSVA-----------YVSQQAWIQNCI 460
Cdd:PRK09984 24 DLNIH--HGEMVALLGPSGSGKSTLLRHLSGlitgdksagsHIELLGRTVQREGRLArdirksrantgYIFQQFNLVNRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 461 -LQENILFGSVMQKQLYERVLEAcaLLPDLEQLPNGDQTEIG------EKGVNISGGQKHRVCLARAVYSGADIYLLDDP 533
Cdd:PRK09984 102 sVLENVLIGALGSTPFWRTCFSW--FTREQKQRALQALTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
|
170
....*....|....
gi 1387192242 534 LSAVDVHVAKQLFE 547
Cdd:PRK09984 180 IASLDPESARIVMD 193
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
396-597 |
3.43e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 60.24 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILG-----------------EME-KLKGIvqrkgsvAYVsqqawIQ 457
Cdd:PRK11650 16 KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGleritsgeiwiggrvvnELEpADRDI-------AMV-----FQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 458 NCIL------QENILFG----SVMQKQLYERVLEACALLpdleqlpngdqtEIGE----KGVNISGGQKHRVCLARAVYS 523
Cdd:PRK11650 84 NYALyphmsvRENMAYGlkirGMPKAEIEERVAEAARIL------------ELEPlldrKPRELSGGQRQRVAMGRAIVR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 524 GADIYLLDDPLSAVDvhvAKqlfekvigssgmLR--------------NKTRILVTHN----LTLlpqMDLIVVMESGRV 585
Cdd:PRK11650 152 EPAVFLFDEPLSNLD---AK------------LRvqmrleiqrlhrrlKTTSLYVTHDqveaMTL---ADRVVVMNGGVA 213
|
250
....*....|..
gi 1387192242 586 AQMGTYQEILAK 597
Cdd:PRK11650 214 EQIGTPVEVYEK 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1014-1217 |
3.63e-09 |
|
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: 60.85 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERS--GGKIIIDGIDISTIGLHDLRGKLNIIPQDP--------- 1082
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEgeIRFDGQDLDGLSRRALRPLRRRMQVVFQDPfgslsprmt 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1083 ----------VLFSG------------TLQ-MNLDP--LDKYPdHElwevlelchlkefvqslpkkllheiseggenLSV 1137
Cdd:COG4172 381 vgqiiaeglrVHGPGlsaaerrarvaeALEeVGLDPaaRHRYP-HE-------------------------------FSG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1138 GQRQLVCLARALLRKTKILILDEATASIDfetdnlvqTTVRKEfsdctILT---------------IAHRLH---SIidS 1199
Cdd:COG4172 429 GQRQRIAIARALILEPKLLVLDEPTSALD--------VSVQAQ-----ILDllrdlqrehglaylfISHDLAvvrAL--A 493
|
250 260
....*....|....*....|....*
gi 1387192242 1200 DRVLVLDSGRITE-------FETPQ 1217
Cdd:COG4172 494 HRVMVMKDGKVVEqgpteqvFDAPQ 518
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
398-600 |
3.67e-09 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 58.47 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 398 PVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAI--L-----GEME--------KLKGIVQRKGSVAYVSQQ--------A 454
Cdd:COG1126 15 EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCInlLeepdsGTITvdgedltdSKKDINKLRRKVGMVFQQfnlfphltV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 455 wIQNCILqenilfGSV----MQKQlyERVLEACALLpdleqlpngDQTEIGEKG----VNISGGQKHRVCLARAVYSGAD 526
Cdd:COG1126 95 -LENVTL------APIkvkkMSKA--EAEERAMELL---------ERVGLADKAdaypAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 527 IYLLDDPLSAVD-------VHVAKQLfekviGSSGMlrnkTRILVTHnltllpQM-------DLIVVMESGRVAQMGTYQ 592
Cdd:COG1126 157 VMLFDEPTSALDpelvgevLDVMRDL-----AKEGM----TMVVVTH------EMgfarevaDRVVFMDGGRIVEEGPPE 221
|
....*...
gi 1387192242 593 EILAKTKN 600
Cdd:COG1126 222 EFFENPQH 229
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
400-594 |
3.72e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 59.36 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 400 LKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVqRKGS--VAYVSQQAWIQNCILQENILFgSVMQKQLYE 477
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV-TVGDivVSSTSKQKEIKPVRKKVGVVF-QFPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 478 R-VLEACALLP--------DLEQLPN------GDQTEIGEKG-VNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHV 541
Cdd:PRK13643 100 EtVLKDVAFGPqnfgipkeKAEKIAAeklemvGLADEFWEKSpFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387192242 542 ---AKQLFEKvIGSSGmlrnKTRILVTHNL-TLLPQMDLIVVMESGRVAQMGT----YQEI 594
Cdd:PRK13643 180 rieMMQLFES-IHQSG----QTVVLVTHLMdDVADYADYVYLLEKGHIISCGTpsdvFQEV 235
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
387-603 |
5.10e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 58.94 E-value: 5.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 387 NASFSWDKtGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKG--------SVAYVSQQAWI-- 456
Cdd:PRK13639 6 DLKYSYPD-GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikydkkSLLEVRKTVGIvf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 457 QNCILQ-------ENILFG----SVMQKQLYERVLEACAllpdleqlpngdqtEIGEKGV------NISGGQKHRVCLAR 519
Cdd:PRK13639 85 QNPDDQlfaptveEDVAFGplnlGLSKEEVEKRVKEALK--------------AVGMEGFenkpphHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 520 AVYSGADIYLLDDPLSAVDVHVAKQLFE--KVIGSSGMlrnkTRILVTHNLTLLP-QMDLIVVMESGRVAQMGTYQEILA 596
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKllYDLNKEGI----TIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFS 226
|
....*..
gi 1387192242 597 KTKNLTN 603
Cdd:PRK13639 227 DIETIRK 233
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
383-593 |
5.73e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 60.64 E-value: 5.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 383 IGFINASFSWdkTGIPVL-KDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGSVAY-VSQQAWIQNCI 460
Cdd:PLN03073 509 ISFSDASFGY--PGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMaVFSQHHVDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 461 LQENILfgsVMQKQLYERVLEacallpdlEQLpngdQTEIGEKGVN----------ISGGQKHRVCLARAVYSGADIYLL 530
Cdd:PLN03073 587 LSSNPL---LYMMRCFPGVPE--------QKL----RAHLGSFGVTgnlalqpmytLSGGQKSRVAFAKITFKKPHILLL 651
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387192242 531 DDPLSAVDVHVAKQLFEKVIGSSGMLrnktrILVTHNLTLLP-QMDLIVVMESGRVAQM-GTYQE 593
Cdd:PLN03073 652 DEPSNHLDLDAVEALIQGLVLFQGGV-----LMVSHDEHLISgSVDELWVVSEGKVTPFhGTFHD 711
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1007-1218 |
5.74e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.52 E-value: 5.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1007 YRDDLGLaLQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVE------RSGGKIIIDGIDISTIGLHDLRGKLNIIPQ 1080
Cdd:PRK14246 19 YINDKAI-LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1081 DPVLFSG-TLQMNLD-PLDKY---PDHELWEVLELCHLKefvQSLPKKLLHEISEGGENLSVGQRQLVCLARALLRKTKI 1155
Cdd:PRK14246 98 QPNPFPHlSIYDNIAyPLKSHgikEKREIKKIVEECLRK---VGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKV 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387192242 1156 LILDEATASIDFETDNLVQTTVRKEFSDCTILTIAHRLHSIID-SDRVLVLDSGRITE-------FETPQN 1218
Cdd:PRK14246 175 LLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEwgssneiFTSPKN 245
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
396-570 |
5.80e-09 |
|
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: 60.53 E-value: 5.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKSSvLSAILGEMEKLKG---IVQRKGSVAYVSQQAWIQNCILQENILF-GSVM 471
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSS-LFRILGELWPVYGgrlTKPAKGKLFYVPQRPYMTLGTLRDQIIYpDSSE 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 472 Q---KQLYERVLEACALLPDLEQLPngdQTEIGEKGVN-----ISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAK 543
Cdd:TIGR00954 543 DmkrRGLSDKDLEQILDNVQLTHIL---EREGGWSAVQdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEG 619
|
170 180
....*....|....*....|....*....
gi 1387192242 544 QLFEkvigssgMLRNK--TRILVTHNLTL 570
Cdd:TIGR00954 620 YMYR-------LCREFgiTLFSVSHRKSL 641
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
399-600 |
5.87e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 58.31 E-value: 5.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 399 VLKDLNIKIPEGALVAVVGQVGSGKSSVLSAI-----LGEMEKLKGIVQRKGSVAYVSQQAWIQ---------------- 457
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPIEvrrevgmvfqypnpfp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 458 NCILQENILFGSVM------QKQLYERV---LEACALLPDLeqlpngdQTEIGEKGVNISGGQKHRVCLARAVYSGADIY 528
Cdd:PRK14267 99 HLTIYDNVAIGVKLnglvksKKELDERVewaLKKAALWDEV-------KDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387192242 529 LLDDPLSAVD-VHVAK---QLFEkvigssgMLRNKTRILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEILAKTKN 600
Cdd:PRK14267 172 LMDEPTANIDpVGTAKieeLLFE-------LKKEYTIVLVTHSPAQAARVsDYVAFLYLGKLIEVGPTRKVFENPEH 241
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
726-926 |
6.68e-09 |
|
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: 58.65 E-value: 6.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 726 GLLGLMQGLFVCSGA--YVVTRGslaASRV---LHAQLLDNVLHLPLQFFETNPIGQVINRFTKDMFIidmrfhyyIRTW 800
Cdd:cd18575 41 LLLAVALVLALASALrfYLVSWL---GERVvadLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTL--------IQTV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 801 VNCTLDV-IGTVLVIVGA----------LPLFILGLIPLVFLYFtiqryyMASSRQIRRLAGASHSPV--ISHFC-ETLL 866
Cdd:cd18575 110 VGSSLSIaLRNLLLLIGGlvmlfitspkLTLLVLLVIPLVVLPI------ILFGRRVRRLSRASQDRLadLSAFAeETLS 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387192242 867 GVSTIRAFGHEQRFIQQNKEVVNENLvcfynnVISNRWLSVR--LEFLGNLMVfFTAVLTVL 926
Cdd:cd18575 184 AIKTVQAFTREDAERQRFATAVEAAF------AAALRRIRARalLTALVIFLV-FGAIVFVL 238
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1015-1178 |
8.52e-09 |
|
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: 57.10 E-value: 8.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTLsnclFRIV---ERSGGKIIIDGIDISTIGLHDLRGKLNIIPQDPVLFSG-TLQ 1090
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTL----LRILaglLPPSAGEVLWNGEPIRDAREDYRRRLAYLGHADGLKPElTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1091 MNLDPL-----DKYPDHELWEVLELCHLKEFVQSLPKkllheiseggeNLSVGQRQLVCLARALLRKTKILILDEATASI 1165
Cdd:COG4133 94 ENLRFWaalygLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170
....*....|...
gi 1387192242 1166 DFETDNLVQTTVR 1178
Cdd:COG4133 163 DAAGVALLAELIA 175
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1014-1218 |
9.23e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.87 E-value: 9.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIG---LHDLRGKLNIIPQDPVlfsgtlq 1090
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPY------- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1091 MNLDPLDK--YPDHELWEVLELCH----------LKEFVQSLPKKLL---HEISEggenlsvGQRQLVCLARALLRKTKI 1155
Cdd:PRK10261 412 ASLDPRQTvgDSIMEPLRVHGLLPgkaaaarvawLLERVGLLPEHAWrypHEFSG-------GQRQRICIARALALNPKV 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387192242 1156 LILDEATASIDF----ETDNLVqTTVRKEFSdCTILTIAHRLhSIID--SDRVLVLDSGRITE-------FETPQN 1218
Cdd:PRK10261 485 IIADEAVSALDVsirgQIINLL-LDLQRDFG-IAYLFISHDM-AVVEriSHRVAVMYLGQIVEigprravFENPQH 557
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1008-1210 |
9.98e-09 |
|
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: 56.73 E-value: 9.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1008 RDDLGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCL--FRIVERSGGkiiidgidisTIGLHDL------RGKLNIIP 1079
Cdd:cd03298 7 RFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIagFETPQSGRV----------LINGVDVtaappaDRPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1080 QDPVLFSG-TLQMNLDpLDKYPDhelwevlelCHLKEFVQSLPKKLLHEISEGG------ENLSVGQRQLVCLARALLRK 1152
Cdd:cd03298 77 QENNLFAHlTVEQNVG-LGLSPG---------LKLTAEDRQAIEVALARVGLAGlekrlpGELSGGERQRVALARVLVRD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387192242 1153 TKILILDEATASID----FETDNLVQTTVRKefSDCTILTIAHRLHSIID-SDRVLVLDSGRI 1210
Cdd:cd03298 147 KPVLLLDEPFAALDpalrAEMLDLVLDLHAE--TKMTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
369-594 |
1.03e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.48 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 369 LPHSIEANYIGDHAIGFINASFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQ------ 442
Cdd:PRK10261 1 MPHSDELDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmll 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 443 --RKGSVAYVSQQAWIQ---------NCILQE-----NILFG---------SVMQKQLYERVLEACALLPDLEQLPNGdQ 497
Cdd:PRK10261 81 rrRSRQVIELSEQSAAQmrhvrgadmAMIFQEpmtslNPVFTvgeqiaesiRLHQGASREEAMVEAKRMLDQVRIPEA-Q 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 498 TEIGEKGVNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQLFE--KVIG---SSGMlrnktrILVTHNLTLLP 572
Cdd:PRK10261 160 TILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQliKVLQkemSMGV------IFITHDMGVVA 233
|
250 260
....*....|....*....|...
gi 1387192242 573 QM-DLIVVMESGRVAQMGTYQEI 594
Cdd:PRK10261 234 EIaDRVLVMYQGEAVETGSVEQI 256
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
387-594 |
1.05e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 58.69 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 387 NASFSWDktGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIV-------------QRKGSVAYVSQq 453
Cdd:PRK11607 24 NLTKSFD--GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQImldgvdlshvppyQRPINMMFQSY- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 454 AWIQNCILQENILFGSVMQK----QLYERVLEACALLPDLEQlpngdqteIGEKGVNISGGQKHRVCLARAVYSGADIYL 529
Cdd:PRK11607 101 ALFPHMTVEQNIAFGLKQDKlpkaEIASRVNEMLGLVHMQEF--------AKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387192242 530 LDDPLSAVDvhvaKQLFEK-------VIGSSGMlrnkTRILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEI 594
Cdd:PRK11607 173 LDEPMGALD----KKLRDRmqlevvdILERVGV----TCVMVTHDQEEAMTMaGRIAIMNRGKFVQIGEPEEI 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1015-1214 |
1.14e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 59.31 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTlsncLFRI-----------VERSGGKiiidgidisTIGlhdlrgklnIIPQDPV 1083
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKST----LLKIlagelepdsgeVSIPKGL---------RIG---------YLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1084 LFSG-----TLQMNldpldkypDHELWEVL----ELCHLKEFVQSLPKK---LLHEISEGGE------------------ 1133
Cdd:COG0488 72 LDDDltvldTVLDG--------DAELRALEaeleELEAKLAEPDEDLERlaeLQEEFEALGGweaearaeeilsglgfpe 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1134 --------NLSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVRKefSDCTILTIAH-R--LHSIidSDRV 1202
Cdd:COG0488 144 edldrpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN--YPGTVLVVSHdRyfLDRV--ATRI 219
|
250
....*....|..
gi 1387192242 1203 LVLDSGRITEFE 1214
Cdd:COG0488 220 LELDRGKLTLYP 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
387-604 |
1.19e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 57.82 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 387 NASFSWDK-TGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGSvAYVSQQAW---------I 456
Cdd:PRK13650 9 NLTFKYKEdQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD-LLTEENVWdirhkigmvF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 457 QN-------CILQENILFG----SVMQKQLYERVLEACALLpdleqlpnGDQTEIGEKGVNISGGQKHRVCLARAVYSGA 525
Cdd:PRK13650 88 QNpdnqfvgATVEDDVAFGlenkGIPHEEMKERVNEALELV--------GMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 526 DIYLLDDPLSAVDVHVAKQLfekvIGSSGMLRNK---TRILVTHNLTLLPQMDLIVVMESGRVAQMGTYQEILAKTKNLT 602
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLEL----IKTIKGIRDDyqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGNDLL 235
|
..
gi 1387192242 603 NL 604
Cdd:PRK13650 236 QL 237
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1014-1223 |
1.34e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.77 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCL----------FRIVERSGGKIIIDGIDISTIGLhdLRGKLNIIPQDPV 1083
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILsgnyqpdagsILIDGQEMRFASTTAALAAGVAI--IYQELHLVPEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1084 ---LFSGTLQMNLDPLDKYpdhelwevlelcHLKEFVQSLPKKLLHEISEGG--ENLSVGQRQLVCLARALLRKTKILIL 1158
Cdd:PRK11288 97 aenLYLGQLPHKGGIVNRR------------LLNYEAREQLEHLGVDIDPDTplKYLSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1159 DEATASIDF-ETDNL--VQTTVRKEfsDCTILTIAHRLHSIID-SDRVLVLDSGR-ITEFETPQNLIHKR 1223
Cdd:PRK11288 165 DEPTSSLSArEIEQLfrVIRELRAE--GRVILYVSHRMEEIFAlCDAITVFKDGRyVATFDDMAQVDRDQ 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
389-596 |
1.34e-08 |
|
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: 58.93 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 389 SFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKS-SVLSaILGEMEKlkGIVQRKGSVAY-------VSQQAWIQ--- 457
Cdd:COG4172 15 AFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALS-ILRLLPD--PAAHPSGSILFdgqdllgLSERELRRirg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 458 ---NCILQE-----NILFgSVmQKQLYE---------------RVLEACAL--LPDLE--------QLpngdqteigekg 504
Cdd:COG4172 92 nriAMIFQEpmtslNPLH-TI-GKQIAEvlrlhrglsgaaaraRALELLERvgIPDPErrldayphQL------------ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 505 vniSGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQLFEkvigssgMLRNKTR------ILVTHNLTLLPQM-DLI 577
Cdd:COG4172 158 ---SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILD-------LLKDLQRelgmalLLITHDLGVVRRFaDRV 227
|
250
....*....|....*....
gi 1387192242 578 VVMESGRVAQMGTYQEILA 596
Cdd:COG4172 228 AVMRQGEIVEQGPTAELFA 246
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
389-636 |
1.42e-08 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 58.17 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 389 SFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKS---------------SVLsaILG-EMEKLKG---IVQRKgSVAY 449
Cdd:COG1135 10 TFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKStlircinllerptsgSVL--VDGvDLTALSErelRAARR-KIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 450 VSQQAwiqNcILQ-----ENILF-----GsVMQKQLYERVLEacaLLpDLeqlpngdqTEIGEKG----VNISGGQKHRV 515
Cdd:COG1135 87 IFQHF---N-LLSsrtvaENVALpleiaG-VPKAEIRKRVAE---LL-EL--------VGLSDKAdaypSQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 516 CLARAVYSGADIYLLDDPLSAVDVHVAKQLFEkvigssgMLR--NK----TRILVTHnltllpQMDLI-------VVMES 582
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDPETTRSILD-------LLKdiNRelglTIVLITH------EMDVVrricdrvAVLEN 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1387192242 583 GRVAQMGTYQEILAKTKnlTNLLQAFSEQETAHALKQVSVINSRTVLKDQILVQ 636
Cdd:COG1135 217 GRIVEQGPVLDVFANPQ--SELTRRFLPTVLNDELPEELLARLREAAGGGRLVR 268
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1014-1213 |
1.44e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 58.20 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFR------IVERSGGKIIIDGIDISTIGLHDLRG-KLNIIPQDPVlfs 1086
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGllaangRIGGSATFNGREILNLPEKELNKLRAeQISMIFQDPM--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1087 gtlqMNLDPLDKYPDhELWEVLELcH--------LKEFVQSL-------PKKLL----HEISEGgenlsvgQRQLVCLAR 1147
Cdd:PRK09473 108 ----TSLNPYMRVGE-QLMEVLML-HkgmskaeaFEESVRMLdavkmpeARKRMkmypHEFSGG-------MRQRVMIAM 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1148 ALLRKTKILILDEATASIDFETDNLVQT---TVRKEFsDCTILTIAHRLHSIIDS-DRVLVLDSGRITEF 1213
Cdd:PRK09473 175 ALLCRPKLLIADEPTTALDVTVQAQIMTllnELKREF-NTAIIMITHDLGVVAGIcDKVLVMYAGRTMEY 243
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
392-590 |
1.47e-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: 59.64 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 392 WDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGSVAYVSQQAWIQNCIL--QENILFG- 468
Cdd:TIGR01257 938 FEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMcpQHNILFHh 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 469 -SVMQKQLY----------ERVLEACALLPDleqlpNGDQTEIGEKGVNISGGQKHRVCLARAVYSGADIYLLDDPLSAV 537
Cdd:TIGR01257 1018 lTVAEHILFyaqlkgrsweEAQLEMEAMLED-----TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1387192242 538 DVHVAKQLFEKVIG-SSGmlrnKTRILVTHNLTLLPQM-DLIVVMESGRVAQMGT 590
Cdd:TIGR01257 1093 DPYSRRSIWDLLLKyRSG----RTIIMSTHHMDEADLLgDRIAIISQGRLYCSGT 1143
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1014-1210 |
1.49e-08 |
|
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: 56.38 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVE--RSGGKIIIDGIDISTIGLHDLRGKLNIIPQDPVLFSgtlqm 1091
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEpdSGTIIIDGLKLTDDKKNINELRQKVGMVFQQFNLFP----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1092 NLDPLD----------KYPDHEL----WEVLELCHLKEFVQSLPKKllheiseggenLSVGQRQLVCLARALLRKTKILI 1157
Cdd:cd03262 90 HLTVLEnitlapikvkGMSKAEAeeraLELLEKVGLADKADAYPAQ-----------LSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1387192242 1158 LDEATASIDFETDNLVQTTVRK-EFSDCTILTIAHRLHSIID-SDRVLVLDSGRI 1210
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
404-596 |
1.58e-08 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 56.69 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 404 NIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIV-------------QRKgsVAYVSQQawiQNCI----LQENIL 466
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIlwngqdltalppaERP--VSMLFQE---NNLFphltVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 467 FG-------SVMQKQLYERVLEACALLPDLEQLPNgdqteigekgvNISGGQKHRVCLARAVYSGADIYLLDDPLSAVD- 538
Cdd:COG3840 94 LGlrpglklTAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDp 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387192242 539 ------VHVAKQLFEKvigssgmlRNKTRILVTHNLT-LLPQMDLIVVMESGRVAQMGTYQEILA 596
Cdd:COG3840 163 alrqemLDLVDELCRE--------RGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALLD 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
402-596 |
1.70e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 56.51 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 402 DLNIKipEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGSVAYVSQQAWIQNCIL-QENILFG------------ 468
Cdd:PRK10771 19 DLTVE--RGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLfQENNLFShltvaqniglgl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 469 ------SVMQKQLYERVLEACALLPDLEQLPNgdqteigekgvNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDV--- 539
Cdd:PRK10771 97 npglklNAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDPalr 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387192242 540 HVAKQLFEKVIGSsgmlRNKTRILVTHNLT----LLPQMDLIVvmeSGRVAQMGTYQEILA 596
Cdd:PRK10771 166 QEMLTLVSQVCQE----RQLTLLMVSHSLEdaarIAPRSLVVA---DGRIAWDGPTDELLS 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
399-568 |
1.80e-08 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 56.97 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 399 VLKDLNIKIPEGALVAVVGQVGSGKSSVLSAI--LGEME---KLKGIVQ----------------RKgSVAYVSQQA--- 454
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIpgaRVEGEILldgediydpdvdvvelRR-RVGMVFQKPnpf 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 455 ----WiqncilqENILFGSVMQ-----KQLYERV---LEACALLPDLEqlpngDQteIGEKGVNISGGQKHRVCLARAVy 522
Cdd:COG1117 105 pksiY-------DNVAYGLRLHgikskSELDEIVeesLRKAALWDEVK-----DR--LKKSALGLSGGQQQRLCIARAL- 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1387192242 523 sgA---DIYLLDDPLSAVDvHVAKQLFEKVIGSsgmLRNK-TRILVTHNL 568
Cdd:COG1117 170 --AvepEVLLMDEPTSALD-PISTAKIEELILE---LKKDyTIVIVTHNM 213
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1135-1205 |
1.83e-08 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 55.70 E-value: 1.83e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387192242 1135 LSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVRKEFSD-CTILTIAHRLHSIIDSDRVLVL 1205
Cdd:NF040873 120 LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHARgATVVVVTHDLELVRRADPCVLL 191
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
396-585 |
1.84e-08 |
|
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: 55.73 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAI---LGEMEKLKGIV------------QRKGSVAYVSQqawiqnci 460
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIhyngipykefaeKYPGEIIYVSE-------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 461 lqENILFGSVMQKQLYERVLEAcallpdleqlpNGDQTEIGekgvnISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVH 540
Cdd:cd03233 91 --EDVHFPTLTVRETLDFALRC-----------KGNEFVRG-----ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1387192242 541 VAKQLFEKvigssgmLRNKTRILVTHNLTLLPQ--------MDLIVVMESGRV 585
Cdd:cd03233 153 TALEILKC-------IRTMADVLKTTTFVSLYQasdeiydlFDKVLVLYEGRQ 198
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
719-925 |
2.00e-08 |
|
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: 57.06 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 719 SKKLSIYGLLGLMQGLFVCS------GAYVVTRgsLAASRVLHAQ--LLDNVLHLPLQFFETNPIGQVINRFTKDMFIID 790
Cdd:cd18551 30 SAGGSSGGLLALLVALFLLQavlsalSSYLLGR--TGERVVLDLRrrLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 791 MRFHYYIRTWVNCTLDVIGTV-----------LVIVGALPLFILGLIPLVFLyftIQRYYMASSRQIRRLAGASHspvis 859
Cdd:cd18551 108 ELITSGLPQLVTGVLTVVGAVvlmflldwvltLVTLAVVPLAFLIILPLGRR---IRKASKRAQDALGELSAALE----- 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 860 hfcETLLGVSTIRAFGHEQRFIQQNKEVVNEnlvCFYNNVISNRWLSVrLEFLGNL--MVFFTAVLTV 925
Cdd:cd18551 180 ---RALSAIRTVKASNAEERETKRGGEAAER---LYRAGLKAAKIEAL-IGPLMGLavQLALLVVLGV 240
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
398-615 |
2.57e-08 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 56.56 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 398 PVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKG-------------SVAYVSQQAWIQNCI-LQE 463
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLALLPQHHLTPEGItVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 464 NILFG-----------SVMQKQLYERVLEACALlpdleqlpngdqTEIGEKGV-NISGGQKHRVCLARAVYSGADIYLLD 531
Cdd:PRK11231 96 LVAYGrspwlslwgrlSAEDNARVNQAMEQTRI------------NHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 532 DPLSAVDVHVAKQLFekvigssGMLR-----NKTRILVTHNLTllpQM----DLIVVMESGRVAQMGTYQEILakTKNLt 602
Cdd:PRK11231 164 EPTTYLDINHQVELM-------RLMRelntqGKTVVTVLHDLN---QAsrycDHLVVLANGHVMAQGTPEEVM--TPGL- 230
|
250
....*....|...
gi 1387192242 603 nLLQAFSEQETAH 615
Cdd:PRK11231 231 -LRTVFDVEAEIH 242
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
382-600 |
2.69e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 56.64 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 382 AIGFINASFSWdkTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGiVQRKGSVAYVSQQAWIQNCIL 461
Cdd:PRK14271 21 AMAAVNLTLGF--AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLLGGRSIFNYRDVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 462 QENILFGSVMQK------QLYERVL---EACALLP--DLEQLPNGDQTEIG----------EKGVNISGGQKHRVCLARA 520
Cdd:PRK14271 98 EFRRRVGMLFQRpnpfpmSIMDNVLagvRAHKLVPrkEFRGVAQARLTEVGlwdavkdrlsDSPFRLSGGQQQLLCLART 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 521 VYSGADIYLLDDPLSAVDVHVAKQLFEKVIGSSGMLrnkTRILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEILAKTK 599
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL---TVIIVTHNLAQAARIsDRAALFFDGRLVEEGPTEQLFSSPK 254
|
.
gi 1387192242 600 N 600
Cdd:PRK14271 255 H 255
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
399-566 |
2.79e-08 |
|
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: 55.19 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 399 VLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGSVAYVSQQAWIQNCI-------------LQENI 465
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLylghapgikttlsVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 466 LFGSVMQKQlyERVLEACAL--LPDLEQLPNGdqteigekgvNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAK 543
Cdd:cd03231 95 RFWHADHSD--EQVEEALARvgLNGFEDRPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180
....*....|....*....|...
gi 1387192242 544 QLFEKVIGSSGmlRNKTRILVTH 566
Cdd:cd03231 163 RFAEAMAGHCA--RGGMVVLTTH 183
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
395-585 |
2.95e-08 |
|
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: 54.75 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 395 TGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGsvayvsqqawiqncilqENILFGSVmqkq 474
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG-----------------KPVTRRSP---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 475 lYERVLEACALLPD--LEQLPNGDQTeIGEkgvNI------SGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQLF 546
Cdd:cd03215 70 -RDAIRAGIAYVPEdrKREGLVLDLS-VAE---NIalssllSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIY 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1387192242 547 EKVIGSSGmlRNKTRILVTHNLTLLPQM-DLIVVMESGRV 585
Cdd:cd03215 145 RLIRELAD--AGKAVLLISSELDELLGLcDRILVMYEGRI 182
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1014-1212 |
3.05e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 57.12 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTL---SNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLNIIPQDPVLFS---- 1086
Cdd:PRK11153 20 ALNNVSLHIPAGEIFGVIGASGAGKSTLircINLLERPTSGRVLVDGQDLTALSEKELRKARRQIGMIFQHFNLLSsrtv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1087 -GTLQMNLDpLDKYPDHEL----WEVLELCHLKEFVQSLPKkllheiseggeNLSVGQRQLVCLARALLRKTKILILDEA 1161
Cdd:PRK11153 100 fDNVALPLE-LAGTPKAEIkarvTELLELVGLSDKADRYPA-----------QLSGGQKQRVAIARALASNPKVLLCDEA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387192242 1162 TASIDFETDNLVQTTVRK---EFSdCTILTIAHRLhSIIDS--DRVLVLDSGRITE 1212
Cdd:PRK11153 168 TSALDPATTRSILELLKDinrELG-LTIVLITHEM-DVVKRicDRVAVIDAGRLVE 221
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
724-951 |
3.07e-08 |
|
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: 56.64 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 724 IYGLLGLMQGLFVCSGA------YVVTRGSLAASRVLHAQLLDNVLHLPLQFFETNPIGQVINRFTKDmfiIDMrfhyyI 797
Cdd:cd18547 44 LLRILLLLLGLYLLSALfsylqnRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTND---VDN-----I 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 798 RTWVNCTL-DVIGTVLVIVGA----------LPLFILGLIPLVFLYFTI-----QRYYMASSRQIRRLAGashspvisHF 861
Cdd:cd18547 116 SQALSQSLtQLISSILTIVGTlimmlyisplLTLIVLVTVPLSLLVTKFiakrsQKYFRKQQKALGELNG--------YI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 862 CETLLGVSTIRAFGHEQRFIQQNKEvVNENLvcfYNNVISNRWLS------VRleFLGNLMVFFTAV---LTVLAGNsID 932
Cdd:cd18547 188 EEMISGQKVVKAFNREEEAIEEFDE-INEEL---YKASFKAQFYSgllmpiMN--FINNLGYVLVAVvggLLVINGA-LT 260
|
250
....*....|....*....
gi 1387192242 933 SAIVGLSISYALNITQTLN 951
Cdd:cd18547 261 VGVIQAFLQYSRQFSQPIN 279
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
382-594 |
3.19e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 56.29 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 382 AIGFINASFSWdKTGIP----VLKDLNIKIPEGALVAVVGQVGSGKSSVL------------SAILGEME-----KLKGI 440
Cdd:PRK13649 2 GINLQNVSYTY-QAGTPfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMqllnglhvptqgSVRVDDTLitstsKNKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 441 VQRKGSVAYVSQQAWIQncILQENIL----FG----SVMQKQLYERVLEACALLPDLEQLPNGDQTEIgekgvniSGGQK 512
Cdd:PRK13649 81 KQIRKKVGLVFQFPESQ--LFEETVLkdvaFGpqnfGVSQEEAEALAREKLALVGISESLFEKNPFEL-------SGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 513 HRVCLARAVYSGADIYLLDDPLSAVDVHVAKQLFE--KVIGSSGMlrnkTRILVTHNLTLLPQM-DLIVVMESGRVAQMG 589
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTlfKKLHQSGM----TIVLVTHLMDDVANYaDFVYVLEKGKLVLSG 227
|
....*
gi 1387192242 590 TYQEI 594
Cdd:PRK13649 228 KPKDI 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
382-584 |
3.64e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 56.76 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 382 AIGFINASFSW-DKtgiPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGS------------VA 448
Cdd:PRK13536 41 AIDLAGVSKSYgDK---AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVpvpararlararIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 449 YVSQ-QAWIQNCILQENIL-FGSVMQkqLYERVLEAcaLLPDL---EQLPNGDQTEIGEkgvnISGGQKHRVCLARAVYS 523
Cdd:PRK13536 118 VVPQfDNLDLEFTVRENLLvFGRYFG--MSTREIEA--VIPSLlefARLESKADARVSD----LSGGMKRRLTLARALIN 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387192242 524 GADIYLLDDPLSAVDVHVAKQLFEKVigSSGMLRNKTRILVTHNLTLLPQM-DLIVVMESGR 584
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERL--RSLLARGKTILLTTHFMEEAERLcDRLCVLEAGR 249
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1015-1219 |
3.88e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 56.25 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLNIIPQDP--VLFSGTLQMN 1092
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdnQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1093 LD---PLDKYPDHELW----EVLELCHLKEFVQSLPKKllheiseggenLSVGQRQLVCLARALLRKTKILILDEATASI 1165
Cdd:PRK13642 103 VAfgmENQGIPREEMIkrvdEALLAVNMLDFKTREPAR-----------LSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387192242 1166 DFETDNLVQTTVR--KEFSDCTILTIAHRLHSIIDSDRVLVLDSGRITEFETPQNL 1219
Cdd:PRK13642 172 DPTGRQEIMRVIHeiKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
398-595 |
4.07e-08 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 55.89 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 398 PVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIV-------------QRKGSVAYVSQQAWIQ-NCILQE 463
Cdd:COG4559 15 TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVrlngrplaawspwELARRRAVLPQHSSLAfPFTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 464 NILFG----SVMQKQLYERVLEACALLpDLEQLPNGDQTEIgekgvniSGGQKHRVCLARA-------VYSGADIYLLDD 532
Cdd:COG4559 95 VVALGraphGSSAAQDRQIVREALALV-GLAHLAGRSYQTL-------SGGEQQRVQLARVlaqlwepVDGGPRWLFLDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387192242 533 PLSAVDVHVAKQLFEkvigssgMLRNKTR-----ILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEIL 595
Cdd:COG4559 167 PTSALDLAHQHAVLR-------LARQLARrgggvVAVLHDLNLAAQYaDRILLLHQGRLVAQGTPEEVL 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1106-1219 |
4.10e-08 |
|
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: 55.42 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1106 EVLELCHLKEFVQSLPkkllheiseggENLSVGQRQLVCLARALLRKTKILILDEATASIDfetdnlvqTTVRKEFSdct 1185
Cdd:cd03296 119 ELLKLVQLDWLADRYP-----------AQLSGGQRQRVALARALAVEPKVLLLDEPFGALD--------AKVRKELR--- 176
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1186 ilTIAHRLHSIID----------------SDRVLVLDSGRITEFETPQNL 1219
Cdd:cd03296 177 --RWLRRLHDELHvttvfvthdqeealevADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
762-925 |
4.23e-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: 56.03 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 762 VLHLPLQFFETNPIGQVINRFTKDMFIIDMrfhyYIRTWVNCTLDVIgTVLVIVG-------ALPLFILGLIPL-VFLYF 833
Cdd:cd18568 85 LLSLPLSFFASRKVGDIITRFQENQKIRRF----LTRSALTTILDLL-MVFIYLGlmfyynlQLTLIVLAFIPLyVLLTL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 834 TIQRYYMASSRQIRRLAGASHspviSHFCETLLGVSTIRAFGHEQRFIQQNKEVVNENLvcfyNNVISNRWLSVRLEFLG 913
Cdd:cd18568 160 LSSPKLKRNSREIFQANAEQQ----SFLVEALTGIATIKALAAERPIRWRWENKFAKAL----NTRFRGQKLSIVLQLIS 231
|
170
....*....|....
gi 1387192242 914 NLMVFF--TAVLTV 925
Cdd:cd18568 232 SLINHLgtIAVLWY 245
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
396-566 |
5.23e-08 |
|
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: 54.67 E-value: 5.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIV------------QRKGSVAYVSQQAWIQNCI-LQ 462
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVrwngtplaeqrdEPHENILYLGHLPGLKPELsAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 463 ENILFGSVMQKQLYERVLEACAL--LPDLEQLPNGdqteigekgvNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVH 540
Cdd:TIGR01189 92 ENLHFWAAIHGGAQRTIEDALAAvgLTGFEDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180
....*....|....*....|....*....
gi 1387192242 541 -VAK--QLFEKVIGSSGMLrnktrILVTH 566
Cdd:TIGR01189 162 gVALlaGLLRAHLARGGIV-----LLTTH 185
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1135-1210 |
5.61e-08 |
|
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: 53.98 E-value: 5.61e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387192242 1135 LSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVRkEFSD--CTILTIAHRLHSIID-SDRVLVLDSGRI 1210
Cdd:cd03215 105 LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIR-ELADagKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
386-538 |
6.04e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.57 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 386 INASFSWDKTgiPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQ------RKGSVAYVSQQAWI--- 456
Cdd:PRK13540 5 IELDFDYHDQ--PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILferqsiKKDLCTYQKQLCFVghr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 457 ----QNCILQENILFGSVMQKQLYErVLEACAL--LPDLEQLPNGdqteigekgvNISGGQKHRVCLARAVYSGADIYLL 530
Cdd:PRK13540 83 sginPYLTLRENCLYDIHFSPGAVG-ITELCRLfsLEHLIDYPCG----------LLSSGQKRQVALLRLWMSKAKLWLL 151
|
....*...
gi 1387192242 531 DDPLSAVD 538
Cdd:PRK13540 152 DEPLVALD 159
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
397-596 |
6.82e-08 |
|
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: 56.62 E-value: 6.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 397 IPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGeMEKLKGIVQRKG-SVAYVSQQAW------IQncilqenILF-- 467
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGqDLDGLSRRALrplrrrMQ-------VVFqd 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 468 --GS------VMQ---------------KQLYERVLEACA---LLPD-LEQLPNgdqteigEkgvnISGGQKHRVCLARA 520
Cdd:COG4172 371 pfGSlsprmtVGQiiaeglrvhgpglsaAERRARVAEALEevgLDPAaRHRYPH-------E----FSGGQRQRIAIARA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 521 VYSGADIYLLDDPLSAVDVHVAKQLFEkvigssgMLRN--KTR----ILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQE 593
Cdd:COG4172 440 LILEPKLLVLDEPTSALDVSVQAQILD-------LLRDlqREHglayLFISHDLAVVRALaHRVMVMKDGKVVEQGPTEQ 512
|
...
gi 1387192242 594 ILA 596
Cdd:COG4172 513 VFD 515
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
727-892 |
7.17e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 55.60 E-value: 7.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 727 LLGLMQGLFVCSGAYVvtrGSLAASRVLH---AQLLDNVLHLPLQFFETNPIGQVINRFTKDmfiIDMrfhyyIRTW-VN 802
Cdd:cd18564 62 GIALLRGLASYAGTYL---TALVGQRVVLdlrRDLFAHLQRLSLSFHDRRRTGDLLSRLTGD---VGA-----IQDLlVS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 803 CTLDVIGTVLVIVGAL--------PLFILGLIPLVFLYFTIQRYY---MASSRQIRRLAGASHSpVIShfcETLLGVSTI 871
Cdd:cd18564 131 GVLPLLTNLLTLVGMLgvmfwldwQLALIALAVAPLLLLAARRFSrriKEASREQRRREGALAS-VAQ---ESLSAIRVV 206
|
170 180
....*....|....*....|....*
gi 1387192242 872 RAFG----HEQRFIQQNKEVVNENL 892
Cdd:cd18564 207 QAFGreehEERRFARENRKSLRAGL 231
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
386-589 |
7.97e-08 |
|
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: 54.30 E-value: 7.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 386 INASFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGsVAYVSQQAWIQNCIlqeNI 465
Cdd:cd03266 7 LTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG-FDVVKEPAEARRRL---GF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 466 LFGSvmqKQLYERV--------------LEACALLPDLEQLpnGDQTEIGE----KGVNISGGQKHRVCLARAVYSGADI 527
Cdd:cd03266 83 VSDS---TGLYDRLtarenleyfaglygLKGDELTARLEEL--ADRLGMEElldrRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387192242 528 YLLDDPLSAVDVHVAKQLFEKVigssGMLRN--KTRILVTHNLTLLPQM-DLIVVMESGRVAQMG 589
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFI----RQLRAlgKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
727-883 |
7.98e-08 |
|
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: 55.18 E-value: 7.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 727 LLGLMQGLFVCSGAYVVTRGSLAASRVLHAQLLDNVLHLPLQFFETNPIGQVINRFTKDMFIIDMRFHYYIRTWVNCTLD 806
Cdd:cd18543 47 ALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGNLLTL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 807 VIGTVLVIVGALPLFILGLIPLVFLYFTIQRY---YMASSRQIRRLAGAshspVISHFCETLLGVSTIRAFGHEQRFIQQ 883
Cdd:cd18543 127 VVGLVVMLVLSPPLALVALASLPPLVLVARRFrrrYFPASRRAQDQAGD----LATVVEESVTGIRVVKAFGRERRELDR 202
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
396-595 |
8.54e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 54.78 E-value: 8.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKG-------------SVAYVSQQAwiqncilq 462
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHS-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 463 eNILF-----------------GSVMQKQLYERVLEACallpDLEQLPNGDQTEigekgvnISGGQKHRVCLARA----- 520
Cdd:PRK13548 86 -SLSFpftveevvamgraphglSRAEDDALVAAALAQV----DLAHLAGRDYPQ-------LSGGEQQRVQLARVlaqlw 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 521 -VYSGADIYLLDDPLSAVDVH-------VAKQLFEKvigssgmlRNKTRILVTHNLTLLPQM-DLIVVMESGRVAQMGTY 591
Cdd:PRK13548 154 ePDGPPRWLLLDEPTSALDLAhqhhvlrLARQLAHE--------RGLAVIVVLHDLNLAARYaDRIVLLHQGRLVADGTP 225
|
....
gi 1387192242 592 QEIL 595
Cdd:PRK13548 226 AEVL 229
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1017-1210 |
8.58e-08 |
|
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: 56.37 E-value: 8.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1017 DITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIG--LHDLRGKLNIIPQD-------PVLFSG 1087
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFINGKPVDIRnpAQAIRAGIAMVPEDrkrhgivPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1088 TlQMNLDPLDKYPDH-ELWEVLELCHLKEFVQSLPKKLLHEISEGGeNLSVGQRQLVCLARALLRKTKILILDEATASID 1166
Cdd:TIGR02633 358 K-NITLSVLKSFCFKmRIDAAAELQIIGSAIQRLKVKTASPFLPIG-RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1387192242 1167 ----FETDNLVQTTVRKEFSdctILTIAHRLHSIID-SDRVLVLDSGRI 1210
Cdd:TIGR02633 436 vgakYEIYKLINQLAQEGVA---IIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
399-585 |
8.61e-08 |
|
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: 54.21 E-value: 8.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 399 VLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGSvayvSQQAWIQNCI--LQEnilfgsvmQKQLY 476
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK----PLDIAARNRIgyLPE--------ERGLY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 477 --ERVLEACALLPDLEQLPNGD----------QTEIGEKGV----NISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVh 540
Cdd:cd03269 83 pkMKVIDQLVYLAQLKGLKKEEarrridewleRLELSEYANkrveELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP- 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1387192242 541 VAKQLFEKVIgSSGMLRNKTRILVTHNLTLLPQM-DLIVVMESGRV 585
Cdd:cd03269 162 VNVELLKDVI-RELARAGKTVILSTHQMELVEELcDRVLLLNKGRA 206
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1017-1210 |
9.55e-08 |
|
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: 53.84 E-value: 9.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1017 DITFQTHgEEKIGIVGRTGAGKSTLSNCLfriversggkiiidgidistIGLHDL-RGKLNIipQDPVLFSGTLQMNLDP 1095
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCI--------------------AGLEKPdGGTIVL--NGTVLFDSRKKINLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1096 LDK-----------YPDHELWEVLElCHLKEFVQSLPKKLLHEISE----------GGENLSVGQRQLVCLARALLRKTK 1154
Cdd:cd03297 73 QQRkiglvfqqyalFPHLNVRENLA-FGLKRKRNREDRISVDELLDllgldhllnrYPAQLSGGEKQRVALARALAAQPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387192242 1155 ILILDEATASIDFETDNLVQTTVRKEFSDCTILTI--------AHRLHsiidsDRVLVLDSGRI 1210
Cdd:cd03297 152 LLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIfvthdlseAEYLA-----DRIVVMEDGRL 210
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1014-1208 |
9.69e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 56.33 E-value: 9.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGlHDLRGKL--NIIPQD-PVLFSGTLQ 1090
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQLgiGIIYQElSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1091 MNLdPLDKYPDHELW--EVLELCHLKEFVQSLPKKL-LH-EISEGGENLSVGQRQLVCLARALLRKTKILILDEATASI- 1165
Cdd:PRK09700 99 ENL-YIGRHLTKKVCgvNIIDWREMRVRAAMMLLRVgLKvDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLt 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1387192242 1166 DFETDNL--VQTTVRKEFSdcTILTIAHRLHSIID-SDRVLVLDSG 1208
Cdd:PRK09700 178 NKEVDYLflIMNQLRKEGT--AIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1106-1217 |
9.87e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 54.64 E-value: 9.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1106 EVLELCHLKEFVQSLPkklLHeiseggenLSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVRkEFSDCT 1185
Cdd:PRK11124 124 KLLERLRLKPYADRFP---LH--------LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIR-ELAETG 191
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1387192242 1186 I--------LTIAHRLHSiidsdRVLVLDSGRITE------FETPQ 1217
Cdd:PRK11124 192 ItqvivtheVEVARKTAS-----RVVYMENGHIVEqgdascFTQPQ 232
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1013-1219 |
1.00e-07 |
|
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: 53.91 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1013 LALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSggkiiidgIDISTIGLHD-------LRGKLNIIPQDPVL- 1084
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPT--------SGRATVAGHDvvrepreVRRRIGIVFQDLSVd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1085 --FSGTLQMNLDP-LDKYPDHELW----EVLELCHLKEFVQSLPKkllheiseggeNLSVGQRQLVCLARALLRKTKILI 1157
Cdd:cd03265 86 deLTGWENLYIHArLYGVPGAERReridELLDFVGLLEAADRLVK-----------TYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387192242 1158 LDEATASIDFETDNLVQTTVRK--EFSDCTILTIAHRLHSIID-SDRVLVLDSGRITEFETPQNL 1219
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1014-1210 |
1.25e-07 |
|
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: 53.37 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSggKIIIDGIDISTIGLHDLRGKLNIIPQDPVLFSG-TLQMN 1092
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPD--SGEITFDGKSYQKNIEALRRIGALIEAPGFYPNlTAREN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1093 LDPLDKY---PDHELWEVLELCHLKEfvqsLPKKLLheiseggENLSVGQRQLVCLARALLRKTKILILDEATASID-FE 1168
Cdd:cd03268 93 LRLLARLlgiRKKRIDEVLDVVGLKD----SAKKKV-------KGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDpDG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1387192242 1169 TDNLVQTTVRKEFSDCTILTIAHRLHSI-IDSDRVLVLDSGRI 1210
Cdd:cd03268 162 IKELRELILSLRDQGITVLISSHLLSEIqKVADRIGIINKGKL 204
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
762-926 |
1.47e-07 |
|
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: 54.37 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 762 VLHLPLQFFETNPIGQVINRFTKDMFIIDMrfhyYIRTWVNCTLDVIgTVLVIVGAL-----PLFILGLIPlVFLYFTIQ 836
Cdd:cd18570 85 LLKLPLSFFETRKTGEIISRFNDANKIREA----ISSTTISLFLDLL-MVIISGIILffynwKLFLITLLI-IPLYILII 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 837 RYYMASSRQIRRLAGASHSPVISHFCETLLGVSTIRAFGHEQRFIQQNKEVvnenlvcfYNNVISNRWLSVRLE-FLGNL 915
Cdd:cd18570 159 LLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKK--------FSKLLKKSFKLGKLSnLQSSI 230
|
170
....*....|.
gi 1387192242 916 MVFFTAVLTVL 926
Cdd:cd18570 231 KGLISLIGSLL 241
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1014-1216 |
1.58e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 54.28 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIII--DGIDISTIGLHDLRGKLNIIPQDP--VLFSGTL 1089
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdgVDITDKKVKLSDIRKKVGLVFQYPeyQLFEETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1090 Q-------MNLDPLDKYPDHELWEVLELCHLKefVQSLPKKLLHEiseggenLSVGQRQLVCLARALLRKTKILILDEAT 1162
Cdd:PRK13637 102 EkdiafgpINLGLSEEEIENRVKRAMNIVGLD--YEDYKDKSPFE-------LSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387192242 1163 ASID----FETDNLVQtTVRKEFSDCTILTIahrlHSIID----SDRVLVLDSGRITEFETP 1216
Cdd:PRK13637 173 AGLDpkgrDEILNKIK-ELHKEYNMTIILVS----HSMEDvaklADRIIVMNKGKCELQGTP 229
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
998-1210 |
1.96e-07 |
|
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: 53.05 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 998 VEFVDYRARYRDDLglALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDL------ 1071
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIgylpee 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1072 RG---KLNIIPQdpVLFSGTLQmNLDPLDKYPDHELW-EVLELCHLKEfvqslpKKLlheiseggENLSVGQRQLVCLAR 1147
Cdd:cd03269 79 RGlypKMKVIDQ--LVYLAQLK-GLKKEEARRRIDEWlERLELSEYAN------KRV--------EELSKGNQQKVQFIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387192242 1148 ALLRKTKILILDEATASIDFETDNLVQTTVRkEFSD--CTILTIAHRLHSIID-SDRVLVLDSGRI 1210
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPVNVELLKDVIR-ELARagKTVILSTHQMELVEElCDRVLLLNKGRA 206
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1017-1211 |
2.27e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.94 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1017 DITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIG--LHDLRGKLNIIPQD-------PVLFSG 1087
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWEGEIFIDGKPVKIRnpQQAIAQGIAMVPEDrkrdgivPVMGVG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1088 TlQMNLDPLDKYPDHE-LWEVLELCHLKEFVQSLPKKLLH-EISEGgeNLSVGQRQLVCLARALLRKTKILILDEATASI 1165
Cdd:PRK13549 360 K-NITLAALDRFTGGSrIDDAAELKTILESIQRLKVKTASpELAIA--RLSGGNQQKAVLAKCLLLNPKILILDEPTRGI 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1387192242 1166 D----FETDNLVQTTVRKEFSdctILTIAHRLHSIID-SDRVLVLDSGRIT 1211
Cdd:PRK13549 437 DvgakYEIYKLINQLVQQGVA---IIVISSELPEVLGlSDRVLVMHEGKLK 484
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1015-1166 |
2.45e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 53.36 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHD--LRGkLNIIPQDPVLFS------ 1086
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHAraRRG-IGYLPQEASIFRrlsvyd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1087 ---GTLQMNLDPLDKYPDHELWEVLELCHLKEFVQSLpkkllheisegGENLSVGQRQLVCLARALLRKTKILILDEATA 1163
Cdd:PRK10895 98 nlmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
...
gi 1387192242 1164 SID 1166
Cdd:PRK10895 167 GVD 169
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
997-1219 |
2.47e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 53.65 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 997 IVEFVDYRARYRDDLGlALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLN 1076
Cdd:PRK13652 3 LIETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1077 IIPQDP--VLFSGTLQ-------MNLDPLDKYPDHELWEVLELCHLKEFVQSLPkkllheiseggENLSVGQRQLVCLAR 1147
Cdd:PRK13652 82 LVFQNPddQIFSPTVEqdiafgpINLGLDEETVAHRVSSALHMLGLEELRDRVP-----------HHLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387192242 1148 ALLRKTKILILDEATASIDFE-TDNLVQTTVR-KEFSDCTILTIAHRLHSIID-SDRVLVLDSGRITEFETPQNL 1219
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQgVKELIDFLNDlPETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
727-928 |
2.56e-07 |
|
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: 53.72 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 727 LLGLMQGLFVCSGAYVVTRG---SLAASRV---LHAQLLDNVLHLPLQFFETNPIGQVINRFTKDMFIIDMRFHYYIRTW 800
Cdd:cd18557 38 LALILLAIYLLQSVFTFVRYylfNIAGERIvarLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 801 VNCTLDVIGTV---LVIVGALPLFILGLIPLVFLYFTIQ-RYYMASSRQIR-RLAGASHspVIShfcETLLGVSTIRAFG 875
Cdd:cd18557 118 LRNILQVIGGLiilFILSWKLTLVLLLVIPLLLIASKIYgRYIRKLSKEVQdALAKAGQ--VAE---ESLSNIRTVRSFS 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1387192242 876 HEQRFIQQNKEVVNEnlvCFYNNVISNRWLSVrLEFLGNLMVFFTAVLTVLAG 928
Cdd:cd18557 193 AEEKEIRRYSEALDR---SYRLARKKALANAL-FQGITSLLIYLSLLLVLWYG 241
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
395-571 |
2.59e-07 |
|
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: 51.77 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 395 TGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQR--KGSVAYVSQQAWIQNCILQENILFgsvmq 472
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpeGEDLLFLPQRPYLPLGTLREQLIY----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 473 kqLYERVLeacallpdleqlpngdqteigekgvniSGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQLFEkvigs 552
Cdd:cd03223 87 --PWDDVL---------------------------SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQ----- 132
|
170 180
....*....|....*....|.
gi 1387192242 553 sgMLRNK--TRILVTHNLTLL 571
Cdd:cd03223 133 --LLKELgiTVISVGHRPSLW 151
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
400-593 |
2.66e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 55.05 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 400 LKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEK-LKGIVQRK--GSVAYVSQQAWIQNCILQENILFGSV------ 470
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgVKGSGSVLlnGMPIDAKEMRAISAYVQQDDLFIPTLtvrehl 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 471 -------MQKQLY--ERVLEACALLPDLeQLPNGDQTEIGEKGV--NISGGQKHRVCLARAVYSGADIYLLDDPLSAVDV 539
Cdd:TIGR00955 121 mfqahlrMPRRVTkkEKRERVDEVLQAL-GLRKCANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 540 HVAKQLFE--KVIGSSGmlrnKTRILVTHNLT--LLPQMDLIVVMESGRVAQMGTYQE 593
Cdd:TIGR00955 200 FMAYSVVQvlKGLAQKG----KTIICTIHQPSseLFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1014-1219 |
2.85e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 53.24 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLH-------DLRGKLNIIPQDPVLFS 1086
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYsprtdtvDLRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1087 GTLQMNL-------DPLDKypdHELWEVLELCHLKEFVQSLPKKLLHEISEGgenLSVGQRQLVCLARALLRKTKILILD 1159
Cdd:PRK14239 100 MSIYENVvyglrlkGIKDK---QVLDEAVEKSLKGASIWDEVKDRLHDSALG---LSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387192242 1160 EATASIDFETDNLVQTTVRKEFSDCTILTIAHRLH--SIIdSDRVLVLDSGRITEFETPQNL 1219
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQqaSRI-SDRTGFFLDGDLIEYNDTKQM 234
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
399-590 |
2.98e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 53.09 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 399 VLKDLNIKIPEGALVAVVGQVGSGKSSVLSAI-LGEMEK------------------LKGIVQRKGSVAYVSQQ--AW-- 455
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMPRsgtlniagnhfdfsktpsDKAIRELRRNVGMVFQQynLWph 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 456 ---IQNCILQENILFGsvMQKQlyERVLEACALLPDLEQLPNGDQTEIgekgvNISGGQKHRVCLARAVYSGADIYLLDD 532
Cdd:PRK11124 97 ltvQQNLIEAPCRVLG--LSKD--QALARAEKLLERLRLKPYADRFPL-----HLSGGQQQRVAIARALMMEPQVLLFDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387192242 533 PLSAVD-------VHVAKQLFEKVIgssgmlrnkTRILVTHNLTLLPQMDLIVV-MESGRVAQMGT 590
Cdd:PRK11124 168 PTAALDpeitaqiVSIIRELAETGI---------TQVIVTHEVEVARKTASRVVyMENGHIVEQGD 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
962-1220 |
3.42e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 53.68 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 962 ANAVSIERVCEYETMDKEAPWIT-SKRPPSQWPSKGIVEFVDYRARYRDDLglALQDITFQTHGEEKIGIVGRTGAGKST 1040
Cdd:PRK13536 5 AVAEEAPRRLELSPIERKHQGISeAKASIPGSMSTVAIDLAGVSKSYGDKA--VVNGLSFTVASGECFGLLGPNGAGKST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1041 LSNCLFRIVERSGgkiiidgidiSTIGLHDL---------RGKLNIIPQ-DPVLFSGTLQMNLDPLDKY---PDHELWEV 1107
Cdd:PRK13536 83 IARMILGMTSPDA----------GKITVLGVpvpararlaRARIGVVPQfDNLDLEFTVRENLLVFGRYfgmSTREIEAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1108 LElcHLKEFVQsLPKKLLHEISEggenLSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVRKEFSDC-TI 1186
Cdd:PRK13536 153 IP--SLLEFAR-LESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGkTI 225
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1387192242 1187 LTIAH------RLhsiidSDRVLVLDSGRITEFETPQNLI 1220
Cdd:PRK13536 226 LLTTHfmeeaeRL-----CDRLCVLEAGRKIAEGRPHALI 260
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1015-1210 |
3.61e-07 |
|
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: 51.78 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCL------------FRIVERSggkiiidgidistIGLHDLRGKLNIIPQDP 1082
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALagrrtglgvsgeVLINGRP-------------LDKRSFRKIIGYVPQDD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1083 VLfsgtlqmnldpldkYPDHELWEVLEL-CHLKefvqslpkkllheiseggeNLSVGQRQLVCLARALLRKTKILILDEA 1161
Cdd:cd03213 92 IL--------------HPTLTVRETLMFaAKLR-------------------GLSGGERKRVSIALELVSNPSLLFLDEP 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1387192242 1162 TASIDFETDNLVQTTVRKEFSD-CTILTIAHRLHSIIDS--DRVLVLDSGRI 1210
Cdd:cd03213 139 TSGLDSSSALQVMSLLRRLADTgRTIICSIHQPSSEIFElfDKLLLLSQGRV 190
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1123-1222 |
3.72e-07 |
|
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: 54.42 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1123 KLLHEISEGGENLSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVRK--EFSDCTILTIAHRLHSIID-S 1199
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIEDlS 236
|
90 100
....*....|....*....|...
gi 1387192242 1200 DRVLVLDSGRITEFETPQNLIHK 1222
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEVVAV 259
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
724-925 |
3.98e-07 |
|
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: 53.26 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 724 IYGLLGLMQGLFVCSGAYVVTRgslAASRVLHA---QLLDNVLHLPLQFFETNPIGQVINRFTKDmfiID--MRFhyyIR 798
Cdd:cd18546 44 AYLAVVLAGWVAQRAQTRLTGR---TGERLLYDlrlRVFAHLQRLSLDFHERETSGRIMTRMTSD---IDalSEL---LQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 799 TWVNCTLDVIGTVLVIVGAL-----PLFI---LGLIPLVFLYFTIQRYYMASSRQIRRLAGAshspVISHFCETLLGVST 870
Cdd:cd18546 115 TGLVQLVVSLLTLVGIAVVLlvldpRLALvalAALPPLALATRWFRRRSSRAYRRARERIAA----VNADLQETLAGIRV 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 871 IRAFGHEQRFIQQNKEVVNENLVCfynNVISNRWLSVR---LEFLGNLMVffTAVLTV 925
Cdd:cd18546 191 VQAFRRERRNAERFAELSDDYRDA---RLRAQRLVAIYfpgVELLGNLAT--AAVLLV 243
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1134-1210 |
4.25e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 52.78 E-value: 4.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1134 NLSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLV-QTTVR--KEFSdCTILTIAHRLHSIID-SDRVLVLDSGR 1209
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVlELTEKivEENN-LTTLMVTHNMEQALDyGNRLIMMHEGR 226
|
.
gi 1387192242 1210 I 1210
Cdd:COG1101 227 I 227
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
402-566 |
4.40e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 51.73 E-value: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 402 DLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQ------RKGSVAYVSQQAWI--QNCI---L--QENILFG 468
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwqgepiRRQRDEYHQDLLYLghQPGIkteLtaLENLRFY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 469 SVMQKQLYERVLEAcAL----LPDLEQLPNGdqteigekgvNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVH-VA- 542
Cdd:PRK13538 99 QRLHGPGDDEALWE-ALaqvgLAGFEDVPVR----------QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQgVAr 167
|
170 180
....*....|....*....|....*
gi 1387192242 543 -KQLFEKVIGSSGMLrnktrILVTH 566
Cdd:PRK13538 168 lEALLAQHAEQGGMV-----ILTTH 187
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
396-596 |
4.59e-07 |
|
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: 52.73 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEME------KLKG----------IVqRKG-------------- 445
Cdd:COG0411 16 GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRptsgriLFDGrditglpphrIA-RLGiartfqnprlfpel 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 446 SVA---YVSQQAWIQNCILQENILFGSVMQ--KQLYERVLEACALLpDLEQLPNgdqteigEKGVNISGGQKHRVCLARA 520
Cdd:COG0411 95 TVLenvLVAAHARLGRGLLAALLRLPRARReeREARERAEELLERV-GLADRAD-------EPAGNLSYGQQRRLEIARA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 521 VYSGADIYLLDDP---LSAVDVHVAKQLFEKVIGSSGMlrnkTRILVTHNLTLLpqMDL---IVVMESGRVAQMGTYQEI 594
Cdd:COG0411 167 LATEPKLLLLDEPaagLNPEETEELAELIRRLRDERGI----TILLIEHDMDLV--MGLadrIVVLDFGRVIAEGTPAEV 240
|
..
gi 1387192242 595 LA 596
Cdd:COG0411 241 RA 242
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
399-585 |
4.72e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 52.77 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 399 VLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILG--------------EMEKLKGIVQR--KGSVAYVSQQA-------- 454
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGlespsqgnvswrgePLAKLNRAQRKafRRDIQMVFQDSisavnprk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 455 ---WIQNCILQENILFGSVMQKQLYERVLEACALLP-DLEQLPNgdqteigekgvNISGGQKHRVCLARAVYSGADIYLL 530
Cdd:PRK10419 107 tvrEIIREPLRHLLSLDKAERLARASEMLRAVDLDDsVLDKRPP-----------QLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1387192242 531 DDPLSAVDVHV---AKQLFEKVIGSSGMlrnkTRILVTHNLTLLPQM-DLIVVMESGRV 585
Cdd:PRK10419 176 DEAVSNLDLVLqagVIRLLKKLQQQFGT----ACLFITHDLRLVERFcQRVMVMDNGQI 230
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
120-342 |
5.12e-07 |
|
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: 52.79 E-value: 5.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 120 VALFKVLADVLSFTSPLIMKQMIlfceqrpDFGWSG------YGYALALFVVVFLQTL--ILQQYqrfkmlTSAKIKTAV 191
Cdd:cd18548 4 APLFKLLEVLLELLLPTLMADII-------DEGIANgdlsyiLRTGLLMLLLALLGLIagILAGY------FAAKASQGF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 192 IGLI----YKKALLLSNVSRKQFSTGEIINLMATDTQQLMD-LMTNINLLWSAPFQ----ILMAVSLLWQeLGPAVLAGV 262
Cdd:cd18548 71 GRDLrkdlFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNfVMMLLRMLVRAPIMligaIIMAFRINPK-LALILLVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 263 AVLVFVIpmnALVANRMKKLKKNQRKNKDKQIKLLNEILHGIKILKLYAWEPSYKKKIIEIREQELEVQKSAGYLAVFSM 342
Cdd:cd18548 150 PILALVV---FLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLN 226
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1014-1166 |
6.52e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 53.30 E-value: 6.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHdlRGKLNIIPQDPVLFSG-TLQMN 1092
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY--QRPINMMFQSYALFPHmTVEQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1093 LD---PLDKYPDHEL----WEVLELCHLKEFVQSLPkkllHEiseggenLSVGQRQLVCLARALLRKTKILILDEATASI 1165
Cdd:PRK11607 112 IAfglKQDKLPKAEIasrvNEMLGLVHMQEFAKRKP----HQ-------LSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
|
.
gi 1387192242 1166 D 1166
Cdd:PRK11607 181 D 181
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
400-594 |
6.99e-07 |
|
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: 51.60 E-value: 6.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 400 LKDLNIKIPEGALVAVVGQVGSGKSSVLSaILGEMEKLKG---------IVQRKGSV----AYVSQQAWIQNCIL-QENI 465
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIK-MLTTLLKPTSgratvaghdVVREPREVrrriGIVFQDLSVDDELTgWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 466 LfgsvMQKQLY--------ERVLEACALLpdleqlpngDQTEIGEKGV-NISGGQKHRVCLARAVYSGADIYLLDDPLSA 536
Cdd:cd03265 95 Y----IHARLYgvpgaerrERIDELLDFV---------GLLEAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387192242 537 VDVHVAKQLFEKVigsSGMLR--NKTRILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEI 594
Cdd:cd03265 162 LDPQTRAHVWEYI---EKLKEefGMTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
398-596 |
7.42e-07 |
|
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: 51.77 E-value: 7.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 398 PVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIV---------------QRKGsVAYVSQQAWI-QNCIL 461
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqditklpmhkrARLG-IGYLPQEASIfRKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 462 QENILFGSVMQKQLY-ERVLEACALLPDLEQLPNGDQteigeKGVNISGGQKHRVCLARAVYSGADIYLLDDPLSAVD-- 538
Cdd:cd03218 93 EENILAVLEIRGLSKkEREEKLEELLEEFHITHLRKS-----KASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDpi 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387192242 539 -VH----VAKQLFEKVIGssgmlrnktrILVT-HNL-TLLPQMDLIVVMESGRVAQMGTYQEILA 596
Cdd:cd03218 168 aVQdiqkIIKILKDRGIG----------VLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1106-1222 |
7.47e-07 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 52.77 E-value: 7.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1106 EVLELCHLKEFVQSLPKkllheiseggeNLSVGQRQLVCLARALLRKTKILILDEATASIDFEtdnL-VQTtvRKEFSD- 1183
Cdd:COG3839 116 EAAELLGLEDLLDRKPK-----------QLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAK---LrVEM--RAEIKRl 179
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1387192242 1184 ------CTI---------LTIAhrlhsiidsDRVLVLDSGRITEFETPQNLIHK 1222
Cdd:COG3839 180 hrrlgtTTIyvthdqveaMTLA---------DRIAVMNDGRIQQVGTPEELYDR 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1106-1219 |
7.63e-07 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 52.79 E-value: 7.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1106 EVLELCHLKEFVQSLPkkllHEiseggenLSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVR---KEFs 1182
Cdd:COG3842 118 ELLELVGLEGLADRYP----HQ-------LSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRrlqREL- 185
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1387192242 1183 DCTILTIAHrlhsiiD-------SDRVLVLDSGRITEFETPQNL 1219
Cdd:COG3842 186 GITFIYVTH------DqeealalADRIAVMNDGRIEQVGTPEEI 223
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
400-630 |
8.46e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.74 E-value: 8.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 400 LKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGSVAYVSQQAWIQ-NCILQENILFGsvMQKQLYER 478
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSgQLTGIENIEFK--MLCMGFKR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 479 VlEACALLPDLEQLpngdqTEIGE---KGV-NISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQLFEKVIGSSG 554
Cdd:PRK13546 118 K-EIKAMTPKIIEF-----SELGEfiyQPVkKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKE 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387192242 555 mlRNKTRILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEILAKTKNLTNLLQAFSEQETAHALKQVSviNSRTVLK 630
Cdd:PRK13546 192 --QNKTIFFVSHNLGQVRQFcTKIAWIEGGKLKDYGELDDVLPKYEAFLNDFKKKSKAEQKEFRNKLD--ESRFVIK 264
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
396-612 |
9.00e-07 |
|
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: 53.27 E-value: 9.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKSsVLSAILGEMEKLKGI-------VQRKGSVAYVSQQAWI-QNCILQENIL- 466
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKS-VLMHVLRGMDQYEPTsgriiyhVALCEKCGYVERPSKVgEPCPVCGGTLe 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 467 -------------FGSVMQK---------QLYE--RVLEAcaLLPDLEQLPNG------------DQTEIGEKGVNI--- 507
Cdd:TIGR03269 91 peevdfwnlsdklRRRIRKRiaimlqrtfALYGddTVLDN--VLEALEEIGYEgkeavgravdliEMVQLSHRITHIard 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 508 -SGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAK---QLFEKVIGSSGMlrnkTRILVTHNLTLLPQM-DLIVVMES 582
Cdd:TIGR03269 169 lSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKlvhNALEEAVKASGI----SMVLTSHWPEVIEDLsDKAIWLEN 244
|
250 260 270
....*....|....*....|....*....|
gi 1387192242 583 GRVAQMGTYQEILAKTKNLTNLLQAFSEQE 612
Cdd:TIGR03269 245 GEIKEEGTPDEVVAVFMEGVSEVEKECEVE 274
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1015-1209 |
9.56e-07 |
|
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: 49.37 E-value: 9.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTLsnclfriversggkiiidgidistiglhdlrgkLNIIPQDPVLFSGTLQMNld 1094
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTL---------------------------------LKLIAGELEPDEGIVTWG-- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1095 pldkypdhelwEVLELCHLkefvqslpkkllheiseggENLSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQ 1174
Cdd:cd03221 61 -----------STVKIGYF-------------------EQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALE 110
|
170 180 190
....*....|....*....|....*....|....*..
gi 1387192242 1175 TTVrKEFsDCTILTIAHRlHSIIDS--DRVLVLDSGR 1209
Cdd:cd03221 111 EAL-KEY-PGTVILVSHD-RYFLDQvaTKIIELEDGK 144
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1014-1221 |
1.02e-06 |
|
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: 51.14 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSggkiiidgidISTIGL--HDLRG-------KLNI--IPQDP 1082
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPR----------SGSIRFdgEDITGlpphriaRLGIgyVPEGR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1083 VLFSG-TLQMNLD------PLDKYPDHELWEVLELC-HLKEFVQSLpkkllheiseGGeNLSVGQRQLVCLARALLRKTK 1154
Cdd:COG0410 88 RIFPSlTVEENLLlgayarRDRAEVRADLERVYELFpRLKERRRQR----------AG-TLSGGEQQMLAIGRALMSRPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387192242 1155 ILILDEATA----SIdfeTDNLVQT--TVRKEfsDCTILTIAHRLHSIID-SDRVLVLDSGRITEFETPQNLIH 1221
Cdd:COG0410 157 LLLLDEPSLglapLI---VEEIFEIirRLNRE--GVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLA 225
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1128-1212 |
1.03e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 51.64 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1128 ISEGGENLSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVRKEFSDCTILTIAHRL-HSIIDSDRVLVLD 1206
Cdd:PRK14271 157 LSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLaQAARISDRAALFF 236
|
....*.
gi 1387192242 1207 SGRITE 1212
Cdd:PRK14271 237 DGRLVE 242
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
727-928 |
1.22e-06 |
|
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: 51.66 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 727 LLGLMQGLFVCSGAYVVTRGSLAASRVLHAQLLDNVLHLPLQFFETNPIGQVINRFTKDMFIIDMRFHYYIRTWVNCTLD 806
Cdd:cd18542 47 GVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 807 VIGTVLVIVG---ALPLFILGLIPLVFLYFT-----IQRYYMASSRQIRRLagashSPVIShfcETLLGVSTIRAFGHE- 877
Cdd:cd18542 127 FIGALIIMFSinwKLTLISLAIIPFIALFSYvffkkVRPAFEEIREQEGEL-----NTVLQ---ENLTGVRVVKAFAREd 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1387192242 878 ---QRFIQQNKEVVNENLVcfyNNVISNRWLSVrLEFLGNLMVfftaVLTVLAG 928
Cdd:cd18542 199 yeiEKFDKENEEYRDLNIK---LAKLLAKYWPL-MDFLSGLQI----VLVLWVG 244
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1106-1219 |
1.34e-06 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 52.07 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1106 EVLELCHLKEFVQSLPKkllheiseggeNLSVGQRQLVCLARALLRKTKILILDEATASIDfetdnlvqTTVRKE----- 1180
Cdd:COG1118 116 ELLELVQLEGLADRYPS-----------QLSGGQRQRVALARALAVEPEVLLLDEPFGALD--------AKVRKElrrwl 176
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1181 -----FSDCTILTIAH------RLhsiidSDRVLVLDSGRITEFETPQNL 1219
Cdd:COG1118 177 rrlhdELGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDEV 221
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1134-1240 |
1.35e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 51.00 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1134 NLSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVRKEFSDCTILTIAHR-LHSIIDSDRVLVLDSGRITE 1212
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIE 228
|
90 100 110
....*....|....*....|....*....|....*
gi 1387192242 1213 -------FETPQNlihkrglffdMLTEAGITQDLG 1240
Cdd:PRK14267 229 vgptrkvFENPEH----------ELTEKYVTGALG 253
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1011-1221 |
1.41e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 52.34 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1011 LGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLR-----------GKLNIIP 1079
Cdd:PRK10070 40 LSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrkkiamvfQSFALMP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1080 QDPVLFSGTLQMNLDPLDKYPDHE-LWEVLELCHLKEFVQSLPkkllheiseggENLSVGQRQLVCLARALLRKTKILIL 1158
Cdd:PRK10070 120 HMTVLDNTAFGMELAGINAEERREkALDALRQVGLENYAHSYP-----------DELSGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1159 DEATASIdfetDNLVQTTVRKEFSDC------TILTIAHRLHSIID-SDRVLVLDSGRITEFETPQNLIH 1221
Cdd:PRK10070 189 DEAFSAL----DPLIRTEMQDELVKLqakhqrTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
401-599 |
1.43e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 51.63 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 401 KDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKG-SVAYVSQQAW------IQnCILQE---------- 463
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkDLLGMKDDEWravrsdIQ-MIFQDplaslnprmt 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 464 --NIL------FGSVMQKQ-LYERVLEACA---LLPDLeqlpngdqteIGEKGVNISGGQKHRVCLARAVYSGADIYLLD 531
Cdd:PRK15079 117 igEIIaeplrtYHPKLSRQeVKDRVKAMMLkvgLLPNL----------INRYPHEFSGGQCQRIGIARALILEPKLIICD 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387192242 532 DPLSAVDVHVAKQ---LFEKVIGSSGMlrnkTRILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEILAKTK 599
Cdd:PRK15079 187 EPVSALDVSIQAQvvnLLQQLQREMGL----SLIFIAHDLAVVKHIsDRVLVMYLGHAVELGTYDEVYHNPL 254
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
997-1210 |
1.47e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 51.27 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 997 IVEFVDYRARYRDDLGlALQDITFQTHGEEKIGIVGRTGAGKSTL---SNCLFrIVERSGGKIIIDGIDISTIglHDLRG 1073
Cdd:PRK13647 4 IIEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLllhLNGIY-LPQRGRVKVMGREVNAENE--KWVRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1074 KLNIIPQDP--VLFSGT---------LQMNLDPldKYPDHELWEVLELCHLKEFVQSLPkkllheiseggENLSVGQRQL 1142
Cdd:PRK13647 80 KVGLVFQDPddQVFSSTvwddvafgpVNMGLDK--DEVERRVEEALKAVRMWDFRDKPP-----------YHLSYGQKKR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1143 VCLARALLRKTKILILDEATASIDFE-TDNLVQTTVRKEFSDCTILTIAHRLHSIID-SDRVLVLDSGRI 1210
Cdd:PRK13647 147 VAIAGVLAMDPDVIVLDEPMAYLDPRgQETLMEILDRLHNQGKTVIVATHDVDLAAEwADQVIVLKEGRV 216
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1013-1210 |
1.50e-06 |
|
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: 50.73 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1013 LALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLNIIPQDPVLFSG----- 1087
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPRKPDQFQKCVAYVRQDDILLPGltvre 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1088 ----TLQMNL-DPLDKYPDHELWEVLELCHLKEfvqslpKKLLHEISEGgenLSVGQRQLVCLARALLRKTKILILDEAT 1162
Cdd:cd03234 101 tltyTAILRLpRKSSDAIRKKRVEDVLLRDLAL------TRIGGNLVKG---ISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1387192242 1163 ASID-FETDNLVQTTVRKEFSDCTILTIAHRLHSIIDS--DRVLVLDSGRI 1210
Cdd:cd03234 172 SGLDsFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRlfDRILLLSSGEI 222
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1106-1219 |
1.83e-06 |
|
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: 50.31 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1106 EVLELCHLKEFVQSLPKKLlheiseggenlSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVrKEFSDCT 1185
Cdd:cd03300 113 EALDLVQLEGYANRKPSQL-----------SGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLEL-KRLQKEL 180
|
90 100 110
....*....|....*....|....*....|....*...
gi 1387192242 1186 ILTIAHRLH----SIIDSDRVLVLDSGRITEFETPQNL 1219
Cdd:cd03300 181 GITFVFVTHdqeeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
396-581 |
2.04e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 52.12 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGemekL----KGIVQR--KGSVAYVSQQAWIQNCILQENILF-- 467
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG----LwpygSGRIARpaGARVLFLPQRPYLPLGTLREALLYpa 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 468 --GSVMQKQLyERVLEAC---ALLPDLEQLPNGDQTeigekgvnISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVA 542
Cdd:COG4178 451 taEAFSDAEL-REALEAVglgHLAERLDEEADWDQV--------LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENE 521
|
170 180 190
....*....|....*....|....*....|....*....
gi 1387192242 543 KQLFEKVIgssGMLRNKTRILVTHNLTLLPQMDLIVVME 581
Cdd:COG4178 522 AALYQLLR---EELPGTTVISVGHRSTLAAFHDRVLELT 557
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1012-1234 |
2.06e-06 |
|
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: 51.25 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1012 GLALqDITFQTHGEEKIGIVGRTGAGKSTLSNCLF--------RIVersggkiiidgidistIG---LHDLRGKLNIIP- 1079
Cdd:COG4148 13 GFTL-DVDFTLPGRGVTALFGPSGSGKTTLLRAIAglerpdsgRIR----------------LGgevLQDSARGIFLPPh 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1080 --------QDPVLFS-----GTLQMNLDPLDKYPDHELW-EVLELCHLKEFVQSLPkkllheiseggENLSVGQRQLVCL 1145
Cdd:COG4148 76 rrrigyvfQEARLFPhlsvrGNLLYGRKRAPRAERRISFdEVVELLGIGHLLDRRP-----------ATLSGGERQRVAI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1146 ARALLRKTKILILDEATASIDFETDN-----LVQttVRKEFsDCTILTIAH------RLhsiidSDRVLVLDSGRITEFE 1214
Cdd:COG4148 145 GRALLSSPRLLLMDEPLAALDLARKAeilpyLER--LRDEL-DIPILYVSHsldevaRL-----ADHVVLLEQGRVVASG 216
|
250 260
....*....|....*....|.
gi 1387192242 1215 TPQNLIHKRGLF-FDMLTEAG 1234
Cdd:COG4148 217 PLAEVLSRPDLLpLAGGEEAG 237
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1030-1212 |
2.57e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 50.30 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1030 IVGRTGAGKSTLSNCLFRIVErsggkiiiDGIDISTIGLHDLRGKlNIIPQDPVLFSGTLQMNLDPLDKYPDHELWEVLE 1109
Cdd:PRK14247 34 LMGPSGSGKSTLLRVFNRLIE--------LYPEARVSGEVYLDGQ-DIFKMDVIELRRRVQMVFQIPNPIPNLSIFENVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1110 L-CHLKEFVQSlPKKLLHEISEGGE-----------------NLSVGQRQLVCLARALLRKTKILILDEATASIDFETDN 1171
Cdd:PRK14247 105 LgLKLNRLVKS-KKELQERVRWALEkaqlwdevkdrldapagKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1387192242 1172 LVQTTVRKEFSDCTILTIAH------RLhsiidSDRVLVLDSGRITE 1212
Cdd:PRK14247 184 KIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVE 225
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1135-1208 |
2.59e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.54 E-value: 2.59e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 1135 LSVGQRQLVCLARALLRKTKILILDEAT-ASIDFETDNLVQttVRKEFSD--CTILTIAHRLHSIID-SDRVLVLDSG 1208
Cdd:PRK10762 142 LSIGEQQMVEIAKVLSFESKVIIMDEPTdALTDTETESLFR--VIRELKSqgRGIVYISHRLKEIFEiCDDVTVFRDG 217
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
398-599 |
2.97e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 50.39 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 398 PVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIV---------QRKGSVAYVSQQAWI-----QNCI--- 460
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgkpldySKRGLLALRQQVATVfqdpeQQIFytd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 461 LQENILFG----SVMQKQLYERVLEACALLpdleqlpngDQTEIGEKGVN-ISGGQKHRVCLARAVYSGADIYLLDDPLS 535
Cdd:PRK13638 95 IDSDIAFSlrnlGVPEAEITRRVDEALTLV---------DAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387192242 536 AVDVHVAKQLFE--KVIGSSGmlrnKTRILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEILAKTK 599
Cdd:PRK13638 166 GLDPAGRTQMIAiiRRIVAQG----NHVIISSHDIDLIYEIsDAVYVLRQGQILTHGAPGEVFACTE 228
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
386-608 |
3.00e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 50.95 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 386 INASFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILG--------------EMEKL--KGIVQRKGSVAY 449
Cdd:PRK11153 7 ISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLlerptsgrvlvdgqDLTALseKELRKARRQIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 450 VSQQawiqncilqenilFGSVMQKQLYERVLeacalLPdLEqLPNGDQTEIGEK--------GV---------NISGGQK 512
Cdd:PRK11153 87 IFQH-------------FNLLSSRTVFDNVA-----LP-LE-LAGTPKAEIKARvtellelvGLsdkadrypaQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 513 HRVCLARAVYSGADIYLLDDPLSAVDVHVAKQLFEkvigssgMLR--NK----TRILVTHnltllpQMDLI-------VV 579
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPATTRSILE-------LLKdiNRelglTIVLITH------EMDVVkricdrvAV 213
|
250 260
....*....|....*....|....*....
gi 1387192242 580 MESGRVAQMGTYQEILAKTKnlTNLLQAF 608
Cdd:PRK11153 214 IDAGRLVEQGTVSEVFSHPK--HPLTREF 240
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1106-1219 |
3.81e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 50.72 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1106 EVLELCHLKEFVQSLPKkllheiseggeNLSVGQRQLVCLARALLRKTKILILDEATASIDFEtdnlvqttVRKEFSD-- 1183
Cdd:PRK09452 127 EALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYK--------LRKQMQNel 187
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1387192242 1184 --------CTILTIAH-RLHSIIDSDRVLVLDSGRITE-------FETPQNL 1219
Cdd:PRK09452 188 kalqrklgITFVFVTHdQEEALTMSDRIVVMRDGRIEQdgtpreiYEEPKNL 239
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
994-1220 |
4.27e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 50.19 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 994 SKGIVEFVDYRARYRDDLglALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVersggkiiidGIDISTIGL----- 1068
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLT----------HPDAGSISLcgepv 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1069 ----HDLRGKLNIIPQ----DPVLfsgTLQMNLDPLDKYPDHELWEVLELC-HLKEFVQsLPKKLLHEISEggenLSVGQ 1139
Cdd:PRK13537 72 psraRHARQRVGVVPQfdnlDPDF---TVRENLLVFGRYFGLSAAAARALVpPLLEFAK-LENKADAKVGE----LSGGM 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1140 RQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVRKEFSDC-TILTIAH------RLhsiidSDRVLVLDSGRITE 1212
Cdd:PRK13537 144 KRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGkTILLTTHfmeeaeRL-----CDRLCVIEEGRKIA 218
|
....*...
gi 1387192242 1213 FETPQNLI 1220
Cdd:PRK13537 219 EGAPHALI 226
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1135-1219 |
4.40e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 50.49 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1135 LSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVR---KEFsDCTILTIAH-RLHSIIDSDRVLVLDSGRI 1210
Cdd:PRK11432 137 ISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRelqQQF-NITSLYVTHdQSEAFAVSDTVIVMNKGKI 215
|
....*....
gi 1387192242 1211 TEFETPQNL 1219
Cdd:PRK11432 216 MQIGSPQEL 224
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
746-883 |
4.58e-06 |
|
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: 49.90 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 746 GSLAASRV---LHAQLLDNVLHLPLQFFETNPIGQVINRF----TKDMFIIDmrfhyyirTWVNCTLDV------IGTVL 812
Cdd:cd18782 66 FTDTANRIdleLGGTIIDHLLRLPLGFFDKRPVGELSTRIseldTIRGFLTG--------TALTTLLDVlfsviyIAVLF 137
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387192242 813 VIVGALPLFILGLIPL-VFLYFTIQRYYmasSRQIRRLAgASHSPVISHFCETLLGVSTIRAFGHEQRFIQQ 883
Cdd:cd18782 138 SYSPLLTLVVLATVPLqLLLTFLFGPIL---RRQIRRRA-EASAKTQSYLVESLTGIQTVKAQNAELKARWR 205
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
508-597 |
4.97e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.96 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 508 SGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQ---LF---EKVIGSSgmlrnktRILVTHNLTLLPQM-DLIVVM 580
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQvlnLMmdlQQELGLS-------YVFISHDLSVVEHIaDEVMVM 228
|
90
....*....|....*..
gi 1387192242 581 ESGRVAQMGTYQEILAK 597
Cdd:PRK11308 229 YLGRCVEKGTKEQIFNN 245
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
400-580 |
5.03e-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: 48.09 E-value: 5.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 400 LKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIvqrKGSVAYVSQQAwiqncilqenilfgsVMQKQLyerv 479
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLI---SFLPKFSRNKL---------------IFIDQL---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 480 leacALLPD--LEQLPngdqteIGEKGVNISGGQKHRVCLARAVYSGAD--IYLLDDPLSAVDVHVAKQLFEKV--IGSS 553
Cdd:cd03238 69 ----QFLIDvgLGYLT------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIkgLIDL 138
|
170 180
....*....|....*....|....*..
gi 1387192242 554 GmlrnKTRILVTHNLTLLPQMDLIVVM 580
Cdd:cd03238 139 G----NTVILIEHNLDVLSSADWIIDF 161
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1015-1219 |
5.04e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 49.83 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTLS---NCLFRIVERSGGKI-IIDGIDISTIGLHDLRGKLNIIPQDP--VLFSGT 1088
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMqhfNALLKPSSGTITIAgYHITPETGNKNLKKLRKKVSLVFQFPeaQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1089 L-------QMNLDPLDKYPDHELWEVLELCHLKEFVqslpkkllheISEGGENLSVGQRQLVCLARALLRKTKILILDEA 1161
Cdd:PRK13641 103 VlkdvefgPKNFGFSEDEAKEKALKWLKKVGLSEDL----------ISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1162 TASIDFET-DNLVQTTVRKEFSDCTILTIAHRLHSIID-SDRVLVLDSGRITEFETPQNL 1219
Cdd:PRK13641 173 AAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEI 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1014-1218 |
6.21e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.47 E-value: 6.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIV--ERSGGKIIIDGIDISTIGLHDLRGKLNIIPQDPvlfSGTLQM 1091
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLInsQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDP---NSSLNP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1092 NLDPLDKypdheLWEVLELCHLKEFVQSLPKKLLHEISEGG----------ENLSVGQRQLVCLARALLRKTKILILDEA 1161
Cdd:PRK15134 378 RLNVLQI-----IEEGLRVHQPTLSAAQREQQVIAVMEEVGldpetrhrypAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 1162 TASIDFETDNLVQTTVRK--EFSDCTILTIAHRLHsIIDS--DRVLVLDSGRITE-------FETPQN 1218
Cdd:PRK15134 453 TSSLDKTVQAQILALLKSlqQKHQLAYLFISHDLH-VVRAlcHQVIVLRQGEVVEqgdcervFAAPQQ 519
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
997-1166 |
6.23e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 49.31 E-value: 6.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 997 IVEFVDYRARYRDDLgLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIII--DGIDISTIGLHDLRGK 1074
Cdd:PRK13639 1 ILETRDLKYSYPDGT-EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkgEPIKYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1075 LNIIPQDP--VLFSGTLQ-------MNLdpldKYPdhelwevlelchlKEFVQSLPKKLLHEIS-EGGEN-----LSVGQ 1139
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEedvafgpLNL----GLS-------------KEEVEKRVKEALKAVGmEGFENkpphhLSGGQ 142
|
170 180
....*....|....*....|....*..
gi 1387192242 1140 RQLVCLARALLRKTKILILDEATASID 1166
Cdd:PRK13639 143 KKRVAIAGILAMKPEIIVLDEPTSGLD 169
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1014-1216 |
6.66e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 48.92 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRI-------VERSggkiiidgidiSTI--------GLH-DLRGKLNI 1077
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGIleptsgrVEVN-----------GRVsallelgaGFHpELTGRENI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1078 IpqdpvlFSGTLQ-MNLDPLDKYPDhelwEVLELCHLKEFVqSLPKKllheiseggeNLSVGQRqlvclAR-----ALLR 1151
Cdd:COG1134 110 Y------LNGRLLgLSRKEIDEKFD----EIVEFAELGDFI-DQPVK----------TYSSGMR-----ARlafavATAV 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387192242 1152 KTKILILDEATA--SIDFetdnlvqttVRK------EFSD--CTILTIAHRLHSIID-SDRVLVLDSGRITEFETP 1216
Cdd:COG1134 164 DPDILLVDEVLAvgDAAF---------QKKclarirELREsgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDP 230
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
383-568 |
9.23e-06 |
|
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: 48.48 E-value: 9.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 383 IGFINASFSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGSVAYVSQQAWIQNcilq 462
Cdd:cd03267 20 IGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRR---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 463 enilFGSVM-QK-QLYER--VLEACALLPDLEQLPNG-------------DQTEIGEKGV-NISGGQKHRVCLARAVYSG 524
Cdd:cd03267 96 ----IGVVFgQKtQLWWDlpVIDSFYLLAAIYDLPPArfkkrldelsellDLEELLDTPVrQLSLGQRMRAEIAAALLHE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1387192242 525 ADIYLLDDPLSAVDVhVAKQLFEKVIGSSGMLRNKTRILVTHNL 568
Cdd:cd03267 172 PEILFLDEPTIGLDV-VAQENIRNFLKEYNRERGTTVLLTSHYM 214
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1015-1206 |
1.00e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 48.57 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSggkiiidgidiSTIGLHDLRGKLNIIPQ----DPVL-FSGTL 1089
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPD-----------EGVIKRNGKLRIGYVPQklylDTTLpLTVNR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1090 QMNLDPLDKYPDheLWEVLELCHLKEFVQSLPKKLlheisEGGENlsvgqrQLVCLARALLRKTKILILDEATASIDFET 1169
Cdd:PRK09544 89 FLRLRPGTKKED--ILPALKRVQAGHLIDAPMQKL-----SGGET------QRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1387192242 1170 D----NLVQtTVRKEFsDCTILTIAHRLHSII-DSDRVLVLD 1206
Cdd:PRK09544 156 QvalyDLID-QLRREL-DCAVLMVSHDLHLVMaKTDEVLCLN 195
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1014-1216 |
1.05e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 49.08 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFqTHGEEKI-GIVGRTGAGKSTLSNCL---------------FRIVERSGGKIIIDGIDISTI-GLHDLRGKLN 1076
Cdd:PRK13631 41 ALNNISY-TFEKNKIyFIIGNSGSGKSTLVTHFnglikskygtiqvgdIYIGDKKNNHELITNPYSKKIkNFKELRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1077 IIPQDP--VLFSGTLQMNL--DPL----DKYPDHELWEV-LELCHLKE-FVQSLPKKLlheiseggenlSVGQRQLVCLA 1146
Cdd:PRK13631 120 MVFQFPeyQLFKDTIEKDImfGPValgvKKSEAKKLAKFyLNKMGLDDsYLERSPFGL-----------SGGQKRRVAIA 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387192242 1147 RALLRKTKILILDEATASIDFETDN-LVQTTVRKEFSDCTILTIAHRLHSIID-SDRVLVLDSGRITEFETP 1216
Cdd:PRK13631 189 GILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTP 260
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
397-596 |
1.18e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 47.95 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 397 IPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGSVAYVSQQAWI---------------QNCIL 461
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKImreavaivpegrrvfSRMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 462 QENILFGSVM--QKQLYERVLEACALLPDLeqlpngdQTEIGEKGVNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDV 539
Cdd:PRK11614 98 EENLAMGGFFaeRDQFQERIKWVYELFPRL-------HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 540 HVAKQLFEKV--IGSSGMlrnkTRILVTHNLT-LLPQMDLIVVMESGRVAQMGTYQEILA 596
Cdd:PRK11614 171 IIIQQIFDTIeqLREQGM----TIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1015-1166 |
1.22e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 47.79 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQ-THGEEKIgIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLNIIPQDPVLFSGTLQMNL 1093
Cdd:PRK10247 23 LNNISFSlRAGEFKL-ITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1094 dpldKYPdhelWEV----LELCHLKEFVQ--SLPKKLLHE-ISEggenLSVGQRQLVCLARALLRKTKILILDEATASID 1166
Cdd:PRK10247 102 ----IFP----WQIrnqqPDPAIFLDDLErfALPDTILTKnIAE----LSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
993-1192 |
1.62e-05 |
|
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: 49.36 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 993 PSKGIVEFVDYRARYrDDLGLA-------LQDITFQTHGEEKIGIVGRTGAGKSTLsnclFRIVERSGGKIIIDGIDist 1065
Cdd:TIGR00954 440 PGRGIVEYQDNGIKF-ENIPLVtpngdvlIESLSFEVPSGNNLLICGPNGCGKSSL----FRILGELWPVYGGRLTK--- 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1066 iglhDLRGKLNIIPQDPVLFSGTLQ-------MNLDPLDK-YPDHELWEVLELCHLKEFVQSlpkkllheisEGG----- 1132
Cdd:TIGR00954 512 ----PAKGKLFYVPQRPYMTLGTLRdqiiypdSSEDMKRRgLSDKDLEQILDNVQLTHILER----------EGGwsavq 577
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387192242 1133 ---ENLSVGQRQLVCLARALLRKTKILILDEATA--SIDFEtDNLVQTTVRKEFsdcTILTIAHR 1192
Cdd:TIGR00954 578 dwmDVLSGGEKQRIAMARLFYHKPQFAILDECTSavSVDVE-GYMYRLCREFGI---TLFSVSHR 638
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1135-1210 |
1.65e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 48.09 E-value: 1.65e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387192242 1135 LSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVR--KEFSDCTILTIAHRL-HSIIDSDRVLVLDSGRI 1210
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVdYALRYCERIVALRQGHV 231
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1114-1217 |
1.68e-05 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 47.82 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1114 KEFVQSLPKKLLHEIS-EGGEN-----LSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVRKEFSDC-TI 1186
Cdd:PRK11264 118 KEEATARARELLAKVGlAGKETsyprrLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKrTM 197
|
90 100 110
....*....|....*....|....*....|....*....
gi 1387192242 1187 LTIAHRLHSIID-SDRVLVLDSGRITE-------FETPQ 1217
Cdd:PRK11264 198 VIVTHEMSFARDvADRAIFMDQGRIVEqgpakalFADPQ 236
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
402-594 |
1.84e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 48.33 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 402 DLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKG-IV------------------QRKgsVAYVSQQAWI-QNCIL 461
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGrIVlngrvlfdaekgiclppeKRR--IGYVFQDARLfPHYKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 462 QENILFG--SVMQKQlYERVLEACALLPDLEQLPngdqteigekgVNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDV 539
Cdd:PRK11144 94 RGNLRYGmaKSMVAQ-FDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387192242 540 HVAKQLF-------EKVigssgmlrnKTRIL-VTHNL-TLLPQMDLIVVMESGRVAQMGTYQEI 594
Cdd:PRK11144 162 PRKRELLpylerlaREI---------NIPILyVSHSLdEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
400-569 |
1.90e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 48.73 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 400 LKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGSVAYVSQQAWIQNCILQ-ENILFGSVMQKQLYER 478
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGiENIELKGLMMGLTKEK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 479 VLEacaLLPDLEQLpngdqTEIGeKGVN-----ISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQLFEKVigSS 553
Cdd:PRK13545 120 IKE---IIPEIIEF-----ADIG-KFIYqpvktYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKM--NE 188
|
170
....*....|....*.
gi 1387192242 554 GMLRNKTRILVTHNLT 569
Cdd:PRK13545 189 FKEQGKTIFFISHSLS 204
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
757-892 |
2.08e-05 |
|
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: 47.79 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 757 QLLDNVLHLPLQFFETNPIGQVINRFTKDMFIIDMRFHYYIRTWVNcTLDVIGTVLVIVGAL--PLFILGLIPLVFLYFT 834
Cdd:cd18541 78 DLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVD-ALFLGVLVLVMMFTIspKLTLIALLPLPLLALL 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387192242 835 -------IQRYYMASSRQIRRLAGASHspvishfcETLLGVSTIRAFGHEQ----RFIQQNKEVVNENL 892
Cdd:cd18541 157 vyrlgkkIHKRFRKVQEAFSDLSDRVQ--------ESFSGIRVIKAFVQEEaeieRFDKLNEEYVEKNL 217
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1134-1209 |
2.23e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.39 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1134 NLSVGQRQLVCLARALLRKTKILILDEATASI-DFETD---NLVQTTVRKefsDCTILTIAHRLHSIID-SDRVLVLDSG 1208
Cdd:PRK13549 143 NLGLGQQQLVEIAKALNKQARLLILDEPTASLtESETAvllDIIRDLKAH---GIACIYISHKLNEVKAiSDTICVIRDG 219
|
.
gi 1387192242 1209 R 1209
Cdd:PRK13549 220 R 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
398-596 |
2.35e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.55 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 398 PVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILG-----EMEKLKGIVQRKG-SVAYVSQQAWIQ------NCILQE-- 463
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTALSILRllpspPVVYPSGDIRFHGeSLLHASEQTLRGvrgnkiAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 464 ---NILfgSVMQKQLYErVL--------EACALlpdlEQLPNGDQTEI--GEKGVN-----ISGGQKHRVCLARAVYSGA 525
Cdd:PRK15134 103 vslNPL--HTLEKQLYE-VLslhrgmrrEAARG----EILNCLDRVGIrqAAKRLTdyphqLSGGERQRVMIAMALLTRP 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 526 DIYLLDDPLSAVDVHVAKQLFEkvigssgMLR------NKTRILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEILA 596
Cdd:PRK15134 176 ELLIADEPTTALDVSVQAQILQ-------LLRelqqelNMGLLFITHNLSIVRKLaDRVAVMQNGRCVEQNRAATLFS 246
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1017-1221 |
2.81e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.16 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1017 DITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIII--------DGIDISTIGLHDLRG-KLNIIPQDPVLfsg 1087
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSgdirfhgeSLLHASEQTLRGVRGnKIAMIFQEPMV--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1088 tlqmNLDPLDKYpDHELWEVLELcH--------LKEFVQSL-------PKKLLHEISeggENLSVGQRQLVCLARALLRK 1152
Cdd:PRK15134 104 ----SLNPLHTL-EKQLYEVLSL-HrgmrreaaRGEILNCLdrvgirqAAKRLTDYP---HQLSGGERQRVMIAMALLTR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387192242 1153 TKILILDEATASIDFETDNLVQTTVR--KEFSDCTILTIAHRLhSIID--SDRVLVLDSGRITEFETPQNLIH 1221
Cdd:PRK15134 175 PELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNL-SIVRklADRVAVMQNGRCVEQNRAATLFS 246
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
399-596 |
2.82e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 47.49 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 399 VLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKG-SVAYVSQQAWIQ------------NCILQENI 465
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGePVPSRARHARQRvgvvpqfdnldpDFTVRENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 466 L-FG---SVMQKQLYERVleacALLPDLEQLPNGDQTEIGEkgvnISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHV 541
Cdd:PRK13537 102 LvFGryfGLSAAAARALV----PPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387192242 542 AKQLFEKVigSSGMLRNKTRILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEILA 596
Cdd:PRK13537 174 RHLMWERL--RSLLARGKTILLTTHFMEEAERLcDRLCVIEEGRKIAEGAPHALIE 227
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1135-1220 |
2.86e-05 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 47.01 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1135 LSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVR---KEFSDCTILT----IAHRLHSiidsdRVLVLDS 1207
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQdlaEEGMTMVIVTheigFAEKVAS-----RLIFIDK 211
|
90
....*....|...
gi 1387192242 1208 GRITEFETPQNLI 1220
Cdd:PRK09493 212 GRIAEDGDPQVLI 224
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
725-879 |
3.12e-05 |
|
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: 47.46 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 725 YGLLGLMQGLFvcsgAYVVTRGSLAASRVLHAQLLDNV----LHLPLQFFETNPIGQVINRFT-----KDMFIIDMrfhy 795
Cdd:cd18567 48 FGLLLLLQALL----SALRSWLVLYLSTSLNLQWTSNLfrhlLRLPLSYFEKRHLGDIVSRFGsldeiQQTLTTGF---- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 796 yirtwVNCTLDviGTVLVIVGALPLF---ILGLIPLVFL-------YFTIQRYYMASSRQIRRLAGAShspviSHFCETL 865
Cdd:cd18567 120 -----VEALLD--GLMAILTLVMMFLyspKLALIVLAAValyallrLALYPPLRRATEEQIVASAKEQ-----SHFLETI 187
|
170
....*....|....
gi 1387192242 866 LGVSTIRAFGHEQR 879
Cdd:cd18567 188 RGIQTIKLFGREAE 201
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
399-600 |
3.53e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 46.89 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 399 VLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGSVAYVSQQAWIQNCILQENIL------------ 466
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADKNQLrllrtrltmvfq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 467 -FGSVMQKQLYERVLEACALLPDLEQLPNG------------DQTEIGEKGVNISGGQKHRVCLARAVYSGADIYLLDDP 533
Cdd:PRK10619 100 hFNLWSHMTVLENVMEAPIQVLGLSKQEAReravkylakvgiDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387192242 534 LSAVD-------VHVAKQLFEKvigssgmlrNKTRILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEILAKTKN 600
Cdd:PRK10619 180 TSALDpelvgevLRIMQQLAEE---------GKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1106-1221 |
4.14e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 47.33 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1106 EVLELCHLkefVQSLPKKLlheiseggenlSVGQRQLVCLARALLRKTKILILDEATASIDFETDnlVQttVRKEFS--- 1182
Cdd:PRK11000 119 EVLQLAHL---LDRKPKAL-----------SGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR--VQ--MRIEISrlh 180
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1387192242 1183 ---DCTILTIAH-RLHSIIDSDRVLVLDSGRITEFETPQNLIH 1221
Cdd:PRK11000 181 krlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLELYH 223
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1014-1166 |
5.45e-05 |
|
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: 45.89 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFR---------IVERSGGKIIIDGIDISTIglHDLRGK--------LN 1076
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnylpdsgsiLVRHDGGWVDLAQASPREI--LALRRRtigyvsqfLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1077 IIPQDPvlfsgTLQMNLDPLdkypdhelwevLELCHLKEFVQSLPKKLLH--EISE-----------GGEnlsvgqRQLV 1143
Cdd:COG4778 104 VIPRVS-----ALDVVAEPL-----------LERGVDREEARARARELLArlNLPErlwdlppatfsGGE------QQRV 161
|
170 180
....*....|....*....|...
gi 1387192242 1144 CLARALLRKTKILILDEATASID 1166
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLD 184
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
400-619 |
5.51e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 46.32 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 400 LKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKG---IVQRK---GSVAYVSQQ------------------AW 455
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGellIDDHPlhfGDYSYRSQRirmifqdpstslnprqriSQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 456 IQNCILQENI-LFGSVMQKQLYErVLEACALLPD-LEQLPNGdqteigekgvnISGGQKHRVCLARAVYSGADIYLLDDP 533
Cdd:PRK15112 109 ILDFPLRLNTdLEPEQREKQIIE-TLRQVGLLPDhASYYPHM-----------LAPGQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 534 LSAVDVHVAKQLFEKVIgssgMLRNK---TRILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEILAKT-KNLTNLLQA- 607
Cdd:PRK15112 177 LASLDMSMRSQLINLML----ELQEKqgiSYIYVTQHLGMMKHIsDQVLVMHQGEVVERGSTADVLASPlHELTKRLIAg 252
|
250
....*....|...
gi 1387192242 608 -FSEQETAHALKQ 619
Cdd:PRK15112 253 hFGEALTADAWRK 265
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1134-1210 |
5.56e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 46.62 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1134 NLSVGQRQLVCLARALLRKTKILILDEATASIDFetdnLVQTTVRkEF-------SDCTILTIAHRLHSIID-SDRVLVL 1205
Cdd:COG4586 154 QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDV----VSKEAIR-EFlkeynreRGTTILLTSHDMDDIEAlCDRVIVI 228
|
....*
gi 1387192242 1206 DSGRI 1210
Cdd:COG4586 229 DHGRI 233
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
493-581 |
5.63e-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: 45.26 E-value: 5.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 493 PNGDQTE-------IGEKGVNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDV----HVAkqlfeKVIGSSGMLRNKTR 561
Cdd:cd03222 51 PNGDNDEwdgitpvYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrlNAA-----RAIRRLSEEGKKTA 125
|
90 100
....*....|....*....|.
gi 1387192242 562 ILVTHNLTLLPQM-DLIVVME 581
Cdd:cd03222 126 LVVEHDLAVLDYLsDRIHVFE 146
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
406-594 |
5.75e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 46.66 E-value: 5.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 406 KIPEGALVAVVGQVGSGKSSVLSAILG------------------EMEKLKGIVQRK--GS-VAYVSQQAW--IQNC--- 459
Cdd:PRK11022 29 SVKQGEVVGIVGESGSGKSVSSLAIMGlidypgrvmaeklefngqDLQRISEKERRNlvGAeVAMIFQDPMtsLNPCytv 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 460 ---ILQENILFGSVMQKQLYERVLEACAL--LPD----LEQLPNgdqteigekgvNISGGQKHRVCLARAVYSGADIYLL 530
Cdd:PRK11022 109 gfqIMEAIKVHQGGNKKTRRQRAIDLLNQvgIPDpasrLDVYPH-----------QLSGGMSQRVMIAMAIACRPKLLIA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387192242 531 DDPLSAVDVHVAKQLFEKVIgSSGMLRNKTRILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEI 594
Cdd:PRK11022 178 DEPTTALDVTIQAQIIELLL-ELQQKENMALVLITHDLALVAEAaHKIIVMYAGQVVETGKAHDI 241
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1028-1220 |
5.86e-05 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 47.14 E-value: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1028 IGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLNIIPQDPVL---FSG--TLQMN-------LDP 1095
Cdd:PRK09536 32 VGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsfeFDVrqVVEMGrtphrsrFDT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1096 LDKYPDHELWEVLELCHLKEFVQslpkkllHEISEggenLSVGQRQLVCLARALLRKTKILILDEATASIDF----ETDN 1171
Cdd:PRK09536 112 WTETDRAAVERAMERTGVAQFAD-------RPVTS----LSGGERQRVLLARALAQATPVLLLDEPTASLDInhqvRTLE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1172 LVQTTVRkefSDCTILTIAHRLH-SIIDSDRVLVLDSGRITEFETPQNLI 1220
Cdd:PRK09536 181 LVRRLVD---DGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
410-596 |
5.95e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.18 E-value: 5.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 410 GALVAVVGQVGSGKSSVLSAILGEMEK--------------LKGIVQRKGSVAyvsqqawiQNCIL------QENILFGS 469
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGnnftgtilannrkpTKQILKRTGFVT--------QDDILyphltvRETLVFCS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 470 VMQ------KQlyERVLEACALLPDLeQLPNGDQTEIGEKGVN-ISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVA 542
Cdd:PLN03211 166 LLRlpksltKQ--EKILVAESVISEL-GLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAA 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 543 KQLFEKVIGssgmLRNKTRILVT---HNLTLLPQM-DLIVVMESGRVAQMGTYQEILA 596
Cdd:PLN03211 243 YRLVLTLGS----LAQKGKTIVTsmhQPSSRVYQMfDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
722-929 |
6.15e-05 |
|
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: 46.35 E-value: 6.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 722 LSIYGLLGLMQGLFvcsgAYVVTRGSLAASRVLHAQLLDNVLHLPLQFFETNPIGQVINRFTKDmfiIDmRFHYYIrtwV 801
Cdd:cd18563 50 AGAYVLSALLGILR----GRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSD---TD-RLQDFL---S 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 802 NCTLDVIGTVLVIVGA----------LPLFILGLIPLVFLYFTIQRYYMassRQIRRLAGASHSPVISHFCETLLGVSTI 871
Cdd:cd18563 119 DGLPDFLTNILMIIGIgvvlfslnwkLALLVLIPVPLVVWGSYFFWKKI---RRLFHRQWRRWSRLNSVLNDTLPGIRVV 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387192242 872 RAFGHE----QRFIQQNKEVVNENLVcfyNNVISNRWLSVrLEFL---GNLMVFFTAVLTVLAGN 929
Cdd:cd18563 196 KAFGQEkreiKRFDEANQELLDANIR---AEKLWATFFPL-LTFLtslGTLIVWYFGGRQVLSGT 256
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1135-1210 |
6.60e-05 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 46.21 E-value: 6.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1135 LSVGQRQLVCLARALLRKTKILILDEATASID----FETDNLVQTTVRKE-FsdcTILTIAHRL-HSIIDSDRVLVLDSG 1208
Cdd:PRK11247 134 LSGGQKQRVALARALIHRPGLLLLDEPLGALDaltrIEMQDLIESLWQQHgF---TVLLVTHDVsEAVAMADRVLLIEEG 210
|
..
gi 1387192242 1209 RI 1210
Cdd:PRK11247 211 KI 212
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1134-1212 |
6.71e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.09 E-value: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1134 NLSVGQRQLVCLARALLRKTKILILDEATASI-DFETDNLVQttVRKEFSD--CTILTIAHRLHSIID-SDRVLVLDSGR 1209
Cdd:NF040905 139 DIGVGKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLD--LLLELKAqgITSIIISHKLNEIRRvADSITVLRDGR 216
|
...
gi 1387192242 1210 ITE 1212
Cdd:NF040905 217 TIE 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1134-1221 |
6.73e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 46.94 E-value: 6.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1134 NLSVGQRQLVCLARALLRKTKILILDEATASIDfetdnlvqttV--RKEfsdctILTIAHRL----HSII----D----- 1198
Cdd:COG1129 394 NLSGGNQQKVVLAKWLATDPKVLILDEPTRGID----------VgaKAE-----IYRLIRELaaegKAVIvissElpell 458
|
90 100 110
....*....|....*....|....*....|
gi 1387192242 1199 --SDRVLVLDSGRIT-EFE----TPQNLIH 1221
Cdd:COG1129 459 glSDRILVMREGRIVgELDreeaTEEAIMA 488
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1134-1236 |
6.77e-05 |
|
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: 45.86 E-value: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1134 NLSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVRK--EFSDCTILTIAHRLHsIID--SDRVLVLDS-- 1207
Cdd:cd03237 115 ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRfaENNEKTAFVVEHDII-MIDylADRLIVFEGep 193
|
90 100
....*....|....*....|....*....
gi 1387192242 1208 GRITEFETPQNLIHKRGLFFDMLteaGIT 1236
Cdd:cd03237 194 SVNGVANPPQSLRSGMNRFLKNL---DIT 219
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1030-1208 |
7.81e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 45.33 E-value: 7.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1030 IVGRTGAGKSTLSNCLFRIVERsggkiiidgidISTIGLHDLrgKLNIIPQDPVLfsgtlqmnLDPLDKYPD-HELWEVL 1108
Cdd:COG2401 61 IVGASGSGKSTLLRLLAGALKG-----------TPVAGCVDV--PDNQFGREASL--------IDAIGRKGDfKDAVELL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1109 ELCHLKEFVqsLPKKLLHEiseggenLSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVRKEFSDC--TI 1186
Cdd:COG2401 120 NAVGLSDAV--LWLRRFKE-------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAgiTL 190
|
170 180
....*....|....*....|....
gi 1387192242 1187 LTIAHR--LHSIIDSDRVLVLDSG 1208
Cdd:COG2401 191 VVATHHydVIDDLQPDLLIFVGYG 214
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1015-1237 |
8.58e-05 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 45.53 E-value: 8.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCL---FRIVERSGGKIIIDGIDISTIGLHDLRGKLniiPQDPVL-FSGTLQ 1090
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALsgeLSPDSGEVRLNGRPLADWSPAELARRRAVL---PQHSSLsFPFTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1091 ----MNLDPLDKYPDHE---LWEVLELCHLKEFVQslpkKLLHEISeGGEnlsvgqRQLVCLARALLR------KTKILI 1157
Cdd:PRK13548 95 evvaMGRAPHGLSRAEDdalVAAALAQVDLAHLAG----RDYPQLS-GGE------QQRVQLARVLAQlwepdgPPRWLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1158 LDEATASIDFetdnLVQTTVrkefsdctiLTIAHR------------LHsiiD-------SDRVLVLDSGRITEFETPQn 1218
Cdd:PRK13548 164 LDEPTSALDL----AHQHHV---------LRLARQlaherglavivvLH---DlnlaaryADRIVLLHQGRLVADGTPA- 226
|
250
....*....|....*....
gi 1387192242 1219 lihkrglffDMLTEAGITQ 1237
Cdd:PRK13548 227 ---------EVLTPETLRR 236
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
402-594 |
9.32e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 46.26 E-value: 9.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 402 DLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKlKGIVqrKGSVAYVSQQawIQNciLQENIL-----------FGSV 470
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAA-NGRI--GGSATFNGRE--ILN--LPEKELnklraeqismiFQDP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 471 MQ---------KQLYErVL-------EACALLPDLEQLpngDQTEIGE--KGVNI-----SGGQKHRVCLARAVYSGADI 527
Cdd:PRK09473 107 MTslnpymrvgEQLME-VLmlhkgmsKAEAFEESVRML---DAVKMPEarKRMKMyphefSGGMRQRVMIAMALLCRPKL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387192242 528 YLLDDPLSAVDVHVAKQLFEkvigssgMLR------NKTRILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEI 594
Cdd:PRK09473 183 LIADEPTTALDVTVQAQIMT-------LLNelkrefNTAIIMITHDLGVVAGIcDKVLVMYAGRTMEYGNARDV 249
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
724-892 |
9.34e-05 |
|
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: 45.94 E-value: 9.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 724 IYGLLGL--MQGLFVCSGAYVVTRGSLAASRVLHAQLLDNVLHLPLQFFETNPIGQVINRFTKDmfiIDMrfhyyIRTWV 801
Cdd:cd18576 39 ALLLLGLflLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSND---VTQ-----IQDTL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 802 NCTL-DVIGTVLVIVGA----------LPLFILGLIPLVFLYFTIqryymaSSRQIRRLAGA-----SHSPVISHfcETL 865
Cdd:cd18576 111 TTTLaEFLRQILTLIGGvvllffiswkLTLLMLATVPVVVLVAVL------FGRRIRKLSKKvqdelAEANTIVE--ETL 182
|
170 180 190
....*....|....*....|....*....|.
gi 1387192242 866 LGVSTIRAFGHE----QRFIQQNKEVVNENL 892
Cdd:cd18576 183 QGIRVVKAFTREdyeiERYRKALERVVKLAL 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1106-1210 |
9.37e-05 |
|
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: 44.94 E-value: 9.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1106 EVLELCHLKEFVQSLPKKLlheiseggenlSVGQRQLVCLARALLRKTKILILDEATASIdfetDNLVQTTVRKEFS--- 1182
Cdd:cd03301 113 EVAELLQIEHLLDRKPKQL-----------SGGQRQRVALGRAIVREPKVFLMDEPLSNL----DAKLRVQMRAELKrlq 177
|
90 100 110
....*....|....*....|....*....|..
gi 1387192242 1183 ---DCTILTIAH-RLHSIIDSDRVLVLDSGRI 1210
Cdd:cd03301 178 qrlGTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
396-568 |
1.29e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 46.16 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKS---SVLSAIL----GEMEkLKGIVQRKGSVAyVSQQAWIQnCILQE----- 463
Cdd:COG1129 16 GVKALDGVSLELRPGEVHALLGENGAGKStlmKILSGVYqpdsGEIL-LDGEPVRFRSPR-DAQAAGIA-IIHQElnlvp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 464 ------NILFGS-------VMQKQLYERVLEACALL-----PDleqlpngdqTEIGEkgvnISGGQKHRVCLARAVYSGA 525
Cdd:COG1129 93 nlsvaeNIFLGReprrgglIDWRAMRRRARELLARLgldidPD---------TPVGD----LSVAQQQLVEIARALSRDA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1387192242 526 DIYLLDDPLSAVDVHVAKQLFEkVIGSsgmLRNK--TRILVTHNL 568
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFR-IIRR---LKAQgvAIIYISHRL 200
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
722-889 |
1.42e-04 |
|
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: 45.20 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 722 LSIYGLLGLMQGLFVCSGAYVVTRGSL---AASRV---LHAQLLDNVLHLPLQFFETNPIGQVINRFTKDMFIIDmrfhy 795
Cdd:cd18573 38 LSLKTFALALLGVFVVGAAANFGRVYLlriAGERIvarLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVG----- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 796 yiRTWVNCTLDVI-GTVLVIVGA---------LPLFILGLIPLVFLYFTI-QRYYMASSRQIR-RLAGASHspVIShfcE 863
Cdd:cd18573 113 --KSLTQNLSDGLrSLVSGVGGIgmmlyispkLTLVMLLVVPPIAVGAVFyGRYVRKLSKQVQdALADATK--VAE---E 185
|
170 180 190
....*....|....*....|....*....|
gi 1387192242 864 TLLGVSTIRAFGHEQ----RFIQQNKEVVN 889
Cdd:cd18573 186 RLSNIRTVRAFAAERkeveRYAKKVDEVFD 215
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1015-1217 |
1.43e-04 |
|
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: 44.73 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTL------------------SNCLFRIVERsggkiiidgidistiGLHDLRG-KL 1075
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLlgllagldrptsgtvrlaGQDLFALDED---------------ARARLRArHV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1076 NIIPQDPVLFsGTLQMnLD----PLdkypdhELW----------EVLELCHLKEFVQSLPKKLlheiSeGGEnlsvgqRQ 1141
Cdd:COG4181 93 GFVFQSFQLL-PTLTA-LEnvmlPL------ELAgrrdarararALLERVGLGHRLDHYPAQL----S-GGE------QQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1142 LVCLARALLRKTKILILDEATASIDFETDNLVQT---TVRKEFSDCTILT-----IAHRlhsiidSDRVLVLDSGRITEF 1213
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATGEQIIDllfELNRERGTTLVLVthdpaLAAR------CDRVLRLRAGRLVED 227
|
....
gi 1387192242 1214 ETPQ 1217
Cdd:COG4181 228 TAAT 231
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
731-925 |
1.46e-04 |
|
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: 45.15 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 731 MQGLFVCSGAYVV----------TRGSLAAS---RVLH---AQLLDNVLHLPLQFFETNPIGQVINRFTKDMFIIDMRFh 794
Cdd:cd18545 36 LSGLLIIALLFLAlnlvnwvasrLRIYLMAKvgqRILYdlrQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLL- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 795 yyirtwVNCTLDVIGTVLVIVGA----------LPLFILGLIPLVFLY-FTIQRYYMASSRQIRRlagaSHSPVISHFCE 863
Cdd:cd18545 115 ------SNGLINLIPDLLTLVGIviimfslnvrLALVTLAVLPLLVLVvFLLRRRARKAWQRVRK----KISNLNAYLHE 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387192242 864 TLLGVSTIRAFGHEQRFIQQNKEVVNENLvcfynnvisNRWLS-VRLEFLGNLMVFFTAVLTV 925
Cdd:cd18545 185 SISGIRVIQSFAREDENEEIFDELNRENR---------KANMRaVRLNALFWPLVELISALGT 238
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1030-1209 |
1.50e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.88 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1030 IVGRTGAGKSTLSNCLFRIVER---SGGKIIIDGIDISTI-----GLHDLRGKLNIIPQDPVlfsgtlqMNLDPLDKYPD 1101
Cdd:PRK10982 29 LMGENGAGKSTLLKCLFGIYQKdsgSILFQGKEIDFKSSKealenGISMVHQELNLVLQRSV-------MDNMWLGRYPT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1102 HELWevleLCHLKEFVQSlpKKLLHEIS------EGGENLSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQT 1175
Cdd:PRK10982 102 KGMF----VDQDKMYRDT--KAIFDELDididprAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFT 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 1387192242 1176 TVRK-EFSDCTILTIAHRLHSIID-SDRVLVLDSGR 1209
Cdd:PRK10982 176 IIRKlKERGCGIVYISHKMEEIFQlCDEITILRDGQ 211
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1014-1235 |
1.57e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 45.11 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIG----LHDLRGKLNIIPQDP--VLFSG 1087
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKPVRKKVGVVFQFPesQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1088 TL-------QMNLDPLDKYPDHELWEVLELCHL-KEFVQSLPKKllheiseggenLSVGQRQLVCLARALLRKTKILILD 1159
Cdd:PRK13643 101 TVlkdvafgPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFE-----------LSGGQMRRVAIAGILAMEPEVLVLD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1160 EATASID----FETDNLVQTTVRkefSDCTILTIAHRLHSIID-SDRVLVLDSGRITEFETPQNLI--------HKRGL- 1225
Cdd:PRK13643 170 EPTAGLDpkarIEMMQLFESIHQ---SGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFqevdflkaHELGVp 246
|
250
....*....|....
gi 1387192242 1226 ----FFDMLTEAGI 1235
Cdd:PRK13643 247 kathFADQLQKTGA 260
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
507-625 |
1.90e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 45.23 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 507 ISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQLFEKVIGSSGmlRNKTRILVTHNL-TLLPQMDLIVVMESGRV 585
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKA--NNKTVFVITHTMeHVLEVADEVIVMDKGKI 254
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1387192242 586 AQMGTYQEIlaktknLTNllQAFSEQETAHALKQVSVINS 625
Cdd:PRK13631 255 LKTGTPYEI------FTD--QHIINSTSIQVPRVIQVIND 286
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1135-1213 |
1.94e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 45.25 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1135 LSVGQRQLVCLARALLRKTKILILDEATASIDF----ETDNLVQtTVRKEFsDCTILTIAHRLHSIID-SDRVLVLDSGR 1209
Cdd:PRK11144 129 LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLE-RLAREI-NIPILYVSHSLDEILRlADRVVVLEQGK 206
|
....
gi 1387192242 1210 ITEF 1213
Cdd:PRK11144 207 VKAF 210
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
396-580 |
1.99e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.57 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKdlnikipEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGSvayvsqqaWiqncilqENIL--F-GSVMQ 472
Cdd:PRK13409 92 GLPIPK-------EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPS--------W-------DEVLkrFrGTELQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 473 ---KQLYERVLEAcALLPD-LEQLP---NGDQTEI----GEKGV-------------------NISGGQKHRVCLARAVY 522
Cdd:PRK13409 150 nyfKKLYNGEIKV-VHKPQyVDLIPkvfKGKVRELlkkvDERGKldevverlglenildrdisELSGGELQRVAIAAALL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387192242 523 SGADIYLLDDPLSAVDVH----VAKQLFEkvigssgMLRNKTRILVTHNLTLLPQM-DLIVVM 580
Cdd:PRK13409 229 RDADFYFFDEPTSYLDIRqrlnVARLIRE-------LAEGKYVLVVEHDLAVLDYLaDNVHIA 284
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1002-1210 |
2.06e-04 |
|
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: 44.07 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1002 DYRARYrddlglALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDlRGKLNII--P 1079
Cdd:cd03218 9 RYGKRK------VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIGylP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1080 QDPVLFSG-TLQMNLD-------PLDKYPDHELWEVLELCHLKEFVQSLpkkllheisegGENLSVGQRQLVCLARALLR 1151
Cdd:cd03218 82 QEASIFRKlTVEENILavleirgLSKKEREEKLEELLEEFHITHLRKSK-----------ASSLSGGERRRVEIARALAT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387192242 1152 KTKILILDEATASID----FETDNLVQTTVRKEFSdctILTIAHRLHSIID-SDRVLVLDSGRI 1210
Cdd:cd03218 151 NPKFLLLDEPFAGVDpiavQDIQKIIKILKDRGIG---VLITDHNVRETLSiTDRAYIIYEGKV 211
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1014-1221 |
2.11e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 45.62 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVE-------------RSGGKIIIDGIDISTIGLHDLRG-KLNIIP 1079
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEqagglvqcdkmllRRRSRQVIELSEQSAAQMRHVRGaDMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1080 QDPVlfsgtlqMNLDPLdkYPDHElwEVLELCHL-----KEFVQSLPKKLLHEI---------SEGGENLSVGQRQLVCL 1145
Cdd:PRK10261 111 QEPM-------TSLNPV--FTVGE--QIAESIRLhqgasREEAMVEAKRMLDQVripeaqtilSRYPHQLSGGMRQRVMI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387192242 1146 ARALLRKTKILILDEATASID--FETDNLVQTTVRKEFSDCTILTIAHRLHSIID-SDRVLVLDSGRITEFETPQNLIH 1221
Cdd:PRK10261 180 AMALSCRPAVLIADEPTTALDvtIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQIFH 258
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
998-1212 |
2.19e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 45.35 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 998 VEFVDYRARYRDDlGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLNI 1077
Cdd:PRK10522 323 LELRNVTFAYQDN-GFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1078 IPQDPVLFSGTlqmnLDPLDKYPDHEL---W-EVLELCHLKEFVQslpkkllHEISEggENLSVGQRQLVCLARALLRKT 1153
Cdd:PRK10522 402 VFTDFHLFDQL----LGPEGKPANPALvekWlERLKMAHKLELED-------GRISN--LKLSKGQKKRLALLLALAEER 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387192242 1154 KILILDEATASIDfetdnlvqTTVRKEF----------SDCTILTIAHRLHSIIDSDRVLVLDSGRITE 1212
Cdd:PRK10522 469 DILLLDEWAADQD--------PHFRREFyqvllpllqeMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
407-567 |
2.28e-04 |
|
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: 44.32 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 407 IPEGALVAVVGQVGSGKSSVLSAILGEMEKLKG-IVQRKGSVAYVSQQAWIQNCILQENILF----GSVMQKQLYERVLE 481
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGdIEIELDTVSYKPQYIKADYEGTVRDLLSsitkDFYTHPYFKTEIAK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 482 ACALLPDLEQLPNgdqteigekgvNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHvAKQLFEKVIGSSGMLRNKTR 561
Cdd:cd03237 102 PLQIEQILDREVP-----------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE-QRLMASKVIRRFAENNEKTA 169
|
....*.
gi 1387192242 562 ILVTHN 567
Cdd:cd03237 170 FVVEHD 175
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
722-892 |
2.32e-04 |
|
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: 44.46 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 722 LSIYGLLGLMQGLF--VCSGAYvvtrgSLAASRV---LHAQLLDNVLHLPLQFFETNPIGQVINRFTKDMFIIDMRFHYY 796
Cdd:cd18572 39 VLLLLLLSVLSGLFsgLRGGCF-----SYAGTRLvrrLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 797 IRTWVNCTLDVIGTVLVIVGA---LPLFILGLIPLVFLYFTI-QRYYMASSRQIR-RLAGASHspvISHfcETLLGVSTI 871
Cdd:cd18572 114 LNVFLRNLVQLVGGLAFMFSLswrLTLLAFITVPVIALITKVyGRYYRKLSKEIQdALAEANQ---VAE--EALSNIRTV 188
|
170 180
....*....|....*....|....*
gi 1387192242 872 RAFGHE----QRFIQQNKEVVNENL 892
Cdd:cd18572 189 RSFATEereaRRYERALDKALKLSV 213
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1015-1217 |
2.74e-04 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 43.95 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLNIIPQDPVL-FSGTLQ--- 1090
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHSSLaFPFTVEevv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1091 -MNLDPLDKYPDHELW---EVLELC---HLKE-FVQSLpkkllheiSeGGEnlsvgqRQLVCLARALL-------RKTKI 1155
Cdd:COG4559 97 aLGRAPHGSSAAQDRQivrEALALVglaHLAGrSYQTL--------S-GGE------QQRVQLARVLAqlwepvdGGPRW 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387192242 1156 LILDEATASIDfetdnL--VQTTVR--KEFSD--CTILTIahrLHsiiD-------SDRVLVLDSGRITEFETPQ 1217
Cdd:COG4559 162 LFLDEPTSALD-----LahQHAVLRlaRQLARrgGGVVAV---LH---DlnlaaqyADRILLLHQGRLVAQGTPE 225
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
117-344 |
3.11e-04 |
|
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: 44.42 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 117 LIQVALFKVLADVLSFTSPLIMKQMI---LFCEQRPDFGWSGYGYALALFVVVFLQTLIlqqyQRFKMLTSAKIKTAVIG 193
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIddvLIQLGPGGNTSLLLLLVLGLAGAYVLSALL----GILRGRLLARLGERITA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 194 LI----YKKA--LLLSNVSRKQfsTGEIINLMATDTQQLMDLMTninllWSAPF---QILMAVS----LLWQElgpAVLA 260
Cdd:cd18563 77 DLrrdlYEHLqrLSLSFFDKRQ--TGSLMSRVTSDTDRLQDFLS-----DGLPDfltNILMIIGigvvLFSLN---WKLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 261 gVAVLVFVIPMNALVANRMKKLKKNQRKNKDKQIKL---LNEILHGIKILKLYAWEPS----YKKKIIEIREQELEVQK- 332
Cdd:cd18563 147 -LLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLnsvLNDTLPGIRVVKAFGQEKReikrFDEANQELLDANIRAEKl 225
|
250
....*....|..
gi 1387192242 333 SAGYLAVFSMLT 344
Cdd:cd18563 226 WATFFPLLTFLT 237
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1014-1220 |
3.33e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.72 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGgkiiidgidiSTIGLH----DLRGKLNIIPQDPVLF---- 1085
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSA----------GTITLHgkkiNNHNANEAINHGFALVteer 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1086 -SGTLQMNLD--------PLDKYPDHelWEVLELCHLKEFVQSL-----PKKLLHEISEGgeNLSVGQRQLVCLARALLR 1151
Cdd:PRK10982 333 rSTGIYAYLDigfnslisNIRNYKNK--VGLLDNSRMKSDTQWVidsmrVKTPGHRTQIG--SLSGGNQQKVIIGRWLLT 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 1152 KTKILILDEATASID----FETDNLVQTTVRKefsDCTILTIAHRLHSIID-SDRVLVLDSGRITEF----ETPQNLI 1220
Cdd:PRK10982 409 QPEILMLDEPTRGIDvgakFEIYQLIAELAKK---DKGIIIISSEMPELLGiTDRILVMSNGLVAGIvdtkTTTQNEI 483
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1134-1209 |
3.34e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 43.83 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1134 NLSVGQRQLVCLARALLRKTKILILDEATASID-FETDNLVQTTV--RKEFsDCTILTIAHRLHSIID-SDRVLVLDSGR 1209
Cdd:PRK11300 153 NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNpKETKELDELIAelRNEH-NVTVLLIEHDMKLVMGiSDRIYVVNQGT 231
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
406-577 |
3.39e-04 |
|
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: 44.78 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 406 KIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGSVAYVSQQAWIQNCILQENILFGSVMQK----QLYERVLE 481
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQYISPDYDGTVEEFLRSANTDDfgssYYKTEIIK 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 482 ACALLPDLEQlpngdqtEIGEkgvnISGGQKHRV----CLARAvysgADIYLLDDPLSAVDV----HVAkqlfeKVIGSS 553
Cdd:COG1245 442 PLGLEKLLDK-------NVKD----LSGGELQRVaiaaCLSRD----ADLYLLDEPSAHLDVeqrlAVA-----KAIRRF 501
|
170 180
....*....|....*....|....
gi 1387192242 554 GMLRNKTRILVTHNLTLlpqMDLI 577
Cdd:COG1245 502 AENRGKTAMVVDHDIYL---IDYI 522
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
396-593 |
3.42e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 43.55 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGS-VAYVSQQAWIQN---CIlQENILFGSVM 471
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdISTLKPEIYRQQvsyCA-QTPTLFGDTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 472 QK------QLYERVLEACALLPDLEQ--LPNgdqtEIGEKGVN-ISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHvA 542
Cdd:PRK10247 98 YDnlifpwQIRNQQPDPAIFLDDLERfaLPD----TILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDES-N 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1387192242 543 KQLFEKVIGSSGMLRNKTRILVTHNLTLLPQMDLIVVMESgrvaQMGTYQE 593
Cdd:PRK10247 173 KHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQP----HAGEMQE 219
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
117-311 |
3.52e-04 |
|
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: 43.95 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 117 LIQVALFKVLADVLSFTSPLIMKQMI--LFCEQRPDFGWsgyGYALALFVVVFLQ--TLILQQYqrfkmlTSAKIKTAVI 192
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLddIFVEKDLEALL---LVPLAIIGLFLLRglASYLQTY------LMAYVGQRVV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 193 ----GLIYKKALLLSnVSR-KQFSTGEIINLMATDTQQLMDLMTN-INLLWSAPFQILMAVSLL----WQelgpavLAGV 262
Cdd:cd18552 72 rdlrNDLFDKLLRLP-LSFfDRNSSGDLISRITNDVNQVQNALTSaLTVLVRDPLTVIGLLGVLfyldWK------LTLI 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1387192242 263 AVLVFviPMNALVANRM-KKLKKNQRKNKDKQ---IKLLNEILHGIKILKLYA 311
Cdd:cd18552 145 ALVVL--PLAALPIRRIgKRLRKISRRSQESMgdlTSVLQETLSGIRVVKAFG 195
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
508-594 |
3.84e-04 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 43.95 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 508 SGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQ---LFEKvigssgmLRNK---TRILVTHNLTLLPQM-DLIVVM 580
Cdd:COG4608 159 SGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQvlnLLED-------LQDElglTYLFISHDLSVVRHIsDRVAVM 231
|
90
....*....|....
gi 1387192242 581 ESGRVAQMGTYQEI 594
Cdd:COG4608 232 YLGKIVEIAPRDEL 245
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1015-1214 |
4.80e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 44.29 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLfriversggkiiidgidistIG-LHDLRGKLNI--------IPQDpvlf 1085
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLL--------------------AGeLEPDSGTVKLgetvkigyFDQH---- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1086 SGTLQMNLDPLDkypdhELWEVLELC---HLKEFVQSL---PKKLLHEISeggeNLSVGQRQLVCLARALLRKTKILILD 1159
Cdd:COG0488 387 QEELDPDKTVLD-----ELRDGAPGGteqEVRGYLGRFlfsGDDAFKPVG----VLSGGEKARLALAKLLLSPPNVLLLD 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1387192242 1160 EATASIDFETDNLVQTTVrKEFsDCTILTIAHRlHSIIDS--DRVLVLDSGRITEFE 1214
Cdd:COG0488 458 EPTNHLDIETLEALEEAL-DDF-PGTVLLVSHD-RYFLDRvaTRILEFEDGGVREYP 511
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
721-883 |
5.09e-04 |
|
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: 43.62 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 721 KLSIYgLLGLMQGLFVCSGAYVVTRgSLAASRVLHA---QLLDNVLHLPLQFFETNPIGQVINRFTKDMFIIDM----RF 793
Cdd:cd18577 48 KYALY-FVYLGIGSFVLSYIQTACW-TITGERQARRirkRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDgigeKL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 794 HYYIRTwvnctldvIGTVLV--IVG-----ALPLFILGLIPLVFLYFTIQRYYMA--SSRQIRRLAGASHspVIShfcET 864
Cdd:cd18577 126 GLLIQS--------LSTFIAgfIIAfiyswKLTLVLLATLPLIAIVGGIMGKLLSkyTKKEQEAYAKAGS--IAE---EA 192
|
170
....*....|....*....
gi 1387192242 865 LLGVSTIRAFGHEQRFIQQ 883
Cdd:cd18577 193 LSSIRTVKAFGGEEKEIKR 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1028-1166 |
6.04e-04 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 43.08 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1028 IGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDLRGKLNIIPQDPVLFSGTLQMNLDPLDKYP------- 1100
Cdd:PRK11231 31 TALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGITVRELVAYGRSPwlslwgr 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387192242 1101 ----DHELWEV-LELCHLKEFVQslpKKLlheiseggENLSVGQRQLVCLARALLRKTKILILDEATASID 1166
Cdd:PRK11231 111 lsaeDNARVNQaMEQTRINHLAD---RRL--------TDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD 170
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1015-1209 |
7.28e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 43.71 E-value: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLfriversggkiiidgidISTIGLHDLRGKL---NIIPQDPVLFSGTLQM 1091
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNAL-----------------AGRIQGNNFTGTIlanNRKPTKQILKRTGFVT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1092 NLDPLdkYPDHELWEVLELCHLKEFVQSLPKK---LLHE--ISEGG----EN----------LSVGQRQLVCLARALLRK 1152
Cdd:PLN03211 147 QDDIL--YPHLTVRETLVFCSLLRLPKSLTKQekiLVAEsvISELGltkcENtiignsfirgISGGERKRVSIAHEMLIN 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387192242 1153 TKILILDEATASIDFETD-NLVQTTVRKEFSDCTILTIAH----RLHSIIDSdrVLVLDSGR 1209
Cdd:PLN03211 225 PSLLILDEPTSGLDATAAyRLVLTLGSLAQKGKTIVTSMHqpssRVYQMFDS--VLVLSEGR 284
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
400-578 |
7.91e-04 |
|
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: 42.60 E-value: 7.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 400 LKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGE--MEKLKGIVQRKGSVAYVSQQAWIQNCIL--QENI---------- 465
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPalARRLHLKKEQPGNHDRIEGLEHIDKVIVidQSPIgrtprsnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 466 ----------LFGSVMQKQLYER--------------VL-----EACALLPDLEQLPNGDQT---------EIGEKGVNI 507
Cdd:cd03271 91 ytgvfdeireLFCEVCKGKRYNRetlevrykgksiadVLdmtveEALEFFENIPKIARKLQTlcdvglgyiKLGQPATTL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387192242 508 SGGQKHRVCLARAVY---SGADIYLLDDPLSAVDVHVAKQLFEkVIGSsgmLRNK--TRILVTHNLTLLPQMDLIV 578
Cdd:cd03271 171 SGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLE-VLQR---LVDKgnTVVVIEHNLDVIKCADWII 242
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1135-1236 |
7.98e-04 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 42.72 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1135 LSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVRKEFSDCTILTIAH------RLhsiidSDRVLVLDSG 1208
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRV-----SDYTAFFYLG 229
|
90 100 110
....*....|....*....|....*....|....*
gi 1387192242 1209 RITE-------FETPQnliHKRglffdmlTEAGIT 1236
Cdd:COG1117 230 ELVEfgpteqiFTNPK---DKR-------TEDYIT 254
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1021-1206 |
8.30e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.64 E-value: 8.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1021 QTHGEEKIGIVGRTGAGKSTLSNCLFRIVErsggkiiidgidiSTIGLHDLRGKLNIIPQ----DpvlFSGTLQMNL--- 1093
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLK-------------PDEGEVDPELKISYKPQyikpD---YDGTVEDLLrsi 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1094 -DPLD-KYPDHELWEVLELCHLkefvqsLPKKLlheiseggENLSVGQRQLVCLARALLRKTKILILDEATASIDFETDN 1171
Cdd:PRK13409 425 tDDLGsSYYKSEIIKPLQLERL------LDKNV--------KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRL 490
|
170 180 190
....*....|....*....|....*....|....*....
gi 1387192242 1172 LVQTTVRK--EFSDCTILTIAHRLhSIID--SDRVLVLD 1206
Cdd:PRK13409 491 AVAKAIRRiaEEREATALVVDHDI-YMIDyiSDRLMVFE 528
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1026-1216 |
8.41e-04 |
|
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: 41.20 E-value: 8.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1026 EKIGIVGRTGAGKSTLSNCLFRIVERsggkiiidgidistiglhdlrgklniiPQDPVLFsgtlqMNLDPLDKYPDHELW 1105
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGP---------------------------PGGGVIY-----IDGEDILEEVLDQLL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1106 EVLelchlkefvqslpkkllheISEGGENLSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQ-------TTVR 1178
Cdd:smart00382 51 LII-------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrlLLLL 111
|
170 180 190
....*....|....*....|....*....|....*...
gi 1387192242 1179 KEFSDCTILTIAHRLHSIIdsDRVLVLDSGRITEFETP 1216
Cdd:smart00382 112 KSEKNLTVILTTNDEKDLG--PALLRRRFDRRIVLLLI 147
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
508-644 |
9.30e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 9.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 508 SGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQLfekvigSSGMLR-NKTRILVTHNLTLLPQM--DLIVVMESGR 584
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWL------ETYLLKwPKTFIVVSHAREFLNTVvtDILHLHGQKL 419
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387192242 585 VAQMGTYqEILAKTK--NLTNLLQAFSEQETAHALKQVSVINSRTVLKDQILVQNDRPLLDQ 644
Cdd:PLN03073 420 VTYKGDY-DTFERTReeQLKNQQKAFESNERSRSHMQAFIDKFRYNAKRASLVQSRIKALDR 480
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
399-589 |
1.21e-03 |
|
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: 41.79 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 399 VLKDLNIKIPEGaLVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKGS------------VAYVSQQ-AWIQN------- 458
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrrIGYLPQEfGVYPNftvrefl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 459 ---CILQEnilfgsVMQKQLYERVLEAcallpdLEQLpngDQTEIGEKGVN-ISGGQKHRVCLARAVYSGADIYLLDDPL 534
Cdd:cd03264 94 dyiAWLKG------IPSKEVKARVDEV------LELV---NLGDRAKKKIGsLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 535 SAVDVhvakqlfEKVIGSSGMLR----NKTRILVTHNLTLLPQM-DLIVVMESGRVAQMG 589
Cdd:cd03264 159 AGLDP-------EERIRFRNLLSelgeDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
117-322 |
1.24e-03 |
|
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: 42.42 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 117 LIQVALFKVLADVLSFTSPLIMKQMI-LFCEQRPDFGWsgygyaLALFVVVFLQTLILQQYQRFKMLTSA--KIKTAVIG 193
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIdALSAGGSSGGL------LALLVALFLLQAVLSALSSYLLGRTGerVVLDLRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 194 LIYKkaLLLSNVSR-KQFSTGEIINLMATDTQQLMDLMTN--INLLwSAPFQILMAVSLL----WQELGpAVLAGVAVLV 266
Cdd:cd18551 75 LWRR--LLRLPVSFfDRRRSGDLVSRVTNDTTLLRELITSglPQLV-TGVLTVVGAVVLMflldWVLTL-VTLAVVPLAF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387192242 267 FVIpmnALVANRMKKLKKNQRKNKDKQIKLLNEILHGIKILKLYAWEPSYKKKIIE 322
Cdd:cd18551 151 LII---LPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGE 203
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
508-595 |
1.41e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 41.84 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 508 SGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQLFEkvigssgMLRNKTR------ILVTHNLT---LLPqmDLIV 578
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLD-------LLRGLVRelglavVIVTHDLAvarLLA--HRLL 223
|
90
....*....|....*..
gi 1387192242 579 VMESGRVAQMGTYQEIL 595
Cdd:PRK11701 224 VMKQGRVVESGLTDQVL 240
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1001-1219 |
1.48e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 41.93 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1001 VDYRARYRDDL-GLALQDI--TFQTHGeeKIGIVGRTGAGKSTLS---NCLfriversggkiiidgidistigLHDLRGK 1074
Cdd:PRK13634 8 VEHRYQYKTPFeRRALYDVnvSIPSGS--YVAIIGHTGSGKSTLLqhlNGL----------------------LQPTSGT 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1075 LNIipQDPVLFSGTLQMNLDPLDK-------YPDHELWE--VL-ELC---------------HLKEFVQ--SLPKKLLHe 1127
Cdd:PRK13634 64 VTI--GERVITAGKKNKKLKPLRKkvgivfqFPEHQLFEetVEkDICfgpmnfgvseedakqKAREMIElvGLPEELLA- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1128 isEGGENLSVGQRQLVCLARALLRKTKILILDEATASIDfetdnlvqTTVRKEFSDCTI-------LTIAHRLHSIID-- 1198
Cdd:PRK13634 141 --RSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD--------PKGRKEMMEMFYklhkekgLTTVLVTHSMEDaa 210
|
250 260
....*....|....*....|...
gi 1387192242 1199 --SDRVLVLDSGRITEFETPQNL 1219
Cdd:PRK13634 211 ryADQIVVMHKGTVFLQGTPREI 233
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1030-1216 |
1.55e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 41.92 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1030 IVGRTGAGKST---LSNCLfrIVERSGGKIIIDGIDISTIG----LHDLRGKLNIIPQDP--VLFSGTLQMNL--DPLDK 1098
Cdd:PRK13645 42 VIGTTGSGKSTmiqLTNGL--IISETGQTIVGDYAIPANLKkikeVKRLRKEIGLVFQFPeyQLFQETIEKDIafGPVNL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1099 YPDHE-----LWEVLELCHL-KEFVQSLPKKLlheiseggenlSVGQRQLVCLARALLRKTKILILDEATASID--FETD 1170
Cdd:PRK13645 120 GENKQeaykkVPELLKLVQLpEDYVKRSPFEL-----------SGGQKRRVALAGIIAMDGNTLVLDEPTGGLDpkGEED 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1387192242 1171 --NLVQtTVRKEFSDcTILTIAHRLHSIID-SDRVLVLDSGRITEFETP 1216
Cdd:PRK13645 189 fiNLFE-RLNKEYKK-RIIMVTHNMDQVLRiADEVIVMHEGKVISIGSP 235
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1014-1212 |
1.56e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 42.26 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRI---VERSGGKIIIDGIDISTIGLHDLRGKLNIIPQDPV------- 1083
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIetpTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNPYgslnprk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1084 ----LFSGTLQMNLDpLDKYPDHE-LWEVLELCHLK-EFVQSLPkkllHEISeGgenlsvGQRQLVCLARALLRKTKILI 1157
Cdd:PRK11308 110 kvgqILEEPLLINTS-LSAAERREkALAMMAKVGLRpEHYDRYP----HMFS-G------GQRQRIAIARALMLDPDVVV 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387192242 1158 LDEATASIDFEtdnlVQTTVRKEFSD------CTILTIAHRLhSIID--SDRVLVLDSGRITE 1212
Cdd:PRK11308 178 ADEPVSALDVS----VQAQVLNLMMDlqqelgLSYVFISHDL-SVVEhiADEVMVMYLGRCVE 235
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
396-584 |
1.75e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.59 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQRKG-SVAYVSQQAWIQNCI------LQ------ 462
Cdd:PRK11288 16 GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqEMRFASTTAALAAGVaiiyqeLHlvpemt 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 463 --ENIL-------FGSVMQKQLYERVLEAcallpdLEQLpnGDQTEIGEKGVNISGGQKHRVCLARAVYSGADIYLLDDP 533
Cdd:PRK11288 96 vaENLYlgqlphkGGIVNRRLLNYEAREQ------LEHL--GVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1387192242 534 LSAVDVHVAKQLFeKVIGSsgmLRNKTRIL--VTHNLTLLPQM-DLIVVMESGR 584
Cdd:PRK11288 168 TSSLSAREIEQLF-RVIRE---LRAEGRVIlyVSHRMEEIFALcDAITVFKDGR 217
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1015-1210 |
2.38e-03 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 42.02 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHDL----RGKLNIIPQDPVLFSG-TL 1089
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLSHlTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1090 QMNLDPLDKYPDHELWEVLELCHlkEFVQSLpkKLLHEISEGGENLSVGQRQLVCLARALLRKTKILILDEATASIDFET 1169
Cdd:PRK10535 104 AQNVEVPAVYAGLERKQRLLRAQ--ELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1387192242 1170 DNLVQTTVrKEFSD--CTILTIAHRLHSIIDSDRVLVLDSGRI 1210
Cdd:PRK10535 180 GEEVMAIL-HQLRDrgHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
386-617 |
2.40e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 41.96 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 386 INASFSwdktGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAIL-------GEMEkLKGIVQRKGSVA-------Y-V 450
Cdd:PRK15439 17 ISKQYS----GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAgivppdsGTLE-IGGNPCARLTPAkahqlgiYlV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 451 SQQAWI-QNCILQENILFGSVMQKQLYERVLEACALLpdleqlpnGDQTEIGEKGVNISGGQKHRVCLARAVYSGADIYL 529
Cdd:PRK15439 92 PQEPLLfPNLSVKENILFGLPKRQASMQKMKQLLAAL--------GCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 530 LDDPLSAVDVHVAKQLFEKVigssGMLRNKTR--ILVTHNLTLLPQM-DLIVVMESGRVAQMGTYQEIlaktkNLTNLLQ 606
Cdd:PRK15439 164 LDEPTASLTPAETERLFSRI----RELLAQGVgiVFISHKLPEIRQLaDRISVMRDGTIALSGKTADL-----STDDIIQ 234
|
250
....*....|.
gi 1387192242 607 AFSEQETAHAL 617
Cdd:PRK15439 235 AITPAAREKSL 245
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
404-644 |
2.41e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.92 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 404 NIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGivQRKGS---VAYVS--QQAWIQNCILQEN---IL------FGS 469
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSG--ERQSQfshITRLSfeQLQKLVSDEWQRNntdMLspgeddTGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 470 VMQK--QLYERVLEACALLPdlEQLpnGDQTEIGEKGVNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQLFE 547
Cdd:PRK10938 101 TTAEiiQDEVKDPARCEQLA--QQF--GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 548 KV--IGSSGMlrnkTRILVTHNLTLLP-QMDLIVVMESGRVAQMGTYQEI--------LAKTKNLTNLlqAFSEQETAHA 616
Cdd:PRK10938 177 LLasLHQSGI----TLVLVLNRFDEIPdFVQFAGVLADCTLAETGEREEIlqqalvaqLAHSEQLEGV--QLPEPDEPSA 250
|
250 260
....*....|....*....|....*...
gi 1387192242 617 LKQVSVINSRTVLKDQILVQNDRPLLDQ 644
Cdd:PRK10938 251 RHALPANEPRIVLNNGVVSYNDRPILHN 278
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1023-1206 |
2.41e-03 |
|
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: 42.08 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1023 HGEEKIGIVGRTGAGKSTLSNCLFRIVErsggkiiidgidiSTIGlhDLRGKLNI------IPQDpvlFSGTLQMNL--- 1093
Cdd:COG1245 364 REGEVLGIVGPNGIGKTTFAKILAGVLK-------------PDEG--EVDEDLKIsykpqyISPD---YDGTVEEFLrsa 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1094 --DPLD-KYPDHELWEVLELchlkefvqslpKKLLH-EISEggenLSVGQRQLVCLARALLRKTKILILDEATASIDFET 1169
Cdd:COG1245 426 ntDDFGsSYYKTEIIKPLGL-----------EKLLDkNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 490
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1387192242 1170 DNLVQTTVRK--EFSDCTILTIAHRLHsIID--SDRVLVLD 1206
Cdd:COG1245 491 RLAVAKAIRRfaENRGKTAMVVDHDIY-LIDyiSDRLMVFE 530
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
724-928 |
2.48e-03 |
|
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: 41.31 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 724 IYGLLGLMQGLFVCSGAYVVTRGSLAAS---RVLH---AQLLDNVLHLPLQFFETNPIGQVINRFTKDmfIIDMrfhyyi 797
Cdd:cd18550 38 LVLLALGMVAVAVASALLGVVQTYLSARigqGVMYdlrVQLYAHLQRMSLAFFTRTRTGEIQSRLNND--VGGA------ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 798 RTWVNCTL-DVIGTVLVIVGA----------LPLFILGLIPLvFLYFTI---QRYYMASSRQIRRLAGAShspviSHFCE 863
Cdd:cd18550 110 QSVVTGTLtSVVSNVVTLVATlvamlaldwrLALLSLVLLPL-FVLPTRrvgRRRRKLTREQQEKLAELN-----SIMQE 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387192242 864 TL--LGVSTIRAFGHE----QRFIQQNKEV----VNENLVcfynnvisNRWLSVRLEFLGNLMvffTAVLTVLAG 928
Cdd:cd18550 184 TLsvSGALLVKLFGREddeaARFARRSRELrdlgVRQALA--------GRWFFAALGLFTAIG---PALVYWVGG 247
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
754-879 |
2.75e-03 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). 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. 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: 349998 [Multi-domain] Cd Length: 299 Bit Score: 41.25 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 754 LHAQLLDNVLHLPLQFFETNPIGQVINRFTKDmfiIDMRFHYYIRTWVNCTLDVIGTVLVIVGALPLFI-LGLIPLVFL- 831
Cdd:cd18554 81 IRKDLFDHLQKLSLRYYANNRSGEIISRVIND---VEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPkLTFVSLVIFp 157
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1387192242 832 -YFTIQRYYMASSRQIRRLAGASHSPVISHFCETLLGVSTIRAFGHEQR 879
Cdd:cd18554 158 fYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKH 206
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
725-883 |
2.76e-03 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 41.33 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 725 YGLLGLMQGLFVCSGAYVVTRGSLAASRVLHAQLLDNVLHLPLQFFETNPIG---QVINRFTKDM-FIIDMRFHYYIRTW 800
Cdd:cd18582 44 YGLARILSSLFNELRDALFARVSQRAVRRLALRVFRHLHSLSLRFHLSRKTGalsRAIERGTRGIeFLLRFLLFNILPTI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 801 VNCTLdVIGTVLVIVGALPLFILGLIPLVFLYFTIqrYYMASSRQIRRLAGASHSPVISHFCETLLGVSTIRAFGHEQRF 880
Cdd:cd18582 124 LELLL-VCGILWYLYGWSYALITLVTVALYVAFTI--KVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYE 200
|
...
gi 1387192242 881 IQQ 883
Cdd:cd18582 201 AER 203
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1015-1217 |
2.84e-03 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 41.61 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTlsncLFRIVE--RSGGKIIIDGIDISTIGLHDLRGKLNIIPQDPVLFSG-TLQM 1091
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTT----LLRIIAglEHQTSGHIRFHGTDVSRLHARDRKVGFVFQHYALFRHmTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1092 NLD------PLDKYPDH--------ELWEVLELCHLKEFVQSlpkkllheiseggeNLSVGQRQLVCLARALLRKTKILI 1157
Cdd:PRK10851 94 NIAfgltvlPRRERPNAaaikakvtQLLEMVQLAHLADRYPA--------------QLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387192242 1158 LDEATASIDfetdnlvqTTVRKEFS----------DCTILTIAHRLHSIID-SDRVLVLDSGRITEFETPQ 1217
Cdd:PRK10851 160 LDEPFGALD--------AQVRKELRrwlrqlheelKFTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPD 222
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1014-1166 |
2.91e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 40.93 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDIsTIGLHDLRG-KLNIIPQDPV--------- 1083
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYSYRSqRIRMIFQDPStslnprqri 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1084 --LFSGTLQMNLDPLDKYPDHELWEVLELCHLkefvqsLPKkllhEISEGGENLSVGQRQLVCLARALLRKTKILILDEA 1161
Cdd:PRK15112 107 sqILDFPLRLNTDLEPEQREKQIIETLRQVGL------LPD----HASYYPHMLAPGQKQRLGLARALILRPKVIIADEA 176
|
....*
gi 1387192242 1162 TASID 1166
Cdd:PRK15112 177 LASLD 181
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
758-889 |
2.94e-03 |
|
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: 41.28 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 758 LLDNVLHLPLQFFETNPIGQVINRFTKDMFIIDMRFHYYIRTWVNCTLDVIGTVLV---IVGALPLFILGLIPLVFLYFT 834
Cdd:cd18549 81 LFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIIlltINVPLTLIVFALLPLMIIFTI 160
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 835 IQRYYM-ASSRQIRRLAGAshspVISHFCETLLGVSTIRAFGHE----QRFIQQNKEVVN 889
Cdd:cd18549 161 YFNKKMkKAFRRVREKIGE----INAQLEDSLSGIRVVKAFANEeyeiEKFDEGNDRFLE 216
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
393-550 |
3.18e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.53 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 393 DKT--GIPVLKDLNIKIPEGALVAVVGQVGSGKSSVlsailgeMEKLKGIVQR-KGSVAYV-----------SQQAWIQ- 457
Cdd:PRK10762 11 DKAfpGVKALSGAALNVYPGRVMALVGENGAGKSTM-------MKVLTGIYTRdAGSILYLgkevtfngpksSQEAGIGi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 458 -----NCILQ----ENIL--------FGSVMQKQLYErvlEACALLPDLeQLPNGDQTEIGEkgvnISGGQKHRVCLARA 520
Cdd:PRK10762 84 ihqelNLIPQltiaENIFlgrefvnrFGRIDWKKMYA---EADKLLARL-NLRFSSDKLVGE----LSIGEQQMVEIAKV 155
|
170 180 190
....*....|....*....|....*....|
gi 1387192242 521 VYSGADIYLLDDPLSAVDVHVAKQLFeKVI 550
Cdd:PRK10762 156 LSFESKVIIMDEPTDALTDTETESLF-RVI 184
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1012-1045 |
3.36e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 40.68 E-value: 3.36e-03
10 20 30
....*....|....*....|....*....|....
gi 1387192242 1012 GLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCL 1045
Cdd:PRK11701 19 RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNAL 52
|
|
| Dynamin_N |
pfam00350 |
Dynamin family; |
413-433 |
3.53e-03 |
|
Dynamin family;
Pssm-ID: 459775 [Multi-domain] Cd Length: 168 Bit Score: 39.52 E-value: 3.53e-03
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
387-452 |
3.74e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.42 E-value: 3.74e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387192242 387 NASFSWDKTgiPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQ--RKGSVAYVSQ 452
Cdd:PRK15064 324 NLTKGFDNG--PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKwsENANIGYYAQ 389
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1014-1209 |
4.30e-03 |
|
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: 41.35 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLH---DLRGKLNIIPQDPvlfsgTLQ 1090
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKASNirdTERAGIVIIHQEL-----TLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1091 MNLDPLDK-YPDHELWEVLELCHLKEFVQSLpKKLLHEISEGGEN-------LSVGQRQLVCLARALLRKTKILILDEAT 1162
Cdd:TIGR02633 91 PELSVAENiFLGNEITLPGGRMAYNAMYLRA-KNLLRELQLDADNvtrpvgdYGGGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1387192242 1163 ASI-DFETDNLVQTTVRKEFSDCTILTIAHRLHSIID-SDRVLVLDSGR 1209
Cdd:TIGR02633 170 SSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
1028-1047 |
4.86e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 40.52 E-value: 4.86e-03
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1106-1217 |
4.87e-03 |
|
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: 41.21 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1106 EVLELCHLKEfvqslPKKLL----HEiseggenLSVGQRQLVCLARALLRKTKILILDEATASIDfetdnlvqTTVRKEf 1181
Cdd:COG4172 136 ELLERVGIPD-----PERRLdaypHQ-------LSGGQRQRVMIAMALANEPDLLIADEPTTALD--------VTVQAQ- 194
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1387192242 1182 sdctILT---------------IAHRLHSIID-SDRVLVLDSGRITE-------FETPQ 1217
Cdd:COG4172 195 ----ILDllkdlqrelgmalllITHDLGVVRRfADRVAVMRQGEIVEqgptaelFAAPQ 249
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
378-596 |
5.31e-03 |
|
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: 40.94 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 378 IGDHAIGFINAS---FSWDKTGIPVLKDLNIKIPEGALVAVVGQVGSGKSSVLSAILGEMEKLKGIVQ-----------R 443
Cdd:TIGR03269 275 VGEPIIKVRNVSkryISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewvdmtK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 444 KGSVAYVSQQAWIqNCILQENILFGsvmQKQLYERVLEACAL-LPD-------LEQLPNGDQTEigEKGVNI-------- 507
Cdd:TIGR03269 355 PGPDGRGRAKRYI-GILHQEYDLYP---HRTVLDNLTEAIGLeLPDelarmkaVITLKMVGFDE--EKAEEIldkypdel 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 508 SGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQLFEKVIGSSGMLrNKTRILVTHNLTLLPQM-DLIVVMESGRVA 586
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEM-EQTFIIVSHDMDFVLDVcDRAALMRDGKIV 507
|
250
....*....|
gi 1387192242 587 QMGTYQEILA 596
Cdd:TIGR03269 508 KIGDPEEIVE 517
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
396-536 |
6.23e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 40.68 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 396 GIPVLKDLNIKIPEGALVAVVGQVGSGKSS---VLSAIL------------GEMEKLKGI--VQRKGSV------AYVSQ 452
Cdd:PRK13549 17 GVKALDNVSLKVRAGEIVSLCGENGAGKSTlmkVLSGVYphgtyegeiifeGEELQASNIrdTERAGIAiihqelALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 453 QAWIQNCILQENILFGSVMQkqlYERVLEACALLpdLEQL-----PNgdqTEIGEKGvnisGGQKHRVCLARAVYSGADI 527
Cdd:PRK13549 97 LSVLENIFLGNEITPGGIMD---YDAMYLRAQKL--LAQLkldinPA---TPVGNLG----LGQQQLVEIAKALNKQARL 164
|
....*....
gi 1387192242 528 YLLDDPLSA 536
Cdd:PRK13549 165 LILDEPTAS 173
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
400-445 |
7.15e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.83 E-value: 7.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1387192242 400 LKDLNIKIPEGALVAVVGQVGSGKSSVLSAIL--GEMEKLKGIVQRKG 445
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLINETLykALARKLNGAKKVPG 672
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
508-596 |
8.48e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 40.07 E-value: 8.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 508 SGGQKHRVCLARAVYSGADIYLLDDPLSAVDVHVAKQLFEKVIGssgmLRNKTR---ILVTHNLTLLPQM-DLIVVMESG 583
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKS----LQQKHQlayLFISHDLHVVRALcHQVIVLRQG 502
|
90
....*....|...
gi 1387192242 584 RVAQMGTYQEILA 596
Cdd:PRK15134 503 EVVEQGDCERVFA 515
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1015-1210 |
8.59e-03 |
|
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: 39.05 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1015 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCL-----FRIVERSGGKIIIDGIDISTiglhDLRGKLNII--PQDPVLFSG 1087
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTImghpkYEVTEGEILFKGEDITDLPP----EERARLGIFlaFQYPPEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1088 TlqmnldpldkypdhelwevlelcHLKEFVQSLpkkllheisegGENLSVGQRQLVCLARALLRKTKILILDEATASIDF 1167
Cdd:cd03217 92 V-----------------------KNADFLRYV-----------NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1387192242 1168 ETDNLVQTTVRKEFS-DCTILTIAH--RLHSIIDSDRVLVLDSGRI 1210
Cdd:cd03217 138 DALRLVAEVINKLREeGKSVLIITHyqRLLDYIKPDRVHVLYDGRI 183
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1014-1211 |
8.68e-03 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 39.09 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERSGGKIIIDGIDISTIGLHD---LRGKLNIIPQD--------- 1081
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDhhllmdrtv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 1082 ------PVLFSGTlqmNLDPLDKYPDHELWEVLELCHLKEF-VQslpkkllheiseggenLSVGQRQLVCLARALLRKTK 1154
Cdd:PRK10908 97 ydnvaiPLIIAGA---SGDDIRRRVSAALDKVGLLDKAKNFpIQ----------------LSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387192242 1155 ILILDEATASID----------FETDNLVQTTVRKEFSDCTIltIAHRlhsiidSDRVLVLDSGRIT 1211
Cdd:PRK10908 158 VLLADEPTGNLDdalsegilrlFEEFNRVGVTVLMATHDIGL--ISRR------SYRMLTLSDGHLH 216
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1014-1043 |
8.85e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.41 E-value: 8.85e-03
10 20 30
....*....|....*....|....*....|
gi 1387192242 1014 ALQDITFQTHGEEKIGIVGRTGAGKSTLSN 1043
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSN 68
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1134-1178 |
9.05e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 39.09 E-value: 9.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1387192242 1134 NLSVGQRQLVCLARALLRKTKILILDEATASIDFETDNLVQTTVR 1178
Cdd:PRK13539 127 YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIR 171
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
410-589 |
9.28e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 40.22 E-value: 9.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 410 GALVAVVGQVGSGKSSVLSAILGEMEKLKGIV----QRKGSVAYVSQQAWIQN--CILQE-------------------- 463
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIifngQRIDTLSPGKLQALRRDiqFIFQDpyasldprqtvgdsimeplr 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387192242 464 --NILFGSVMQKQLYErVLEACALLPDLE-QLPNgdqteigekgvNISGGQKHRVCLARAVYSGADIYLLDDPLSAVDVH 540
Cdd:PRK10261 430 vhGLLPGKAAAARVAW-LLERVGLLPEHAwRYPH-----------EFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387192242 541 VAKQLFEkvigssgMLRNKTR------ILVTHNLTLLPQMD-LIVVMESGRVAQMG 589
Cdd:PRK10261 498 IRGQIIN-------LLLDLQRdfgiayLFISHDMAVVERIShRVAVMYLGQIVEIG 546
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
1027-1047 |
9.98e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 37.21 E-value: 9.98e-03
|
| |
