|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
258-1630 |
1.14e-123 |
|
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: 431.36 E-value: 1.14e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 258 CFLFFCIIRFSPLTYYISAGVTRERK-KMKGLMAVMGLRDSAFWLSWGLLYGVIVFVVTLLSTTIVKLVQFVFLTGFMVI 336
Cdd:TIGR01257 654 CFPIFMVLAWIYSVSMTVKSIVLEKElRLKETLKNQGVSNAVIWCTWFLDSFSIMSMSIFLLTIFIMHGRILHYSDPFIL 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 337 FSLFFFYGLSLISLSFLMSVLLKKSFLTdlvvflltVSCGSLGFTALYryLP------------VSLEWLLSLLSPFAFM 404
Cdd:TIGR01257 734 FLFLLAFSTATIMQCFLLSTFFSKASLA--------AACSGVIYFTLY--LPhilcfawqdrmtADLKTAVSLLSPVAFG 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 405 LGMVQLLRLDYD------VNSNADPM-GNPNEVIGTIFMLFFDGVFYLLLTFYFEKVLPSEYGRRHPPLFFLKSSFWSG- 476
Cdd:TIGR01257 804 FGTEYLVRFEEQglglqwSNIGNSPLeGDEFSFLLSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWLGg 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 477 ---QNPANRTALDNETDYEFSDDSFEPVSME--FHGKE------AIRIRNLTKDYiQKSKRTeALKDLTLDVYKGQITAI 545
Cdd:TIGR01257 884 egcSTREERALEKTEPLTEEMEDPEHPEGINdsFFERElpglvpGVCVKNLVKIF-EPSGRP-AVDRLNITFYENQITAF 961
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 546 LGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSemTDLENISKLTGVCPQCNVQFDFLTVRENLRLFAKIKGIQAHEVD 625
Cdd:TIGR01257 962 LGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE--TNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQ 1039
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 626 NEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRVVLFSTQF 705
Cdd:TIGR01257 1040 LEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHH 1119
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 706 MDEADILADRKVFISKGKLKCAGSSLFLKKKWGIGYHLSL-----------------------QLSETC----------- 751
Cdd:TIGR01257 1120 MDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLvrkmkniqsqrggcegtcsctskGFSTRCparvdeitpeq 1199
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 752 -----VHErITSLVKQHIPDSKLSAESEGKLSYILPLE--RTNKFPDLYRDLERS-PDLGIENYGVSITTLTEVFLKLEG 823
Cdd:TIGR01257 1200 vldgdVNE-LMDLVYHHVPEAKLVECIGQELIFLLPNKnfKQRAYASLFRELEETlADLGLSSFGISDTPLEEIFLKVTE 1278
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 824 KSSIDQSDIGMTEDVQAG-GARSP-----ERFAEVEQ---------LVSLLNGR---------CKMKGGMALWWQQLCAV 879
Cdd:TIGR01257 1279 DADSGSLFAGGAQQKRENaNLRHPcsgptEKAGQTPQashtcspgqPAAHPEGQpppepedpgVPLNTGARLILQHVQAL 1358
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 880 TRLRFlklKHERKSIVILILVLGIGLLHILSANIYRMVRQ--SDY-CWELAPHMY-----FL------------------ 933
Cdd:TIGR01257 1359 LVKRF---QHTIRSHKDFLAQIVLPATFVFLALMLSIIIPpfGEYpALTLHPWMYgqqytFFsmdepnsehlevladvll 1435
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 934 -----------------------TPGQQP--QPPLTNLLIVNKTGA---------------------------------- 954
Cdd:TIGR01257 1436 nkpgfgnrclkeewlpeypcgnsTPWKTPsvSPNITHLFQKQKWTAahpspscrcstrekltmlpecpegagglpppqrt 1515
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 955 -KIDDFIHSLEQQNI---------ALEVDAFGTRNGTEDSQYNG--------AIILSGD--------------------- 995
Cdd:TIGR01257 1516 qRSTEILQDLTDRNIsdflvktypALIRSSLKSKFWVNEQRYGGisiggklpAIPITGEalvgflsdlgqmmnvsggpvt 1595
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 996 --------------EKNYNFTLACNTKRLNCFPVLVDIVSNGLLglfapSAHIQTDRStfPEE----------NDHRK-- 1049
Cdd:TIGR01257 1596 reaskempdflkhlETEDNIKVWFNNKGWHALVSFLNVAHNAIL-----RASLPKDRD--PEEygitvisqplNLTKEql 1668
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1050 ---------FDYLAYFFLwVLLMACVPPYISMTSIDDYKNRAQFQLWISGLSPSAYWFGQALFEV---PVYCALILSIFI 1117
Cdd:TIGR01257 1669 seitvlttsVDAVVAICV-IFAMSFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDImnyAVSAGLVVGIFI 1747
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1118 AFYASAPPESKFTVGDLFIQILYvgGYAmsVIFMTYVISFIYRKGRK--------------NSglwSLCFYIVSFFSMCF 1183
Cdd:TIGR01257 1748 GFQKKAYTSPENLPALVALLMLY--GWA--VIPMMYPASFLFDVPSTayvalscanlfigiNS---SAITFVLELFENNR 1820
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1184 MLIDYfrDISLFVLIALVPPATLGGCTLLHFENREFSEIIFEPEREYSYLFF---------LAPLLHFAIFVVILRCMER 1254
Cdd:TIGR01257 1821 TLLRF--NAMLRKLLIVFPHFCLGRGLIDLALSQAVTDVYAQFGEEHSANPFqwdligknlVAMAVEGVVYFLLTLLIQH 1898
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1255 KFGMKTMRTDPVfrISPRSDrvfnnpedpdgEDEDVSQERVWTANALTSADFqekpaIIASCLRKEYKGkkkcfvlksKK 1334
Cdd:TIGR01257 1899 HFFLSRWIAEPA--KEPIFD-----------EDDDVAEERQRIISGGNKTDI-----LRLNELTKVYSG---------TS 1951
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1335 KIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSS----TGDTPGFLGYCPQENALWLNLTVRE 1410
Cdd:TIGR01257 1952 SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiltnISDVHQNMGYCPQFDAIDDLLTGRE 2031
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1411 HLEIFAAIKGMRKSD----ANVAIERLADALkLQDQLKSpvkTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQ 1486
Cdd:TIGR01257 2032 HLYLYARLRGVPAEEiekvANWSIQSLGLSL-YADRLAG---TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1487 QMWQAIQATFSNtERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKEYLLEMKVKTPS-----QVEPLN 1561
Cdd:TIGR01257 2108 MLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSPKddllpDLNPVE 2186
|
1610 1620 1630 1640 1650 1660
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081362 1562 TEIMRLFPQAARQERYSSLMVYKLPREDvqpLSQAFFKLETVKQSFDLEEYSLSQSTLEQVFLELSKEQ 1630
Cdd:TIGR01257 2187 QFFQGNFPGSVQRERHYNMLQFQVSSSS---LARIFQLLISHKDSLLIEEYSVTQTTLDQVFVNFAKQQ 2252
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1317-1538 |
1.03e-86 |
|
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: 282.09 E-value: 1.03e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1317 LRKEYKgkkkcfvlkSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTP----GF 1392
Cdd:cd03263 6 LTKTYK---------KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRkaarQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1393 LGYCPQENALWLNLTVREHLEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVL 1472
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 1473 LDEPSTGMDPEGQQQMWQAIQATFSNteRGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLK 1538
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKG--RSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
511-734 |
1.21e-82 |
|
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: 270.53 E-value: 1.21e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGwvTIHNNKLSEMTDLENISKL 590
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSG--TAYINGYSIRTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFL 670
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081362 671 LDEPTAGLDPFSRHRVWNFLKERRADRVVLFSTQFMDEADILADRKVFISKGKLKCAGSSLFLK 734
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1317-1541 |
5.06e-73 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 243.43 E-value: 5.06e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1317 LRKEYKGKKkcfvlkskkkiATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTP----GF 1392
Cdd:COG1131 6 LTKRYGDKT-----------ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPaevrRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1393 LGYCPQENALWLNLTVREHLEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVL 1472
Cdd:COG1131 75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081362 1473 LDEPSTGMDPEGQQQMWQAIQAtFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKF 1541
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRE-LAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
511-729 |
9.79e-68 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 228.41 E-value: 9.79e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSemTDLENISKL 590
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA--RDPAEVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFL 670
Cdd:COG1131 75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 671 LDEPTAGLDPFSRHRVWNFLKE-RRADRVVLFSTQFMDEADILADRKVFISKGKLKCAGS 729
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGT 214
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1333-1544 |
2.51e-59 |
|
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: 204.71 E-value: 2.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1333 KKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKG-SSTGDTPGF---LGYCPQENALWLNLTV 1408
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGeDVRKEPREArrqIGVLPDERGLYDRLTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1409 REHLEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1488
Cdd:COG4555 92 RENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 1489 WQAIQAtFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKE 1544
Cdd:COG4555 172 REILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1334-1631 |
8.81e-56 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 196.48 E-value: 8.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1334 KKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSS-TGDTPGFLGYCPQENALWLNLTVREHL 1412
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPlDPEDRRRIGYLPEERGLYPKMKVGEQL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1413 EIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAI 1492
Cdd:COG4152 93 VYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1493 QATfsnTERGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKEYLlemKVKTPSQVEPLNTeimrlFPQ 1570
Cdd:COG4152 173 REL---AAKGTtvIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTL---RLEADGDAGWLRA-----LPG 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081362 1571 AARQERYSSLMVYKLPRE-DVQPLsqaffkLETVKQSFDLEEYSLSQSTLEQVFLELSKEQE 1631
Cdd:COG4152 242 VTVVEEDGDGAELKLEDGaDAQEL------LRALLARGPVREFEEVRPSLNEIFIEVVGEKA 297
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1333-1528 |
3.60e-55 |
|
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: 189.92 E-value: 3.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1333 KKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTP----GFLGYCPQENALWLNLTV 1408
Cdd:cd03230 11 GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPeevkRRIGYLPEEPSLYENLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1409 REHLEifaaikgmrksdanvaierladalklqdqlkspvktLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1488
Cdd:cd03230 91 RENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREF 134
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907081362 1489 WQAIQaTFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1528
Cdd:cd03230 135 WELLR-ELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
511-729 |
1.72e-54 |
|
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: 190.45 E-value: 1.72e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIhNNKLSEMTDLENISKL 590
Cdd:COG4555 2 IEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILI-DGEDVRKEPREARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 tGVCPQCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFL 670
Cdd:COG4555 77 -GVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 671 LDEPTAGLDPFSRHRVWNFLKE-RRADRVVLFSTQFMDEADILADRKVFISKGKLKCAGS 729
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGS 215
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
1337-1626 |
1.35e-53 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 190.29 E-value: 1.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGFL----GYCPQENALWLNLTVREHL 1412
Cdd:TIGR01188 8 AVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVrrsiGIVPQYASVDEDLTGRENL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1413 EIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAI 1492
Cdd:TIGR01188 88 EMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1493 QAtFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKEYlLEMKVKTPSQVEPLNTE-IMRLFP-Q 1570
Cdd:TIGR01188 168 RA-LKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDT-LESRPRDIQSLKVEVSMlIAELGEtG 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 1571 AARQERYSSLMVYKLPREDVQPLSQAFFKlETVKQSFDLEEYSLSQSTLEQVFLEL 1626
Cdd:TIGR01188 246 LGLLAVTVDSDRIKILVPDGDETVPEIVE-AAIRNGIRIRSISTERPSLDDVFLKL 300
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
511-724 |
1.01e-52 |
|
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: 182.60 E-value: 1.01e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEmtDLENISKL 590
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK--EPEEVKRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVQFDFLTVRENLRLfakikgiqahevdnevqrvlleldmkntqnilvqnlSGGQKRKLTFGIAILGDPQIFL 670
Cdd:cd03230 75 IGYLPEEPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 671 LDEPTAGLDPFSRHRVWNFLKERRADRV-VLFSTQFMDEADILADRKVFISKGKL 724
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKtILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1337-1538 |
2.22e-51 |
|
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: 180.64 E-value: 2.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKG----SSTGDTPGFLGYCPQENALWLNLTVREHL 1412
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvREPREVRRRIGIVFQDLSVDDELTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1413 EIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW--- 1489
Cdd:cd03265 95 YIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWeyi 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907081362 1490 QAIQATFSNTergALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLK 1538
Cdd:cd03265 175 EKLKEEFGMT---ILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1311-1554 |
3.94e-48 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 175.28 E-value: 3.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1311 AIIASCLRKEYKGKKKCFVLKS----------KKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVL 1380
Cdd:COG4586 1 IIEVENLSKTYRVYEKEPGLKGalkglfrreyREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1381 lkgsstgdtpgFLGYCP----------------QENALWLNLTVREHLEIFAAIKGMRKSDANVAIERLADALKLQDQLK 1444
Cdd:COG4586 81 -----------VLGYVPfkrrkefarrigvvfgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1445 SPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQATfsNTERGA--LLTTHYMAEAEAVCDRVAI 1522
Cdd:COG4586 150 TPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEY--NRERGTtiLLTSHDMDDIEALCDRVIV 227
|
250 260 270
....*....|....*....|....*....|..
gi 1907081362 1523 MVSGRLRCIGSIQHLKSKFGKEYLLEMKVKTP 1554
Cdd:COG4586 228 IDHGRIIYDGSLEELKERFGPYKTIVLELAEP 259
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1335-1532 |
1.25e-47 |
|
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: 169.77 E-value: 1.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1335 KIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPG-FLGYCPQENALWLNLTVREHLE 1413
Cdd:cd03269 13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARnRIGYLPEERGLYPKMKVIDQLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1414 IFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQ 1493
Cdd:cd03269 93 YLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIR 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907081362 1494 ATFSNtERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1532
Cdd:cd03269 173 ELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1315-1529 |
5.13e-47 |
|
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: 167.78 E-value: 5.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1315 SCLRKEYKGKKkcfVLKskkkiatrNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGFL- 1393
Cdd:cd03268 4 NDLTKTYGKKR---VLD--------DISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1394 --GYCPQENALWLNLTVREHLEIFAAIKGMRKSDanvaIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVV 1471
Cdd:cd03268 73 riGALIEAPGFYPNLTARENLRLLARLLGIRKKR----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081362 1472 LLDEPSTGMDPEGQQQMWQAIQAtFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLR 1529
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILS-LRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
511-725 |
7.87e-47 |
|
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: 167.37 E-value: 7.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqksKRTEALKDLTLDVYKGqITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDleNISKL 590
Cdd:cd03264 1 LQLENLTKRY----GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ--KLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQcnvQFDF---LTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQ 667
Cdd:cd03264 74 IGYLPQ---EFGVypnFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081362 668 IFLLDEPTAGLDPFSRHRVWNFLKERRADRVVLFSTQFMDEADILADRKVFISKGKLK 725
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1333-1529 |
5.89e-45 |
|
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: 161.98 E-value: 5.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1333 KKKIATRNISFCVRKGeVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTP----GFLGYCPQENALWLNLTV 1408
Cdd:cd03264 11 GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPqklrRRIGYLPQEFGVYPNFTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1409 REHLEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEgqqqm 1488
Cdd:cd03264 90 REFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE----- 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907081362 1489 wQAIQatFSN------TERGALLTTHYMAEAEAVCDRVAIMVSGRLR 1529
Cdd:cd03264 165 -ERIR--FRNllselgEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
511-734 |
5.00e-44 |
|
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: 159.84 E-value: 5.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQkskrTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIhnNKLSEMTDLENISKL 590
Cdd:cd03265 1 IEVENLVKKYGD----FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATV--AGHDVVREPREVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFL 670
Cdd:cd03265 75 IGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 671 LDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEADILADRKVFISKGKLKCAGSSLFLK 734
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
511-724 |
2.73e-43 |
|
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: 157.65 E-value: 2.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTD------- 583
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEkelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 584 LENIskltGVCPQcnvQF---DFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGI 660
Cdd:cd03255 81 RRHI----GFVFQ---SFnllPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 661 AILGDPQIFLLDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEADiLADRKVFISKGKL 724
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
512-723 |
2.91e-43 |
|
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: 157.24 E-value: 2.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 512 RIRNLTKDYiqKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEmTDLENISKLT 591
Cdd:cd03225 1 ELKNLSFSY--PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTK-LSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 592 GVCPQ-CNVQFDFLTVRENLrLFA-KIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIF 669
Cdd:cd03225 78 GLVFQnPDDQFFGPTVEEEV-AFGlENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 670 LLDEPTAGLDPFSRHRVWNFLKERRADRV-VLFSTQFMDEADILADRKVFISKGK 723
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKtIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
511-729 |
3.99e-43 |
|
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: 157.49 E-value: 3.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqkSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEmTDLENISKL 590
Cdd:COG1122 1 IELENLSFSY---PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK-KNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQcN--VQFDFLTVRENLrLFA-KIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLtfgiAILG--- 664
Cdd:COG1122 77 VGLVFQ-NpdDQLFAPTVEEDV-AFGpENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRV----AIAGvla 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081362 665 -DPQIFLLDEPTAGLDPFSRHRVWNFLKE-RRADRVVLFSTQFMDEADILADRKVFISKGKLKCAGS 729
Cdd:COG1122 151 mEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
527-823 |
5.41e-43 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 159.48 E-value: 5.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 527 TEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIhnNKLSEMTDLENISKLTGVCPQCNVQFDFLTV 606
Cdd:TIGR01188 6 FKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARV--AGYDVVREPRKVRRSIGIVPQYASVDEDLTG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 607 RENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRV 686
Cdd:TIGR01188 84 RENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 687 WNFL-KERRADRVVLFSTQFMDEADILADRKVFISKGKLKCAGSSLFLKKKWGiGYHLSLQLSETCVHERITSLVKQHIP 765
Cdd:TIGR01188 164 WDYIrALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLG-KDTLESRPRDIQSLKVEVSMLIAELG 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081362 766 DSKLSAESEGKLS---YILPLERTNKFPDLYRDLERSpdlGIENYGVSIT--TLTEVFLKLEG 823
Cdd:TIGR01188 243 ETGLGLLAVTVDSdriKILVPDGDETVPEIVEAAIRN---GIRIRSISTErpSLDDVFLKLTG 302
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
511-728 |
1.29e-42 |
|
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: 155.60 E-value: 1.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTI-----HNNKLSEMTDLE 585
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVdgfdvVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 586 NISKLTGVcpqcnvqFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGD 665
Cdd:cd03266 82 FVSDSTGL-------YDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081362 666 PQIFLLDEPTAGLDPFSRHRVWNFLKE-RRADRVVLFSTQFMDEADILADRKVFISKGKLKCAG 728
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQlRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1326-1532 |
5.13e-42 |
|
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: 153.68 E-value: 5.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1326 KCFVLKSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTP----GFLGYCPQENA 1401
Cdd:cd03266 9 KRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPaearRRLGFVSDSTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1402 LWLNLTVREHLEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMD 1481
Cdd:cd03266 89 LYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 1482 PEGQQQMWQAIQAtFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1532
Cdd:cd03266 169 VMATRALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
511-724 |
7.06e-41 |
|
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: 150.06 E-value: 7.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKskrtEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIhnnKLSEMTDLENISKL 590
Cdd:cd03268 1 LKTNDLTKTYGKK----RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF---DGKSYQKNIEALRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVQFDFLTVRENLRLFAKIKGIQahevDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFL 670
Cdd:cd03268 74 IGALIEAPGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 671 LDEPTAGLDPFSRHRVWNFL-KERRADRVVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
508-724 |
3.07e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 146.34 E-value: 3.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 508 KEAIRIRNLTKDYIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTD---- 583
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSErela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 584 ---LENIskltGVCPQcnvQF---DFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQK---- 653
Cdd:COG1136 82 rlrRRHI----GFVFQ---FFnllPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQqrva 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 654 --RkltfgiAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEADIlADRKVFISKGKL 724
Cdd:COG1136 155 iaR------ALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAAR-ADRVIRLRDGRI 222
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1335-1633 |
4.52e-39 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 148.41 E-value: 4.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1335 KIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTgdtPGF-------LGYCPQENALWLNLT 1407
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV---PSRarharqrVGVVPQFDNLDPDFT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1408 VREHLEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1487
Cdd:PRK13537 97 VRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1488 MWQAIQATFSnteRGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL-KSKFGKEyLLEMKVKTPsqvEPLNTEi 1564
Cdd:PRK13537 177 MWERLRSLLA---RGKtiLLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALiESEIGCD-VIEIYGPDP---VALRDE- 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1565 mrLFPQAARQE-RYSSLMVYKlprEDVQPLsqaffkLETVKQSFDLeEYSLSQSTLEQVFLELSKEQELD 1633
Cdd:PRK13537 249 --LAPLAERTEiSGETLFCYV---RDPEPL------HARLKGRAGL-RYLHRPANLEDVFLRLTGREMQD 306
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1305-1528 |
4.76e-39 |
|
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: 145.94 E-value: 4.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1305 DFQEKPAIIASCLRKEYKGKKKcfvlkskKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGS 1384
Cdd:cd03267 11 RVYSKEPGLIGSLKSLFKRKYR-------EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1385 STGD-TPGFL-------GycpQENALWLNLTVREHLEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKR 1456
Cdd:cd03267 84 VPWKrRKKFLrrigvvfG---QKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081362 1457 KLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQATfsNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1528
Cdd:cd03267 161 RAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEY--NRERGTtvLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1339-1508 |
6.50e-39 |
|
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: 144.54 E-value: 6.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTP----GFLGYCPQENALWLNLTVREHLEI 1414
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARedyrRRLAYLGHADGLKPELTVRENLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1415 FAAIKGMRKSDAnvAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQA 1494
Cdd:COG4133 99 WAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
170
....*....|....*.
gi 1907081362 1495 tfsNTERG--ALLTTH 1508
Cdd:COG4133 177 ---HLARGgaVLLTTH 189
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
530-676 |
2.15e-38 |
|
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: 140.86 E-value: 2.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 530 LKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSeMTDLENISKLTGVCPQCNVQFDFLTVREN 609
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT-DDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 610 LRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQN----LSGGQKRKLTFGIAILGDPQIFLLDEPTA 676
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
511-721 |
1.06e-37 |
|
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: 141.46 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEmtdlenISKL 590
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG------PGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFL 670
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907081362 671 LDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEADILADRKVFISK 721
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
254-821 |
6.50e-37 |
|
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: 153.25 E-value: 6.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 254 TTTDCFLFFCII---RFSPLTYYISagVTRER-KKMKGLMAVMGLRDSAFWLSwGLLYGVIVFVVTllsttiVKLVQFVF 329
Cdd:TIGR01257 1676 TSVDAVVAICVIfamSFVPASFVLY--LIQERvNKAKHLQFISGVSPTTYWLT-NFLWDIMNYAVS------AGLVVGIF 1746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 330 LtGFM-----------VIFSLFFFYGLSLISLSFLMSVLLK------------------KSFLTDLVVFLLTVSCGSLGF 380
Cdd:TIGR01257 1747 I-GFQkkaytspenlpALVALLMLYGWAVIPMMYPASFLFDvpstayvalscanlfigiNSSAITFVLELFENNRTLLRF 1825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 381 TALYRYLPVSLEWllsllspFAFMLGMVQLLR----LDYDVNSNADPMGNPN--EVIG-TIFMLFFDGVFYLLLTFYFEk 453
Cdd:TIGR01257 1826 NAMLRKLLIVFPH-------FCLGRGLIDLALsqavTDVYAQFGEEHSANPFqwDLIGkNLVAMAVEGVVYFLLTLLIQ- 1897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 454 vlpseygrRHpplFFLksSFWSGQnPANRTALDNETDYEfsdDSFEPVSMEFHGKEAIRIRNLTKDYIQKSkrTEALKDL 533
Cdd:TIGR01257 1898 --------HH---FFL--SRWIAE-PAKEPIFDEDDDVA---EERQRIISGGNKTDILRLNELTKVYSGTS--SPAVDRL 1958
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 534 TLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLseMTDLENISKLTGVCPQCNVQFDFLTVRENLRLF 613
Cdd:TIGR01257 1959 CVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTNISDVHQNMGYCPQFDAIDDLLTGREHLYLY 2036
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 614 AKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWN-FLKE 692
Cdd:TIGR01257 2037 ARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNtIVSI 2116
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 693 RRADRVVLFSTQFMDEADILADRKVFISKGKLKCAGSSLFLKKKWGIGYHLSLQLSETCVH-----ERITSLVKQHIPDS 767
Cdd:TIGR01257 2117 IREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSPKDDllpdlNPVEQFFQGNFPGS 2196
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 768 KLSAESEGKLSYILPlerTNKFPDLYRDLERSPD-LGIENYGVSITTLTEVFLKL 821
Cdd:TIGR01257 2197 VQRERHYNMLQFQVS---SSSLARIFQLLISHKDsLLIEEYSVTQTTLDQVFVNF 2248
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
511-728 |
7.54e-37 |
|
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: 138.57 E-value: 7.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEmtdlENISKL 590
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI----AARNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 tGVCPQCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFL 670
Cdd:cd03269 73 -GYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081362 671 LDEPTAGLDPFSRHRVWNFLKE-RRADRVVLFSTQFMDEADILADRKVFISKGKLKCAG 728
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
510-722 |
1.17e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 139.84 E-value: 1.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEmtdlenISK 589
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG------PGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 LTGVCPQCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLtfGIA--ILGDPQ 667
Cdd:COG1116 81 DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRV--AIAraLANDPE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081362 668 IFLLDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEADILADRKVFISKG 722
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1311-1527 |
3.27e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 141.12 E-value: 3.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1311 AIIASCLRKEYKGKkkcfvlkskkkIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTP 1390
Cdd:PRK13536 41 AIDLAGVSKSYGDK-----------AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1391 GF----LGYCPQENALWLNLTVREHLEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILG 1466
Cdd:PRK13536 110 RLararIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALIN 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081362 1467 NPSVVLLDEPSTGMDPEGQQQMWQAIQATFSnteRGA--LLTTHYMAEAEAVCDRVAIMVSGR 1527
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRSLLA---RGKtiLLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
512-723 |
5.20e-36 |
|
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: 134.29 E-value: 5.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 512 RIRNLTKDYIQKskrtEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMtDLENISKLT 591
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKL-PLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 592 GVCPQcnvqfdfltvrenlrlfakikgiqahevdnevqrvlleldmkntqnilvqnLSGGQKRKLTFGIAILGDPQIFLL 671
Cdd:cd00267 76 GYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907081362 672 DEPTAGLDPFSRHRVWNFLKERRADRV-VLFSTQFMDEADILADRKVFISKGK 723
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRtVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
511-723 |
8.04e-36 |
|
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: 135.68 E-value: 8.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqkSKRTeALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLENiSKL 590
Cdd:COG4133 3 LEAENLSCRR---GERL-LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYR-RRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVqFDFLTVRENLRLFAKIKGIQAHEVDneVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFL 670
Cdd:COG4133 78 AYLGHADGL-KPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907081362 671 LDEPTAGLDPFSRHRVWNFLKERRAD-RVVLFSTQfmDEADILADRKVFISKGK 723
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARgGAVLLTTH--QPLELAAARVLDLGDFK 206
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1339-1478 |
2.63e-35 |
|
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: 132.00 E-value: 2.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKG-SSTGDTPGFL----GYCPQENALWLNLTVREHLE 1413
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqDLTDDERKSLrkeiGYVFQDPQLFPRLTVRENLR 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081362 1414 IFAAIKGMRKSDANVAIERLADALKLQDQLKSPV----KTLSEGVKRKLCFVLSILGNPSVVLLDEPST 1478
Cdd:pfam00005 82 LGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1327-1527 |
3.98e-35 |
|
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: 133.75 E-value: 3.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1327 CFVLKSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTP-----GFLGYCPQ--E 1399
Cdd:cd03225 6 SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSlkelrRKVGLVFQnpD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1400 NALwLNLTVREHLEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCfVLSIL-GNPSVVLLDEPST 1478
Cdd:cd03225 86 DQF-FGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVA-IAGVLaMDPDILLLDEPTA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907081362 1479 GMDPEGQQQMWQAIqATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1527
Cdd:cd03225 164 GLDPAGRRELLELL-KKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
511-723 |
5.73e-35 |
|
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: 131.74 E-value: 5.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMtDLENISKL 590
Cdd:cd03228 1 IEFKNVSFSY--PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDL-DLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVQFDFlTVRENLrlfakikgiqahevdnevqrvlleldmkntqnilvqnLSGGQKRKLTFGIAILGDPQIFL 670
Cdd:cd03228 78 IAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907081362 671 LDEPTAGLDPFSRHRVWNFLKERRADRVVLFSTQFMDEADiLADRKVFISKGK 723
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
511-724 |
8.74e-35 |
|
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: 133.78 E-value: 8.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqkSKRTeALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMT--DLENIS 588
Cdd:cd03261 1 IELRGLTKSF---GGRT-VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 589 KLTGVCPQCNVQFDFLTVREN----LRLFAKIKgiqAHEVDnevQRVLLELDM---KNTQNILVQNLSGGQKRKLTFGIA 661
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENvafpLREHTRLS---EEEIR---EIVLEKLEAvglRGAEDLYPAELSGGMKKRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 662 ILGDPQIFLLDEPTAGLDPFSRHRVWNF---LKERRADRVVLFSTQfMDEADILADRKVFISKGKL 724
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLirsLKKELGLTSIMVTHD-LDTAFAIADRIAVLYDGKI 215
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1339-1548 |
9.16e-35 |
|
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: 133.23 E-value: 9.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPG-----FLGYCPQ--ENALwLNLTVREh 1411
Cdd:COG1122 18 DDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLrelrrKVGLVFQnpDDQL-FAPTVEE- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1412 lEI-FAAI-KGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCF--VLSIlgNPSVVLLDEPSTGMDPEGQQQ 1487
Cdd:COG1122 96 -DVaFGPEnLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIagVLAM--EPEVLVLDEPTAGLDPRGRRE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 1488 MWQAIQAtFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLkskFGKEYLLE 1548
Cdd:COG1122 173 LLELLKR-LNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV---FSDYELLE 229
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
510-729 |
1.12e-34 |
|
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: 134.02 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLEnISK 589
Cdd:COG1120 1 MLEAENLSVGY----GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE-LAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 LTGVCPQ-CNVQFDFlTVRENLRL--FAKIKGIQAH-EVDNE-VQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILG 664
Cdd:COG1120 76 RIAYVPQePPAPFGL-TVRELVALgrYPHLGLFGRPsAEDREaVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081362 665 DPQIFLLDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEADILADRKVFISKGKLKCAGS 729
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1312-1533 |
1.49e-34 |
|
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: 133.05 E-value: 1.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1312 IIASCLRKEYKGKKkcfvlkskkkiATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPG 1391
Cdd:cd03218 1 LRAENLSKRYGKRK-----------VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1392 F------LGYCPQENALWLNLTVREHLEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSIL 1465
Cdd:cd03218 70 HkrarlgIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081362 1466 GNPSVVLLDEPSTGMDPEGQQQMwQAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1533
Cdd:cd03218 150 TNPKFLLLDEPFAGVDPIAVQDI-QKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGT 216
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
511-724 |
1.53e-34 |
|
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: 132.84 E-value: 1.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKSKRT-----------------EALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTI 573
Cdd:cd03267 1 IEVSNLSKSYRVYSKEPgligslkslfkrkyrevEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 574 HNNKLSEMTD--LENISKLTGVCPQcnVQFDfLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGG 651
Cdd:cd03267 81 AGLVPWKRRKkfLRRIGVVFGQKTQ--LWWD-LPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 652 QKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADR--VVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:cd03267 158 QRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1337-1527 |
1.58e-34 |
|
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: 132.56 E-value: 1.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGF------LGYCPQENALWLNLTVRE 1410
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHeraragIGYVPEGRRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1411 HLEIFAAIKGMRKSDAnvAIERLADAL-KLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW 1489
Cdd:cd03224 95 NLLLGAYARRRAKRKA--RLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIF 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907081362 1490 QAIQaTFSNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1527
Cdd:cd03224 173 EAIR-ELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
511-749 |
1.18e-33 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 131.40 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKSKRteALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLENISKL 590
Cdd:TIGR04520 1 IEVENVSFSYPESEKP--ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQcNV--QFDFLTVR-------ENLrlfakikGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKltfgIA 661
Cdd:TIGR04520 79 VGMVFQ-NPdnQFVGATVEddvafglENL-------GVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQR----VA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 662 ILG----DPQIFLLDEPTAGLDPFSRHRVWNFLKERRADR--VVLFSTQFMDEAdILADRKVFISKGKLKCAGS--SLFL 733
Cdd:TIGR04520 147 IAGvlamRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEA-VLADRVIVMNKGKIVAEGTprEIFS 225
|
250 260
....*....|....*....|....
gi 1907081362 734 K----KKWGIG----YHLSLQLSE 749
Cdd:TIGR04520 226 QvellKEIGLDvpfiTELAKALKK 249
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1312-1533 |
1.48e-33 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 130.15 E-value: 1.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1312 IIASCLRKEYKGKKkcfVLKskkkiatrNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTP- 1390
Cdd:COG1137 4 LEAENLVKSYGKRT---VVK--------DVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPm 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1391 ------GfLGYCPQENALWLNLTVREHLEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSI 1464
Cdd:COG1137 73 hkrarlG-IGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 1465 LGNPSVVLLDEPSTGMDP----EgqqqmwqaIQATFSN-TERGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1533
Cdd:COG1137 152 ATNPKFILLDEPFAGVDPiavaD--------IQKIIRHlKERGIgvLITDHNVRETLGICDRAYIISEGKVLAEGT 219
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
510-723 |
2.25e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 131.85 E-value: 2.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYIQKSkrteALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLENISk 589
Cdd:PRK13537 7 PIDFRNVEKRYGDKL----VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 lTGVCPQC-NVQFDFlTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQI 668
Cdd:PRK13537 82 -VGVVPQFdNLDPDF-TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 669 FLLDEPTAGLDPFSRHRVWNFLKERRA-DRVVLFSTQFMDEADILADRKVFISKGK 723
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLArGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1334-1532 |
2.53e-33 |
|
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: 128.79 E-value: 2.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1334 KKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTP---GFLGYCPQENALWLNLTVRE 1410
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPperRNIGMVFQDYALFPHLTVAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1411 HLEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQ 1490
Cdd:cd03259 92 NIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELRE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907081362 1491 AIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1532
Cdd:cd03259 172 ELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1337-1528 |
5.90e-33 |
|
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: 129.00 E-value: 5.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSS-TGDTP------G----FlgycpQENALWLN 1405
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDiTGLPPhriarlGiartF-----QNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1406 LTVREHLEI----------FAAIKGMRKS-----DANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSV 1470
Cdd:COG0411 94 LTVLENVLVaaharlgrglLAALLRLPRArreerEARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1471 VLLDEPSTGMDPEGQQQMWQAIQATfsNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1528
Cdd:COG0411 174 LLLDEPAAGLNPEETEELAELIRRL--RDERGItiLLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
511-724 |
6.34e-33 |
|
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: 128.08 E-value: 6.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEM--TDLENIS 588
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 589 KLTGVCPQcnvQFDFL---TVRENLRLFAKIKGIQAHEVDNEVQRvLLEL-DMKNTQNILVQNLSGGQKRKLTFGIAILG 664
Cdd:cd03258 82 RRIGMIFQ---HFNLLssrTVFENVALPLEIAGVPKAEIEERVLE-LLELvGLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081362 665 DPQIFLLDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
510-729 |
9.73e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 129.84 E-value: 9.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEmTDLENISK 589
Cdd:COG4152 1 MLELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP-EDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 L---TGVCPQcnvqfdfLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDP 666
Cdd:COG4152 76 LpeeRGLYPK-------MKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081362 667 QIFLLDEPTAGLDPFSRHRVWNFLKERRA-DRVVLFSTQFMDEADILADRKVFISKGKLKCAGS 729
Cdd:COG4152 149 ELLILDEPFSGLDPVNVELLKDVIRELAAkGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGS 212
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
510-723 |
1.05e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 131.11 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYIQKSkrteALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLENisK 589
Cdd:PRK13536 41 AIDLAGVSKSYGDKA----VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLAR--A 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 LTGVCPQC-NVQFDFlTVRENLRLFAKIKGIQAHEVDnEVQRVLLEL-DMKNTQNILVQNLSGGQKRKLTFGIAILGDPQ 667
Cdd:PRK13536 115 RIGVVPQFdNLDLEF-TVRENLLVFGRYFGMSTREIE-AVIPSLLEFaRLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081362 668 IFLLDEPTAGLDPFSRHRVWNFLKERRA-DRVVLFSTQFMDEADILADRKVFISKGK 723
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLArGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
511-724 |
2.53e-32 |
|
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: 125.71 E-value: 2.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIhNNKlsEMTDLENISKL 590
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILI-DGR--DVTGVPPERRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFL 670
Cdd:cd03259 74 IGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 671 LDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:cd03259 154 LDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
510-743 |
2.58e-32 |
|
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: 134.51 E-value: 2.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYiqKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMtDLENISK 589
Cdd:COG4987 333 SLELEDVSFRY--PGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDL-DEDDLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 LTGVCPQCNVQFDfLTVRENLRLFAKikgiQAHevDNEVQRVL----LE---------LDMkntqniLV----QNLSGGQ 652
Cdd:COG4987 410 RIAVVPQRPHLFD-TTLRENLRLARP----DAT--DEELWAALervgLGdwlaalpdgLDT------WLgeggRRLSGGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 653 KRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRVVLFSTQFMDEADiLADRKVFISKGKLKCAGSSLF 732
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLE-RMDRILVLEDGRIVEQGTHEE 555
|
250
....*....|.
gi 1907081362 733 LKKKWGIGYHL 743
Cdd:COG4987 556 LLAQNGRYRQL 566
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
511-724 |
3.69e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 125.31 E-value: 3.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKskrtEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMtDLENISKL 590
Cdd:COG4619 1 LELEGLSFRVGGK----PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM-PPPEWRRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVQFDfLTVRENLRLFAKIKGIQA--HEVDNEVQRVLLELDMKNTQnilVQNLSGGQKRKLTFGIAILGDPQI 668
Cdd:COG4619 76 VAYVPQEPALWG-GTVRDNLPFPFQLRERKFdrERALELLERLGLPPDILDKP---VERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081362 669 FLLDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1337-1528 |
3.78e-32 |
|
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: 126.01 E-value: 3.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSS-TGDTP------GfLGYCPQENALWLNLTVR 1409
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDiTGLPPheiarlG-IGRTFQIPRLFPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1410 EHLEI----------FAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTG 1479
Cdd:cd03219 94 ENVMVaaqartgsglLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907081362 1480 MDPEGQQQMWQAIQAtFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1528
Cdd:cd03219 174 LNPEETEELAELIRE-LRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
514-724 |
7.73e-32 |
|
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: 123.82 E-value: 7.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 514 RNLTK--DYIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGL--CVPTKGWVTIhNNKlseMTDLENISK 589
Cdd:cd03213 7 RNLTVtvKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLI-NGR---PLDKRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 LTGVCPQCNVQFDFLTVRENLRLFAKIKGIqahevdnevqrvlleldmkntqnilvqnlSGGQKRKLTFGIAILGDPQIF 669
Cdd:cd03213 83 IIGYVPQDDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLL 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081362 670 LLDEPTAGLDPFSRHRVWNFLKeRRAD--RVVLFST-QFMDEADILADRKVFISKGKL 724
Cdd:cd03213 134 FLDEPTSGLDSSSALQVMSLLR-RLADtgRTIICSIhQPSSEIFELFDKLLLLSQGRV 190
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
510-729 |
2.07e-31 |
|
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: 131.42 E-value: 2.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYIQkskRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMtDLENISK 589
Cdd:COG4988 336 SIELEDVSFSYPG---GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDL-DPASWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 LTGVCPQcNVQFDFLTVRENLRLFAK-------IKGIQAHEVDNEVQRVLLELDMKntqnilV----QNLSGGQKRKLTF 658
Cdd:COG4988 412 QIAWVPQ-NPYLFAGTIRENLRLGRPdasdeelEAALEAAGLDEFVAALPDGLDTP------LgeggRGLSGGQAQRLAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081362 659 GIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRVVLFSTQfmDEADI-LADRKVFISKGKLKCAGS 729
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITH--RLALLaQADRILVLDDGRIVEQGT 554
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1330-1527 |
2.46e-31 |
|
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: 120.81 E-value: 2.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1330 LKSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGF-----LGYCPQenalwl 1404
Cdd:cd00267 7 FRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEelrrrIGYVPQ------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1405 nltvrehleifaaikgmrksdanvaierladalklqdqlkspvktLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEG 1484
Cdd:cd00267 81 ---------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPAS 115
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907081362 1485 QQQMWQAIQAtFSNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1527
Cdd:cd00267 116 RERLLELLRE-LAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
511-723 |
3.75e-31 |
|
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: 121.14 E-value: 3.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKskrtEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTD-LENISK 589
Cdd:cd03229 1 LELKNVSKRYGQK----TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDeLPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 LTGVCPQCNVQFDFLTVRENLRLfakikgiqahevdnevqrvlleldmkntqnilvqNLSGGQKRKLTFGIAILGDPQIF 669
Cdd:cd03229 77 RIGMVFQDFALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 670 LLDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEADILADRKVFISKGK 723
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSlqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
511-724 |
3.84e-31 |
|
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: 122.67 E-value: 3.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKskrtEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGL-----CVPTKGWVTIHN-NKLSEMTDL 584
Cdd:cd03260 1 IELRDLNVYYGDK----HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGkDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 585 ENISKLTGVCPQCNVQFDfLTVRENLRLFAKIKGIQAHEVDNEVQRVLLEL-----DMKNTQNILvqNLSGGQKRKLTFG 659
Cdd:cd03260 77 LELRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKaalwdEVKDRLHAL--GLSGGQQQRLCLA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 660 IAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRVVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
511-745 |
7.84e-31 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 123.72 E-value: 7.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKSK-RTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKL--SEMTDLENI 587
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItaKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 588 SKLTGVcpqcnVqFDF-------LTVRE-------NLrlfakikGIQAHEVDNEVQRVLLELDMKntQNILVQN---LSG 650
Cdd:TIGR04521 81 RKKVGL-----V-FQFpehqlfeETVYKdiafgpkNL-------GLSEEEAEERVKEALELVGLD--EEYLERSpfeLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 651 GQKRKltfgIAILG----DPQIFLLDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:TIGR04521 146 GQMRR----VAIAGvlamEPEVLILDEPTAGLDPKGRKEILDLFKRlhKEKGLTVILVTHSMEDVAEYADRVIVMHKGKI 221
|
250 260
....*....|....*....|...
gi 1907081362 725 KCAGSS--LFLKKKWGIGYHLSL 745
Cdd:TIGR04521 222 VLDGTPreVFSDVDELEKIGLDV 244
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
510-743 |
8.45e-31 |
|
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: 131.11 E-value: 8.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYIQKSKrtEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMtDLENISK 589
Cdd:COG2274 473 DIELENVSFRYPGDSP--PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQI-DPASLRR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 LTGVCPQCNVQFdFLTVRENLRLF------------AKIKGIqahevDNEVQRvlleLDMK-NTQnilV----QNLSGGQ 652
Cdd:COG2274 550 QIGVVLQDVFLF-SGTIRENITLGdpdatdeeiieaARLAGL-----HDFIEA----LPMGyDTV---VgeggSNLSGGQ 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 653 KRKLtfGIA--ILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRVVLFSTQfmDEADI-LADRKVFISKGKLKCAGS 729
Cdd:COG2274 617 RQRL--AIAraLLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAH--RLSTIrLADRIIVLDKGRIVEDGT 692
|
250
....*....|....
gi 1907081362 730 SLFLKKKWGIGYHL 743
Cdd:COG2274 693 HEELLARKGLYAEL 706
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
510-729 |
2.16e-30 |
|
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: 121.24 E-value: 2.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMT--DLENI 587
Cdd:COG1127 5 MIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 588 SKLTGVCPQCNVQFDFLTVREN----LRLFAKIKgiqAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLtfGIA-- 661
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENvafpLREHTDLS---EAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRV--ALAra 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081362 662 ILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADR-----VVlfsTQFMDEADILADRKVFISKGKLKCAGS 729
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELgltsvVV---THDLDSAFAIADRVAVLADGKIIAEGT 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
511-723 |
2.31e-30 |
|
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: 120.62 E-value: 2.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTdLENISKL 590
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLP-PHERARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 tGV--CPQCNVQFDFLTVRENLRLFAKIKGIqaHEVDNEVQRVlLEL-----DMKNTqniLVQNLSGGQKRKLTFGIAIL 663
Cdd:cd03224 76 -GIgyVPEGRRIFPELTVEENLLLGAYARRR--AKRKARLERV-YELfprlkERRKQ---LAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 664 GDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRV-VLFSTQFMDEADILADRKVFISKGK 723
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVtILLVEQNARFALEIADRAYVLERGR 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1334-1536 |
3.05e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 120.96 E-value: 3.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1334 KKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGFLGYCPQENAL-W-LNLTVRE- 1410
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVPQRAEVdWdFPITVRDv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1411 -------HLEIFaaiKGMRKSDANVAIERLaDALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1483
Cdd:COG1121 98 vlmgrygRRGLF---RRPSRADREAVDEAL-ERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907081362 1484 GQQQMWQAIQAtFSNTERGALLTTHYMAEAEAVCDRVaIMVSGRLRCIGSIQH 1536
Cdd:COG1121 174 TEEALYELLRE-LRREGKTILVVTHDLGAVREYFDRV-LLLNRGLVAHGPPEE 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1328-1532 |
3.61e-30 |
|
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: 119.94 E-value: 3.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1328 FVLKSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSST---GDTPGFLGycpqenalwl 1404
Cdd:cd03220 28 RKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSsllGLGGGFNP---------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1405 NLTVREHLEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEP-STGmDPE 1483
Cdd:cd03220 98 ELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVlAVG-DAA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907081362 1484 GQQQMWQAIQATFSNTeRGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1532
Cdd:cd03220 177 FQEKCQRRLRELLKQG-KTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1339-1546 |
5.13e-30 |
|
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: 119.70 E-value: 5.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGF------LGYCPQENALWLNLTVREHL 1412
Cdd:COG0410 20 HGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHriarlgIGYVPEGRRIFPSLTVEENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1413 EIFAAIKGMRKSDAnvaiERLADAL----KLQDQLKSPVKTLSEGVKRklcfVLSI----LGNPSVVLLDEPSTGMDPEG 1484
Cdd:COG0410 100 LLGAYARRDRAEVR----ADLERVYelfpRLKERRRQRAGTLSGGEQQ----MLAIgralMSRPKLLLLDEPSLGLAPLI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 1485 QQQMWQAIQATfsnTERGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKS--KFGKEYL 1546
Cdd:COG0410 172 VEEIFEIIRRL---NREGVtiLLVEQNARFALEIADRAYVLERGRIVLEGTAAELLAdpEVREAYL 234
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
510-761 |
7.47e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 122.12 E-value: 7.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYIQKSKRT-----------------EALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVT 572
Cdd:COG4586 1 IIEVENLSKTYRVYEKEPglkgalkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 573 I--HNNKLSEMTDLENISKLTGvcpqcnvQ-----FDfLTVRENLRLFAKIKGIQAHEVDNEVQRV--LLEL-DMKNTQn 642
Cdd:COG4586 81 VlgYVPFKRRKEFARRIGVVFG-------QrsqlwWD-LPAIDSFRLLKAIYRIPDAEYKKRLDELveLLDLgELLDTP- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 643 ilVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADR--VVLFSTQFMDeaDI--LADRKVF 718
Cdd:COG4586 152 --VRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMD--DIeaLCDRVIV 227
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1907081362 719 ISKGKLKCAGSSLFLKKKWGIGYHLSLQLSETCVHERITSLVK 761
Cdd:COG4586 228 IDHGRIIYDGSLEELKERFGPYKTIVLELAEPVPPLELPRGGE 270
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
512-728 |
9.24e-30 |
|
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: 117.15 E-value: 9.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 512 RIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLEnISKLT 591
Cdd:cd03214 1 EVENLSVGY----GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE-LARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 592 GVCPQCNVQFDfltvrenlrlfakikgiqahevdnevqrvLLELDMKNtqnilVQNLSGGQKRKLTFGIAILGDPQIFLL 671
Cdd:cd03214 76 AYVPQALELLG-----------------------------LAHLADRP-----FNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081362 672 DEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEADILADRKVFISKGKLKCAG 728
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
515-724 |
1.02e-29 |
|
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: 118.91 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 515 NLTKDYIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLcVP----TKGWVTIHNNKLSEMTDLENISKL 590
Cdd:cd03234 8 DVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR-VEgggtTSGQILFNGQPRKPDQFQKCVAYV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 tgvcPQCNVQFDFLTVRENLRLFAKIKG--IQAHEVDNEVQRVLLELDMKNTQ--NILVQNLSGGQKRKLTFGIAILGDP 666
Cdd:cd03234 87 ----RQDDILLPGLTVRETLTYTAILRLprKSSDAIRKKRVEDVLLRDLALTRigGNLVKGISGGERRRVSIAVQLLWDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 667 QIFLLDEPTAGLDPFSRHRVWNFLKE-RRADRVVLFSTQfMDEADI--LADRKVFISKGKL 724
Cdd:cd03234 163 KVLILDEPTSGLDSFTALNLVSTLSQlARRNRIVILTIH-QPRSDLfrLFDRILLLSSGEI 222
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
512-725 |
1.07e-29 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 118.13 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 512 RIRNLTKDYiqkSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLENIsklt 591
Cdd:cd03226 1 RIENISFSY---KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSI---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 592 GVCPQ-CNVQFDFLTVRENLRLFAKikgiQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFL 670
Cdd:cd03226 74 GYVMQdVDYQLFTDSVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 671 LDEPTAGLDPFSRHRVWN-FLKERRADRVVLFSTQFMDEADILADRKVFISKGKLK 725
Cdd:cd03226 150 FDEPTSGLDYKNMERVGElIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1339-1533 |
1.10e-29 |
|
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: 119.38 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPG-----FLGYCPQENALWLNLTVRE--- 1410
Cdd:COG1120 18 DDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRrelarRIAYVPQEPPAPFGLTVRElva 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1411 -----HLEIFAaikGMRKSDANV---AIERLaDALKLQDQlksPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDP 1482
Cdd:COG1120 98 lgrypHLGLFG---RPSAEDREAveeALERT-GLEHLADR---PVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 1483 EGQQQMWQAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1533
Cdd:COG1120 171 AHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
510-729 |
2.09e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 118.27 E-value: 2.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEmtDLENISK 589
Cdd:COG1121 6 AIELENLTVSY----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR--ARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 LtgvcPQ-CNVQFDF-LTVRE--------NLRLFAKIKgiqaHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFG 659
Cdd:COG1121 80 V----PQrAEVDWDFpITVRDvvlmgrygRRGLFRRPS----RADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 660 IAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKE-RRADRVVLFSTQFMDEADILADRKVFISKGKLkCAGS 729
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGP 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1335-1532 |
2.10e-29 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 117.25 E-value: 2.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1335 KIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGFLGYCPQ-ENALW-LNLTVRE-- 1410
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQrRSIDRdFPISVRDvv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1411 ------HLEIFAAIKGMRKSDANVAIERLaDALKLQDQlksPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEG 1484
Cdd:cd03235 92 lmglygHKGLFRRLSKADKAKVDEALERV-GLSELADR---QIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907081362 1485 QQQMWQAIqATFSNTERGALLTTHYMAEAEAVCDRVaIMVSGRLRCIG 1532
Cdd:cd03235 168 QEDIYELL-RELRREGMTILVVTHDLGLVLEYFDRV-LLLNRTVVASG 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
511-692 |
4.50e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 116.69 E-value: 4.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqkSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDlENISKL 590
Cdd:COG2884 2 IRFENVSKRY---PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKR-REIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 ---TGVCPQcnvqfDF-----LTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLtfGI-- 660
Cdd:COG2884 78 rrrIGVVFQ-----DFrllpdRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRV--AIar 150
|
170 180 190
....*....|....*....|....*....|..
gi 1907081362 661 AILGDPQIFLLDEPTAGLDPFSRHRVWNFLKE 692
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEE 182
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
510-729 |
7.64e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 117.78 E-value: 7.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYIQKSKrtEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTdLENISK 589
Cdd:PRK13632 7 MIKVENVSFSYPNSEN--NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN-LKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 LTGVCPQC-NVQFDFLTVR-------ENLRL-FAKIKGIqaheVDNEVQRVllelDMKNTQNILVQNLSGGQKRKLTFGI 660
Cdd:PRK13632 84 KIGIIFQNpDNQFIGATVEddiafglENKKVpPKKMKDI----IDDLAKKV----GMEDYLDKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 661 AILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERR--ADRVVLFSTQFMDEAdILADRKVFISKGKLKCAGS 729
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRktRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGK 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
511-680 |
1.11e-28 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 119.03 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHN---NKLSEmTDLENI 587
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGvdlTALSE-RELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 588 SKLTGVCPQcnvQFDFL---TVRENLRLFAKIKGIQAHEVDnevQRV--LLEL----DMKN---TQnilvqnLSGGQKRK 655
Cdd:COG1135 81 RRKIGMIFQ---HFNLLssrTVAENVALPLEIAGVPKAEIR---KRVaeLLELvglsDKADaypSQ------LSGGQKQR 148
|
170 180
....*....|....*....|....*..
gi 1907081362 656 LtfGIA--ILGDPQIFLLDEPTAGLDP 680
Cdd:COG1135 149 V--GIAraLANNPKVLLCDEATSALDP 173
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
510-724 |
1.15e-28 |
|
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: 116.44 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLENisk 589
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 ltgvcpQCNVQFDF----------LTVRENLRLFAKIKGIQahEVDNEVQRVLLELDMknTQNIL---VQNLSGGQKRKL 656
Cdd:COG1124 78 ------RRRVQMVFqdpyaslhprHTVDRILAEPLRIHGLP--DREERIAELLEQVGL--PPSFLdryPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 657 TFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADR--VVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
512-729 |
1.76e-28 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 115.31 E-value: 1.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 512 RIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLENISKLT 591
Cdd:TIGR03410 2 EVSNLNVYY----GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 592 GVCPQCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVqrvlLEL-----DMKNTQNilvQNLSGGQKRKLTFGIAILGDP 666
Cdd:TIGR03410 78 AYVPQGREIFPRLTVEENLLTGLAALPRRSRKIPDEI----YELfpvlkEMLGRRG---GDLSGGQQQQLAIARALVTRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081362 667 QIFLLDEPTAGLDPfS----RHRVWNFLKERRaDRVVLFSTQFMDEADILADRKVFISKGKLKCAGS 729
Cdd:TIGR03410 151 KLLLLDEPTEGIQP-SiikdIGRVIRRLRAEG-GMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
526-703 |
2.17e-28 |
|
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: 114.55 E-value: 2.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 526 RTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMtdleniSKLTGVCPQ-CNVQFDF- 603
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE------RKRIGYVPQrRSIDRDFp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 604 LTVRE--------NLRLFAKIKGIQAHEVDNEVQRVLLElDMKNTQnilVQNLSGGQKRKLTFGIAILGDPQIFLLDEPT 675
Cdd:cd03235 85 ISVRDvvlmglygHKGLFRRLSKADKAKVDEALERVGLS-ELADRQ---IGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180
....*....|....*....|....*....
gi 1907081362 676 AGLDPFSRHRVWNFLKE-RRADRVVLFST 703
Cdd:cd03235 161 AGVDPKTQEDIYELLRElRREGMTILVVT 189
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1326-1527 |
2.32e-28 |
|
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: 114.49 E-value: 2.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1326 KCFVLKSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGFLGYCPQENAL--W 1403
Cdd:cd03293 8 KTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQQDALlpW 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1404 lnLTVREHLEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1483
Cdd:cd03293 88 --LTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907081362 1484 GQQQMWQAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMvSGR 1527
Cdd:cd03293 166 TREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL-SAR 208
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1331-1534 |
2.87e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 115.18 E-value: 2.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1331 KSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTgdTP-----GFLGycpqenalwlN 1405
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVS--ALlelgaGFHP----------E 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1406 LTVREHLEIFAAIKGMRKSDANvaiERLADALK---LQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEP-STGmD 1481
Cdd:COG1134 103 LTGRENIYLNGRLLGLSRKEID---EKFDEIVEfaeLGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVlAVG-D 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907081362 1482 PEGQQQMWQAIQAtFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSI 1534
Cdd:COG1134 179 AAFQKKCLARIRE-LRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
511-724 |
6.77e-28 |
|
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: 113.40 E-value: 6.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDY------------------IQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVT 572
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 573 IHNnklsemtdleNISKLTGVcpqcNVQFDF-LTVRENLRLFAKIKGIQAHEVDNEVQRVL----LE--LDMKntqnilV 645
Cdd:cd03220 81 VRG----------RVSSLLGL----GGGFNPeLTGRENIYLNGRLLGLSRKEIDEKIDEIIefseLGdfIDLP------V 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 646 QNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRAD-RVVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:cd03220 141 KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQgKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
507-730 |
6.96e-28 |
|
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: 120.01 E-value: 6.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 507 GKEAIRIRNLTKDY-IQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMT--D 583
Cdd:COG1123 257 AEPLLEVRNLSKRYpVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrS 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 584 LENISKLTGVCPQ-CNVQFD-FLTVRENLRLFAKIKGIQ-AHEVDNEVQRVL----LELDMKNTqniLVQNLSGGQKRKL 656
Cdd:COG1123 337 LRELRRRVQMVFQdPYSSLNpRMTVGDIIAEPLRLHGLLsRAERRERVAELLervgLPPDLADR---YPHELSGGQRQRV 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 657 TFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRV--VLFSTQFMDEADILADRKVFISKGKLKCAGSS 730
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGltYLFISHDLAVVRYIADRVAVMYDGRIVEDGPT 489
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
511-724 |
6.97e-28 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 113.12 E-value: 6.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNklsEMTDLENISKL 590
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR---DVTDLPPKDRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFL 670
Cdd:cd03301 74 IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 671 LDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
509-729 |
7.00e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 114.02 E-value: 7.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 509 EAIRIRNLTKDYIQKSKRTE------------------ALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGW 570
Cdd:COG1134 3 SMIEVENVSKSYRLYHEPSRslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 571 VTIHnnklsemtdlENISKL----TGVCPQcnvqfdfLTVRENLRLFAKIKGIQAHEVDNEVQRVL----LE--LDMKnt 640
Cdd:COG1134 83 VEVN----------GRVSALlelgAGFHPE-------LTGRENIYLNGRLLGLSRKEIDEKFDEIVefaeLGdfIDQP-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 641 qnilVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRAD-RVVLFSTQFMDEADILADRKVFI 719
Cdd:COG1134 144 ----VKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESgRTVIFVSHSMGAVRRLCDRAIWL 219
|
250
....*....|
gi 1907081362 720 SKGKLKCAGS 729
Cdd:COG1134 220 EKGRLVMDGD 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1337-1537 |
8.88e-28 |
|
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: 119.62 E-value: 8.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSA---GQVLLKGSSTGDTPGFL-----GYCPQENALWLN-LT 1407
Cdd:COG1123 21 AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALrgrriGMVFQDPMTQLNpVT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1408 VREHLEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1487
Cdd:COG1123 101 VGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1488 MWQAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1537
Cdd:COG1123 181 ILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
510-729 |
1.03e-27 |
|
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: 119.62 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYiqKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPT---KGWVTIHNNKLSEMTDLEn 586
Cdd:COG1123 4 LLEVRDLSVRY--PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 587 ISKLTGVCPQ-CNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGD 665
Cdd:COG1123 81 RGRRIGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 666 PQIFLLDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEADILADRKVFISKGKLKCAGS 729
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
511-725 |
1.14e-27 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 112.88 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEmTDLENISKL 590
Cdd:TIGR03740 1 LETKNLSKRF----GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTR-KDLHKIGSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQcnvqFDFLTVRENLRLFAKIKGIQahevDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFL 670
Cdd:TIGR03740 76 IESPPL----YENLTARENLKVHTTLLGLP----DSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLI 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081362 671 LDEPTAGLDPFS----RHRVWNFLKErraDRVVLFSTQFMDEADILADRKVFISKGKLK 725
Cdd:TIGR03740 148 LDEPTNGLDPIGiqelRELIRSFPEQ---GITVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
510-724 |
1.24e-27 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 113.23 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYiqkSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMT--DLENI 587
Cdd:COG3638 2 MLELRNLSKRY---PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgrALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 588 SKLTGVCPQcnvQFDF---LTVREN---------------LRLFAKIKGIQAHEvdnevqrvLLE-LDMKNTQNILVQNL 648
Cdd:COG3638 79 RRRIGMIFQ---QFNLvprLSVLTNvlagrlgrtstwrslLGLFPPEDRERALE--------ALErVGLADKAYQRADQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 649 SGGQKRKLtfGIA--ILGDPQIFLLDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:COG3638 148 SGGQQQRV--AIAraLVQEPKLILADEPVASLDPKTARQVMDLLRRiaREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
511-701 |
1.26e-27 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 112.92 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLEnISKL 590
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE-IARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 tGVCP--QcNVQ-FDFLTVRENLRL----------FAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLT 657
Cdd:cd03219 76 -GIGRtfQ-IPRlFPELTVLENVMVaaqartgsglLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907081362 658 FGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKE-RRADRVVLF 701
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRElRERGITVLL 198
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1338-1532 |
1.62e-27 |
|
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: 112.00 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1338 TRNISFCVrKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGFL---------GYCPQENALWLNLTV 1408
Cdd:cd03297 14 TLKIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInlppqqrkiGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1409 REHLEIfaAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1488
Cdd:cd03297 93 RENLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907081362 1489 WQAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1532
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
532-728 |
2.26e-27 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 111.43 E-value: 2.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 532 DLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNnklSEMTDLENISKLTGVCPQCNVQFDFLTVRENLR 611
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING---VDVTAAPPADRPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 612 LfAKIKGIQAHEVDNE-VQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFL 690
Cdd:cd03298 93 L-GLSPGLKLTAEDRQaIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907081362 691 KERRADR--VVLFSTQFMDEADILADRKVFISKGKLKCAG 728
Cdd:cd03298 172 LDLHAETkmTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
507-729 |
3.14e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 113.26 E-value: 3.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 507 GKEAIRIRNLTKDYI--QKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDL 584
Cdd:PRK13633 1 MNEMIKCKNVSYKYEsnEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 585 ENISKLTGVCPQcN---------VQFDFLTVRENLrlfakikGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRK 655
Cdd:PRK13633 81 WDIRNKAGMVFQ-NpdnqivatiVEEDVAFGPENL-------GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 656 ltfgIAILG----DPQIFLLDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEAdILADRKVFISKGKLKCAGS 729
Cdd:PRK13633 153 ----VAIAGilamRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGT 227
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
510-724 |
5.62e-27 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 114.42 E-value: 5.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNklsEMTDLE---- 585
Cdd:COG3842 5 ALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGR---DVTGLPpekr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 586 NIskltGVCPQCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQK------Rkltfg 659
Cdd:COG3842 78 NV----GMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQqrvalaR----- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081362 660 iAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFST--QfmDEADILADRKVFISKGKL 724
Cdd:COG3842 149 -ALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVThdQ--EEALALADRIAVMNDGRI 214
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
512-730 |
5.95e-27 |
|
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: 110.84 E-value: 5.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 512 RIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNnklsemtdlENISKLT 591
Cdd:COG0410 5 EVENLHAGY----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG---------EDITGLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 592 ---------GVCPQC-NVqFDFLTVRENLRLFAKIKGIQAhEVDNEVQRVlLEL--DMKNTQNILVQNLSGGQKRKLTFG 659
Cdd:COG0410 72 phriarlgiGYVPEGrRI-FPSLTVEENLLLGAYARRDRA-EVRADLERV-YELfpRLKERRRQRAGTLSGGEQQMLAIG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081362 660 IAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRV-VLFSTQFMDEADILADRKVFISKGKLKCAGSS 730
Cdd:COG0410 149 RALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVtILLVEQNARFALEIADRAYVLERGRIVLEGTA 220
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
510-724 |
1.22e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 113.24 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIhNNKLseMTDLEnisk 589
Cdd:COG3839 3 SLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILI-GGRD--VTDLP---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 ltgvcPQC-NV----Q----FDFLTVRENLrLFA-KIKGIQAHEVDNEVQRV--LLELDmkntqNIL---VQNLSGGQKR 654
Cdd:COG3839 72 -----PKDrNIamvfQsyalYPHMTVYENI-AFPlKLRKVPKAEIDRRVREAaeLLGLE-----DLLdrkPKQLSGGQRQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081362 655 KLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRlhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1333-1527 |
1.52e-26 |
|
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: 108.04 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1333 KKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGFL-------GYCPQENALWLN 1405
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplrrriGMVFQDFALFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1406 LTVREhleifaaikgmrksdaNVAIerladalklqdqlkspvkTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQ 1485
Cdd:cd03229 91 LTVLE----------------NIAL------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITR 136
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907081362 1486 QQMWQAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1527
Cdd:cd03229 137 REVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1320-1537 |
1.54e-26 |
|
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: 109.59 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1320 EYKGKKKCFVLKSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGF------- 1392
Cdd:cd03258 3 ELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKelrkarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1393 -LGYCPQE-NALWlNLTVREHLEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSV 1470
Cdd:cd03258 83 rIGMIFQHfNLLS-SRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081362 1471 VLLDEPSTGMDPEGQQQMWQAIQATfsNTERG--ALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1537
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDI--NRELGltIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
511-724 |
6.94e-26 |
|
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: 107.59 E-value: 6.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTD--LENIS 588
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 589 KltgvcpqcNVQFDF----------LTVRENLRlfakiKGIQAHEVDN---EVQRVLLELDMKNTQNILVQN-----LSG 650
Cdd:cd03257 82 K--------EIQMVFqdpmsslnprMTIGEQIA-----EPLRIHGKLSkkeARKEAVLLLLVGVGLPEEVLNrypheLSG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 651 GQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADR--VVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
511-724 |
7.31e-26 |
|
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: 105.59 E-value: 7.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQkskrTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKlsemtdleniskl 590
Cdd:cd03216 1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 tgvcpqcnvqFDFLTVRENLRLfakikGIQahevdnevqrvlleldmkntqniLVQNLSGGQKRKLTFGIAILGDPQIFL 670
Cdd:cd03216 64 ----------VSFASPRDARRA-----GIA-----------------------MVYQLSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 671 LDEPTAGLDPFSRHRVWNFLKERRADRV-VLFSTQFMDEADILADRKVFISKGKL 724
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQGVaVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
512-700 |
7.75e-26 |
|
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: 108.59 E-value: 7.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 512 RIRNLTKDY--IQkskrteALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNnklsemtdlENISK 589
Cdd:COG0411 6 EVRGLTKRFggLV------AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDG---------RDITG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 LTgvcP------------QcNVQ-FDFLTVRENLRLfakikGIQAH--------------------EVDNEVQRVLLELD 636
Cdd:COG0411 71 LP---PhriarlgiartfQ-NPRlFPELTVLENVLV-----AAHARlgrgllaallrlprarreerEARERAEELLERVG 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081362 637 MKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADR---VVL 700
Cdd:COG0411 142 LADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERgitILL 208
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
511-723 |
7.87e-26 |
|
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: 108.04 E-value: 7.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqkSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTI----------------- 573
Cdd:cd03256 1 IEVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIdgtdinklkgkalrqlr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 574 --------HNNKLSEMTDLENIskLTGVCPQCNvqfdflTVRENLRLFAKIkgiqahevdnEVQRVL--LE-LDMKNTQN 642
Cdd:cd03256 78 rqigmifqQFNLIERLSVLENV--LSGRLGRRS------TWRSLFGLFPKE----------EKQRALaaLErVGLLDKAY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 643 ILVQNLSGGQKRKLtfGIA--ILGDPQIFLLDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEADILADRKVF 718
Cdd:cd03256 140 QRADQLSGGQQQRV--AIAraLMQQPKLILADEPVASLDPASSRQVMDLLKRinREEGITVIVSLHQVDLAREYADRIVG 217
|
....*
gi 1907081362 719 ISKGK 723
Cdd:cd03256 218 LKDGR 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
511-724 |
1.12e-25 |
|
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: 107.39 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqkSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLENISKL 590
Cdd:cd03295 1 IEFENVTKRY---GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVqFDFLTVRENLRLFAKIKGIQAHEVDnevQRV-----LLELDMKNTQNILVQNLSGGQKRKLTFGIAILGD 665
Cdd:cd03295 78 GYVIQQIGL-FPHMTVEENIALVPKLLKWPKEKIR---ERAdellaLVGLDPAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 666 PQIFLLDEPTAGLDPFSRHRVWN-FLK-ERRADRVVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEeFKRlQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
509-729 |
1.84e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 107.55 E-value: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 509 EAIRIRNLTkdyIQKSKRTeALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLEnIS 588
Cdd:PRK13548 1 AMLEARNLS---VRLGGRT-LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAE-LA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 589 KLTGVCPQ-CNVQFDFlTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQK------RKLTFGIA 661
Cdd:PRK13548 76 RRRAVLPQhSSLSFPF-TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQqrvqlaRVLAQLWE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081362 662 ILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADR-----VVL----FSTQFmdeadilADRKVFISKGKLKCAGS 729
Cdd:PRK13548 155 PDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglaviVVLhdlnLAARY-------ADRIVLLHQGRLVADGT 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
510-729 |
3.76e-25 |
|
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: 105.88 E-value: 3.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLE-NIs 588
Cdd:cd03296 2 SIEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQErNV- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 589 kltGVCPQCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEV-QRV--LLEL-DMKNTQNILVQNLSGGQKRKLTFGIAILG 664
Cdd:cd03296 77 ---GFVFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIrAKVheLLKLvQLDWLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081362 665 DPQIFLLDEPTAGLDPFSRHRVWNFLKeRRADRV---VLFSTQFMDEADILADRKVFISKGKLKCAGS 729
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLR-RLHDELhvtTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
511-729 |
5.39e-25 |
|
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: 105.40 E-value: 5.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKSkrteALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNklsEMTDLENISKL 590
Cdd:cd03300 1 IELENVSKFYGGFV----ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGK---DITNLPPHKRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFL 670
Cdd:cd03300 74 VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 671 LDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEADILADRKVFISKGKLKCAGS 729
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRlqKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
511-724 |
7.97e-25 |
|
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: 104.15 E-value: 7.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKskrtEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLS-EMTDLENISK 589
Cdd:cd03262 1 IEIKNLHKSFGDF----HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTdDKKNINELRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 LTGVCPQcnvQFDF---LTVRENLRL-FAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGD 665
Cdd:cd03262 77 KVGMVFQ---QFNLfphLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 666 PQIFLLDEPTAGLDPFSRHRVWNFLKE-RRADRVVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLDVMKDlAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1337-1533 |
8.23e-25 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 107.88 E-value: 8.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSS-TGDTPG--FLGYCPQENALWLNLTVREHLE 1413
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDvTGLPPEkrNVGMVFQDYALFPHLTVAENVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1414 IFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEG-----------VKRklcfvlsilgnPSVVLLDEPSTGMDP 1482
Cdd:COG3842 100 FGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGqqqrvalaralAPE-----------PRVLLLDEPLSALDA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 1483 EGQQQMWQ---AIQAtfsntERG--ALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1533
Cdd:COG3842 169 KLREEMREelrRLQR-----ELGitFIYVTHDQEEALALADRIAVMNDGRIEQVGT 219
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
511-730 |
8.76e-25 |
|
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: 104.55 E-value: 8.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLENISKL 590
Cdd:cd03218 1 LRAENLSKRY----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFL 670
Cdd:cd03218 77 IGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081362 671 LDEPTAGLDPFSRH---RVWNFLKERRADrvVLFSTQFMDEADILADRKVFISKGKLKCAGSS 730
Cdd:cd03218 157 LDEPFAGVDPIAVQdiqKIIKILKDRGIG--VLITDHNVRETLSITDRAYIIYEGKVLAEGTP 217
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1339-1532 |
1.07e-24 |
|
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: 102.51 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPG-----FLGYCPQenalwlnltvrehle 1413
Cdd:cd03214 16 DDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPkelarKIAYVPQ--------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1414 ifaaikgmrksdanvAIERLaDALKLQDQlksPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQ 1493
Cdd:cd03214 81 ---------------ALELL-GLAHLADR---PFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLR 141
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907081362 1494 ATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1532
Cdd:cd03214 142 RLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1317-1528 |
1.17e-24 |
|
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: 103.72 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1317 LRKEYK-GKKKCFVLKskkkiatrNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPG---- 1391
Cdd:cd03255 6 LSKTYGgGGEKVQALK--------GVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEkela 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1392 -----FLGYCPQENALWLNLTVREHLEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILG 1466
Cdd:cd03255 78 afrrrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081362 1467 NPSVVLLDEPSTGMDPEGQQQMWQAIQATfsNTERGA--LLTTHYMAEAEAvCDRVAIMVSGRL 1528
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLREL--NKEAGTtiVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
530-728 |
2.16e-24 |
|
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: 103.14 E-value: 2.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 530 LKDLTLDV---YKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLENIS---KLTGVCPQCNVQFDF 603
Cdd:cd03297 10 LPDFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPpqqRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 604 LTVRENLrLFAkIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSR 683
Cdd:cd03297 90 LNVRENL-AFG-LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907081362 684 HRVWNFLKERRAD--RVVLFSTQFMDEADILADRKVFISKGKLKCAG 728
Cdd:cd03297 168 LQLLPELKQIKKNlnIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1334-1554 |
2.28e-24 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 104.43 E-value: 2.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1334 KKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDtpgflgycpqENALWlnlTVREHL- 1412
Cdd:TIGR04520 14 EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLD----------EENLW---EIRKKVg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1413 --------EIFAAI-----------KG-----MRKsdanvaieRLADALK---LQDQLKSPVKTLSEGVKRKLCfVLSIL 1465
Cdd:TIGR04520 81 mvfqnpdnQFVGATveddvafglenLGvpreeMRK--------RVDEALKlvgMEDFRDREPHLLSGGQKQRVA-IAGVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1466 G-NPSVVLLDEPsTGM-DPEGQQQMWQAIQATfsNTERGA--LLTTHYMAEAeAVCDRVAIMVSGRLRCIGSIQHLKSKf 1541
Cdd:TIGR04520 152 AmRPDIIILDEA-TSMlDPKGRKEVLETIRKL--NKEEGItvISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQ- 226
|
250
....*....|...
gi 1907081362 1542 gKEYLLEMKVKTP 1554
Cdd:TIGR04520 227 -VELLKEIGLDVP 238
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
528-745 |
2.34e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 104.86 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 528 EALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTD---LENISKLTGVC---PQCNVQF 601
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyIRPVRKRIGMVfqfPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 602 DflTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMknTQNILVQN---LSGGQKRKLTFgIAILG-DPQIFLLDEPTAG 677
Cdd:PRK13646 101 D--TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGF--SRDVMSQSpfqMSGGQMRKIAI-VSILAmNPDIIVLDEPTAG 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081362 678 LDPFSRHRVWNFLKERRAD--RVVLFSTQFMDEADILADRKVFISKGKL--KCAGSSLFLKKKWGIGYHLSL 745
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARYADEVIVMKEGSIvsQTSPKELFKDKKKLADWHIGL 247
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
509-722 |
3.03e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 103.79 E-value: 3.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 509 EAIRIRNLTKDYIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLsemtdlENIS 588
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV------TGPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 589 KLTGVCPQCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLtfGIA--ILGDP 666
Cdd:COG4525 76 ADRGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRV--GIAraLAADP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081362 667 QIFLLDEPTAGLDPFSRH-------RVWnflkeRRADRVVLFSTQFMDEADILADRKVFISKG 722
Cdd:COG4525 154 RFLLMDEPFGALDALTREqmqelllDVW-----QRTGKGVFLITHSVEEALFLATRLVVMSPG 211
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1333-1532 |
6.97e-24 |
|
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: 101.56 E-value: 6.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1333 KKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGF---LGYCPQENALWLNLTVR 1409
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKdrdIAMVFQNYALYPHMTVY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1410 EHLEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW 1489
Cdd:cd03301 91 DNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907081362 1490 QAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1532
Cdd:cd03301 171 AELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
527-724 |
9.47e-24 |
|
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: 101.13 E-value: 9.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 527 TEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMtDLENISKLTGVCPQcNVQFDFLTV 606
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL-DPADLRRNIGYVPQ-DVTLFYGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 607 RENLRLFAkikgiQAHEvDNEVQRVL-------LELDMKNTQNILV----QNLSGGQKRKLTFGIAILGDPQIFLLDEPT 675
Cdd:cd03245 95 RDNITLGA-----PLAD-DERILRAAelagvtdFVNKHPNGLDLQIgergRGLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907081362 676 AGLDPFSRHRVWNFLKERRADRVVLFSTQFMDEADiLADRKVFISKGKL 724
Cdd:cd03245 169 SAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
511-724 |
1.19e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 102.46 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqkSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLS-EMTDLENISK 589
Cdd:PRK13639 2 LETRDLKYSY---PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSLLEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 LTGVCPQ-CNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKltfgIAILG---- 664
Cdd:PRK13639 79 TVGIVFQnPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKR----VAIAGilam 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 665 DPQIFLLDEPTAGLDPFSRHRVWNFLKE-RRADRVVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDlNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
511-729 |
1.26e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 102.82 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKSK-RTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHN-NKLSEMTDLENIS 588
Cdd:PRK13637 3 IKIENLTHIYMEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvDITDKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 589 KLTGVCPQC-NVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRV--LLELDMKNTQNILVQNLSGGQKRKltfgIAILG- 664
Cdd:PRK13637 83 KKVGLVFQYpEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAmnIVGLDYEDYKDKSPFELSGGQKRR----VAIAGv 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 665 ---DPQIFLLDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEADILADRKVFISKGKLKCAGS 729
Cdd:PRK13637 159 vamEPKILILDEPTAGLDPKGRDEILNKIKElhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGT 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
511-728 |
1.28e-23 |
|
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: 99.69 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKSKrtEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDleNISKL 590
Cdd:cd03247 1 LSINNVSFSYPEQEQ--QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK--ALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVQFDfLTVRENLrlfakikGIQahevdnevqrvlleldmkntqnilvqnLSGGQKRKLTFGIAILGDPQIFL 670
Cdd:cd03247 77 ISVLNQRPYLFD-TTLRNNL-------GRR---------------------------FSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081362 671 LDEPTAGLDPFSRHRVWNFLKERRADRVVLFSTQFMDEADiLADRKVFISKGKLKCAG 728
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIE-HMDKILFLENGKIIMQG 178
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
529-700 |
2.51e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 100.96 E-value: 2.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 529 ALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLEnISKLtGVC-----PqcNVqFDF 603
Cdd:COG4674 25 ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHE-IARL-GIGrkfqkP--TV-FEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 604 LTVRENLR------------LFAKIKGIQAHEVDnevqRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFLL 671
Cdd:COG4674 100 LTVFENLElalkgdrgvfasLFARLTAEERDRIE----EVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLL 175
|
170 180
....*....|....*....|....*....
gi 1907081362 672 DEPTAGLDPFSRHRVWNFLKERRADRVVL 700
Cdd:COG4674 176 DEPVAGMTDAETERTAELLKSLAGKHSVV 204
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1337-1546 |
2.58e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 107.90 E-value: 2.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTG----DTPGFLGYCPQENALWLNLTVREHL 1412
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDagdiATRRRVGYMSQAFSLYGELTVRQNL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1413 EIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAI 1492
Cdd:NF033858 361 ELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLL 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081362 1493 -------QAT-FsntergalLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSKFGKEYL 1546
Cdd:NF033858 441 ielsredGVTiF--------ISTHFMNEAER-CDRISLMHAGRVLASDTPAALVAARGAATL 493
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
511-724 |
3.35e-23 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 102.96 E-value: 3.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLE----- 585
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 586 -NIskltGVCPQcnvQFDFL---TVRENLRLFAKIKGIQAHEVDnevQRV--LLEL----DMKNTqniLVQNLSGGQKRK 655
Cdd:PRK11153 82 rQI----GMIFQ---HFNLLssrTVFDNVALPLELAGTPKAEIK---ARVteLLELvglsDKADR---YPAQLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081362 656 LtfGIA--ILGDPQIFLLDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:PRK11153 149 V--AIAraLASNPKVLLCDEATSALDPATTRSILELLKDinRELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
508-728 |
3.70e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 101.25 E-value: 3.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 508 KEAIRIRNLTKDYIQKSKRteALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLEnI 587
Cdd:PRK13635 3 EEIIRVEHISFRYPDAATY--ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWD-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 588 SKLTGVCPQC-NVQFDFLTVRENLRLFAKIKGIQAHEVdneVQRVLLELDMKNTQNILVQ---NLSGGQKRKltfgIAIL 663
Cdd:PRK13635 80 RRQVGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEM---VERVDQALRQVGMEDFLNRephRLSGGQKQR----VAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 664 G----DPQIFLLDEPTAGLDPFSRHRVWNFLKERRADR--VVLFSTQFMDEAdILADRKVFISKGKLKCAG 728
Cdd:PRK13635 153 GvlalQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEA-AQADRVIVMNKGEILEEG 222
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1339-1546 |
3.70e-23 |
|
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: 100.10 E-value: 3.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTP----GFlGYCPQENALWLNLTVREHLEI 1414
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPpekrDI-SYVPQNYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1415 FAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQA 1494
Cdd:cd03299 95 GLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKK 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 1495 TFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQ----HLKSKFGKEYL 1546
Cdd:cd03299 175 IRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEevfkKPKNEFVAEFL 230
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
508-724 |
3.72e-23 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 106.02 E-value: 3.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 508 KEAIRIRNLTKDYiqkSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMtDLENI 587
Cdd:COG1132 337 RGEIEFENVSFSY---PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDL-TLESL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 588 SKLTGVCPQCNVQFDfLTVRENLRLF------------AKIkgIQAHEvdnevqrVLLELDMK-NTQnilV----QNLSG 650
Cdd:COG1132 413 RRQIGVVPQDTFLFS-GTIRENIRYGrpdatdeeveeaAKA--AQAHE-------FIEALPDGyDTV---VgergVNLSG 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 651 GQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRVVL-----FSTqfmdeadIL-ADRKVFISKGKL 724
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIviahrLST-------IRnADRILVLDDGRI 552
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
511-680 |
4.49e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 100.55 E-value: 4.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiQKSKRTE--ALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLE--- 585
Cdd:COG1101 2 LELKNLSKTF-NPGTVNEkrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKrak 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 586 NISK-----LTGVCPQcnvqfdfLTVRENLRLFAK-------IKGIQAHEVDNEVQRV-LLELDMKNTQNILVQNLSGGQ 652
Cdd:COG1101 81 YIGRvfqdpMMGTAPS-------MTIEENLALAYRrgkrrglRRGLTKKRRELFRELLaTLGLGLENRLDTKVGLLSGGQ 153
|
170 180
....*....|....*....|....*...
gi 1907081362 653 KRKLTFGIAILGDPQIFLLDEPTAGLDP 680
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDP 181
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1317-1528 |
5.44e-23 |
|
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: 99.50 E-value: 5.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1317 LRKEYKGKKKCFVlkskkkiATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGFL--- 1393
Cdd:cd03257 7 LSVSFPTGGGSVK-------ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrki 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1394 -----GYCPQENALWLN--LTVREHLE--IFAAIKGMRKSDANVAIERLADALKL-QDQLKSPVKTLSEGVKRKLCFVLS 1463
Cdd:cd03257 80 rrkeiQMVFQDPMSSLNprMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081362 1464 ILGNPSVVLLDEPSTGMDPEGQQQmwqaIQATFSN--TERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1528
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQ----ILDLLKKlqEELGLtlLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
511-724 |
6.49e-23 |
|
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: 98.63 E-value: 6.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqkSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDlENISKL 590
Cdd:cd03292 1 IEFINVTKTY---PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRG-RAIPYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 ---TGVCPQCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQ 667
Cdd:cd03292 77 rrkIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081362 668 IFLLDEPTAGLDPFSRHRVWNFLKE-RRADRVVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKiNKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
511-724 |
6.78e-23 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 99.68 E-value: 6.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqkSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEM--TDLENIS 588
Cdd:TIGR02315 2 LEVENLSKVY---PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLrgKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 589 KLTGVCPQcnvQFDF---LTVRENL---RLFAK--IKGI--QAHEVDNEVQRVLLE-LDMKNTQNILVQNLSGGQKRKLT 657
Cdd:TIGR02315 79 RRIGMIFQ---HYNLierLTVLENVlhgRLGYKptWRSLlgRFSEEDKERALSALErVGLADKAYQRADQLSGGQQQRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081362 658 FGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:TIGR02315 156 IARALAQQPDLILADEPIASLDPKTSKQVMDYLKRinKEDGITVIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
510-728 |
1.07e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 99.81 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYiqkSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLENISK 589
Cdd:PRK13647 4 IIEVEDLHFRY---KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 LTGVCPQCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKltfgIAILG----D 665
Cdd:PRK13647 81 VGLVFQDPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKR----VAIAGvlamD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081362 666 PQIFLLDEPTAGLDPFSRHRVWNFLKE-RRADRVVLFSTQFMDEADILADRKVFISKGKLKCAG 728
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
511-735 |
1.10e-22 |
|
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: 98.45 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKSKrteALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTdLENISKL 590
Cdd:cd03254 3 IEFENVNFSYDEKKP---VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS-RKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCnvqfDFL---TVRENLRLFAKIkgIQAHEVDNEVQRV-LLELDMKNTQNILVQ------NLSGGQKRKLTFGI 660
Cdd:cd03254 79 IGVVLQD----TFLfsgTIMENIRLGRPN--ATDEEVIEAAKEAgAHDFIMKLPNGYDTVlgenggNLSQGERQLLAIAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 661 AILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRVVL-----FSTqfmdeadIL-ADRKVFISKGKLKCAGS--SLF 732
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIiiahrLST-------IKnADKILVLDDGKIIEEGThdELL 225
|
...
gi 1907081362 733 LKK 735
Cdd:cd03254 226 AKK 228
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
526-709 |
1.35e-22 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 97.11 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 526 RTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKL--SEMTDLENISKLTGVCPQCNVQFDF 603
Cdd:TIGR01166 4 GPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdySRKGLLERRQRVGLVFQDPDDQLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 604 LTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSR 683
Cdd:TIGR01166 84 ADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGR 163
|
170 180
....*....|....*....|....*..
gi 1907081362 684 HRVWNFLKERRAD-RVVLFSTQFMDEA 709
Cdd:TIGR01166 164 EQMLAILRRLRAEgMTVVISTHDVDLA 190
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1317-1537 |
1.42e-22 |
|
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: 103.83 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1317 LRKEYKGKKKcfvlksKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPG----- 1391
Cdd:COG1123 266 LSKRYPVRGK------GGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1392 ---FLGYCPQENALWLN--LTVREHL-EIFAAIKGMRKSDANVAIERLADALKLQDQL--KSPvKTLSEGVKRKLCFVLS 1463
Cdd:COG1123 340 lrrRVQMVFQDPYSSLNprMTVGDIIaEPLRLHGLLSRAERRERVAELLERVGLPPDLadRYP-HELSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081362 1464 ILGNPSVVLLDEPSTGMDPEGQQQMWQAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1537
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
506-724 |
1.69e-22 |
|
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: 99.26 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 506 HGKEAIRIRNLTKDYIQKSKRTE---ALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMT 582
Cdd:cd03294 13 NPQKAFKLLAKGKSKEEILKKTGqtvGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 583 D--LENI-SKLTGVCPQCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFG 659
Cdd:cd03294 93 RkeLRELrRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081362 660 IAILGDPQIFLLDEPTAGLDPFSRHRVWN-FLK-ERRADRVVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:cd03294 173 RALAVDPDILLMDEAFSALDPLIRREMQDeLLRlQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1312-1533 |
2.13e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 98.04 E-value: 2.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1312 IIASCLRKEYKGKKkcfvlkskkkiATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPG 1391
Cdd:PRK10895 4 LTAKNLAKAYKGRR-----------VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1392 F------LGYCPQENALWLNLTVREHLEIFAAIKG-----MRKSDANVAIERLADAlKLQDQLKspvKTLSEGVKRKLCF 1460
Cdd:PRK10895 73 HararrgIGYLPQEASIFRRLSVYDNLMAVLQIRDdlsaeQREDRANELMEEFHIE-HLRDSMG---QSLSGGERRRVEI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081362 1461 VLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQAtFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1533
Cdd:PRK10895 149 ARALAANPKFILLDEPFAGVDPISVIDIKRIIEH-LRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
514-691 |
2.23e-22 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 96.54 E-value: 2.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 514 RNLTKDYIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLS-----GLcvpTKGWVTIHNNKLSemtdlENIS 588
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrktaGV---ITGEILINGRPLD-----KNFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 589 KLTGVCPQCNVQFDFLTVRENLRLFAKIKGiqahevdnevqrvlleldmkntqnilvqnLSGGQKRKLTFGIAILGDPQI 668
Cdd:cd03232 79 RSTGYVEQQDVHSPNLTVREALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSI 129
|
170 180
....*....|....*....|...
gi 1907081362 669 FLLDEPTAGLDPFSRHRVWNFLK 691
Cdd:cd03232 130 LFLDEPTSGLDSQAAYNIVRFLK 152
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
504-724 |
2.29e-22 |
|
type I secretion system ATPase, LssB 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. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 104.18 E-value: 2.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 504 EFHGKeaIRIRNLTKDYiQKSKRTeALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMtD 583
Cdd:TIGR03375 459 RLQGE--IEFRNVSFAY-PGQETP-ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQI-D 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 584 LENISKLTGVCPQCNVQFdFLTVRENLRLFAkikgiqAHEVDNEVQRV-----LLE--------LDMkntqniLV----Q 646
Cdd:TIGR03375 534 PADLRRNIGYVPQDPRLF-YGTLRDNIALGA------PYADDEEILRAaelagVTEfvrrhpdgLDM------QIgergR 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 647 NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRVVLFST---QFMDeadiLADRKVFISKGK 723
Cdd:TIGR03375 601 SLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVThrtSLLD----LVDRIIVMDNGR 676
|
.
gi 1907081362 724 L 724
Cdd:TIGR03375 677 I 677
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1337-1528 |
2.72e-22 |
|
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: 95.19 E-value: 2.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGsstgdtpgflgycpQEnalwlnltvrehleifa 1416
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG--------------KE----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1417 aikgmrksdanVAIERLADALKL------QdqlkspvktLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQ 1490
Cdd:cd03216 64 -----------VSFASPRDARRAgiamvyQ---------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK 123
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907081362 1491 AIQATfsnTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1528
Cdd:cd03216 124 VIRRL---RAQGVavIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
511-714 |
3.06e-22 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 97.37 E-value: 3.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEM-TDLENISK 589
Cdd:COG1126 2 IEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSkKDINKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 LTGVCPQcnvQFD-F--LTVRENLRLfA--KIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQK-RkltfgIAI- 662
Cdd:COG1126 78 KVGMVFQ---QFNlFphLTVLENVTL-ApiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQqR-----VAIa 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 663 --LG-DPQIFLLDEPTAGLDP----------------------------FSRhRVwnflkerrADRVVlfstqFMDEADI 711
Cdd:COG1126 149 raLAmEPKVMLFDEPTSALDPelvgevldvmrdlakegmtmvvvthemgFAR-EV--------ADRVV-----FMDGGRI 214
|
...
gi 1907081362 712 LAD 714
Cdd:COG1126 215 VEE 217
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
510-717 |
4.28e-22 |
|
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: 102.36 E-value: 4.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYiqkSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMtDLENISK 589
Cdd:TIGR02857 321 SLEFSGVSVAY---PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADA-DADSWRD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 LTGVCPQCNVQFDfLTVRENLRLFAkiKGIQAHEVDNEVQRV-LLELDMKNTQNILVQ------NLSGGQKRKLTFGIAI 662
Cdd:TIGR02857 397 QIAWVPQHPFLFA-GTIAENIRLAR--PDASDAEIREALERAgLDEFVAALPQGLDTPigeggaGLSGGQAQRLALARAF 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 663 LGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRVVLFSTQfmDEADI-LADRKV 717
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH--RLALAaLADRIV 527
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
530-729 |
4.31e-22 |
|
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: 99.79 E-value: 4.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 530 LKDLTLDV----YKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNnklsemTDLENISKLT---------GVCPQ 596
Cdd:COG4148 11 RGGFTLDVdftlPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG------EVLQDSARGIflpphrrriGYVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 597 cnvQ---FDFLTVRENL-----RLFAKIKGIQAHEVdneVQrvLLE----LDMKntqnilVQNLSGGQKRKLTFGIAILG 664
Cdd:COG4148 85 ---EarlFPHLSVRGNLlygrkRAPRAERRISFDEV---VE--LLGighlLDRR------PATLSGGERQRVAIGRALLS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081362 665 DPQIFLLDEPTAGLDPFSRHRVWNFLkERRADRV---VLFSTQFMDEADILADRKVFISKGKLKCAGS 729
Cdd:COG4148 151 SPRLLLMDEPLAALDLARKAEILPYL-ERLRDELdipILYVSHSLDEVARLADHVVLLEQGRVVASGP 217
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1328-1528 |
5.39e-22 |
|
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: 96.12 E-value: 5.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1328 FVLKSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTG-----DTPGFLGYCPQENAL 1402
Cdd:cd03245 10 FSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRqldpaDLRRNIGYVPQDVTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1403 wLNLTVREHLEIFAA-------IKGMRKSDANVAIERLADALKLQDQLKSpvKTLSEGVKRKLCFVLSILGNPSVVLLDE 1475
Cdd:cd03245 90 -FYGTLRDNITLGAPladderiLRAAELAGVTDFVNKHPNGLDLQIGERG--RGLSGGQRQAVALARALLNDPPILLLDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907081362 1476 PSTGMDPEGQQQMWQAIQATFSntERGALLTTHYMAeAEAVCDRVAIMVSGRL 1528
Cdd:cd03245 167 PTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPS-LLDLVDRIIVMDSGRI 216
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
529-745 |
5.53e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 98.17 E-value: 5.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 529 ALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMT---DLENISKLTGVCpqcnvqFDF-- 603
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKknkKLKPLRKKVGIV------FQFpe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 604 -----LTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMknTQNILVQN---LSGGQKRKltfgIAILG----DPQIFLL 671
Cdd:PRK13634 96 hqlfeETVEKDICFGPMNFGVSEEDAKQKAREMIELVGL--PEELLARSpfeLSGGQMRR----VAIAGvlamEPEVLVL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081362 672 DEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEADILADRKVFISKGKLKCAGS--SLFLKKKWGIGYHLSL 745
Cdd:PRK13634 170 DEPTAGLDPKGRKEMMEMFYKlhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTprEIFADPDELEAIGLDL 247
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
511-728 |
7.01e-22 |
|
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: 96.25 E-value: 7.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqkskRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVtIHNNKlsEMTDLENISKL 590
Cdd:cd03299 1 LKVENLSKDW-----KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKI-LLNGK--DITNLPPEKRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFL 670
Cdd:cd03299 73 ISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 671 LDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEADILADRKVFISKGKLKCAG 728
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKirKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVG 212
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1335-1533 |
8.89e-22 |
|
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: 95.77 E-value: 8.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1335 KIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGF---LGYCPQENALWLNLTVREH 1411
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHkrpVNTVFQNYALFPHLTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1412 LEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQA 1491
Cdd:cd03300 93 IAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907081362 1492 IQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1533
Cdd:cd03300 173 LKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1331-1528 |
9.62e-22 |
|
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: 94.54 E-value: 9.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1331 KSKKKIaTRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSA--GQVLLKGSSTGDT--PGFLGYCPQENALWLNL 1406
Cdd:cd03213 19 KSGKQL-LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRsfRKIIGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1407 TVREHLEIFAAIKGmrksdanvaierladalklqdqlkspvktLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQ 1486
Cdd:cd03213 98 TVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907081362 1487 QMWQAIQAtFSNTERGALLTTHYM-AEAEAVCDRVAIMVSGRL 1528
Cdd:cd03213 149 QVMSLLRR-LADTGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
510-680 |
1.10e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 95.85 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNK--LSEMTDLENI 587
Cdd:PRK11124 2 SIQLNGINCFY----GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdFSKTPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 588 SKL---TGVCPQcnvQFDF---LTVRENL-RLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGI 660
Cdd:PRK11124 78 RELrrnVGMVFQ---QYNLwphLTVQQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIAR 154
|
170 180
....*....|....*....|
gi 1907081362 661 AILGDPQIFLLDEPTAGLDP 680
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDP 174
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
510-729 |
1.57e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 96.79 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYiqKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVP---TKGWVTIHNNKLSEMTDLEN 586
Cdd:PRK13640 5 IVEFKHVSFTY--PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 587 ISKLTGVCPQCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKltfgIAILG-- 664
Cdd:PRK13640 83 REKVGIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQR----VAIAGil 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081362 665 --DPQIFLLDEPTAGLDPFSRHRVWNFLKERRADR-VVLFS-TQFMDEADiLADRKVFISKGKLKCAGS 729
Cdd:PRK13640 159 avEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnLTVISiTHDIDEAN-MADQVLVLDDGKLLAQGS 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
510-744 |
1.77e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 96.44 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLtkDYI---QKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMT---D 583
Cdd:PRK13641 2 SIKFENV--DYIyspGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgnkN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 584 LENISKLTGVCPQ-CNVQFDFLTVRENLRLFAKIKGIQAHEVDNE----VQRVLLELDMKNTQNIlvqNLSGGQKRKLTF 658
Cdd:PRK13641 80 LKKLRKKVSLVFQfPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKalkwLKKVGLSEDLISKSPF---ELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 659 GIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKE-RRADRVVLFSTQFMDEADILADRKVFISKGKL--KCAGSSLFLKK 735
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDyQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLikHASPKEIFSDK 236
|
....*....
gi 1907081362 736 KWGIGYHLS 744
Cdd:PRK13641 237 EWLKKHYLD 245
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1339-1508 |
1.81e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 94.17 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDT--PGFLGYCPQENALWLNLTVREHLEIFA 1416
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPdvAEACHYLGHRNAMKPALTVAENLEFWA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1417 AIKGMRKSDANVAIErladALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQAtf 1496
Cdd:PRK13539 99 AFLGGEELDIAAALE----AVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRA-- 172
|
170
....*....|....
gi 1907081362 1497 sNTERG--ALLTTH 1508
Cdd:PRK13539 173 -HLAQGgiVIAATH 185
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1339-1527 |
2.67e-21 |
|
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: 95.15 E-value: 2.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVL-LKGSSTGDTPGF-----LGYCPQENALWL--NLTVRe 1410
Cdd:COG1119 20 DDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrLFGERRGGEDVWelrkrIGLVSPALQLRFprDETVL- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1411 hlEI-----FAAIkGMRK--SDANVAI-ERLADALKLQDQLKSPVKTLSEGVKRKlcfVL---SILGNPSVVLLDEPSTG 1479
Cdd:COG1119 99 --DVvlsgfFDSI-GLYRepTDEQRERaRELLELLGLAHLADRPFGTLSQGEQRR---VLiarALVKDPELLILDEPTAG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907081362 1480 MDPEGQQQMWQAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1527
Cdd:COG1119 173 LDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
508-724 |
3.41e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 94.84 E-value: 3.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 508 KEAIRIRNLTKDYIQKskrtEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLC-----VPTKGWVTIH-NNKLSEM 581
Cdd:PRK14239 3 EPILQVSDLSVYYNKK----KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlnpeVTITGSIVYNgHNIYSPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 582 TDLENISKLTGVCPQCNVQFDFlTVRENLRLFAKIKGIQAHEV-DNEVQRVLLELDMKN-TQNILVQN---LSGGQKRKL 656
Cdd:PRK14239 79 TDTVDLRKEIGMVFQQPNPFPM-SIYENVVYGLRLKGIKDKQVlDEAVEKSLKGASIWDeVKDRLHDSalgLSGGQQQRV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081362 657 TFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRVVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1339-1547 |
3.92e-21 |
|
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: 100.29 E-value: 3.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTP-----GFLGYCPQENALWlNLTVREHLE 1413
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDpaslrRQIGVVLQDVFLF-SGTIRENIT 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1414 IFaaikgmrksDANVAIERLADALK----------LQDQLKSPV----KTLSEGVKRKLCFVLSILGNPSVVLLDEPSTG 1479
Cdd:COG2274 571 LG---------DPDATDEEIIEAARlaglhdfieaLPMGYDTVVgeggSNLSGGQRQRLAIARALLRNPRILILDEATSA 641
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081362 1480 MDPEGQQQMWQAIQATFSNteRGALLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSKFGKEYLL 1547
Cdd:COG2274 642 LDAETEAIILENLRRLLKG--RTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1339-1538 |
4.59e-21 |
|
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: 94.11 E-value: 4.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKG------SSTGDTPGFL--GYCPQENALWLNLTV-- 1408
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglSEAELYRLRRrmGMLFQSGALFDSLTVfe 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1409 ------REHLEIFAAIkgmrksdanvaIERLAdALKLQ------DQLKSPVKtLSEGVKRKLCFVLSILGNPSVVLLDEP 1476
Cdd:cd03261 97 nvafplREHTRLSEEE-----------IREIV-LEKLEavglrgAEDLYPAE-LSGGMKKRVALARALALDPELLLYDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 1477 STGMDPEGQ---QQMWQAIQATFSNTergALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLK 1538
Cdd:cd03261 164 TAGLDPIASgviDDLIRSLKKELGLT---SIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1327-1527 |
4.92e-21 |
|
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: 91.68 E-value: 4.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1327 CFVLKSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVL-----LKGSSTGDTPGFLGYCPQENA 1401
Cdd:cd03228 7 SFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILidgvdLRDLDLESLRKNIAYVPQDPF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1402 LWlNLTVREhleifaaikgmrksdaNVaierladalklqdqlkspvktLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMD 1481
Cdd:cd03228 87 LF-SGTIRE----------------NI---------------------LSGGQRQRIAIARALLRDPPILILDEATSALD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907081362 1482 PEGQQQMWQAIQATFSNteRGALLTTHYMAEAEAvCDRVAIMVSGR 1527
Cdd:cd03228 129 PETEALILEALRALAKG--KTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
529-717 |
5.23e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 92.30 E-value: 5.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 529 ALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMtdLENISKLTGVCPqcnvqfdfLTVRE 608
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAY--VPQRSEVPDSLP--------LTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 609 --NLRLFAKIKGIQAH------EVDNEVQRVLLElDMKNTQnilVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDP 680
Cdd:NF040873 77 lvAMGRWARRGLWRRLtrddraAVDDALERVGLA-DLAGRQ---LGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907081362 681 FSRHRVWNFLKERRAD-RVVLFSTQFMDEAdILADRKV 717
Cdd:NF040873 153 ESRERIIALLAEEHARgATVVVVTHDLELV-RRADPCV 189
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
511-729 |
5.69e-21 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 94.41 E-value: 5.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTkdYIQKSKRTeaLKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLEnISKL 590
Cdd:COG4559 2 LEAENLS--VRLGGRTL--LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWE-LARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQ-CNVQFDFlTVRENLRLfakikGIQAH-----EVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAIL- 663
Cdd:COG4559 77 RAVLPQhSSLAFPF-TVEEVVAL-----GRAPHgssaaQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAq 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 664 ------GDPQIFLLDEPTAGLDPFSRHRVWNFLKeRRADR-----VVL----FSTQFmdeadilADRKVFISKGKLKCAG 728
Cdd:COG4559 151 lwepvdGGPRWLFLDEPTSALDLAHQHAVLRLAR-QLARRgggvvAVLhdlnLAAQY-------ADRILLLHQGRLVAQG 222
|
.
gi 1907081362 729 S 729
Cdd:COG4559 223 T 223
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
510-680 |
6.63e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 93.54 E-value: 6.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYIQkskrTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNK--LSEMTDLENI 587
Cdd:COG4161 2 SIQLKNINCFYGS----HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdFSQKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 588 SKLTG----VCPQCNVqFDFLTVRENLrLFAKIK--GIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIA 661
Cdd:COG4161 78 RLLRQkvgmVFQQYNL-WPHLTVMENL-IEAPCKvlGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARA 155
|
170
....*....|....*....
gi 1907081362 662 ILGDPQIFLLDEPTAGLDP 680
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDP 174
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
511-680 |
7.73e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 93.56 E-value: 7.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNnklsemtdlENISKL 590
Cdd:COG1137 4 LEAENLVKSY----GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDG---------EDITHL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 T---------GVCPQCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIA 661
Cdd:COG1137 71 PmhkrarlgiGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARA 150
|
170
....*....|....*....
gi 1907081362 662 ILGDPQIFLLDEPTAGLDP 680
Cdd:COG1137 151 LATNPKFILLDEPFAGVDP 169
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1340-1535 |
7.86e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.07 E-value: 7.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1340 NISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGF-----LGYCPQENALWLNLTVREHLEI 1414
Cdd:PRK13548 20 DVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAelarrRAVLPQHSSLSFPFTVEEVVAM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1415 FAAIKGMRKSDANVAIE---RLADALKLQDqlkSPVKTLSEGVK------RKLCFVLSILGNPSVVLLDEPSTGMDPEGQ 1485
Cdd:PRK13548 100 GRAPHGLSRAEDDALVAaalAQVDLAHLAG---RDYPQLSGGEQqrvqlaRVLAQLWEPDGPPRWLLLDEPTSALDLAHQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081362 1486 QQMWQaIQATFSNTERGAL--------LTTHYmaeaeavCDRVAIMVSGRLRCIGSIQ 1535
Cdd:PRK13548 177 HHVLR-LARQLAHERGLAVivvlhdlnLAARY-------ADRIVLLHQGRLVADGTPA 226
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
511-736 |
8.93e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 94.53 E-value: 8.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqkSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLS-EMTDLENISK 589
Cdd:PRK13636 6 LKVEELNYNY---SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDySRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 LTGVCPQC-NVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQI 668
Cdd:PRK13636 83 SVGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081362 669 FLLDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEADILADRKVFISKGKLKCAG--SSLFLKKK 736
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEmqKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGnpKEVFAEKE 234
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
535-725 |
1.57e-20 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 91.85 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 535 LDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLEN-ISKLTgvcpQCNVQFDFLTVRENLRLF 613
Cdd:TIGR01277 19 LNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRpVSMLF----QENNLFAHLTVRQNIGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 614 AKiKGIQAHEVDNE-VQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKE 692
Cdd:TIGR01277 95 LH-PGLKLNAEQQEkVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQ 173
|
170 180 190
....*....|....*....|....*....|....*
gi 1907081362 693 --RRADRVVLFSTQFMDEADILADRKVFISKGKLK 725
Cdd:TIGR01277 174 lcSERQRTLLMVTHHLSDARAIASQIAVVSQGKIK 208
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
532-729 |
1.64e-20 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 95.18 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 532 DLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKL---SEMTDLENISKLTGVCPQCNVQFDFLTVRE 608
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsRKGIFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 609 NLRL-FAKIKGIQAHEVDNEVQRVLleldmkNTQNILVQ---NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRH 684
Cdd:TIGR02142 95 NLRYgMKRARPSERRISFERVIELL------GIGHLLGRlpgRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907081362 685 RVWNFLkERRADRV---VLFSTQFMDEADILADRKVFISKGKLKCAGS 729
Cdd:TIGR02142 169 EILPYL-ERLHAEFgipILYVSHSLQEVLRLADRVVVLEDGRVAAAGP 215
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1321-1526 |
1.87e-20 |
|
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: 91.16 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1321 YKGKKKCFVLKskkkiatrNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGS--STGDTPGFLGYCPQ 1398
Cdd:cd03226 7 FSYKKGTEILD--------DLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKpiKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1399 E-NALWLNLTVREHLEIFAaikgMRKSDANVAIERLADALKLQD-QLKSPvKTLSEGVKRKLCFVLSILGNPSVVLLDEP 1476
Cdd:cd03226 79 DvDYQLFTDSVREELLLGL----KELDAGNEQAETVLKDLDLYAlKERHP-LSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1477 STGMDPEGQQQMWQAIQaTFSNTERGALLTTHYMAEAEAVCDRVAIMVSG 1526
Cdd:cd03226 154 TSGLDYKNMERVGELIR-ELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
530-722 |
2.27e-20 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 91.76 E-value: 2.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 530 LKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSE-----MTDLENISKLTgvcpqcnvqfdFL 604
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEpgpdrMVVFQNYSLLP-----------WL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 605 TVRENLRLfaKIKGIQAHEVDNEVQRVLLE-LDM---KNTQNILVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDP 680
Cdd:TIGR01184 70 TVRENIAL--AVDRVLPDLSKSERRAIVEEhIALvglTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907081362 681 FSR----HRVWNFLKERRAdrVVLFSTQFMDEADILADRKVFISKG 722
Cdd:TIGR01184 148 LTRgnlqEELMQIWEEHRV--TVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
511-723 |
2.41e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 91.74 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqkskRTEALK-DLTLDvyKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNnklsemtdlENISK 589
Cdd:COG3840 2 LRLDDLTYRY-----GDFPLRfDLTIA--AGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNG---------QDLTA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 LTgvcP---------QCNVQFDFLTVREN--------LRLFAKikgiQAHEVDNEVQRVLLE--LDMKNTQnilvqnLSG 650
Cdd:COG3840 66 LP---PaerpvsmlfQENNLFPHLTVAQNiglglrpgLKLTAE----QRAQVEQALERVGLAglLDRLPGQ------LSG 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 651 GQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADR--VVLFSTQFMDEADILADRKVFISKGK 723
Cdd:COG3840 133 GQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
510-729 |
2.50e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.77 E-value: 2.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLEnisK 589
Cdd:PRK10851 2 SIEIANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 LTGVCPQCNVQFDFLTVREN----LRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGD 665
Cdd:PRK10851 75 KVGFVFQHYALFRHMTVFDNiafgLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081362 666 PQIFLLDEPTAGLDPFSRH--RVW--NFLKERRADRVvlFSTQFMDEADILADRKVFISKGKLKCAGS 729
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKelRRWlrQLHEELKFTSV--FVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1339-1534 |
3.52e-20 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 91.37 E-value: 3.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTgDTPG------FLGYcpqenALWLNLTVREH- 1411
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI-TEPGpdrmvvFQNY-----SLLPWLTVRENi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1412 -LEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQ 1490
Cdd:TIGR01184 76 aLAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907081362 1491 AIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSI 1534
Cdd:TIGR01184 156 ELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQI 199
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
511-743 |
4.20e-20 |
|
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: 91.14 E-value: 4.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTdLENISKL 590
Cdd:cd03251 1 VEFKNVTFRY--PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT-LASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVQFDFlTVRENLRlFAK-----------IKGIQAHEvdnevqrVLLELDMKNTQNILVQ--NLSGGQKRKLT 657
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENIA-YGRpgatreeveeaARAANAHE-------FIMELPEGYDTVIGERgvKLSGGQRQRIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 658 FGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRVVL-----FSTqFMDeadilADRKVFISKGKLKCAGSSLF 732
Cdd:cd03251 149 IARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFviahrLST-IEN-----ADRIVVLEDGKIVERGTHEE 222
|
250
....*....|.
gi 1907081362 733 LKKKWGIGYHL 743
Cdd:cd03251 223 LLAQGGVYAKL 233
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
509-728 |
4.36e-20 |
|
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: 91.68 E-value: 4.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 509 EAIRIRNLTkdyIQKSKRTeALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGW-VTIHNNKLSEmTDLENI 587
Cdd:COG1119 2 PLLELRNVT---VRRGGKT-ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGG-EDVWEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 588 SKLTG-VCPQcnVQFDF---LTVRENLR--LFAKIkGIQAHEVDNEVQR---VLLELDMKNTQNILVQNLSGGQKRKLTF 658
Cdd:COG1119 77 RKRIGlVSPA--LQLRFprdETVLDVVLsgFFDSI-GLYREPTDEQRERareLLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081362 659 GIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEadILA--DRKVFISKGKLKCAG 728
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEE--IPPgiTHVLLLKDGRVVAAG 225
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1337-1483 |
5.19e-20 |
|
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: 90.16 E-value: 5.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPG--------FLGYCPQENALWLNLTV 1408
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGraipylrrKIGVVFQDFRLLPDRNV 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081362 1409 REHLEIFAAIKGMRKSDANvaiERLADALKLQDqLKSPVKT----LSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1483
Cdd:cd03292 96 YENVAFALEVTGVPPREIR---KRVPAALELVG-LSHKHRAlpaeLSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
527-753 |
5.87e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 92.10 E-value: 5.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 527 TEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHN---NKLSEMTDLENISKLTGVCPQC-NVQFD 602
Cdd:PRK13643 19 SRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvSSTSKQKEIKPVRKKVGVVFQFpESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 603 FLTVRENLRLFAKIKGIQAHEVDNEVQRvllELDMKNTQNILVQN----LSGGQKRKLTFGIAILGDPQIFLLDEPTAGL 678
Cdd:PRK13643 99 EETVLKDVAFGPQNFGIPKEKAEKIAAE---KLEMVGLADEFWEKspfeLSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 679 DPFSRHRVWNFLKE-RRADRVVLFSTQFMDEADILADRKVFISKGKLKCAGSSL-------FLK-KKWGI--GYHLSLQL 747
Cdd:PRK13643 176 DPKARIEMMQLFESiHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSdvfqevdFLKaHELGVpkATHFADQL 255
|
....*.
gi 1907081362 748 SETCVH 753
Cdd:PRK13643 256 QKTGAV 261
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
511-729 |
6.15e-20 |
|
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: 90.25 E-value: 6.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKSKrtEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMtDLENISKL 590
Cdd:cd03244 3 IEFKNVSLRYRPNLP--PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI-GLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVQFDFlTVRENL---------RLFAKIKGIQAHEVdneVQRVLLELDMKNTQNILvqNLSGGQKRKLTFGIA 661
Cdd:cd03244 80 ISIIPQDPVLFSG-TIRSNLdpfgeysdeELWQALERVGLKEF---VESLPGGLDTVVEEGGE--NLSVGQRQLLCLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081362 662 ILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRVVLFSTQ----FMDeadilADRKVFISKGKLKCAGS 729
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHrldtIID-----SDRILVLDKGRVVEFDS 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
511-678 |
7.38e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 95.24 E-value: 7.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLENISKL 590
Cdd:PRK09700 6 ISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVQFDFLTVRENL---RLFAK----IKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAIL 663
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLyigRHLTKkvcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170
....*....|....*
gi 1907081362 664 GDPQIFLLDEPTAGL 678
Cdd:PRK09700 162 LDAKVIIMDEPTSSL 176
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1337-1540 |
9.58e-20 |
|
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: 95.21 E-value: 9.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGF-----LGYCPQeNALWLNLTVREH 1411
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswrrqIAWVPQ-NPYLFAGTIREN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1412 LeifaaikgmRKSDANVAIERLADALK----------LQDQLKSPV----KTLSEGVKRKLCFVLSILGNPSVVLLDEPS 1477
Cdd:COG4988 431 L---------RLGRPDASDEELEAALEaagldefvaaLPDGLDTPLgeggRGLSGGQAQRLALARALLRDAPLLLLDEPT 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081362 1478 TGMDPEGQQQMWQAIQATFSNteRGALLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSK 1540
Cdd:COG4988 502 AHLDAETEAEILQALRRLAKG--RTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
528-680 |
1.18e-19 |
|
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: 94.73 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 528 EALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLEnISKLTGVCPQCNVQFDfLTVR 607
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE-VRRRVSVCAQDAHLFD-TTVR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 608 ENLRLFAkiKGIQAHEVDNEVQRVLLELDMKNTQNIL-------VQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDP 680
Cdd:TIGR02868 427 ENLRLAR--PDATDEELWAALERVGLADWLRALPDGLdtvlgegGARLSGGERQRLALARALLADAPILLLDEPTEHLDA 504
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
529-729 |
1.27e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 90.96 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 529 ALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKL---SEMTDLENISKLTGVC---PQCNVqFD 602
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstSKNKDIKQIRKKVGLVfqfPESQL-FE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 603 fLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMknTQNILVQN---LSGGQKRKltfgIAILG----DPQIFLLDEPT 675
Cdd:PRK13649 101 -ETVLKDVAFGPQNFGVSQEEAEALAREKLALVGI--SESLFEKNpfeLSGGQMRR----VAIAGilamEPKILVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 676 AGLDPFSRHRVWNFLKE-RRADRVVLFSTQFMDEADILADRKVFISKGKLKCAGS 729
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKlHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
511-723 |
1.49e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 92.59 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLEnisKL 590
Cdd:PRK11607 20 LEIRNLTKSF----DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ---RP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFL 670
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081362 671 LDEPTAGLDPFSRHR----VWNFLkERRADRVVLFsTQFMDEADILADRKVFISKGK 723
Cdd:PRK11607 173 LDEPMGALDKKLRDRmqleVVDIL-ERVGVTCVMV-THDQEEAMTMAGRIAIMNRGK 227
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
510-710 |
2.12e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 95.19 E-value: 2.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNklsemtDLENISK 589
Cdd:NF033858 1 VARLEGVSHRY----GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGG------DMADARH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 LTGVCPQC---------NVQFDfLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGI 660
Cdd:NF033858 71 RRAVCPRIaympqglgkNLYPT-LSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCC 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907081362 661 AILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRV---VLFSTQFMDEAD 710
Cdd:NF033858 150 ALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPgmsVLVATAYMEEAE 202
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
511-729 |
2.50e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.05 E-value: 2.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqkSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLENISKL 590
Cdd:PRK13644 2 IRLENVSYSY---PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQC-NVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIF 669
Cdd:PRK13644 79 VGIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 670 LLDEPTAGLDPFSRHRVWNFLKE-RRADRVVLFSTQFMDEADIlADRKVFISKGKLKCAGS 729
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKlHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1339-1528 |
2.66e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.54 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSS-TGDTP------GfLGYCPQENALWLNLTVREH 1411
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPvRFRSPrdaqaaG-IAIIHQELNLVPNLSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1412 leIF----AAIKG-MRKSDANVAIERLADALKLQDQLKSPVKTLSEGvKRKLcfVL---SILGNPSVVLLDEPSTGMDPE 1483
Cdd:COG1129 100 --IFlgrePRRGGlIDWRAMRRRARELLARLGLDIDPDTPVGDLSVA-QQQL--VEiarALSRDARVLILDEPTASLTER 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907081362 1484 GQQQMWQAIQATfsnTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1528
Cdd:COG1129 175 EVERLFRIIRRL---KAQGVaiIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
511-729 |
2.69e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 89.79 E-value: 2.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKSKRTeALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLENISKL 590
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKY-TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFL 670
Cdd:PRK13650 84 GMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 671 LDEPTAGLDPFSRHRVWNFLKERRADR--VVLFSTQFMDEAdILADRKVFISKGKLKCAGS 729
Cdd:PRK13650 164 LDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEV-ALSDRVLVMKNGQVESTST 223
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
523-692 |
2.83e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 93.96 E-value: 2.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 523 KSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLC---VPTKGWVTIHNNKLsemtDLENISKLTGVCPQCNV 599
Cdd:TIGR00955 34 ERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSpkgVKGSGSVLLNGMPI----DAKEMRAISAYVQQDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 600 QFDFLTVRENLRLFAKIKgIQAHEVDNE----VQRVLLELDMKNTQNIL------VQNLSGGQKRKLTFGIAILGDPQIF 669
Cdd:TIGR00955 110 FIPTLTVREHLMFQAHLR-MPRRVTKKEkrerVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDPPLL 188
|
170 180
....*....|....*....|...
gi 1907081362 670 LLDEPTAGLDPFSRHRVWNFLKE 692
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKG 211
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1339-1529 |
3.99e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.82 E-value: 3.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLkGSSTgdtpgFLGYCPQENA-LWLNLTVREHLEifAA 1417
Cdd:COG0488 332 DDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV-----KIGYFDQHQEeLDPDKTVLDELR--DG 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1418 IKGMRKSDanvAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQaTFS 1497
Cdd:COG0488 404 APGGTEQE---VRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALD-DFP 479
|
170 180 190
....*....|....*....|....*....|..
gi 1907081362 1498 NTergALLTTHYMAEAEAVCDRVAIMVSGRLR 1529
Cdd:COG0488 480 GT---VLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1339-1483 |
4.21e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 87.80 E-value: 4.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGS-----STGDTPGF---LGYCPQENALWLNLTVRE 1410
Cdd:COG2884 19 SDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsrlKRREIPYLrrrIGVVFQDFRLLPDRTVYE 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 1411 HLEIFAAIKGMRKSDANvaiERLADALK---LQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1483
Cdd:COG2884 99 NVALPLRVTGKSRKEIR---RRVREVLDlvgLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPE 171
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1335-1528 |
6.27e-19 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 86.33 E-value: 6.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1335 KIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSS-TGDTPGF-----LGYCP---QENALWLN 1405
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPvTRRSPRDairagIAYVPedrKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1406 LTVREhleifaaikgmrksdaNVAIERLadalklqdqlkspvktLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQ 1485
Cdd:cd03215 93 LSVAE----------------NIALSSL----------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907081362 1486 QQMWQAIQATfsnTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1528
Cdd:cd03215 141 AEIYRLIREL---ADAGKavLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
515-729 |
6.75e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 88.03 E-value: 6.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 515 NLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLENISKLTGVC 594
Cdd:PRK10895 8 NLAKAY----KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 595 PQCNVQFDFLTVRENLRLFAKI-KGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFLLDE 673
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081362 674 PTAGLDPFSRHRVWNFLKERRADRV-VLFSTQFMDEADILADRKVFISKGKLKCAGS 729
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRDSGLgVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1336-1528 |
6.93e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.01 E-value: 6.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1336 IATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKG-----SSTGDtpgflgycpqenALWL------ 1404
Cdd:COG3845 19 VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpvriRSPRD------------AIALgigmvh 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1405 -------NLTVREHL-----EIFAAIKGMRKsdANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVL 1472
Cdd:COG3845 87 qhfmlvpNLTVAENIvlglePTKGGRLDRKA--ARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081362 1473 LDEPSTGMDPegqqqmwQAIQATFSN----TERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1528
Cdd:COG3845 165 LDEPTAVLTP-------QEADELFEIlrrlAAEGKsiIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1317-1528 |
7.17e-19 |
|
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: 86.81 E-value: 7.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1317 LRKEYKGKKkcfVLKskkkiatrNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSS-TGDTPGF--- 1392
Cdd:cd03262 6 LHKSFGDFH---VLK--------GIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKlTDDKKNInel 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1393 ---LGYCPQENALWLNLTVREHLeIFAAIK--GMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGN 1467
Cdd:cd03262 75 rqkVGMVFQQFNLFPHLTVLENI-TLAPIKvkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081362 1468 PSVVLLDEPSTGMDPEGQQQMWQAIQATfsnTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1528
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLDVMKDL---AEEGMtmVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
510-715 |
9.34e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 91.62 E-value: 9.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLENISK 589
Cdd:COG1129 4 LLEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 ltGV---------CPQcnvqfdfLTVRENL---RLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQK---- 653
Cdd:COG1129 80 --GIaiihqelnlVPN-------LSVAENIflgREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQqlve 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 654 --RkltfgiAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRV-VLFSTQFMDEADILADR 715
Cdd:COG1129 151 iaR------ALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVaIIYISHRLDEVFEIADR 209
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
510-724 |
1.05e-18 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 87.78 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYIQKskrtEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLC--VP---TKGWVTIHN-NKLSEMTD 583
Cdd:COG1117 11 KIEVRNLNVYYGDK----QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPgarVEGEILLDGeDIYDPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 584 LENISKLTG-VCPQCNVqfdF-LTVRENLRLFAKIKGIQA-HEVDNEVQRVLLEL----DMKNTQNILVQNLSGGQKRKL 656
Cdd:COG1117 87 VVELRRRVGmVFQKPNP---FpKSIYDNVAYGLRLHGIKSkSELDEIVEESLRKAalwdEVKDRLKKSALGLSGGQQQRL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 657 TfgIA--ILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRVVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:COG1117 164 C--IAraLAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
530-738 |
1.08e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 89.55 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 530 LKDLTLDV-----YKGqITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSemtDLENiskltGVC-P--QCNVQF 601
Cdd:PRK11144 10 LGDLCLTVnltlpAQG-ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLF---DAEK-----GIClPpeKRRIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 602 DF--------LTVRENLRLfaKIKGIQAHEVDNEVQrvLLELDmkntqNILVQ---NLSGGQKRKLTFGIAILGDPQIFL 670
Cdd:PRK11144 81 VFqdarlfphYKVRGNLRY--GMAKSMVAQFDKIVA--LLGIE-----PLLDRypgSLSGGEKQRVAIGRALLTAPELLL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 671 LDEPTAGLDPFSRHRVWNFLkERRADRV---VLFSTQFMDEADILADRKVFISKGKLKCAGSslfLKKKWG 738
Cdd:PRK11144 152 MDEPLASLDLPRKRELLPYL-ERLAREInipILYVSHSLDEILRLADRVVVLEQGKVKAFGP---LEEVWA 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1339-1476 |
1.47e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.28 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTgdtpgfLGYCPQENALWLNLTVRE-----HLE 1413
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLR------IGYLPQEPPLDDDLTVLDtvldgDAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1414 IFAAIKGMRKSDANVA---------------------------IERLADALKL-QDQLKSPVKTLSEGVKRK--LCFVLs 1463
Cdd:COG0488 89 LRALEAELEELEAKLAepdedlerlaelqeefealggweaearAEEILSGLGFpEEDLDRPVSELSGGWRRRvaLARAL- 167
|
170
....*....|...
gi 1907081362 1464 iLGNPSVVLLDEP 1476
Cdd:COG0488 168 -LSEPDLLLLDEP 179
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
527-680 |
1.68e-18 |
|
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: 85.49 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 527 TEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDL--ENI---SKLTGVCPQcnvqf 601
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEphENIlylGHLPGLKPE----- 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081362 602 dfLTVRENLRLFAKIKGIQAHEVDNEVQRVllelDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDP 680
Cdd:TIGR01189 88 --LSALENLHFWAAIHGGAQRTIEDALAAV----GLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
529-722 |
1.82e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 87.06 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 529 ALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLsemtdlENISKLTGVCPQCNVQFDFLTVRE 608
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV------EGPGAERGVVFQNEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 609 NLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRH---- 684
Cdd:PRK11248 90 NVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREqmqt 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907081362 685 ---RVWnflkeRRADRVVLFSTQFMDEADILADRKVFISKG 722
Cdd:PRK11248 170 lllKLW-----QETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1317-1528 |
2.15e-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: 86.08 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1317 LRKEYKGKKkcfVLKskkkiatrNISFCVRKGEVVGLLGHNGAGKSTSIKMITG-----ETKPSAGQVLLKGSSTGDtpg 1391
Cdd:cd03260 6 LNVYYGDKH---ALK--------DISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYD--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1392 flgycPQENALWL--------------NLTVREHLEIFAAIKGMRKSDAnvAIERLADALK---LQDQLKSPVK--TLSE 1452
Cdd:cd03260 72 -----LDVDVLELrrrvgmvfqkpnpfPGSIYDNVAYGLRLHGIKLKEE--LDERVEEALRkaaLWDEVKDRLHalGLSG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 1453 GVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQATfsNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1528
Cdd:cd03260 145 GQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1337-1546 |
3.01e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 88.74 E-value: 3.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGF---LGYCPQENALWLNLTVREHLE 1413
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYqrpINMMFQSYALFPHMTVEQNIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1414 IFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQ 1493
Cdd:PRK11607 114 FGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVV 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081362 1494 ATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS----IQHLKSKFGKEYL 1546
Cdd:PRK11607 194 DILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEpeeiYEHPTTRYSAEFI 250
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
507-724 |
3.71e-18 |
|
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: 84.02 E-value: 3.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 507 GKEAIRIRNLTKDYiqkskrteALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLEN 586
Cdd:cd03215 1 GEPVLEVRGLSVKG--------AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 587 IS----------KLTGVCPQcnvqfdfLTVRENLrlfakikgiqahevdnevqrvlleldmkntqnILVQNLSGGQKRKL 656
Cdd:cd03215 73 IRagiayvpedrKREGLVLD-------LSVAENI--------------------------------ALSSLLSGGNQQKV 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 657 TFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADR--VVLFSTQfMDEADILADRKVFISKGKL 724
Cdd:cd03215 114 VLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGkaVLLISSE-LDELLGLCDRILVMYEGRI 182
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
508-724 |
4.43e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 85.66 E-value: 4.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 508 KEAIRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLC-----VPTKGWVTIHN-NKLSEM 581
Cdd:PRK14267 2 KFAIETVNLRVYY----GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGrNIYSPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 582 TDLENISKLTGVCPQCNVQFDFLTVRENLRLFAKIKGI--QAHEVDNEVQRVL----LELDMKNTQNILVQNLSGGQKRK 655
Cdd:PRK14267 78 VDPIEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALkkaaLWDEVKDRLNDYPSNLSGGQRQR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081362 656 LTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRVVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
511-731 |
4.64e-18 |
|
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: 89.86 E-value: 4.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGL--CVPTKGWVTIHNNKLSEMTDLENIS 588
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVALCEKCGYVERPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 589 KLTGVCPQCNVQF-----DFL----TVRENL---------RLFA----------KIKGIQ--AHEVDNEVQRVLLELDMK 638
Cdd:TIGR03269 77 KVGEPCPVCGGTLepeevDFWnlsdKLRRRIrkriaimlqRTFAlygddtvldnVLEALEeiGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 639 NTQNI---LVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEADILA 713
Cdd:TIGR03269 157 QLSHRithIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIEDLS 236
|
250
....*....|....*...
gi 1907081362 714 DRKVFISKGKLKCAGSSL 731
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPD 254
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
514-692 |
4.87e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 85.25 E-value: 4.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 514 RNLTKDYIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMT-----DLEN-- 586
Cdd:PRK11629 9 DNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaakaELRNqk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 587 ---ISKLTGVCPqcnvqfDFlTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAIL 663
Cdd:PRK11629 89 lgfIYQFHHLLP------DF-TALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALV 161
|
170 180
....*....|....*....|....*....
gi 1907081362 664 GDPQIFLLDEPTAGLDPFSRHRVWNFLKE 692
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNADSIFQLLGE 190
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
511-743 |
6.16e-18 |
|
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: 84.90 E-value: 6.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKsKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMtDLENISKL 590
Cdd:cd03249 1 IEFKNVSFRYPSR-PDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDL-NLRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVQFDfLTVRENLRlFAKIKGIQAHEVDNEVQRVLLELDMK--NTQNILVQN----LSGGQKRKLTFGIAILG 664
Cdd:cd03249 79 IGLVSQEPVLFD-GTIAENIR-YGKPDATDEEVEEAAKKANIHDFIMSlpDGYDTLVGErgsqLSGGQKQRIAIARALLR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 665 DPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRVVL-----FSTqfmdeadIL-ADRKVFISKGKLKCAGSSLFLKKKWG 738
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIviahrLST-------IRnADLIAVLQNGQVVEQGTHDELMAQKG 229
|
....*
gi 1907081362 739 IGYHL 743
Cdd:cd03249 230 VYAKL 234
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1331-1528 |
6.95e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 85.91 E-value: 6.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1331 KSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDtpgflgycpqENALWlnlTVRE 1410
Cdd:PRK13633 19 ESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSD----------EENLW---DIRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1411 HL---------EIFAAIkgmrkSDANVAI-------------ERLADALK---LQDQLKSPVKTLSEGVKRKLCFVLSIL 1465
Cdd:PRK13633 86 KAgmvfqnpdnQIVATI-----VEEDVAFgpenlgippeeirERVDESLKkvgMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081362 1466 GNPSVVLLDEPSTGMDPEGQQQMWQAIQATFSNTERGALLTTHYMAEAeAVCDRVAIMVSGRL 1528
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKV 222
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
514-729 |
7.54e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 87.78 E-value: 7.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 514 RNLTKDYI-QKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLENIS---K 589
Cdd:PRK10070 27 QGLSKEQIlEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 LTGVCPQCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIF 669
Cdd:PRK10070 107 KIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081362 670 LLDEPTAGLDPFSRHRVWNFLKERRA--DRVVLFSTQFMDEADILADRKVFISKGKLKCAGS 729
Cdd:PRK10070 187 LMDEAFSALDPLIRTEMQDELVKLQAkhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
530-695 |
1.26e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.00 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 530 LKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNnklSEMTDLENISKLTGVCPQ--CNvqfDFLTVR 607
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEACHYLGHRnaMK---PALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 608 ENLRLFAKIKGiqAHEVDneVQRVLLELDMKNTQNILVQNLSGGQKRKLtfGIAIL---GDPqIFLLDEPTAGLDPFSRH 684
Cdd:PRK13539 92 ENLEFWAAFLG--GEELD--IAAALEAVGLAPLAHLPFGYLSAGQKRRV--ALARLlvsNRP-IWILDEPTAALDAAAVA 164
|
170
....*....|.
gi 1907081362 685 RVWNFLKERRA 695
Cdd:PRK13539 165 LFAELIRAHLA 175
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1319-1533 |
1.67e-17 |
|
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: 83.89 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1319 KEYKGKKKcfvlkskkkiATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGF-----L 1393
Cdd:cd03295 8 KRYGGGKK----------AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVelrrkI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1394 GYCPQENALWLNLTVREHLEIFAAIKGMRKSDanvAIERLADALKLQDQlkSPVK-------TLSEGVKRKLCFVLSILG 1466
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALVPKLLKWPKEK---IRERADELLALVGL--DPAEfadryphELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1467 NPSVVLLDEPSTGMDP---EGQQQMWQAIQATFSNTergALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1533
Cdd:cd03295 153 DPPLLLMDEPFGALDPitrDQLQEEFKRLQQELGKT---IVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1328-1547 |
1.73e-17 |
|
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: 83.69 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1328 FVLKSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGS--STGDTPGF---LGYCPQENAL 1402
Cdd:cd03252 8 FRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlALADPAWLrrqVGVVLQENVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1403 wLNLTVREHLEIFAAIKGMRKSdanVAIERLADALKLQDQLKSPVKT--------LSEGVKRKLCFVLSILGNPSVVLLD 1474
Cdd:cd03252 88 -FNRSIRDNIALADPGMSMERV---IEAAKLAGAHDFISELPEGYDTivgeqgagLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081362 1475 EPSTGMDPEGQQQMWQAIQATFSNteRGALLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFGKEYLL 1547
Cdd:cd03252 164 EATSALDYESEHAIMRNMHDICAG--RTVIIIAHRLSTVKNA-DRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1339-1528 |
2.07e-17 |
|
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: 81.49 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKG---SSTG--DTPGFLGYCPQENALwLNLTVREhle 1413
Cdd:cd03246 19 RNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGadiSQWDpnELGDHVGYLPQDDEL-FSGSIAE--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1414 ifaaikgmrksdaNVaierladalklqdqlkspvktLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQ 1493
Cdd:cd03246 95 -------------NI---------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIA 140
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907081362 1494 ATfsnTERGA--LLTTHYMaEAEAVCDRVAIMVSGRL 1528
Cdd:cd03246 141 AL---KAAGAtrIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
511-729 |
2.10e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 84.47 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqkSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEmTDLENISKL 590
Cdd:PRK13652 4 IETRDLCYSY---SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK-ENIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVQFDFLTVRENLRLFAKIK-GIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIF 669
Cdd:PRK13652 80 VGLVFQNPDDQIFSPTVEQDIAFGPINlGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081362 670 LLDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEADILADRKVFISKGKLKCAGS 729
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDlpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGT 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
511-680 |
2.17e-17 |
|
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: 81.49 E-value: 2.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTkdYIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEmTDLENISKL 590
Cdd:cd03246 1 LEVENVS--FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQ-WDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQcnvqfdfltvreNLRLFAkikGIQAhevdnevqrvlleldmkntQNIlvqnLSGGQKRKLTFGIAILGDPQIFL 670
Cdd:cd03246 78 VGYLPQ------------DDELFS---GSIA-------------------ENI----LSGGQRQRLGLARALYGNPRILV 119
|
170
....*....|
gi 1907081362 671 LDEPTAGLDP 680
Cdd:cd03246 120 LDEPNSHLDV 129
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
529-728 |
2.35e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 84.03 E-value: 2.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 529 ALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVtIHNNKLSEMTDLENISKLTGVCPQ--------CNVQ 600
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI-FYNNQAITDDNFEKLRKHIGIVFQnpdnqfvgSIVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 601 FDFLTVRENlrlfakiKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKltfgIAILG----DPQIFLLDEPTA 676
Cdd:PRK13648 103 YDVAFGLEN-------HAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQR----VAIAGvlalNPSVIILDEATS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907081362 677 GLDPFSRHRVWNFLKERRADR-VVLFS-TQFMDEAdILADRKVFISKGKLKCAG 728
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKSEHnITIISiTHDLSEA-MEADHVIVMNKGTVYKEG 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1327-1528 |
2.35e-17 |
|
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: 83.09 E-value: 2.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1327 CFVLKSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITG---ETKPSAGQVLLKG--SSTGDTPGFLGYCPQENA 1401
Cdd:cd03234 12 KAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGqpRKPDQFQKCVAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1402 LWLNLTVREHLEIFAAIKGMRKS--------DANVAIERLADAlKLQDQLkspVKTLSEGVKRKLCFVLSILGNPSVVLL 1473
Cdd:cd03234 92 LLPGLTVRETLTYTAILRLPRKSsdairkkrVEDVLLRDLALT-RIGGNL---VKGISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 1474 DEPSTGMDPEGQQQMWQaIQATFSNTERGALLTTHY-MAEAEAVCDRVAIMVSGRL 1528
Cdd:cd03234 168 DEPTSGLDSFTALNLVS-TLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEI 222
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1337-1533 |
2.45e-17 |
|
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: 83.16 E-value: 2.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGF---LGYCPQENALWLNLTVREHLE 1413
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQernVGFVFQHYALFRHMTVFDNVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1414 IFAAIKGMRKSDANVAIERLADAL-------KLQDQLKSpvkTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQ 1486
Cdd:cd03296 97 FGLRVKPRSERPPEAEIRAKVHELlklvqldWLADRYPA---QLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907081362 1487 QMWQAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1533
Cdd:cd03296 174 ELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
529-720 |
2.51e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 83.68 E-value: 2.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 529 ALKDLTLDVYKGQITAILGHSGAGKSTLL---NVLSGLcVPT---KGWVTIHNNKL-SEMTDLENISKLTGVCPQCNVQF 601
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDL-IPGfrvEGKVTFHGKNLyAPDVDPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 602 DfLTVRENLRLFAKIKGIQAhEVDNEVQRVL----LELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAG 677
Cdd:PRK14243 104 P-KSIYDNIAYGARINGYKG-DMDELVERSLrqaaLWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907081362 678 LDPFSRHRVWNFLKERRADRVVLFSTQFMDEADILADRKVFIS 720
Cdd:PRK14243 182 LDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFN 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
528-743 |
2.80e-17 |
|
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: 82.92 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 528 EALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSeMTDLENISKLTGVCPQCNVQFDfLTVR 607
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLA-LADPAWLRRQVGVVLQENVLFN-RSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 608 ENLRL------------FAKIKGiqAHEvdnevqrVLLELDMKNTQnILVQN---LSGGQKRKLTFGIAILGDPQIFLLD 672
Cdd:cd03252 94 DNIALadpgmsmervieAAKLAG--AHD-------FISELPEGYDT-IVGEQgagLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 673 EPTAGLDPFSRHRVWNFLKERRADRVVLFSTQFMdEADILADRKVFISKGKLKCAGSSLFLKKKWGIGYHL 743
Cdd:cd03252 164 EATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
511-679 |
3.01e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 83.52 E-value: 3.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKSkrteALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLEnISKL 590
Cdd:PRK11231 3 LRTENLTVGYGTKR----ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ-LARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVQFDFLTVRE--------NLRLFAKIKGIQAHEVDNEVQRV-LLELDMKntqniLVQNLSGGQKRKLTFGIA 661
Cdd:PRK11231 78 LALLPQHHLTPEGITVRElvaygrspWLSLWGRLSAEDNARVNQAMEQTrINHLADR-----RLTDLSGGQRQRAFLAMV 152
|
170
....*....|....*...
gi 1907081362 662 ILGDPQIFLLDEPTAGLD 679
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLD 170
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1335-1534 |
3.08e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 83.94 E-value: 3.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1335 KIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGFLGYCPQENALWLNLTVREHLE- 1413
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVGLVFQYPEYQLFEe 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1414 -IFAAIK------GMRKSDANVAIERLADALKLQDQL---KSPVKtLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1483
Cdd:PRK13637 100 tIEKDIAfgpinlGLSEEEIENRVKRAMNIVGLDYEDykdKSPFE-LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 1484 GQQQMWQAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSI 1534
Cdd:PRK13637 179 GRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
511-710 |
3.34e-17 |
|
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: 81.75 E-value: 3.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKSKRTE-ALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNklsemtdlenisk 589
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 lTGVCPqcnvQFDFL---TVRENLrLFAKikgiqahEVDNE-VQRVL----LELDMKntqnILVQ-----------NLSG 650
Cdd:cd03250 68 -IAYVS----QEPWIqngTIRENI-LFGK-------PFDEErYEKVIkacaLEPDLE----ILPDgdlteigekgiNLSG 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 651 GQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWN--FLKERRADRVVLFST---QFMDEAD 710
Cdd:cd03250 131 GQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNKTRILVThqlQLLPHAD 195
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
510-724 |
3.70e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 82.88 E-value: 3.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNnklSEMTDLENISK 589
Cdd:PRK11264 3 AIEVKNLVKKF----HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGD---ITIDTARSLSQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 LTGVCPQCNVQFDFltVRENLRLFAK-------------IKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKL 656
Cdd:PRK11264 76 QKGLIRQLRQHVGF--VFQNFNLFPHrtvleniiegpviVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081362 657 TFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLK----ERRADRVVlfsTQFMDEADILADRKVFISKGKL 724
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPELVGEVLNTIRqlaqEKRTMVIV---THEMSFARDVADRAIFMDQGRI 222
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1341-1508 |
4.37e-17 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 81.39 E-value: 4.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1341 ISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGFLgycpQENALWLN--------LTVREHL 1412
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSI----ARGLLYLGhapgikttLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1413 EIFAAIKGmrksdaNVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAI 1492
Cdd:cd03231 95 RFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAM 168
|
170
....*....|....*...
gi 1907081362 1493 QAtfsNTERG--ALLTTH 1508
Cdd:cd03231 169 AG---HCARGgmVVLTTH 183
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1339-1508 |
4.62e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 81.39 E-value: 4.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSStgdtpgfLGYCPQE---NALWLN--------LT 1407
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP-------IRRQRDEyhqDLLYLGhqpgikteLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1408 VREHLEIFAAIKGMRKSDAnvaierLADALK---LQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEG 1484
Cdd:PRK13538 91 ALENLRFYQRLHGPGDDEA------LWEALAqvgLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQG 164
|
170 180
....*....|....*....|....*..
gi 1907081362 1485 QQQmwqaIQATFS-NTERG--ALLTTH 1508
Cdd:PRK13538 165 VAR----LEALLAqHAEQGgmVILTTH 187
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
511-729 |
4.65e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 85.00 E-value: 4.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIhnnklsemtDLENISKL 590
Cdd:PRK09452 15 VELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIML---------DGQDITHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 tgvcPQCNVQ----------FDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGI 660
Cdd:PRK09452 82 ----PAENRHvntvfqsyalFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 661 AILGDPQIFLLDEPTAGLDPFSRHRVWNFLK--ERRADRVVLFSTQFMDEADILADRKVFISKGKLKCAGS 729
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALDYKLRKQMQNELKalQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
511-701 |
4.70e-17 |
|
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: 82.28 E-value: 4.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKSKrteALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTdLENISKL 590
Cdd:cd03253 1 IEFENVTFAYDPGRP---VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT-LDSLRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVQFDfLTVRENLRlFAK--------IKGIQAHEVDNEVQRvlleldMKNTQNILVQN----LSGGQKRKLTF 658
Cdd:cd03253 77 IGVVPQDTVLFN-DTIGYNIR-YGRpdatdeevIEAAKAAQIHDKIMR------FPDGYDTIVGErglkLSGGEKQRVAI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907081362 659 GIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRVVLF 701
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIV 191
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
526-732 |
5.38e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 82.23 E-value: 5.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 526 RTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLENISKLTGVCPQCNVQFDFLT 605
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRRVFSRMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 606 VRENLRL---FAKIKgiQAHEVDNEVQRVLLELDMKNTQNilVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFS 682
Cdd:PRK11614 97 VEENLAMggfFAERD--QFQERIKWVYELFPRLHERRIQR--AGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907081362 683 RHRVWNFLKERRADRVVLFST-QFMDEADILADRKVFISKGK--LKCAGSSLF 732
Cdd:PRK11614 173 IQQIFDTIEQLREQGMTIFLVeQNANQALKLADRGYVLENGHvvLEDTGDALL 225
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
511-724 |
6.47e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 82.27 E-value: 6.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQkskrTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLC-----VPTKGWVTIHNNKLSEMtDLE 585
Cdd:PRK14247 4 IEIRDLKVSFGQ----VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKM-DVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 586 NISKLTGVCPQCNVQFDFLTVRENLRLFAKIKGI--QAHEVDNEVQRVL----LELDMKNTQNILVQNLSGGQKRKLTFG 659
Cdd:PRK14247 79 ELRRRVQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALekaqLWDEVKDRLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 660 IAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRVVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1337-1546 |
6.61e-17 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 84.40 E-value: 6.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSikmitgetkpsAGQVLLKGSSTGDTP-GFLGYCPQENALWLNL--------- 1406
Cdd:NF000106 28 AVDGVDLDVREGTVLGVLGP*GAA**RG-----------ALPAHV*GPDAGRRPwRF*TWCANRRALRRTIg*hrpvr*g 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1407 -----TVREHLEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMD 1481
Cdd:NF000106 97 rresfSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 1482 PEGQQQMWQAIQATFSNTERgALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKEYL 1546
Cdd:NF000106 177 PRTRNEVWDEVRSMVRDGAT-VLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTL 240
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1337-1532 |
7.03e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 86.01 E-value: 7.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKgssTGD------TPGF---------LGYCPQENA 1401
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVR---VGDewvdmtKPGPdgrgrakryIGILHQEYD 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1402 LWLNLTVREHLEIFAAIK-----GMRKsdanvAIERLA----DALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVL 1472
Cdd:TIGR03269 376 LYPHRTVLDNLTEAIGLElpdelARMK-----AVITLKmvgfDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVI 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1473 LDEPSTGMDPEGQQQMWQAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1532
Cdd:TIGR03269 451 LDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIG 510
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
507-729 |
7.69e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 83.36 E-value: 7.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 507 GKEAIRIRNLTKDYIQK-SKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLE 585
Cdd:PRK13631 18 DDIILRVKNLYCVFDEKqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 586 N---------------ISKLTGVCPQCNVQFDFLTVRENLRLFAKIK-GIQAHEVDNEVQRVLLELDMKNTqnILVQN-- 647
Cdd:PRK13631 98 ElitnpyskkiknfkeLRRRVSMVFQFPEYQLFKDTIEKDIMFGPVAlGVKKSEAKKLAKFYLNKMGLDDS--YLERSpf 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 648 -LSGGQKRKltfgIAILG----DPQIFLLDEPTAGLDPFSRHRVWNFLKERRAD-RVVLFSTQFMDEADILADRKVFISK 721
Cdd:PRK13631 176 gLSGGQKRR----VAIAGilaiQPEILIFDEPTAGLDPKGEHEMMQLILDAKANnKTVFVITHTMEHVLEVADEVIVMDK 251
|
....*...
gi 1907081362 722 GKLKCAGS 729
Cdd:PRK13631 252 GKILKTGT 259
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
431-679 |
7.75e-17 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 87.09 E-value: 7.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 431 IGTIFMLFFDGVFYLLLTFYFEKVLPSEYgrrhppLFFLKSSFWSGQNpANRTALDNETDYEFSDDS-FEPVSMEFH--- 506
Cdd:TIGR00956 674 IIIGFTVFFFFVYILLTEFNKGAKQKGEI------LVFRRGSLKRAKK-AGETSASNKNDIEAGEVLgSTDLTDESDdvn 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 507 ---------GKEAIRIRNLTKDYIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCvpTKGWVTiHNNK 577
Cdd:TIGR00956 747 dekdmekesGEDIFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV--TTGVIT-GGDR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 578 LSEMTDL-ENISKLTGVCPQCNVQFDFLTVRENLRLFAKI---KGIQAHEVDNEVQRVLLELDMKNTQNILV----QNLS 649
Cdd:TIGR00956 824 LVNGRPLdSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLrqpKSVSKSEKMEYVEEVIKLLEMESYADAVVgvpgEGLN 903
|
250 260 270
....*....|....*....|....*....|.
gi 1907081362 650 GGQKRKLTFGIAILGDPQIFL-LDEPTAGLD 679
Cdd:TIGR00956 904 VEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 934
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
510-722 |
1.01e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 83.74 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYIQKskrTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLsemTDLE---- 585
Cdd:PRK11650 3 GLKLQAVRKSYDGK---TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV---NELEpadr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 586 NISKLtgvcpqcnvqfdF--------LTVRENLRLFAKIKGIQAHEVDNEVQRV--LLE----LDMKNTQnilvqnLSGG 651
Cdd:PRK11650 77 DIAMV------------FqnyalyphMSVRENMAYGLKIRGMPKAEIEERVAEAarILEleplLDRKPRE------LSGG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 652 QKRKLTFGIAILGDPQIFLLDEPTAGLDpfSRHRVWNFLKERRADRVV----LFSTQFMDEADILADRKVFISKG 722
Cdd:PRK11650 139 QRQRVAMGRAIVREPAVFLFDEPLSNLD--AKLRVQMRLEIQRLHRRLkttsLYVTHDQVEAMTLADRVVVMNGG 211
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
506-724 |
1.06e-16 |
|
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: 80.98 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 506 HGKEAIRIRNLTKDYIQKSKrTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSeMTDLE 585
Cdd:cd03248 7 HLKGIVKFQNVTFAYPTRPD-TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS-QYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 586 NISKLTGVCPQCNVQFDfLTVRENL----------RLFAKIKGIQAHEVDNEVQR-VLLELDMKNTQnilvqnLSGGQKR 654
Cdd:cd03248 85 YLHSKVSLVGQEPVLFA-RSLQDNIayglqscsfeCVKEAAQKAHAHSFISELASgYDTEVGEKGSQ------LSGGQKQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 655 KLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRVVLFSTQFMDEADiLADRKVFISKGKL 724
Cdd:cd03248 158 RVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
510-718 |
1.14e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 82.01 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDY-IQKskrteALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLC-----VPTKGWVTIHNNKLSEMTd 583
Cdd:PRK14258 7 AIKVNNLSFYYdTQK-----ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNeleseVRVEGRVEFFNQNIYERR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 584 lENISKL----TGVCPQCNVqFDfLTVRENLRLFAKIKGIQAH-EVDNEVQRVLLELDM----KNTQNILVQNLSGGQKR 654
Cdd:PRK14258 81 -VNLNRLrrqvSMVHPKPNL-FP-MSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 655 KLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKER--RADRVVLFSTQFMDEADILADRKVF 718
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlRSELTMVIVSHNLHQVSRLSDFTAF 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
513-725 |
1.26e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.12 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 513 IRNLTKDYiqkSKRTeALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNK-----------LSEM 581
Cdd:COG0488 1 LENLSKSF---GGRP-LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLrigylpqepplDDDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 582 TDLENIskLTGVCPQCNVQFDFLTVRENL-----------RLFAKIKGIQAHEVDNEVQRVLLELDMKNTQ-NILVQNLS 649
Cdd:COG0488 77 TVLDTV--LDGDAELRALEAELEELEAKLaepdedlerlaELQEEFEALGGWEAEARAEEILSGLGFPEEDlDRPVSELS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 650 GGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHrvW--NFLKERRA-------DRVvlfstqFMDEadiLADRKVFIS 720
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE--WleEFLKNYPGtvlvvshDRY------FLDR---VATRILELD 223
|
....*
gi 1907081362 721 KGKLK 725
Cdd:COG0488 224 RGKLT 228
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
510-709 |
1.35e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 85.95 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTK---DYIqkskrteALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIhnnkLSEMTDLEN 586
Cdd:NF033858 266 AIEARGLTMrfgDFT-------AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWL----FGQPVDAGD 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 587 IS--KLTGVCPQCnvqfdF-----LTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFG 659
Cdd:NF033858 335 IAtrRRVGYMSQA-----FslygeLTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLA 409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907081362 660 IAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKE-RRADRVVLF-STQFMDEA 709
Cdd:NF033858 410 VAVIHKPELLILDEPTSGVDPVARDMFWRLLIElSREDGVTIFiSTHFMNEA 461
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
511-742 |
1.48e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 83.54 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKlseMTDLENISKL 590
Cdd:PRK11000 4 VTLRNVTKAY----GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKR---MNDVPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRV--------LLELDMKNtqnilvqnLSGGQKRKLTFGIAI 662
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVaevlqlahLLDRKPKA--------LSGGQRQRVAIGRTL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 663 LGDPQIFLLDEPTAGLDPFSR--HRVWNFLKERRADRVVLFSTQFMDEADILADRKVFISKGKLKCAGSSLFLkkkwgig 740
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDAALRvqMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL------- 221
|
..
gi 1907081362 741 YH 742
Cdd:PRK11000 222 YH 223
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1339-1535 |
1.49e-16 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 81.32 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPG-----FLGYCPQENALWLNLTVREHLE 1413
Cdd:COG4559 18 DDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPwelarRRAVLPQHSSLAFPFTVEEVVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1414 IFAAIKGMRKSDANVAIER---LADALKLQDQLkspVKTLSEGVK------RKLCFVL-SILGNPSVVLLDEPSTGMDPE 1483
Cdd:COG4559 98 LGRAPHGSSAAQDRQIVREalaLVGLAHLAGRS---YQTLSGGEQqrvqlaRVLAQLWePVDGGPRWLFLDEPTSALDLA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081362 1484 GQQQMWQaIQATFSNTERGAL-------LTTHYmaeaeavCDRVAIMVSGRLRCIGSIQ 1535
Cdd:COG4559 175 HQHAVLR-LARQLARRGGGVVavlhdlnLAAQY-------ADRILLLHQGRLVAQGTPE 225
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1336-1527 |
1.67e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 81.19 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1336 IATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGF----LGYCP--QENALWLNLTVR 1409
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHqiarMGVVRtfQHVRLFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1410 E--------HLE--IFA---AIKGMRKSDANvAIERLA---DALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLL 1473
Cdd:PRK11300 99 EnllvaqhqQLKtgLFSgllKTPAFRRAESE-ALDRAAtwlERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907081362 1474 DEPSTGMDPEGQQQMWQAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1527
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1339-1528 |
1.87e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 84.30 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSS-TGDTP------GfLGYCP---QENALWLNLTV 1408
Cdd:COG1129 269 RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPvRIRSPrdairaG-IAYVPedrKGEGLVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1409 RE-----HLEIFAAIKGMRKSDANVAIERLADALKL----QDQlksPVKTLSEGVKRKLcfVLS--ILGNPSVVLLDEPS 1477
Cdd:COG1129 348 REnitlaSLDRLSRGGLLDRRRERALAEEYIKRLRIktpsPEQ---PVGNLSGGNQQKV--VLAkwLATDPKVLILDEPT 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907081362 1478 TGMDPEGQQQMWQAIQATfsnTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1528
Cdd:COG1129 423 RGIDVGAKAEIYRLIREL---AAEGKavIVISSELPELLGLSDRILVMREGRI 472
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
507-852 |
2.02e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 82.86 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 507 GKEAIRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAG--KSTLLNVLSGLCVPTKGWvtihnNKLSEMTDL 584
Cdd:NF000106 10 ARNAVEVRGLVKHF----GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPW-----RF*TWCANR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 585 ENISKLTGVC-PQCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAIL 663
Cdd:NF000106 81 RALRRTIG*HrPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 664 GDPQIFLLDEPTAGLDPFSRHRVWNFLKER-RADRVVLFSTQFMDEADILADRKVFISKGKLKCAGSSLFLKKKWGiGYH 742
Cdd:NF000106 161 GRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG-GRT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 743 LSLQLSETCVHERITSLVKQHIPDSKLSAESEGKLSYI-LPLERTNKFPDLYRDL-ERSpdLGIENYGVSITTLTEVFLK 820
Cdd:NF000106 240 LQIRPAHAAELDRMVGAIAQAGLDGIAGATADHEDGVVnVPIVSDEQLSAVVGMLgERG--FTISGHQHPSAQL*EVFLA 317
|
330 340 350
....*....|....*....|....*....|..
gi 1907081362 821 LEGKSSIDQSDIGMTEDVQAGGARSPERFAEV 852
Cdd:NF000106 318 ITGQKTSEAADGGPQDGPQDQQGVQDKQYEEV 349
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1309-1526 |
2.63e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.95 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1309 KPAIIASCLRKEYKGKKkcfVLKSkkkiatrnISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSS-TG 1387
Cdd:PRK15439 9 PPLLCARSISKQYSGVE---VLKG--------IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPcAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1388 DTPGF---LG-Y-CPQENALWLNLTVREHLeIFaaikGMRKSdaNVAIERLADALK-LQDQLK--SPVKTLsEGVKRKLC 1459
Cdd:PRK15439 78 LTPAKahqLGiYlVPQEPLLFPNLSVKENI-LF----GLPKR--QASMQKMKQLLAaLGCQLDldSSAGSL-EVADRQIV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081362 1460 FVL-SILGNPSVVLLDEPSTGMDPEGQQQMWQAIQAtFSNTERGALLTTHYMAEAEAVCDRVAIMVSG 1526
Cdd:PRK15439 150 EILrGLMRDSRILILDEPTASLTPAETERLFSRIRE-LLAQGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1345-1520 |
2.78e-16 |
|
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: 80.14 E-value: 2.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1345 VRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSStgdtpgfLGYCPQENALWLNLTVREHLeiFAAIKGMRKS 1424
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-------VSYKPQYIKADYEGTVRDLL--SSITKDFYTH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1425 daNVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQATFSNTERGAL 1504
Cdd:cd03237 93 --PYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAF 170
|
170
....*....|....*.
gi 1907081362 1505 LTTHYMAEAEAVCDRV 1520
Cdd:cd03237 171 VVEHDIIMIDYLADRL 186
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1335-1482 |
2.79e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 80.52 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1335 KIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGF--------------LGYCPqen 1400
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYkrakyigrvfqdpmMGTAP--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1401 alwlNLTVREHLEIfAAIKGMR--------KSDANVAIERLAD-ALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVV 1471
Cdd:COG1101 96 ----SMTIEENLAL-AYRRGKRrglrrgltKKRRELFRELLATlGLGLENRLDTKVGLLSGGQRQALSLLMATLTKPKLL 170
|
170
....*....|.
gi 1907081362 1472 LLDEPSTGMDP 1482
Cdd:COG1101 171 LLDEHTAALDP 181
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1341-1532 |
2.91e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.97 E-value: 2.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1341 ISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKG-----SSTGDTPGFLGYCPQENALWLNLTVRE----- 1410
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddveaLSARAASRRVASVPQDTSLSFEFDVRQvvemg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1411 ---HLEIFAaikGMRKSDANV---AIERlADALKLQDQlksPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEG 1484
Cdd:PRK09536 102 rtpHRSRFD---TWTETDRAAverAMER-TGVAQFADR---PVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907081362 1485 QQQMWQAIQaTFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1532
Cdd:PRK09536 175 QVRTLELVR-RLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
510-703 |
4.82e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 83.72 E-value: 4.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYIQKSkrTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDlENISK 589
Cdd:PRK11160 338 SLTLNNVSFTYPDQP--QPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE-AALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 LTGVCPQcNVQFDFLTVRENLRLFAKikgiQAHevDNEVQRVLLELDMKNtqniLVQN--------------LSGGQKRK 655
Cdd:PRK11160 415 AISVVSQ-RVHLFSATLRDNLLLAAP----NAS--DEALIEVLQQVGLEK----LLEDdkglnawlgeggrqLSGGEQRR 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907081362 656 LTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRVVLFST 703
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMIT 531
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1340-1537 |
5.21e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 79.03 E-value: 5.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1340 NISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPgflgycP---------QENALWLNLTVRE 1410
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP------PaerpvsmlfQENNLFPHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1411 HLEIfaAIK-GMRKSDAN-VAIERLADALKLQDQLKSPVKTLSEGVKRKL----CFVlsiLGNPsVVLLDEPSTGMDPEG 1484
Cdd:COG3840 91 NIGL--GLRpGLKLTAEQrAQVEQALERVGLAGLLDRLPGQLSGGQRQRValarCLV---RKRP-ILLLDEPFSALDPAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 1485 QQQMWQAIQATfsNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1537
Cdd:COG3840 165 RQEMLDLVDEL--CRERGLtvLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
545-730 |
5.25e-16 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 81.00 E-value: 5.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 545 ILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEM-TDLENIskltGVCPQCNVQFDFLTVRENLRLFAKIKGIQAHE 623
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVpPHLRHI----NMVFQSYALFPHMTVEENVAFGLKMRKVPRAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 624 VDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLK--ERRADRVVLF 701
Cdd:TIGR01187 77 IKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKtiQEQLGITFVF 156
|
170 180
....*....|....*....|....*....
gi 1907081362 702 STQFMDEADILADRKVFISKGKLKCAGSS 730
Cdd:TIGR01187 157 VTHDQEEAMTMSDRIAIMRKGKIAQIGTP 185
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1333-1542 |
5.77e-16 |
|
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: 78.81 E-value: 5.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1333 KKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTP-----GFLGYCPQENALwLNLT 1407
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISrkslrSMIGVVLQDTFL-FSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1408 VREHL----------EIFAAIKGMRksdANVAIERLADAlkLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPS 1477
Cdd:cd03254 93 IMENIrlgrpnatdeEVIEAAKEAG---AHDFIMKLPNG--YDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEAT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 1478 TGMDPEGQQQMWQAIQATFSNteRGALLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFG 1542
Cdd:cd03254 168 SNIDTETEKLIQEALEKLMKG--RTSIIIAHRLSTIKNA-DKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
511-686 |
5.77e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 79.36 E-value: 5.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEmTDLENISKL 590
Cdd:COG4604 2 IEIKNVSKRY----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVAT-TPSRELAKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVQFDFLTVREnL-----------RLFAKikgiqahevDNE-VQRVLLELDMKNTQNILVQNLSGGQkRKLTF 658
Cdd:COG4604 77 LAILRQENHINSRLTVRE-LvafgrfpyskgRLTAE---------DREiIDEAIAYLDLEDLADRYLDELSGGQ-RQRAF 145
|
170 180 190
....*....|....*....|....*....|
gi 1907081362 659 gIA--ILGDPQIFLLDEPTAGLDPfsRHRV 686
Cdd:COG4604 146 -IAmvLAQDTDYVLLDEPLNNLDM--KHSV 172
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
509-722 |
7.31e-16 |
|
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: 78.63 E-value: 7.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 509 EAIRIRNLTKDYI---QKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNklSEMTDLE 585
Cdd:COG4778 3 TLLEVENLSKTFTlhlQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHD--GGWVDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 586 NISKLT---------GVCPQcnvqfdFLTVR----------ENLRLfakiKGIQAHEVDNEVQRVLLELDMKntqnilvQ 646
Cdd:COG4778 81 QASPREilalrrrtiGYVSQ------FLRVIprvsaldvvaEPLLE----RGVDREEARARARELLARLNLP-------E 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 647 NL--------SGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRVVLFSTqFMDEA--DILADRK 716
Cdd:COG4778 144 RLwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGI-FHDEEvrEAVADRV 222
|
....*.
gi 1907081362 717 VFISKG 722
Cdd:COG4778 223 VDVTPF 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
511-732 |
8.07e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 79.75 E-value: 8.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEmTDLENISKL 590
Cdd:PRK13642 5 LEVENLVFKY-EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA-ENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQC-NVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIF 669
Cdd:PRK13642 83 IGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081362 670 LLDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEAdILADRKVFISKGKL--KCAGSSLF 732
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEikEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIikEAAPSELF 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1334-1540 |
9.25e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 79.87 E-value: 9.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1334 KKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKG----SSTGDTP--------GFLGYCPqENA 1401
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNlkklrkkvSLVFQFP-EAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1402 LWLNlTVREHLEIFAAIKGMRKSDANVAIERLADALKLQDQL--KSPVKtLSEGVKRKLCFVLSILGNPSVVLLDEPSTG 1479
Cdd:PRK13641 98 LFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLisKSPFE-LSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081362 1480 MDPEGQQQMWQaiqaTFSNTERGA---LLTTHYMAEAEAVCDRVAIMVSGRLrcigsIQHLKSK 1540
Cdd:PRK13641 176 LDPEGRKEMMQ----LFKDYQKAGhtvILVTHNMDDVAEYADDVLVLEHGKL-----IKHASPK 230
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1335-1527 |
1.01e-15 |
|
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: 78.38 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1335 KIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGF--------LGYCPQENALWLNL 1406
Cdd:cd03256 14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrqlrrqIGMIFQQFNLIERL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1407 TVRE--------HLEIFAAIKGM-RKSDANVAIERLaDALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPS 1477
Cdd:cd03256 94 SVLEnvlsgrlgRRSTWRSLFGLfPKEEKQRALAAL-ERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907081362 1478 TGMDPEGQQQMWQAIQATfsNTERG--ALLTTHYMAEAEAVCDRVAIMVSGR 1527
Cdd:cd03256 173 ASLDPASSRQVMDLLKRI--NREEGitVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
534-724 |
1.06e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 78.09 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 534 TLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLEN-ISKLTgvcpQCNVQFDFLTVRENLRL 612
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRpVSMLF----QENNLFSHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 613 ----FAKIKGIQAHEVDNEVQRVLLEldmkNTQNILVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWN 688
Cdd:PRK10771 95 glnpGLKLNAAQREKLHAIARQMGIE----DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907081362 689 FLKERRADR--VVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:PRK10771 171 LVSQVCQERqlTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1328-1528 |
1.10e-15 |
|
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: 76.58 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1328 FVLKSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGFL----GYCPQENALW 1403
Cdd:cd03247 8 FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALssliSVLNQRPYLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1404 lNLTVREHLeifaaikGMRksdanvaierladalklqdqlkspvktLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1483
Cdd:cd03247 88 -DTTLRNNL-------GRR---------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPI 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907081362 1484 GQQQMWQAIqatFSNTE-RGALLTTHYMAEAEAVcDRVAIMVSGRL 1528
Cdd:cd03247 133 TERQLLSLI---FEVLKdKTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1334-1546 |
1.13e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 82.86 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1334 KKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDT-------PGfLGYCPQ---ENaLW 1403
Cdd:NF033858 13 KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADArhrravcPR-IAYMPQglgKN-LY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1404 LNLTVREHLEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRK--LCFVLsiLGNPSVVLLDEPSTGMD 1481
Cdd:NF033858 91 PTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKlgLCCAL--IHDPDLLILDEPTTGVD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081362 1482 PEGQQQMWQAIQATfsNTERGA---LLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSKFGKEYL 1546
Cdd:NF033858 169 PLSRRQFWELIDRI--RAERPGmsvLVATAYMEEAER-FDWLVAMDAGRVLATGTPAELLARTGADTL 233
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1322-1554 |
1.21e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 78.88 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1322 KGKKKCFVLKSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKG-----SSTGDTPGFLGYC 1396
Cdd:PRK13632 9 KVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1397 PQ--ENAlWLNLTVREHLEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCfVLSILG-NPSVVLL 1473
Cdd:PRK13632 89 FQnpDNQ-FIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVA-IASVLAlNPEIIIF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1474 DEpSTGM-DPEGQQQMWQAIQATFSNTERGALLTTHYMAEAeAVCDRVAIMVSGRLRCIGSIQH-LKSkfgKEYLLEMKV 1551
Cdd:PRK13632 167 DE-STSMlDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEiLNN---KEILEKAKI 241
|
...
gi 1907081362 1552 KTP 1554
Cdd:PRK13632 242 DSP 244
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
507-724 |
1.35e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 81.61 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 507 GKEAIRIRNLTkdyIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLEN 586
Cdd:COG3845 254 GEVVLEVENLS---VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRER 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 587 ISK----------LTGVCPQcnvqfdfLTVRENLRL-------FAKIKGIQAHEVDNEVQRVLLELDMKnTQNI--LVQN 647
Cdd:COG3845 331 RRLgvayipedrlGRGLVPD-------MSVAENLILgryrrppFSRGGFLDRKAIRAFAEELIEEFDVR-TPGPdtPARS 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081362 648 LSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADR--VVLFSTQfMDEADILADRKVFISKGKL 724
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGaaVLLISED-LDEILALSDRIAVMYEGRI 480
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
511-723 |
1.39e-15 |
|
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: 75.18 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKskrtEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNklsemtdlENISKL 590
Cdd:cd03221 1 IELENLSKTYGGK----LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST--------VKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 tgvcPQcnvqfdfltvrenlrlfakikgiqahevdnevqrvlleldmkntqnilvqnLSGGQKRKLTFGIAILGDPQIFL 670
Cdd:cd03221 69 ----EQ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 671 LDEPTAGLDPFSRHRVWNFLKERRadRVVLFST---QFMDEadiLADRKVFISKGK 723
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEYP--GTVILVShdrYFLDQ---VATKIIELEDGK 144
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1345-1528 |
1.55e-15 |
|
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: 77.15 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1345 VRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKG-----SSTGDTPGFLGYcpQENALWLNLTVREHLEIfAAIK 1419
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaAPPADRPVSMLF--QENNLFAHLTVEQNVGL-GLSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1420 GMR-KSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQATFSN 1498
Cdd:cd03298 98 GLKlTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAE 177
|
170 180 190
....*....|....*....|....*....|
gi 1907081362 1499 TERGALLTTHYMAEAEAVCDRVAIMVSGRL 1528
Cdd:cd03298 178 TKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1337-1554 |
1.84e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 78.74 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKG-----SSTG-----DTPGFLGYCPqENALWlNL 1406
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpidySRKGlmklrESVGMVFQDP-DNQLF-SA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1407 TVREHLEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQ 1486
Cdd:PRK13636 99 SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVS 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081362 1487 QMWQAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKfgKEYLLEMKVKTP 1554
Cdd:PRK13636 179 EIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE--KEMLRKVNLRLP 244
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
513-724 |
2.11e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 77.80 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 513 IRNLTKDYIQKskrtEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVtihnnklsemtdleniskLTG 592
Cdd:PRK11247 15 LNAVSKRYGER----TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------------------LAG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 593 VCPQCNVQFDFLTVRENLRLFAKIKGIqahevDN-----------EVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIA 661
Cdd:PRK11247 73 TAPLAEAREDTRLMFQDARLLPWKKVI-----DNvglglkgqwrdAALQALAAVGLADRANEWPAALSGGQKQRVALARA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 662 ILGDPQIFLLDEPTAGLDPFSR-------HRVWnflkeRRADRVVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTRiemqdliESLW-----QQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
503-697 |
2.12e-15 |
|
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: 77.47 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 503 MEFHGKEAIRIRNLTKDYIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMt 582
Cdd:COG4181 1 MSSSSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 583 DLENISKLTGVcpqcNVQFDF--------LTVRENLRLFAKIKGI-----QAHEvdnEVQRVLLE--LDMKNTQnilvqn 647
Cdd:COG4181 80 DEDARARLRAR----HVGFVFqsfqllptLTALENVMLPLELAGRrdaraRARA---LLERVGLGhrLDHYPAQ------ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 648 LSGG-QKRkltfgIAI----LGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADR 697
Cdd:COG4181 147 LSGGeQQR-----VALarafATEPAILFADEPTGNLDAATGEQIIDLLFELNRER 196
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
529-715 |
2.74e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 80.73 E-value: 2.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 529 ALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLENISklTGVC---------PQcnv 599
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALA--AGVAiiyqelhlvPE--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 600 qfdfLTVRENL---RLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTA 676
Cdd:PRK11288 94 ----MTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907081362 677 GLDPFSRHRVWNFLKERRAD-RVVLFSTQFMDEADILADR 715
Cdd:PRK11288 170 SLSAREIEQLFRVIRELRAEgRVILYVSHRMEEIFALCDA 209
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1337-1545 |
2.86e-15 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 81.09 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSST--GDTPGFLGycpqenalwlNLTVREHLEI 1414
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAliAISSGLNG----------QLTGIENIEL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1415 FAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQa 1494
Cdd:PRK13545 109 KGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMN- 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907081362 1495 TFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFG---KEY 1545
Cdd:PRK13545 188 EFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDeflKKY 241
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
507-683 |
3.07e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.88 E-value: 3.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 507 GKEAIRIRNLTKDYIQKskrtEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTI-HNNKLsemtdle 585
Cdd:COG0488 312 GKKVLELEGLSKSYGDK----TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgETVKI------- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 586 niskltGVCPQCNVQFDF-LTVRENLRLFAkiKGIQAHEVDNEVQRVLLELDMKNTQnilVQNLSGGQKRKLTFGIAILG 664
Cdd:COG0488 381 ------GYFDQHQEELDPdKTVLDELRDGA--PGGTEQEVRGYLGRFLFSGDDAFKP---VGVLSGGEKARLALAKLLLS 449
|
170
....*....|....*....
gi 1907081362 665 DPQIFLLDEPTAGLDPFSR 683
Cdd:COG0488 450 PPNVLLLDEPTNHLDIETL 468
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1340-1546 |
3.22e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 76.98 E-value: 3.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1340 NISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSS------TGDTPGFL-----GYCPQENALWLNLTV 1408
Cdd:COG4161 20 DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfsqkPSEKAIRLlrqkvGMVFQQYNLWPHLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1409 REHLeIFAAIK--GMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQ 1486
Cdd:COG4161 100 MENL-IEAPCKvlGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081362 1487 QMWQAIQaTFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLK----SKFgKEYL 1546
Cdd:COG4161 179 QVVEIIR-ELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHFTqpqtEAF-AHYL 240
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1337-1528 |
3.93e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 76.45 E-value: 3.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSS-----TGDTPgFL----GYCPQENALWLNLT 1407
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrlkNREVP-FLrrqiGMIFQDHHLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1408 VREHLEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1487
Cdd:PRK10908 96 VYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907081362 1488 MWQAIQaTFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1528
Cdd:PRK10908 176 ILRLFE-EFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
507-730 |
4.34e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 77.01 E-value: 4.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 507 GKEAIRIRNLTKDYIQKSKRTeALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLC------VPTKGWVTIHNNKLSE 580
Cdd:PRK14246 4 GKSAEDVFNISRLYLYINDKA-ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskIKVDGKVLYFGKDIFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 581 MtDLENISKLTGVCPQCNVQFDFLTVRENLRLFAKIKGIQAHE-----VDNEVQRVLLELDMKNTQNILVQNLSGGQKRK 655
Cdd:PRK14246 83 I-DAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKReikkiVEECLRKVGLWKEVYDRLNSPASQLSGGQQQR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 656 LTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRVVLFSTQFMDEADILADRKVFISKGKLKCAGSS 730
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSS 236
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
511-724 |
4.44e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 76.67 E-value: 4.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQkskrTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNK-LSEMTDLENISK 589
Cdd:PRK09493 2 IEFKNVSKHFGP----TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvNDPKVDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 LTG-VCPQCNVqFDFLTVRENLrLFA--KIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDP 666
Cdd:PRK09493 78 EAGmVFQQFYL-FPHLTALENV-MFGplRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 667 QIFLLDEPTAGLDPFSRH---RVWNFLKERRADRVVLfsTQFMDEADILADRKVFISKGKL 724
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHevlKVMQDLAEEGMTMVIV--THEIGFAEKVASRLIFIDKGRI 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
507-724 |
5.62e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 79.85 E-value: 5.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 507 GKEAIRIRNLTKDYIQKSKRT-EALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKG--WVTIhNNKLSEMTD 583
Cdd:TIGR03269 276 GEPIIKVRNVSKRYISVDRGVvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRV-GDEWVDMTK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 584 LE-----NISKLTGVCPQCNVQFDFLTVRENL---------RLFAKIKGIqahevdneVQRVLLELDMKNTQNILVQ--- 646
Cdd:TIGR03269 355 PGpdgrgRAKRYIGILHQEYDLYPHRTVLDNLteaiglelpDELARMKAV--------ITLKMVGFDEEKAEEILDKypd 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 647 NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWN-FLKERRA-DRVVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:TIGR03269 427 ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
510-724 |
6.00e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.69 E-value: 6.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDY--IQkskrteALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLsemtdleNI 587
Cdd:COG3845 5 ALELRGITKRFggVV------ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-------RI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 588 S-----------------KLtgvcpqcnvqFDFLTVRENLRLFAKIKG---IQAHEVDNEVQRVL----LELDMkntqNI 643
Cdd:COG3845 72 RsprdaialgigmvhqhfML----------VPNLTVAENIVLGLEPTKggrLDRKAARARIRELSerygLDVDP----DA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 644 LVQNLSGGQKRKLTfgI--AILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRAD-RVVLFSTQFMDEADILADRKVFIS 720
Cdd:COG3845 138 KVEDLSVGEQQRVE--IlkALYRGARILILDEPTAVLTPQEADELFEILRRLAAEgKSIIFITHKLREVMAIADRVTVLR 215
|
....
gi 1907081362 721 KGKL 724
Cdd:COG3845 216 RGKV 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1317-1528 |
6.36e-15 |
|
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: 77.79 E-value: 6.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1317 LRKEYKGKKKcfVLKskkkiATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKP---SAGQVLLKGSSTGDTPG-- 1391
Cdd:COG0444 7 LKVYFPTRRG--VVK-----AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEke 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1392 -------FLGYCPQE--NALwlN--LTVREHL-EIFAAIKGMRKSDAnvaIERLADALKLQdQLKSPVKT-------LSE 1452
Cdd:COG0444 80 lrkirgrEIQMIFQDpmTSL--NpvMTVGDQIaEPLRIHGGLSKAEA---RERAIELLERV-GLPDPERRldrypheLSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1453 GVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ---MWQAIQAtfsntERGA--LLTTHYMAEAEAVCDRVAIMVSGR 1527
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQilnLLKDLQR-----ELGLaiLFITHDLGVVAEIADRVAVMYAGR 228
|
.
gi 1907081362 1528 L 1528
Cdd:COG0444 229 I 229
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
513-694 |
7.24e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 80.15 E-value: 7.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 513 IRNLTKDYIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMtDLENISKLT- 591
Cdd:PRK10535 7 LKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATL-DADALAQLRr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 592 ---GVCPQCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQI 668
Cdd:PRK10535 86 ehfGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQV 165
|
170 180
....*....|....*....|....*.
gi 1907081362 669 FLLDEPTAGLDPFSRHRVWNFLKERR 694
Cdd:PRK10535 166 ILADEPTGALDSHSGEEVMAILHQLR 191
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1320-1528 |
7.55e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 77.92 E-value: 7.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1320 EYKGKKKCFVLKSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSS-TGdtpgfLGycpq 1398
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDlTA-----LS---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1399 ENALWL------------NL----TVREH----LEifaaIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKL 1458
Cdd:PRK11153 74 EKELRKarrqigmifqhfNLlssrTVFDNvalpLE----LAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081362 1459 CFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQ---AIQATFSNTergALLTTHYMAEAEAVCDRVAIMVSGRL 1528
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILEllkDINRELGLT---IVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1337-1535 |
8.56e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.44 E-value: 8.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGD-TPGF-----LGYCPQENALWLNLTVRE 1410
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKlDHKLaaqlgIGIIYQELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1411 HLEI-------FAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1483
Cdd:PRK09700 100 NLYIgrhltkkVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907081362 1484 GQQQMWqAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQ 1535
Cdd:PRK09700 180 EVDYLF-LIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVS 230
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
517-702 |
8.98e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 76.58 E-value: 8.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 517 TKDYIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKL--SEMTDLENISKLTGVC 594
Cdd:PRK13638 4 TSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 595 PQCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFLLDEP 674
Cdd:PRK13638 84 QDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190
....*....|....*....|....*....|
gi 1907081362 675 TAGLDPFSRHRVWNFLKE--RRADRVVLFS 702
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRivAQGNHVIISS 193
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
532-679 |
9.38e-15 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 74.84 E-value: 9.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 532 DLTLDvyKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDlENISKLTGVCPQCNVQfDFLTVRENLR 611
Cdd:cd03231 20 SFTLA--AGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIARGLLYLGHAPGIK-TTLSVLENLR 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081362 612 LFAKIKGiqahevDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 679
Cdd:cd03231 96 FWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1340-1526 |
1.21e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.54 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1340 NISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTgdtpgfLGYCPQEnaLWLNLTVREHLEIFAAIK 1419
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLR------IGYVPQK--LYLDTTLPLTVNRFLRLR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1420 -GMRKSDANVAIERLaDALKLQDQlksPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQATFSN 1498
Cdd:PRK09544 94 pGTKKEDILPALKRV-QAGHLIDA---PMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRE 169
|
170 180 190
....*....|....*....|....*....|...
gi 1907081362 1499 TERGALLTTH----YMAEA-EAVCDRVAIMVSG 1526
Cdd:PRK09544 170 LDCAVLMVSHdlhlVMAKTdEVLCLNHHICCSG 202
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
213-450 |
1.43e-14 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 77.04 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 213 ALQAAINAAIIEVTTNHSVMEEMMSLTGKYIKIDSFVGQEGTTT------DCFLFFCIIrFSPLtyYISAGVTRER-KKM 285
Cdd:pfam12698 115 LILNALQSLLQQLNASALVLLLEALSTSAPIPVESTPLFNPQSGyayylvGLILMIIIL-IGAA--IIAVSIVEEKeSRI 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 286 KGLMAVMGLRDSAFWLSWGLLYGVIVFVVTLLSTTIVkLVQFVFLTGFMVIFSLFFFYGLSLISLSFLMSVLLKKSFLTD 365
Cdd:pfam12698 192 KERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLL-FGIGIPFGNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQ 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 366 LVVFLLTVS-CGSLGFTALYRYLPVSLEWLLSLLSPFAFMLGMVQLLrldydvnsnadpMGNPN-EVIGTIFMLFFDGVF 443
Cdd:pfam12698 271 SIIGIVILLlSGFFGGLFPLEDPPSFLQWIFSIIPFFSPIDGLLRLI------------YGDSLwEIAPSLIILLLFAVV 338
|
....*..
gi 1907081362 444 YLLLTFY 450
Cdd:pfam12698 339 LLLLALL 345
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1337-1558 |
1.90e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 75.41 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGD---TPG---FLGYCPQE-NALWLNLTVR 1409
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfskLQGirkLVGIVFQNpETQFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1410 EHLEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW 1489
Cdd:PRK13644 97 EDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 1490 QAIQATFsntERGALL--TTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFGKEYLlemKVKTPSQVE 1558
Cdd:PRK13644 177 ERIKKLH---EKGKTIvyITHNLEELHDA-DRIIVMDRGKIVLEGEPENVLSDVSLQTL---GLTPPSLIE 240
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1340-1554 |
2.00e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 75.54 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1340 NISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKG-----SSTGDTPGFLGYCPQE-NALWLNLTVREHLE 1413
Cdd:PRK13650 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllteENVWDIRHKIGMVFQNpDNQFVGATVEDDVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1414 IFAAIKGMRKSDanvAIERLADALKL---QD-QLKSPVKtLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMW 1489
Cdd:PRK13650 105 FGLENKGIPHEE---MKERVNEALELvgmQDfKEREPAR-LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELI 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 1490 QAIQATFSNTERGALLTTHYMAEAeAVCDRVAIMVSGRLRCIGSIQHLKSKfgKEYLLEMKVKTP 1554
Cdd:PRK13650 181 KTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSR--GNDLLQLGLDIP 242
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
511-679 |
2.22e-14 |
|
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: 76.25 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLcVP----TKGWVTIHNNKLSEMTDlEN 586
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGL-LPppgiTSGEILFDGEDLLKLSE-KE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 587 ISKLTGVcpqcNVQFDF----------LTVR----ENLRLFAKIKGIQAHEvdnEVQRVLLELDMKNTQNILVQ---NLS 649
Cdd:COG0444 80 LRKIRGR----EIQMIFqdpmtslnpvMTVGdqiaEPLRIHGGLSKAEARE---RAIELLERVGLPDPERRLDRyphELS 152
|
170 180 190
....*....|....*....|....*....|
gi 1907081362 650 GGQKRKLTFGIAILGDPQIFLLDEPTAGLD 679
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALD 182
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1301-1533 |
2.36e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 76.91 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1301 LTSADFQEKPAIIASCLRKEYKGKKkcfvlkskkkiATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVL 1380
Cdd:PRK09452 4 LNKQPSSLSPLVELRGISKSFDGKE-----------VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1381 LKGSSTGDTPG--------FLGYcpqenALWLNLTVREHLEIfaAIKgMRKSDANVAIERLADALK---LQDQLKSPVKT 1449
Cdd:PRK09452 73 LDGQDITHVPAenrhvntvFQSY-----ALFPHMTVFENVAF--GLR-MQKTPAAEITPRVMEALRmvqLEEFAQRKPHQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1450 LSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQA-------TFsntergaLLTTHYMAEAEAVCDRVAI 1522
Cdd:PRK09452 145 LSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKAlqrklgiTF-------VFVTHDQEEALTMSDRIVV 217
|
250
....*....|.
gi 1907081362 1523 MVSGRLRCIGS 1533
Cdd:PRK09452 218 MRDGRIEQDGT 228
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
529-728 |
2.78e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.92 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 529 ALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIhnnkLSEMTDLENISKLTGVCPQCN-VQFDFLTVR 607
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI----LGQPTRQALQKNLVAYVPQSEeVDWSFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 608 ENLRLFAKIKGI----QAHEVDNE-VQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFS 682
Cdd:PRK15056 98 EDVVMMGRYGHMgwlrRAKKRDRQiVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907081362 683 RHRVWNFLKERRAD-RVVLFSTQFMDEADILADRKVFIsKGKLKCAG 728
Cdd:PRK15056 178 EARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASG 223
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
511-679 |
3.35e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 73.66 E-value: 3.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMtDLENISKL 590
Cdd:PRK10584 7 VEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQM-DEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVcpqcNVQFDF--------LTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAI 662
Cdd:PRK10584 86 RAK----HVGFVFqsfmliptLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAF 161
|
170
....*....|....*..
gi 1907081362 663 LGDPQIFLLDEPTAGLD 679
Cdd:PRK10584 162 NGRPDVLFADEPTGNLD 178
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1333-1533 |
3.41e-14 |
|
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: 72.94 E-value: 3.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1333 KKKIaTRNISFCVRKGEVVGLLGHNGAGKSTSIKMITG--ETKPSAGQVLLKGSSTGDTPgflgycPQENALwlnltvre 1410
Cdd:cd03217 12 GKEI-LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDLP------PEERAR-------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1411 hLEIFAAIKgmrksdANVAIErladALKLQDQLKSPVKTLSEGvKRKLCFVLSILG-NPSVVLLDEPSTGMDPEGQQQMW 1489
Cdd:cd03217 77 -LGIFLAFQ------YPPEIP----GVKNADFLRYVNEGFSGG-EKKRNEILQLLLlEPDLAILDEPDSGLDIDALRLVA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907081362 1490 QAIQaTFSNTERGALLTTHYMAEAEAV-CDRVAIMVSGRLRCIGS 1533
Cdd:cd03217 145 EVIN-KLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGD 188
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1317-1528 |
3.77e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 75.50 E-value: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1317 LRKEYKGKKKCFVlkskkkiATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPgflgyc 1396
Cdd:COG1135 7 LSKTFPTKGGPVT-------ALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALS------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1397 pqENALWL------------NL----TVREH----LEifaaIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVK- 1455
Cdd:COG1135 74 --ERELRAarrkigmifqhfNLlssrTVAENvalpLE----IAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKq 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1456 -----RKLCfvlsilGNPSVVLLDEPSTGMDPEgqqqmwqaiqATFS--------NTERGA--LLTTHYMAEAEAVCDRV 1520
Cdd:COG1135 148 rvgiaRALA------NNPKVLLCDEATSALDPE----------TTRSildllkdiNRELGLtiVLITHEMDVVRRICDRV 211
|
....*...
gi 1907081362 1521 AIMVSGRL 1528
Cdd:COG1135 212 AVLENGRI 219
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
511-724 |
4.50e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 75.12 E-value: 4.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKSKrTE--ALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKG--------WVTIHNNKLSE 580
Cdd:PRK13651 3 IKVKNIVKIFNKKLP-TElkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkdEKNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 581 MTDLENISKLT---------GVCPQCNVQFDFL-------TVRENLRLFAKIKGIQAHEVDNEVQRV--LLELDmkntQN 642
Cdd:PRK13651 82 KVLEKLVIQKTrfkkikkikEIRRRVGVVFQFAeyqlfeqTIEKDIIFGPVSMGVSKEEAKKRAAKYieLVGLD----ES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 643 ILVQ---NLSGGQKRKltfgIAILG----DPQIFLLDEPTAGLDPFSRHRVWNFLKE-RRADRVVLFSTQFMDEADILAD 714
Cdd:PRK13651 158 YLQRspfELSGGQKRR----VALAGilamEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNVLEWTK 233
|
250
....*....|
gi 1907081362 715 RKVFISKGKL 724
Cdd:PRK13651 234 RTIFFKDGKI 243
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1337-1528 |
5.00e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 74.34 E-value: 5.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTG-DTPGFLGYCPQENALWLNL-------TV 1408
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSLLEVRKTVGIVFQNPddqlfapTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1409 REHLEIFAAIKGMRKSDANvaiERLADALK---LQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQ 1485
Cdd:PRK13639 97 EEDVAFGPLNLGLSKEEVE---KRVKEALKavgMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907081362 1486 QQMWQAIqatFSNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1528
Cdd:PRK13639 174 SQIMKLL---YDLNKEGItiIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1339-1533 |
5.59e-14 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 76.74 E-value: 5.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTP-----GFLGYCPQENALwLNLTVREHL- 1412
Cdd:COG1132 357 KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTleslrRQIGVVPQDTFL-FSGTIRENIr 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1413 ---------EIFAAIKgmrksDANVA--IERLAdalklqDQLKSPV----KTLSEGVKRKLCFVLSILGNPSVVLLDEPS 1477
Cdd:COG1132 436 ygrpdatdeEVEEAAK-----AAQAHefIEALP------DGYDTVVgergVNLSGGQRQRIAIARALLKDPPILILDEAT 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 1478 TGMDPEGQQQMWQAIQATFSNteRGALLTTHYMAEAEAvCDRVAIMVSGRLRCIGS 1533
Cdd:COG1132 505 SALDTETEALIQEALERLMKG--RTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1312-1527 |
7.78e-14 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 72.72 E-value: 7.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1312 IIASCLRKEYKGKKkcfVLKskkkiatrNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPG 1391
Cdd:COG1126 2 IEIENLHKSFGDLE---VLK--------GISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1392 FL-------GYCPQENALWLNLTVREHLeIFAAIK--GMRKSDAnvaiERLADAL----KLQDQLKSPVKTLSEGVK--- 1455
Cdd:COG1126 71 DInklrrkvGMVFQQFNLFPHLTVLENV-TLAPIKvkKMSKAEA----EERAMELlervGLADKADAYPAQLSGGQQqrv 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1456 ---RKLCFvlsilgNPSVVLLDEPSTGMDPE------------GQQQMwqaiqaTFsntergaLLTTHYMAEAEAVCDRV 1520
Cdd:COG1126 146 aiaRALAM------EPKVMLFDEPTSALDPElvgevldvmrdlAKEGM------TM-------VVVTHEMGFAREVADRV 206
|
....*..
gi 1907081362 1521 AIMVSGR 1527
Cdd:COG1126 207 VFMDGGR 213
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1336-1508 |
8.06e-14 |
|
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: 76.25 E-value: 8.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1336 IATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGFL-----GYCPQENALWlNLTVRE 1410
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrrrvSVCAQDAHLF-DTTVRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1411 HLEIfaAIKGMRKSDANVAIER--LADALK-LQDQLKSPV----KTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1483
Cdd:TIGR02868 428 NLRL--ARPDATDEELWAALERvgLADWLRaLPDGLDTVLgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAE 505
|
170 180
....*....|....*....|....*
gi 1907081362 1484 GQQQMWQAIQATFSntERGALLTTH 1508
Cdd:TIGR02868 506 TADELLEDLLAALS--GRTVVLITH 528
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
528-728 |
8.13e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 73.46 E-value: 8.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 528 EALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLENI-------------SKLTGVC 594
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQlkvadknqlrllrTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 595 PQCNVqFDFLTVREN-LRLFAKIKGIQAHEVDNEVQRVLLELDM-KNTQNILVQNLSGGQKRKLTFGIAILGDPQIFLLD 672
Cdd:PRK10619 99 QHFNL-WSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081362 673 EPTAGLDP---FSRHRVWNFLKERRADRVVLfsTQFMDEADILADRKVFISKGKLKCAG 728
Cdd:PRK10619 178 EPTSALDPelvGEVLRIMQQLAEEGKTMVVV--THEMGFARHVSSHVIFLHQGKIEEEG 234
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1331-1556 |
8.55e-14 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 73.31 E-value: 8.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1331 KSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKG--SSTGDTPGFLGycpqenalwlNLTV 1408
Cdd:PRK13546 33 KNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGevSVIAISAGLSG----------QLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1409 REHLEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1488
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081362 1489 WQAIQaTFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFgKEYLLEMKVKTPSQ 1556
Cdd:PRK13546 183 LDKIY-EFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKY-EAFLNDFKKKSKAE 248
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1339-1533 |
8.72e-14 |
|
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: 72.06 E-value: 8.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTP-----GFLGYCPQENALwLNLTVREHLE 1413
Cdd:cd03369 25 KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPledlrSSLTIIPQDPTL-FSGTIRSNLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1414 IFAaikgmRKSDanvaiERLADALKlqdqLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQ 1493
Cdd:cd03369 104 PFD-----EYSD-----EEIYGALR----VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907081362 1494 ATFSNTergALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1533
Cdd:cd03369 170 EEFTNS---TILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
511-715 |
1.00e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.86 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTdlENISKL 590
Cdd:PRK15439 12 LCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT--PAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGV--CPQCNVQFDFLTVRENLrLFakikGIQAHEVDNE-VQRVL------LELDMK-NTQNI----LVQNLSGgqkrkl 656
Cdd:PRK15439 86 LGIylVPQEPLLFPNLSVKENI-LF----GLPKRQASMQkMKQLLaalgcqLDLDSSaGSLEVadrqIVEILRG------ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 657 tfgiaILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRV-VLFSTQFMDEADILADR 715
Cdd:PRK15439 155 -----LMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVgIVFISHKLPEIRQLADR 209
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1337-1523 |
1.18e-13 |
|
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: 75.79 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTP-----GFLGYCPQENALwLNLTVREH 1411
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADadswrDQIAWVPQHPFL-FAGTIAEN 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1412 LeifaaikGMRKSDANVA-IERLADALKLQDQLKS-PVKT----------LSEGVKRKLCFVLSILGNPSVVLLDEPSTG 1479
Cdd:TIGR02857 416 I-------RLARPDASDAeIREALERAGLDEFVAAlPQGLdtpigeggagLSGGQAQRLALARAFLRDAPLLLLDEPTAH 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907081362 1480 MDPEGQQQMWQAIQATFSNteRGALLTTHYMAEAEAvCDRVAIM 1523
Cdd:TIGR02857 489 LDAETEAEVLEALRALAQG--RTVLLVTHRLALAAL-ADRIVVL 529
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1337-1528 |
1.26e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 75.33 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKG-----SSTGDTpgfLG------YcpQENALWLN 1405
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqemrfASTTAA---LAagvaiiY--QELHLVPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1406 LTVREHLEI------FAAI-KGMRKSDANVAIERLADALKLQdqlkSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPST 1478
Cdd:PRK11288 94 MTVAENLYLgqlphkGGIVnRRLLNYEAREQLEHLGVDIDPD----TPLKYLSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1479 GMDPEGQQQMWQAIQATFSNTeRGALLTTHYMAEAEAVCDRVAIMVSGRL 1528
Cdd:PRK11288 170 SLSAREIEQLFRVIRELRAEG-RVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
530-743 |
1.37e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 75.91 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 530 LKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMtDLENISKLTGVCPQCNVQFDfLTVREN 609
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQY-DHHYLHRQVALVGQEPVLFS-GSVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 610 L----------RLFAKIKGIQAHE-VDNEVQRVLLELDMKNTQnilvqnLSGGQKRKLTFGIAILGDPQIFLLDEPTAGL 678
Cdd:TIGR00958 575 IaygltdtpdeEIMAAAKAANAHDfIMEFPNGYDTEVGEKGSQ------LSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 679 DPFSRHRVWNFLKerRADRVVLFSTQFMDEADiLADRKVFISKGKLKCAGSSLFLKKKWGIGYHL 743
Cdd:TIGR00958 649 DAECEQLLQESRS--RASRTVLLIAHRLSTVE-RADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
528-743 |
1.63e-13 |
|
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: 75.55 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 528 EALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMtDLENISKLTGVCPQCNVQFDFlTVR 607
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI-DRHTLRQFINYLPQEPYIFSG-SIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 608 ENLRLFAKiKGIQAHEVDNEVQRVLLELDMKNTQ-------NILVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDP 680
Cdd:TIGR01193 566 ENLLLGAK-ENVSQDEIWAACEIAEIKDDIENMPlgyqtelSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDT 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081362 681 FSRHRVWNFLKERRaDRVVLFSTQFMDEADiLADRKVFISKGKLKCAGSSLFLKKKWGIGYHL 743
Cdd:TIGR01193 645 ITEKKIVNNLLNLQ-DKTIIFVAHRLSVAK-QSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
540-686 |
2.18e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 75.30 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 540 GQITAILGHSGAGKSTLLNVLSGLCVPT--KGWVTIHNNKLSEmtdleNISKLTGVCPQCNVQFDFLTVRENLRLFAKI- 616
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTK-----QILKRTGFVTQDDILYPHLTVRETLVFCSLLr 168
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081362 617 --KGIQAHEVDNEVQRVLLELDMKNTQNILVQN-----LSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRV 686
Cdd:PLN03211 169 lpKSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
526-704 |
3.09e-13 |
|
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: 74.31 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 526 RTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMtDLENISKLTGVCPQcNVQFDFLT 605
Cdd:TIGR01842 330 KKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQW-DRETFGKHIGYLPQ-DVELFPGT 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 606 VRENLRLF------------AKIKGiqAHEVdnevqrvLLELDMKNTQNILV--QNLSGGQKRKLTFGIAILGDPQIFLL 671
Cdd:TIGR01842 408 VAENIARFgenadpekiieaAKLAG--VHEL-------ILRLPDGYDTVIGPggATLSGGQRQRIALARALYGDPKLVVL 478
|
170 180 190
....*....|....*....|....*....|....
gi 1907081362 672 DEPTAGLDPFSRHRVWNFLKERRADRV-VLFSTQ 704
Cdd:TIGR01842 479 DEPNSNLDEEGEQALANAIKALKARGItVVVITH 512
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1345-1524 |
3.20e-13 |
|
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: 74.44 E-value: 3.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1345 VRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSstgdtpgfLGYCPQENALWLNLTVREHLEifAAIKgmRKS 1424
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK--------ISYKPQYISPDYDGTVEEFLR--SANT--DDF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1425 DANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQATFSNTERGAL 1504
Cdd:COG1245 431 GSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAM 510
|
170 180
....*....|....*....|
gi 1907081362 1505 LTTHYMAEAEAVCDRvaIMV 1524
Cdd:COG1245 511 VVDHDIYLIDYISDR--LMV 528
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
511-700 |
3.60e-13 |
|
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: 74.37 E-value: 3.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTdLENISKL 590
Cdd:TIGR02203 331 VEFRNVTFRY--PGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT-LASLRRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVQFDFlTVRENLRlFAKIKGIqaheVDNEVQRVLlelDMKNTQNILVQ--------------NLSGGQKRKL 656
Cdd:TIGR02203 408 VALVSQDVVLFND-TIANNIA-YGRTEQA----DRAEIERAL---AAAYAQDFVDKlplgldtpigengvLLSGGQRQRL 478
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907081362 657 TFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRVVL 700
Cdd:TIGR02203 479 AIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTL 522
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
511-730 |
3.63e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 71.58 E-value: 3.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKskrtEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTK---------GWVTIHNNKLSEm 581
Cdd:PRK09984 5 IRVEKLAKTFNQH----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGRLAR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 582 tDLENISKLTGVCPQcnvQFDF---LTVREN---------------LRLFAKIKGIQAHevdnevqRVLLELDMKNTQNI 643
Cdd:PRK09984 80 -DIRKSRANTGYIFQ---QFNLvnrLSVLENvligalgstpfwrtcFSWFTREQKQRAL-------QALTRVGMVHFAHQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 644 LVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKE-RRADRV-VLFSTQFMDEADILADRKVFISK 721
Cdd:PRK09984 149 RVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDiNQNDGItVVVTLHQVDYALRYCERIVALRQ 228
|
....*....
gi 1907081362 722 GKLKCAGSS 730
Cdd:PRK09984 229 GHVFYDGSS 237
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1321-1543 |
3.71e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 74.31 E-value: 3.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1321 YKGKKKCFVLKSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPS---AGQVLLKGSSTgDTPGF---LG 1394
Cdd:TIGR00955 24 VSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI-DAKEMraiSA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1395 YCPQENALWLNLTVREHLEIFAAIK---GMRKSDANVAIERLADALKLQD------QLKSPVKTLSEGVKRKLCFVLSIL 1465
Cdd:TIGR00955 103 YVQQDDLFIPTLTVREHLMFQAHLRmprRVTKKEKRERVDEVLQALGLRKcantriGVPGRVKGLSGGERKRLAFASELL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1466 GNPSVVLLDEPSTGMDPEGQQQMWQAIQAtFSNTERGALLTTHyMAEAEAVC--DRVAIMVSGRLRCIGSIQHLKSKFGK 1543
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKG-LAQKGKTIICTIH-QPSSELFElfDKIILMAEGRVAYLGSPDQAVPFFSD 260
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
516-714 |
3.73e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.78 E-value: 3.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 516 LTKDYIQKSKRTEA-LKDLTLDVYKGQITAILGHSGAGKSTLLNVLSG-LCVP-------TKGWVTIHNNKLSEMtDLEN 586
Cdd:PRK13547 2 LTADHLHVARRHRAiLRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGgaprgarVTGDVTLNGEPLAAI-DAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 587 ISKLTGVCPQCNVQ-FDFlTVRENLRL----FAKIKGIQAHEvDNEVQRVLLEL-DMKNTQNILVQNLSGGQKRKLTFGI 660
Cdd:PRK13547 81 LARLRAVLPQAAQPaFAF-SAREIVLLgrypHARRAGALTHR-DGEIAWQALALaGATALVGRDVTTLSGGELARVQFAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 661 AI---------LGDPQIFLLDEPTAGLDPFSRHRV----------WNF----------LKERRADRVVLFStqfmdEADI 711
Cdd:PRK13547 159 VLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLldtvrrlardWNLgvlaivhdpnLAARHADRIAMLA-----DGAI 233
|
...
gi 1907081362 712 LAD 714
Cdd:PRK13547 234 VAH 236
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
503-729 |
4.13e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 71.96 E-value: 4.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 503 MEFHGKeaIRIRNLTKDYIQKSK-RTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHN------ 575
Cdd:PRK13645 1 FDFSKD--IILDNVSYTYAKKTPfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipan 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 576 -NKLSEMTDLENISKLTGVCPQCNVQFDflTVRENLRLFAKIKGIQAHEVDNEVQRVlleLDMKNTQNILVQ----NLSG 650
Cdd:PRK13645 79 lKKIKEVKRLRKEIGLVFQFPEYQLFQE--TIEKDIAFGPVNLGENKQEAYKKVPEL---LKLVQLPEDYVKrspfELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 651 GQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNF---LKERRADRVVLFsTQFMDEADILADRKVFISKGKLKCA 727
Cdd:PRK13645 154 GQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLferLNKEYKKRIIMV-THNMDQVLRIADEVIVMHEGKVISI 232
|
..
gi 1907081362 728 GS 729
Cdd:PRK13645 233 GS 234
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1322-1546 |
4.89e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 73.14 E-value: 4.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1322 KGKKKCFVL-KSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGF-------- 1392
Cdd:PRK10070 27 QGLSKEQILeKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAelrevrrk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1393 -LGYCPQENALWLNLTVREHLEIFAAIKGMRKSDANvaiERLADALK---LQDQLKSPVKTLSEGVKRKLCFVLSILGNP 1468
Cdd:PRK10070 107 kIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERR---EKALDALRqvgLENYAHSYPDELSGGMRQRVGLARALAINP 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081362 1469 SVVLLDEPSTGMDPEGQQQMWQAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKEYL 1546
Cdd:PRK10070 184 DILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYV 261
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1339-1533 |
5.04e-13 |
|
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: 70.22 E-value: 5.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSI----KMITgetkPSAGQVLLKGSSTGDTP-----GFLGYCPQENALwLNLTVR 1409
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSLLlalfRLVE----LSSGSILIDGVDISKIGlhdlrSRISIIPQDPVL-FSGTIR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1410 EHLEIFAaikgmRKSDanvaiERLADALKlQDQLKSPVKT---------------LSEGVKRKLCFVLSILGNPSVVLLD 1474
Cdd:cd03244 96 SNLDPFG-----EYSD-----EELWQALE-RVGLKEFVESlpggldtvveeggenLSVGQRQLLCLARALLRKSKILVLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081362 1475 EPSTGMDPEGQQQMWQAIQATFSNTergALLT-THYMaeaEAV--CDRVAIMVSGRLRCIGS 1533
Cdd:cd03244 165 EATASVDPETDALIQKTIREAFKDC---TVLTiAHRL---DTIidSDRILVLDKGRVVEFDS 220
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
506-725 |
5.25e-13 |
|
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: 69.75 E-value: 5.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 506 HGKeaIRIRNLTKDYiqKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMtDLE 585
Cdd:cd03369 4 HGE--IEVENLSVRY--APDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI-PLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 586 NISKLTGVCPQCNVQFDFlTVRENLRLFAKIKGIQAHEVdnevqrvlleLDMKNTQNilvqNLSGGQKRKLTFGIAILGD 665
Cdd:cd03369 79 DLRSSLTIIPQDPTLFSG-TIRSNLDPFDEYSDEEIYGA----------LRVSEGGL----NLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 666 PQIFLLDEPTAGLDPFSRHRVWNFLKERRADRVVL-FSTQFMDEADIlaDRKVFISKGKLK 725
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILtIAHRLRTIIDY--DKILVMDAGEVK 202
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1341-1536 |
6.09e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.41 E-value: 6.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1341 ISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKG-----SSTGDT--PGFLgYCP--------------QE 1399
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpidiRSPRDAirAGIM-LCPedrkaegiipvhsvAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1400 NalwLNLTVREHLEIFAAIKGMRKSDANVA--IERLADALKLQDQlksPVKTLSEGVKRKlcfvlSILG-----NPSVVL 1472
Cdd:PRK11288 351 N---INISARRHHLRAGCLINNRWEAENADrfIRSLNIKTPSREQ---LIMNLSGGNQQK-----AILGrwlseDMKVIL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 1473 LDEPSTGMDPEGQQQMWQAIqatFSNTERG--ALLTTHYMAEAEAVCDRVAIMVSGRLRciGSIQH 1536
Cdd:PRK11288 420 LDEPTRGIDVGAKHEIYNVI---YELAAQGvaVLFVSSDLPEVLGVADRIVVMREGRIA--GELAR 480
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
511-725 |
6.19e-13 |
|
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: 71.04 E-value: 6.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKSkrTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLcVPTKGWVTIHNNKLSEMTdLENISKL 590
Cdd:cd03289 3 MTVKDLTAKYTEGG--NAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVP-LQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVQFDFlTVRENLRLFAKIKgiqahevDNEVQRVLLELDMKNTQN--------ILVQN---LSGGQKRKLTFG 659
Cdd:cd03289 79 FGVIPQKVFIFSG-TFRKNLDPYGKWS-------DEEIWKVAEEVGLKSVIEqfpgqldfVLVDGgcvLSHGHKQLMCLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 660 IAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRVVLFSTQFMdEADILADRKVFISKGKLK 725
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKVR 215
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1317-1483 |
6.54e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 73.43 E-value: 6.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1317 LRKEYKGKKKcfVLKskkkiatrNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKgsstgdtPGF-LGY 1395
Cdd:TIGR03719 10 VSKVVPPKKE--ILK--------DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-------PGIkVGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1396 CPQENALWLNLTVREHL---------------EIFAA-----------IKGMRK----------SDANVAIERLADALKL 1439
Cdd:TIGR03719 73 LPQEPQLDPTKTVRENVeegvaeikdaldrfnEISAKyaepdadfdklAAEQAElqeiidaadaWDLDSQLEIAMDALRC 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907081362 1440 QDQlKSPVKTLSEGVKRK--LCFVLsiLGNPSVVLLDEPSTGMDPE 1483
Cdd:TIGR03719 153 PPW-DADVTKLSGGERRRvaLCRLL--LSKPDMLLLDEPTNHLDAE 195
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1317-1483 |
6.79e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 73.23 E-value: 6.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1317 LRKEYKGKKKcfVLKskkkiatrNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLkgsstgdTPGF-LGY 1395
Cdd:PRK11819 12 VSKVVPPKKQ--ILK--------DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP-------APGIkVGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1396 CPQENALWLNLTVREHLE-----IFAAIK-----GMRKSDANVAIERLADAL-KLQDQLKS------------------- 1445
Cdd:PRK11819 75 LPQEPQLDPEKTVRENVEegvaeVKAALDrfneiYAAYAEPDADFDALAAEQgELQEIIDAadawdldsqleiamdalrc 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907081362 1446 -----PVKTLSEGVKRK--LCFVLsiLGNPSVVLLDEPSTGMDPE 1483
Cdd:PRK11819 155 ppwdaKVTKLSGGERRRvaLCRLL--LEKPDMLLLDEPTNHLDAE 197
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1337-1599 |
6.82e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.92 E-value: 6.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGdtpgflgycpQENALWL------------ 1404
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN----------AENEKWVrskvglvfqdpd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1405 ----NLTVREHLEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGM 1480
Cdd:PRK13647 90 dqvfSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1481 DPEGQQQMwQAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGsiqhlkskfGKEYLLEMKVKTPSQVE-P 1559
Cdd:PRK13647 170 DPRGQETL-MEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG---------DKSLLTDEDIVEQAGLRlP 239
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1907081362 1560 LNTEIMRLFPQAARQerysslmvyKLPR---EDVQPLSQAFFK 1599
Cdd:PRK13647 240 LVAQIFEDLPELGQS---------KLPLtvkEAVQIIRKLLTK 273
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1339-1508 |
8.37e-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: 67.47 E-value: 8.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTgdtpgfLGYCPQenalwlnltvrehleifaai 1418
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK------IGYFEQ-------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1419 kgmrksdanvaierladalklqdqlkspvktLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQqqmwQAIQATFSN 1498
Cdd:cd03221 71 -------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESI----EALEEALKE 115
|
170
....*....|
gi 1907081362 1499 TERGALLTTH 1508
Cdd:cd03221 116 YPGTVILVSH 125
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1339-1528 |
8.56e-13 |
|
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: 69.42 E-value: 8.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKG---------------SSTGDTPGFLGYCPQENALW 1403
Cdd:cd03248 31 QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisqyehkylhskvSLVGQEPVLFARSLQDNIAY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1404 lNLTVREHLEIFAAikgMRKSDANVAIERLADALKLQDQLKSpvKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1483
Cdd:cd03248 111 -GLQSCSFECVKEA---AQKAHAHSFISELASGYDTEVGEKG--SQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907081362 1484 GQQQMWQAIQAtfSNTERGALLTTHYMAEAEAVcDRVAIMVSGRL 1528
Cdd:cd03248 185 SEQQVQQALYD--WPERRTVLVIAHRLSTVERA-DQILVLDGGRI 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
540-703 |
9.65e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 72.96 E-value: 9.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 540 GQITAILGHSGAGKSTLLNVLSGLcVPTKGWVTIHNNKLSEMtDLE----NISKLtGVCPQcnvqfdfL---TVRENLRL 612
Cdd:PRK11174 376 GQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELREL-DPEswrkHLSWV-GQNPQ-------LphgTLRDNVLL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 613 fAKikgIQAHevDNEVQRVLLELDMKNTQNILVQNL-----------SGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPF 681
Cdd:PRK11174 446 -GN---PDAS--DEQLQQALENAWVSEFLPLLPQGLdtpigdqaaglSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
170 180
....*....|....*....|..
gi 1907081362 682 SRHRVWNFLKERRADRVVLFST 703
Cdd:PRK11174 520 SEQLVMQALNAASRRQTTLMVT 541
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1336-1481 |
1.19e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 69.48 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1336 IATR--NISFCVRKGEVVGLLGHNGAGKSTSIKMITGETkPSAGQVLLKGSSTGDTPG-----FLGYCPQENALWLNLTV 1408
Cdd:COG4138 8 VAGRlgPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAaelarHRAYLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1409 REHLEIFAAIKGMRKSDANVaIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSIL-----GNPS--VVLLDEPSTGMD 1481
Cdd:COG4138 87 FQYLALHQPAGASSEAVEQL-LAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPEgqLLLLDEPMNSLD 165
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
511-724 |
1.27e-12 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 69.83 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDY-----IQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMT--- 582
Cdd:TIGR02769 3 LEVRDVTHTYrtgglFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 583 ------DLENISK--LTGVCPQCNVQFdflTVRENLRLFAKIKGIQAHEVDNEVQRvLLELDMKNTQNiLVQNLSGGQKR 654
Cdd:TIGR02769 83 rrafrrDVQLVFQdsPSAVNPRMTVRQ---IIGEPLRHLTSLDESEQKARIAELLD-MVGLRSEDADK-LPRQLSGGQLQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081362 655 KLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRAD--RVVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:TIGR02769 158 RINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfgTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1341-1481 |
1.27e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.58 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1341 ISFCVRKGEVVGLLGHNGAGKSTSIKMITGETkPSAGQVLLKGSSTGDTPG-----FLGYCPQENALWLNLTVREHLEIF 1415
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAaelarHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081362 1416 AAiKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSIL-----GNPS--VVLLDEPSTGMD 1481
Cdd:PRK03695 94 QP-DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPAgqLLLLDEPMNSLD 165
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1328-1567 |
1.37e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 70.04 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1328 FVLKSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQV-----LLKGSSTGDTPGFLGYCPQ--EN 1400
Cdd:PRK13635 13 FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTItvggmVLSEETVWDVRRQVGMVFQnpDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1401 AlWLNLTVREHLEIFAAIKGMRKSDanvAIERLADALKL---QDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPS 1477
Cdd:PRK13635 93 Q-FVGATVQDDVAFGLENIGVPREE---MVERVDQALRQvgmEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEAT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1478 TGMDPEGQQQMWQAIQATFSNTERGALLTTHYMAEAeAVCDRVAIMVSGRLRCIGsiqhlkskfgkeyllemkvkTPSQV 1557
Cdd:PRK13635 169 SMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEG--------------------TPEEI 227
|
250
....*....|
gi 1907081362 1558 EPLNTEIMRL 1567
Cdd:PRK13635 228 FKSGHMLQEI 237
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1341-1508 |
1.38e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 68.72 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1341 ISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKG--SSTGDTPGFLGYCPQENALWLNLTVREHLEIFAAI 1418
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGktATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1419 KGMRK----SDAnVAIERLADalkLQDQLkspVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQA 1494
Cdd:PRK13543 110 HGRRAkqmpGSA-LAIVGLAG---YEDTL---VRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISA 182
|
170
....*....|....
gi 1907081362 1495 TFsNTERGALLTTH 1508
Cdd:PRK13543 183 HL-RGGGAALVTTH 195
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
507-724 |
1.47e-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: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 507 GKEAIRIRNLTkdyiqkskRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLsemtDLEN 586
Cdd:COG1129 253 GEVVLEVEGLS--------VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV----RIRS 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 587 IS--------------KLTGVCPQcnvqfdfLTVREN-----LRLFAKIKGIQAHEVDNEVQRVLLELDMKnTQNI--LV 645
Cdd:COG1129 321 PRdairagiayvpedrKGEGLVLD-------LSIRENitlasLDRLSRGGLLDRRRERALAEEYIKRLRIK-TPSPeqPV 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 646 QNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKErRADR---VVLFSTQfMDEADILADRKVFISKG 722
Cdd:COG1129 393 GNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRE-LAAEgkaVIVISSE-LPELLGLSDRILVMREG 470
|
..
gi 1907081362 723 KL 724
Cdd:COG1129 471 RI 472
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1348-1537 |
1.67e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 69.43 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1348 GEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTG--DTPGF---LGYCPQENALWLNLTVREHLEI-----FAA 1417
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswSSKAFarkVAYLPQQLPAAEGMTVRELVAIgrypwHGA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1418 IKGMRKSDAnvaiERLADALKLQDqLKsP-----VKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAI 1492
Cdd:PRK10575 117 LGRFGAADR----EKVEEAISLVG-LK-PlahrlVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALV 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907081362 1493 QATfsNTERGALLTT--HYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1537
Cdd:PRK10575 191 HRL--SQERGLTVIAvlHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
498-679 |
1.83e-12 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 72.96 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 498 FEPVSMEFHG-KEAIRIRNLTKDYIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLcvPTKGWVTiHNN 576
Cdd:PLN03140 863 FTPLAMSFDDvNYFVDMPAEMKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGR--KTGGYIE-GDI 939
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 577 KLSEMTDL-ENISKLTGVCPQCNVQFDFLTVRENLRLFAKI---KGIQAHEVDNEVQRVLLELDMKNTQNILV-----QN 647
Cdd:PLN03140 940 RISGFPKKqETFARISGYCEQNDIHSPQVTVRESLIYSAFLrlpKEVSKEEKMMFVDEVMELVELDNLKDAIVglpgvTG 1019
|
170 180 190
....*....|....*....|....*....|..
gi 1907081362 648 LSGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 679
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1340-1537 |
2.21e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 70.52 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1340 NISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTP--------GFLGYcpqenALWLNLTVREH 1411
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSiqqrdicmVFQSY-----ALFPHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1412 LEIFAAIKGMRKSDANvaiERLADALKLQDQL---KSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1488
Cdd:PRK11432 99 VGYGLKMLGVPKEERK---QRVKEALELVDLAgfeDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907081362 1489 WQAI---QATFSNTergALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1537
Cdd:PRK11432 176 REKIrelQQQFNIT---SLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1340-1546 |
3.08e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 68.12 E-value: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1340 NISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKG------SSTGDTPGFL-----GYCPQENALWLNLTV 1408
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRElrrnvGMVFQQYNLWPHLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1409 REHLeIFAAIK--GMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQ 1486
Cdd:PRK11124 100 QQNL-IEAPCRvlGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081362 1487 QMWQAIQAtFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLK----SKFgKEYL 1546
Cdd:PRK11124 179 QIVSIIRE-LAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTqpqtEAF-KNYL 240
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1337-1493 |
3.16e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 68.37 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGF------LGYCPQENALWLNLTVRE 1410
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkimreaVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1411 HLEI---FAaikgmRKSDANVAIERLADAL-KLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQ 1486
Cdd:PRK11614 100 NLAMggfFA-----ERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
....*..
gi 1907081362 1487 QMWQAIQ 1493
Cdd:PRK11614 175 QIFDTIE 181
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1330-1531 |
3.23e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.97 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1330 LKSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSS-TGDTP--------GFLGYCPQEN 1400
Cdd:PRK09700 271 VTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDiSPRSPldavkkgmAYITESRRDN 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1401 ALWLNLTVREHLEIFAAIKGMRKSDA-----NVAIERLADALKLQDQLK-----SPVKTLSEGVKRKLCFVLSILGNPSV 1470
Cdd:PRK09700 351 GFFPNFSIAQNMAISRSLKDGGYKGAmglfhEVDEQRTAENQRELLALKchsvnQNITELSGGNQQKVLISKWLCCCPEV 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 1471 VLLDEPSTGMDPEGQQQMWQaIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCI 1531
Cdd:PRK09700 431 IIFDEPTRGIDVGAKAEIYK-VMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1339-1508 |
3.33e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.28 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTG-DTPGF---LGYCPQENALWLNLTVREHlei 1414
Cdd:PRK13540 18 QQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKkDLCTYqkqLCFVGHRSGINPYLTLREN--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1415 faAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQA 1494
Cdd:PRK13540 95 --CLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQE 172
|
170
....*....|....*
gi 1907081362 1495 tfSNTERGA-LLTTH 1508
Cdd:PRK13540 173 --HRAKGGAvLLTSH 185
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
532-680 |
3.40e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 68.64 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 532 DLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKG--WVTIHNNKLSEMTDLENISKLTGVCPQCNVQFDFLTVREN 609
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGeiLFDGENIPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081362 610 ----LRLFAKIKGIQAHEVdnevqrVLLELD---MKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDP 680
Cdd:PRK11831 105 vaypLREHTQLPAPLLHST------VMMKLEavgLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1329-1528 |
3.89e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.83 E-value: 3.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1329 VLKSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSS-TGDTP------GfLGYCPQE-- 1399
Cdd:COG3845 265 VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDiTGLSPrerrrlG-VAYIPEDrl 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1400 -NALWLNLTVREHLeIFAAIKGMRKSDANV----AIERLADAL------KLQDqLKSPVKTLSEGVKRKlcFVLS--ILG 1466
Cdd:COG3845 344 gRGLVPDMSVAENL-ILGRYRRPPFSRGGFldrkAIRAFAEELieefdvRTPG-PDTPARSLSGGNQQK--VILAreLSR 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081362 1467 NPSVVLLDEPSTGMDPEGQQQMWQAIQATfsnTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1528
Cdd:COG3845 420 DPKLLIAAQPTRGLDVGAIEFIHQRLLEL---RDAGAavLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
508-729 |
4.59e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 70.76 E-value: 4.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 508 KEAIRIRNLTKDYIQKSkrtEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTdLENI 587
Cdd:PRK13657 332 KGAVEFDDVSFSYDNSR---QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT-RASL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 588 SKLTGVCPQCNVQFDfLTVRENLR----------LFAKIKGIQAHEVdneVQRVLLELDMkntqniLV----QNLSGGQK 653
Cdd:PRK13657 408 RRNIAVVFQDAGLFN-RSIEDNIRvgrpdatdeeMRAAAERAQAHDF---IERKPDGYDT------VVgergRQLSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 654 RKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRvvlfsTQFMDeADIL-----ADRKVFISKGKLKCAG 728
Cdd:PRK13657 478 QRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGR-----TTFII-AHRLstvrnADRILVFDNGRVVESG 551
|
.
gi 1907081362 729 S 729
Cdd:PRK13657 552 S 552
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
530-679 |
6.43e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.45 E-value: 6.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 530 LKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGwVTIHNNKLSemtdlenisklTGVCPQcNVQFDF---LTV 606
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG-VIKRNGKLR-----------IGYVPQ-KLYLDTtlpLTV 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081362 607 RENLRLFAkikGIQAHEVDNEVQRV----LLELDMkntqnilvQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 679
Cdd:PRK09544 87 NRFLRLRP---GTKKEDILPALKRVqaghLIDAPM--------QKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1327-1547 |
7.12e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 67.91 E-value: 7.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1327 CFVLKSKKKiATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKG-----SSTGDTPGFLGYCPQENA 1401
Cdd:PRK13652 10 CYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitkENIREVRKFVGLVFQNPD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1402 LWLNLTVREHLEIFAAIKgMRKSDANVAiERLADALK---LQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPST 1478
Cdd:PRK13652 89 DQIFSPTVEQDIAFGPIN-LGLDEETVA-HRVSSALHmlgLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081362 1479 GMDPEGQQQMWQAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLkskFGKEYLL 1547
Cdd:PRK13652 167 GLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI---FLQPDLL 232
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
513-702 |
7.64e-12 |
|
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: 70.71 E-value: 7.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 513 IRNLTKDYIQKSKrtEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLcVPTKGWVTIHNNKLSEMTdLENISKLTG 592
Cdd:TIGR01271 1220 VQGLTAKYTEAGR--AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVT-LQTWRKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 593 VCPQCNVQFDFlTVRENLRLFAKIKgiqahevDNEVQRVLLELDMKNTQN--------ILVQN---LSGGQKRKLTFGIA 661
Cdd:TIGR01271 1296 VIPQKVFIFSG-TFRKNLDPYEQWS-------DEEIWKVAEEVGLKSVIEqfpdkldfVLVDGgyvLSNGHKQLMCLARS 1367
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907081362 662 ILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRVVLFS 702
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILS 1408
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1308-1528 |
7.68e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 66.76 E-value: 7.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1308 EKPAIIASCLRKEYK-GKKKCFVLkskkkiatRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSST 1386
Cdd:PRK11629 2 NKILLQCDNLCKRYQeGSVQTDVL--------HNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPM 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1387 GDTPGF---------LGYCPQENALWLNLTVREHLEIFAAIKGMRKSDAN-VAIERLAdALKLQDQLKSPVKTLSEGVKR 1456
Cdd:PRK11629 74 SKLSSAakaelrnqkLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINsRALEMLA-AVGLEHRANHRPSELSGGERQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081362 1457 KLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQATfsNTERGA--LLTTHYMAEAEAVcDRVAIMVSGRL 1528
Cdd:PRK11629 153 RVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGEL--NRLQGTafLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
530-679 |
1.18e-11 |
|
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: 65.75 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 530 LKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLcvpTKGWVTIHNN-KLSEMTDLENISKLTG---VCPQCNVQFDFLT 605
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEGDiHYNGIPYKEFAEKYPGeiiYVSEEDVHFPTLT 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081362 606 VRENLRLFAKIKGiqahevdNEVQRVLleldmkntqnilvqnlSGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 679
Cdd:cd03233 100 VRETLDFALRCKG-------NEFVRGI----------------SGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
529-680 |
1.27e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 66.55 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 529 ALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDlENISKLTGVCPQCNVQ-FDFLTVR 607
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPG-HQIARMGVVRTFQHVRlFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 608 ENL----------RLFA---KIKGIQAHE---VDNEVQ---RVLLeLDMKNTQnilVQNLSGGQKRKLTFGIAILGDPQI 668
Cdd:PRK11300 99 ENLlvaqhqqlktGLFSgllKTPAFRRAEseaLDRAATwleRVGL-LEHANRQ---AGNLAYGQQRRLEIARCMVTQPEI 174
|
170
....*....|..
gi 1907081362 669 FLLDEPTAGLDP 680
Cdd:PRK11300 175 LMLDEPAAGLNP 186
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
513-733 |
1.27e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 68.21 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 513 IRNLTKDYiqkSKRTeALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIhnnklsemtDLENISKLT- 591
Cdd:PRK11432 9 LKNITKRF---GSNT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI---------DGEDVTHRSi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 592 ---GVCP--QCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDP 666
Cdd:PRK11432 76 qqrDICMvfQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081362 667 QIFLLDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQFMDEADILADRKVFISKGKLKCAGS---------SLFL 733
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREKIRElqQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSpqelyrqpaSRFM 233
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1339-1483 |
1.43e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 69.15 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVllKGSSTGDtpgfLGYCPQENALWLNltvrEHLEIFAAI 1418
Cdd:PRK15064 336 KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--KWSENAN----IGYYAQDHAYDFE----NDLTLFDWM 405
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081362 1419 KGMRKSDANVAIER--LADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1483
Cdd:PRK15064 406 SQWRQEGDDEQAVRgtLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDME 472
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
532-679 |
1.44e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.60 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 532 DLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEM-----TDLENISKLTGVCPQcnvqfdfLTV 606
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhQDLLYLGHQPGIKTE-------LTA 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081362 607 RENLRLFAKIkgiqAHEVDNE-VQRVLLELDMKNTQNILVQNLSGGQKRKltfgIAI----LGDPQIFLLDEPTAGLD 679
Cdd:PRK13538 92 LENLRFYQRL----HGPGDDEaLWEALAQVGLAGFEDVPVRQLSAGQQRR----VALarlwLTRAPLWILDEPFTAID 161
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1338-1532 |
1.47e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 68.13 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1338 TRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGF---LGYCPQENALWLNLTVREHLEI 1414
Cdd:PRK11000 19 SKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAergVGMVFQSYALYPHLSVAENMSF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1415 FAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQA 1494
Cdd:PRK11000 99 GLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISR 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907081362 1495 TFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1532
Cdd:PRK11000 179 LHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1337-1558 |
1.49e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 67.11 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKG----SSTGD--------TPGFLGYCPqENALWL 1404
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDkyirpvrkRIGMVFQFP-ESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1405 NLTVREhleifaAIKGMRKSDANVAiERLADALKLQDQL--------KSPVKtLSEGVKRKLCFVlSILG-NPSVVLLDE 1475
Cdd:PRK13646 101 DTVERE------IIFGPKNFKMNLD-EVKNYAHRLLMDLgfsrdvmsQSPFQ-MSGGQMRKIAIV-SILAmNPDIIVLDE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1476 PSTGMDPEGQQQMWQAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKfgKEYLLEMKVKTPS 1555
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD--KKKLADWHIGLPE 249
|
...
gi 1907081362 1556 QVE 1558
Cdd:PRK13646 250 IVQ 252
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1337-1547 |
1.53e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 69.08 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPgflgycpqENALWLNLTV---REHle 1413
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS--------EAALRQAISVvsqRVH-- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1414 IFAA-------IKGMRKSDanvaiERLADALK---LQDQLKSPV----------KTLSEGVKRKLCFVLSILGNPSVVLL 1473
Cdd:PRK11160 425 LFSAtlrdnllLAAPNASD-----EALIEVLQqvgLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALLHDAPLLLL 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081362 1474 DEPSTGMDPEGQQQMWQAIQATFSNteRGALLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFGKEYLL 1547
Cdd:PRK11160 500 DEPTEGLDAETERQILELLAEHAQN--KTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1329-1493 |
2.18e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 64.57 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1329 VLKSKKKIATrNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPS--AGQVLLKGSSTGDT-PGFLGYCPQENALWLN 1405
Cdd:cd03232 15 VKGGKRQLLN-NISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDKNfQRSTGYVEQQDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1406 LTVREHLEIFAAIKGmrksdanvaierladaLKLQDQlkspvKTLSEGVKrklcfvlsILGNPSVVLLDEPSTGMDPEGQ 1485
Cdd:cd03232 94 LTVREALRFSALLRG----------------LSVEQR-----KRLTIGVE--------LAAKPSILFLDEPTSGLDSQAA 144
|
....*...
gi 1907081362 1486 QQMWQAIQ 1493
Cdd:cd03232 145 YNIVRFLK 152
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1339-1508 |
2.22e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 65.36 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETK--PSAGQVLLkgsstgdtpgflgycpQENALWLNLTVREHLeifa 1416
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDV----------------PDNQFGREASLIDAI---- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1417 aikgMRKSDANVAIERLADAlKLQDQ--LKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQA 1494
Cdd:COG2401 107 ----GRKGDFKDAVELLNAV-GLSDAvlWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQK 181
|
170
....*....|....
gi 1907081362 1495 TFSNTERGALLTTH 1508
Cdd:COG2401 182 LARRAGITLVVATH 195
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1345-1524 |
2.57e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.30 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1345 VRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVL--LKGSstgdtpgflgYCPQENALWLNLTVREHLEifaAIKGmr 1422
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDpeLKIS----------YKPQYIKPDYDGTVEDLLR---SITD-- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1423 KSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQATFSNTERG 1502
Cdd:PRK13409 427 DLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREAT 506
|
170 180
....*....|....*....|..
gi 1907081362 1503 ALLTTHYMAEAEAVCDRvaIMV 1524
Cdd:PRK13409 507 ALVVDHDIYMIDYISDR--LMV 526
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1350-1533 |
3.04e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.80 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1350 VVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTP-GFLGYC---------PQENALWLNLTVrehlEIFAAIK 1419
Cdd:PRK13638 29 VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKrGLLALRqqvatvfqdPEQQIFYTDIDS----DIAFSLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1420 GMRKSDANVAiERLADALKLQDQL---KSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQATF 1496
Cdd:PRK13638 105 NLGVPEAEIT-RRVDEALTLVDAQhfrHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIV 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907081362 1497 SNTERgALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1533
Cdd:PRK13638 184 AQGNH-VIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
511-673 |
3.16e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 67.99 E-value: 3.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKSKRTEALKDL----------------TLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVtih 574
Cdd:PRK13545 5 VKFEHVTKKYKMYNKPFDKLKDLffrskdgeyhyalnniSFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 575 nnklsemtDLENISKLTGVCPQCNVQfdfLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKR 654
Cdd:PRK13545 82 --------DIKGSAALIAISSGLNGQ---LTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKS 150
|
170
....*....|....*....
gi 1907081362 655 KLTFGIAILGDPQIFLLDE 673
Cdd:PRK13545 151 RLGFAISVHINPDILVIDE 169
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
511-722 |
4.30e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.59 E-value: 4.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKSKRTE-------------------ALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSG--LCVPTKG 569
Cdd:COG2401 8 FVLMRVTKVYSSVLDLSErvaivleafgvelrvveryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 570 WVTIHNNKL-SEMTDLENISKLTgvcpqcnvqfDFLTVRENLrlfaKIKGIqahevdNEVQRVLLELDmkntqnilvqNL 648
Cdd:COG2401 88 CVDVPDNQFgREASLIDAIGRKG----------DFKDAVELL----NAVGL------SDAVLWLRRFK----------EL 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081362 649 SGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRV-WNFLKE-RRADRVVLFSTQFMD-EADILADRKVFISKG 722
Cdd:COG2401 138 STGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVaRNLQKLaRRAGITLVVATHHYDvIDDLQPDLLIFVGYG 214
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1342-1539 |
5.04e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 64.60 E-value: 5.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1342 SFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPgflgycP---------QENALWLNLTVREHL 1412
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP------PsrrpvsmlfQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1413 EIFAAiKGMRKSDANVA-IERLADALKLQDQLKSPVKTLSEGVKRKL----CFVLSilgNPsVVLLDEPSTGMDPEGQQQ 1487
Cdd:PRK10771 93 GLGLN-PGLKLNAAQREkLHAIARQMGIEDLLARLPGQLSGGQRQRValarCLVRE---QP-ILLLDEPFSALDPALRQE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907081362 1488 MWQAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKS 1539
Cdd:PRK10771 168 MLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
510-679 |
6.21e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 66.84 E-value: 6.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYIQKskrtEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVtihnnKLSEMTDLenisk 589
Cdd:PRK15064 319 ALEVENLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----KWSENANI----- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 ltGVCPQcNVQFDF---LTVRENLRLFAKIKgiqahevDNE--VQRVLLEL-----DMKNTqnilVQNLSGGQKRKLTFG 659
Cdd:PRK15064 385 --GYYAQ-DHAYDFendLTLFDWMSQWRQEG-------DDEqaVRGTLGRLlfsqdDIKKS----VKVLSGGEKGRMLFG 450
|
170 180
....*....|....*....|
gi 1907081362 660 IAILGDPQIFLLDEPTAGLD 679
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMD 470
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1339-1528 |
6.38e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.95 E-value: 6.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTpgflgyCPQE---------------NALW 1403
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTR------SPQDglangivyisedrkrDGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1404 LNLTVREH-----LEIFAAIKG-MRKSDANVAIERLADALKL----QDQlksPVKTLSEGVKRKLCFVLSILGNPSVVLL 1473
Cdd:PRK10762 343 LGMSVKENmsltaLRYFSRAGGsLKHADEQQAVSDFIRLFNIktpsMEQ---AIGLLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 1474 DEPSTGMDPEGQQQMWQAIQaTFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1528
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQLIN-QFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1311-1528 |
6.97e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 64.39 E-value: 6.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1311 AIIASCLRKEYKGKKkcfVLKSkkkiatrnISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLkGSSTGDTP 1390
Cdd:PRK11264 3 AIEVKNLVKKFHGQT---VLHG--------IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GDITIDTA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1391 GFL--------------GYCPQENALWLNLTVREH-LEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVK 1455
Cdd:PRK11264 71 RSLsqqkglirqlrqhvGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081362 1456 RKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQAtFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1528
Cdd:PRK11264 151 QRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQ-LAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1339-1542 |
7.47e-11 |
|
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: 64.17 E-value: 7.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGS--STGDTPGF---LGYCPQENALWlNLTVREHle 1413
Cdd:cd03253 18 KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdiREVTLDSLrraIGVVPQDTVLF-NDTIGYN-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1414 ifaaIKGMRKSDANVAIERLADALKLQDQ-LKSPVK----------TLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDP 1482
Cdd:cd03253 95 ----IRYGRPDATDEEVIEAAKAAQIHDKiMRFPDGydtivgerglKLSGGEKQRVAIARAILKNPPILLLDEATSALDT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1483 EGQQQMWQAIQATFSNteRGALLTTHYMAEAeAVCDRVAIMVSGRLRCIGSIQHLKSKFG 1542
Cdd:cd03253 171 HTEREIQAALRDVSKG--RTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELLAKGG 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
511-724 |
8.21e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 63.74 E-value: 8.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKSkrtEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKG--WVTIHNNKLSEMTDLENIS 588
Cdd:PRK10908 2 IRFEHVSKAYLGGR---QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGkiWFSGHDITRLKNREVPFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 589 KLTGVCPQCNVQFDFLTVRENLRLFAKIKGIQAHEVDnevQRVLLELD----MKNTQNILVQnLSGGQKRKLTFGIAILG 664
Cdd:PRK10908 79 RQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIR---RRVSAALDkvglLDKAKNFPIQ-LSGGEQQRVGIARAVVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 665 DPQIFLLDEPTAGLDPFSRHRVWNFLKE-RRADRVVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEfNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1339-1527 |
8.37e-11 |
|
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: 63.26 E-value: 8.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSstgdtpgfLGYCPQENalWL-NLTVREHLeIFAA 1417
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--------IAYVSQEP--WIqNGTIRENI-LFGK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1418 IkgMRKsdanvaiERLADALK---LQDQLKSPVK-----------TLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1483
Cdd:cd03250 91 P--FDE-------ERYEKVIKacaLEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAH 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907081362 1484 -GQQQMWQAIQATFSNtERGALLTTHYMAEAEAvCDRVAIMVSGR 1527
Cdd:cd03250 162 vGRHIFENCILGLLLN-NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1331-1527 |
8.70e-11 |
|
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: 63.05 E-value: 8.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1331 KSKKKIaTRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSA---GQVLLKGSSTGDT----PGFLGYCPQENALW 1403
Cdd:cd03233 17 RSKIPI-LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFaekyPGEIIYVSEEDVHF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1404 LNLTVREHLEIFAAIKGmrksDANvaierladalklqdqlkspVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1483
Cdd:cd03233 96 PTLTVRETLDFALRCKG----NEF-------------------VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907081362 1484 GQQQMWQAIQaTFSNTERGALLTTHYMA--EAEAVCDRVAIMVSGR 1527
Cdd:cd03233 153 TALEILKCIR-TMADVLKTTTFVSLYQAsdEIYDLFDKVLVLYEGR 197
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1335-1575 |
9.32e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 64.66 E-value: 9.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1335 KIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLkGSSTgDTPGF-----------LGYCPQ--ENA 1401
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERV-ITAGKknkklkplrkkVGIVFQfpEHQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1402 LWlNLTVREHLeIFAAIK-GMRKSDAnvaiERLAD-ALKL----QDQL-KSPVKtLSEGVKRKLCF--VLSIlgNPSVVL 1472
Cdd:PRK13634 98 LF-EETVEKDI-CFGPMNfGVSEEDA----KQKAReMIELvglpEELLaRSPFE-LSGGQMRRVAIagVLAM--EPEVLV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1473 LDEPSTGMDPEGQQQMWQaiqaTFSNTERGALLT----THYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKS--------- 1539
Cdd:PRK13634 169 LDEPTAGLDPKGRKEMME----MFYKLHKEKGLTtvlvTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAdpdeleaig 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1907081362 1540 -------KFGKEylLEMKV-----KTPSQVEPLNTEIMRLFPQAARQE 1575
Cdd:PRK13634 245 ldlpetvKFKRA--LEEKFgisfpKPCLTLEELAHEVVQLLRKGGHES 290
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
511-679 |
9.32e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 64.24 E-value: 9.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqkSKRTEAlKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLEnISKL 590
Cdd:PRK10253 8 LRGEQLTLGY---GKYTVA-ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE-VARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVQFDFLTVRE--------NLRLFAKIKgiqaHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAI 662
Cdd:PRK10253 83 IGLLAQNATTPGDITVQElvargrypHQPLFTRWR----KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVL 158
|
170
....*....|....*..
gi 1907081362 663 LGDPQIFLLDEPTAGLD 679
Cdd:PRK10253 159 AQETAIMLLDEPTTWLD 175
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1327-1547 |
9.40e-11 |
|
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: 63.79 E-value: 9.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1327 CFVLKSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSstgDTPGF--------LGYCPQ 1398
Cdd:cd03251 7 TFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGH---DVRDYtlaslrrqIGLVSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1399 ENALWlNLTVREHLeifaAIKGMRKSDANV-AIERLADAL----KLQDQLKSPVK----TLSEGVKRKLCFVLSILGNPS 1469
Cdd:cd03251 84 DVFLF-NDTVAENI----AYGRPGATREEVeEAARAANAHefimELPEGYDTVIGergvKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081362 1470 VVLLDEPSTGMDPEGQQQMWQAIQATFSNteRGALLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFGKEYLL 1547
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKN--RTTFVIAHRLSTIENA-DRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1339-1528 |
1.08e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.83 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTG---DTPGFLGYCPQENA-------------- 1401
Cdd:PRK10619 22 KGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrDKDGQLKVADKNQLrllrtrltmvfqhf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1402 -LWLNLTVREH-LEIFAAIKGMRKSDANVAIERLADALKLQD--QLKSPVKtLSEGVKRKLCFVLSILGNPSVVLLDEPS 1477
Cdd:PRK10619 102 nLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDEraQGKYPVH-LSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 1478 TGMDPEGQQQMWQAIQaTFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1528
Cdd:PRK10619 181 SALDPELVGEVLRIMQ-QLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1322-1533 |
1.11e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 64.37 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1322 KGKKKCFVLKSKKKIATR---NISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTP-------- 1390
Cdd:PRK13643 3 KFEKVNYTYQPNSPFASRalfDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeikpv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1391 ----GFLGYCPQENALwlNLTVREHLEIFAAIKGMRKSDA-NVAIERLaDALKLQDQL--KSPVKtLSEGVKRKLCFVLS 1463
Cdd:PRK13643 83 rkkvGVVFQFPESQLF--EETVLKDVAFGPQNFGIPKEKAeKIAAEKL-EMVGLADEFweKSPFE-LSGGQMRRVAIAGI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1464 ILGNPSVVLLDEPSTGMDPEGQQQMWQAIQaTFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1533
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFE-SIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1328-1526 |
1.24e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 64.00 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1328 FVLKSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTpgflgycpqenalwlNLT 1407
Cdd:PRK13648 15 FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDD---------------NFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1408 -VREHLEIFAA------IKGMRKSDANVAIE-----------RLADALK---LQDQLKSPVKTLSEGVKRKLCFVLSILG 1466
Cdd:PRK13648 80 kLRKHIGIVFQnpdnqfVGSIVKYDVAFGLEnhavpydemhrRVSEALKqvdMLERADYEPNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1467 NPSVVLLDEPSTGMDPEGQQQMWQAIQATFSNTERGALLTTHYMAEAeAVCDRVAIMVSG 1526
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKG 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1314-1543 |
1.29e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 63.94 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1314 ASCLRKEYKGKKkcFVLKSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTG------ 1387
Cdd:PRK10419 6 VSGLSHHYAHGG--LSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAklnraq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1388 -------------DTPGFLGycPQENALWLnltVRE---HLeifaaiKGMRKSDANVAIERLADALKLQDQL--KSPvKT 1449
Cdd:PRK10419 84 rkafrrdiqmvfqDSISAVN--PRKTVREI---IREplrHL------LSLDKAERLARASEMLRAVDLDDSVldKRP-PQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1450 LSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRL- 1528
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIv 231
|
250
....*....|....*..
gi 1907081362 1529 --RCIGSIQHLKSKFGK 1543
Cdd:PRK10419 232 etQPVGDKLTFSSPAGR 248
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1341-1528 |
1.40e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 63.96 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1341 ISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSS-TGDTP-------GFLGYCPQENalWLNLTVREHL 1412
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELlTAENVwnlrrkiGMVFQNPDNQ--FVGATVEDDV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1413 EIFAAIKGMRKSDanvAIERLADAL----KLQDQLKSPVKtLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1488
Cdd:PRK13642 104 AFGMENQGIPREE---MIKRVDEALlavnMLDFKTREPAR-LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907081362 1489 WQAIQATFSNTERGALLTTHYMAEAeAVCDRVAIMVSGRL 1528
Cdd:PRK13642 180 MRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEI 218
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
520-715 |
1.59e-10 |
|
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: 63.20 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 520 YIQKSKrteALKDLTLDV-----YKGQITAILGHSGAGKSTLLNVLSGLCVPTKGwvtihnnklSEMTDLENIS-Kltgv 593
Cdd:cd03237 3 YPTMKK---TLGEFTLEVeggsiSESEVIGILGPNGIGKTTFIKMLAGVLKPDEG---------DIEIELDTVSyK---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 594 cPQcNVQFDF-LTVRENLRLFAKIKGIQAH---EVDNEVQrvlLELDMKNtqniLVQNLSGGQKRKLTFGIAILGDPQIF 669
Cdd:cd03237 67 -PQ-YIKADYeGTVRDLLSSITKDFYTHPYfktEIAKPLQ---IEQILDR----EVPELSGGELQRVAIAACLSKDADIY 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907081362 670 LLDEPTAGLDPFSRHRVWNFLKerradRVVLF--STQFMDEADI-----LADR 715
Cdd:cd03237 138 LLDEPSAYLDVEQRLMASKVIR-----RFAENneKTAFVVEHDIimidyLADR 185
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
530-679 |
1.78e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 63.32 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 530 LKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLcVPTKGWVTIHNNKLSEMtDLENISKLTGVCPQCNVQFDFLTVREN 609
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDW-SAAELARHRAYLSQQQSPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 610 LRLFAkikgiQAHEVDNEVQRVL------LELDMKNTQNilVQNLSGG--QKRKLTfgiAIL--------GDPQIFLLDE 673
Cdd:COG4138 90 LALHQ-----PAGASSEAVEQLLaqlaeaLGLEDKLSRP--LTQLSGGewQRVRLA---AVLlqvwptinPEGQLLLLDE 159
|
....*.
gi 1907081362 674 PTAGLD 679
Cdd:COG4138 160 PMNSLD 165
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1317-1541 |
2.18e-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: 65.21 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1317 LRKEYKGKKkcfVLKskkkiatrNISFCVRKGEVVGLLGHNGAGKSTSIKMITG--ETKPSAGQVLLKGS---STG--DT 1389
Cdd:TIGR03269 6 LTKKFDGKE---VLK--------NISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHVAlceKCGyvER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1390 PGFLGY-CP--------QENALW-----LNLTVREHLEI-----FA----------AIKGMRKS--DANVAIERLADAL- 1437
Cdd:TIGR03269 75 PSKVGEpCPvcggtlepEEVDFWnlsdkLRRRIRKRIAImlqrtFAlygddtvldnVLEALEEIgyEGKEAVGRAVDLIe 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1438 --KLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQATFSNTERGALLTTHYMAEAEA 1515
Cdd:TIGR03269 155 mvQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIED 234
|
250 260
....*....|....*....|....*.
gi 1907081362 1516 VCDRVAIMVSGRLRCIGSIQHLKSKF 1541
Cdd:TIGR03269 235 LSDKAIWLENGEIKEEGTPDEVVAVF 260
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
527-728 |
2.37e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 64.48 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 527 TEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLsEMTDLENISKLTGVCPQ-CNVQFDFlT 605
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV-EALSARAASRRVASVPQdTSLSFEF-D 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 606 VRENLRLfakikGIQAH--------EVDNE-VQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTA 676
Cdd:PRK09536 94 VRQVVEM-----GRTPHrsrfdtwtETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 677 GLDpfSRHRVWNFLKERR---ADRVVLFSTQFMDEADILADRKVFISKGKLKCAG 728
Cdd:PRK09536 169 SLD--INHQVRTLELVRRlvdDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
533-680 |
2.68e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.17 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 533 LTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTI--HNNKLSEMTD-LENISKLTGVCPQcnvqfdfLTVREN 609
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIdgKTATRGDRSRfMAYLGHLPGLKAD-------LSTLEN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 610 LRLFAKIKGIQAHEVDNEVQRVLLELDMKNTqniLVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDP 680
Cdd:PRK13543 103 LHFLCGLHGRRAKQMPGSALAIVGLAGYEDT---LVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
530-679 |
2.79e-10 |
|
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: 65.15 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 530 LKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMtDLENISKLTGVCPQcNVQ-FDFlTVRE 608
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQW-DREELGRHIGYLPQ-DVElFDG-TIAE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 609 NLRLFAKI---KGIQA------HEVdnevqrvLLEL-DMKNTQnilV----QNLSGGQKRKLTFGIAILGDPQIFLLDEP 674
Cdd:COG4618 425 NIARFGDAdpeKVVAAaklagvHEM-------ILRLpDGYDTR---IgeggARLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
....*
gi 1907081362 675 TAGLD 679
Cdd:COG4618 495 NSNLD 499
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
530-700 |
2.80e-10 |
|
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: 65.23 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 530 LKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIhnnklsemtDLENISKLT--------GVCPQCNVQF 601
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILI---------DGQDIRDVTqaslraaiGIVPQDTVLF 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 602 -DflTVRENLR----------LFAKIKGIQAHE--------VDNEV-QRVLleldmKntqnilvqnLSGGQKRKLtfGIA 661
Cdd:COG5265 445 nD--TIAYNIAygrpdaseeeVEAAARAAQIHDfieslpdgYDTRVgERGL-----K---------LSGGEKQRV--AIA 506
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907081362 662 --ILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRVVL 700
Cdd:COG5265 507 rtLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTL 547
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1340-1494 |
3.01e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 64.96 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1340 NISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVllkgsSTGDTPGfLGYCPQE-NALWLNLTVRE-------H 1411
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI-----EIGETVK-LAYVDQSrDALDPNKTVWEeisggldI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1412 LEIfaaikGMRKSDANVAIERLadALKLQDQLKsPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQA 1491
Cdd:TIGR03719 414 IKL-----GKREIPSRAYVGRF--NFKGSDQQK-KVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEA 485
|
...
gi 1907081362 1492 IQA 1494
Cdd:TIGR03719 486 LLN 488
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
508-724 |
3.11e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.75 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 508 KEAI-RIRNLTkdyiqkSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLEN 586
Cdd:PRK10982 247 GEVIlEVRNLT------SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 587 IS----------KLTGVCPQCNVQFDFLTvrENLRLF-AKIKGIQAHEVDNEVQRVLLELDMKN-TQNILVQNLSGGQKR 654
Cdd:PRK10982 321 INhgfalvteerRSTGIYAYLDIGFNSLI--SNIRNYkNKVGLLDNSRMKSDTQWVIDSMRVKTpGHRTQIGSLSGGNQQ 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 655 KLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKE-RRADRVVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:PRK10982 399 KVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAElAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
507-725 |
3.25e-10 |
|
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: 64.46 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 507 GKEAIRIRNLTKDYIQKSKRtEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGlCVPTK--GWVTIHNNKLSEMTDL 584
Cdd:TIGR02633 254 GDVILEARNLTCWDVINPHR-KRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGKfeGNVFINGKPVDIRNPA 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 585 ENIS----------KLTGVCPQcnvqfdfLTVRENLRL-----FAKIKGIQAHEVDNEVQRVLLELDMKNTQNIL-VQNL 648
Cdd:TIGR02633 332 QAIRagiamvpedrKRHGIVPI-------LGVGKNITLsvlksFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLpIGRL 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081362 649 SGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQfMDEADILADRKVFISKGKLK 725
Cdd:TIGR02633 405 SGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlaQEGVAIIVVSSE-LAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1339-1528 |
3.31e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 62.62 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITG--ETKPSA---GQVLLKGSSTGDTPGFLGYCPQENALWL-----NLTV 1408
Cdd:PRK14247 20 DGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEArvsGEVYLDGQDIFKMDVIELRRRVQMVFQIpnpipNLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1409 REHLEIFAAIKGMRKSDANVAiERLADALK-------LQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMD 1481
Cdd:PRK14247 100 FENVALGLKLNRLVKSKKELQ-ERVRWALEkaqlwdeVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907081362 1482 PEGQQQmwqaIQATF--SNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1528
Cdd:PRK14247 179 PENTAK----IESLFleLKKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1337-1554 |
3.37e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 63.10 E-value: 3.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLL----------KGSSTGDTPGFLGYCPQ--ENALWL 1404
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipanlkKIKEVKRLRKEIGLVFQfpEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1405 NlTVREHLEIFAAIKGMRKSDANVAIERLADALKL-QDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1483
Cdd:PRK13645 106 E-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 1484 GQQQMWQAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKfgKEYLLEMKVKTP 1554
Cdd:PRK13645 185 GEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN--QELLTKIEIDPP 253
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1339-1547 |
3.48e-10 |
|
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: 62.17 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTP-----GFLGYCPQENALwLNLTVREHL- 1412
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNlrwlrSQIGLVSQEPVL-FDGTIAENIr 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1413 ---------EIFAAIKgmrksDANVA--IERLADalKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMD 1481
Cdd:cd03249 99 ygkpdatdeEVEEAAK-----KANIHdfIMSLPD--GYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081362 1482 PEGQQQmwqaIQATFSNTERG--ALLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSKFGKEYLL 1547
Cdd:cd03249 172 AESEKL----VQEALDRAMKGrtTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMAQKGVYAKL 234
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1335-1545 |
3.51e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 62.41 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1335 KIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGFLGYCPQENAL--WLNltVREHL 1412
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEGLlpWRN--VQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1413 EIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAI 1492
Cdd:PRK11248 92 AFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907081362 1493 QATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCigsIQHLKSKFGKEY 1545
Cdd:PRK11248 172 LKLWQETGKQVLLITHDIEEAVFMATELVLLSPGPGRV---VERLPLNFARRF 221
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
527-686 |
4.97e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 61.27 E-value: 4.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 527 TEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDlENISKLTGVCPQCNVQF-DflT 605
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP-EIYRQQVSYCAQTPTLFgD--T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 606 VRENLRLFAKIKGIQAHEvdnevQRVLLELDMKN-TQNILVQN---LSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPF 681
Cdd:PRK10247 97 VYDNLIFPWQIRNQQPDP-----AIFLDDLERFAlPDTILTKNiaeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
....*
gi 1907081362 682 SRHRV 686
Cdd:PRK10247 172 NKHNV 176
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1337-1537 |
5.00e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.11 E-value: 5.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTS-------IKMITGETkpSAGQVLLK-------------GSSTGDTPGF-LGY 1395
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTalalmrlLEQAGGLV--QCDKMLLRrrsrqvielseqsAAQMRHVRGAdMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1396 CPQENALWLN--LTVREHL-EIFAAIKGMRKSDANVAIERLADALKL---QDQLKSPVKTLSEGVKRKLCFVLSILGNPS 1469
Cdd:PRK10261 109 IFQEPMTSLNpvFTVGEQIaESIRLHQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081362 1470 VVLLDEPSTGMDPEGQQQMWQAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1537
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1334-1566 |
7.87e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 61.18 E-value: 7.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1334 KKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGD-TPGFLGYC----PQENALWLNLTV 1408
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlSSRQLARRlallPQHHLTPEGITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1409 RE--------HLEIFAAIKGMRKSDANVAIER-----LADalklqdqlkSPVKTLSEGvKRKLCFVLSILG-NPSVVLLD 1474
Cdd:PRK11231 94 RElvaygrspWLSLWGRLSAEDNARVNQAMEQtrinhLAD---------RRLTDLSGG-QRQRAFLAMVLAqDTPVVLLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1475 EPSTGMDPEGQQQMWQAIQATfsNTERGALLTT-HYMAEAEAVCDRVAIMVSGRLRCIGSIQhlkskfgkeyllemKVKT 1553
Cdd:PRK11231 164 EPTTYLDINHQVELMRLMREL--NTQGKTVVTVlHDLNQASRYCDHLVVLANGHVMAQGTPE--------------EVMT 227
|
250
....*....|....*.
gi 1907081362 1554 PS---QVEPLNTEIMR 1566
Cdd:PRK11231 228 PGllrTVFDVEAEIHP 243
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1355-1508 |
7.93e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 60.27 E-value: 7.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1355 GHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPG-FLGYCPQENALWLNLTVREHLEIFAAIkgmrkSDANVAIERL 1433
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKpYCTYIGHNLGLKLEMTVFENLKFWSEI-----YNSAETLYAA 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 1434 ADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIqATFSNTERGALLTTH 1508
Cdd:PRK13541 108 IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI-VMKANSGGIVLLSSH 181
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1339-1537 |
8.45e-10 |
|
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: 64.16 E-value: 8.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITgETKPSAGQVLLKGSSTGDTP-----GFLGYCPQEnALWLNLTVREHLE 1413
Cdd:TIGR01271 1236 QDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGVSWNSVTlqtwrKAFGVIPQK-VFIFSGTFRKNLD 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1414 IFAaikgmRKSDANV-----------AIERLADalKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDP 1482
Cdd:TIGR01271 1314 PYE-----QWSDEEIwkvaeevglksVIEQFPD--KLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP 1386
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 1483 EGQQQMWQAIQATFSNTErgALLTTHYMaEAEAVCDRVAIMVSGRLRCIGSIQHL 1537
Cdd:TIGR01271 1387 VTLQIIRKTLKQSFSNCT--VILSEHRV-EALLECQQFLVIEGSSVKQYDSIQKL 1438
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
492-679 |
1.05e-09 |
|
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: 63.81 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 492 EFSDDSFEPVSMEFHGKEAIRIRNLTKDYIQKSKRTeaLKDLTLDVYKGQITAILGHSGAGKSTLLNVLsglcvptkgwv 571
Cdd:TIGR00957 618 ELEPDSIERRTIKPGEGNSITVHNATFTWARDLPPT--LNGITFSIPEGALVAVVGQVGCGKSSLLSAL----------- 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 572 tihnnkLSEMTDLENISKLTG----VCPQCNVQFDflTVRENLrLFAKIKGIQAHEVDNEVQRVLLELDM--KNTQNILV 645
Cdd:TIGR00957 685 ------LAEMDKVEGHVHMKGsvayVPQQAWIQND--SLRENI-LFGKALNEKYYQQVLEACALLPDLEIlpSGDRTEIG 755
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907081362 646 Q---NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 679
Cdd:TIGR00957 756 EkgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
510-679 |
1.06e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 63.20 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 510 AIRIRNLTKDYiQKSKRTeaLKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTD--LENi 587
Cdd:PRK10790 340 RIDIDNVSFAY-RDDNLV--LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHsvLRQ- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 588 skltGVcpqCNVQFDFL----TVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILV----QNLSGGQKRKLTFG 659
Cdd:PRK10790 416 ----GV---AMVQQDPVvladTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLgeqgNNLSVGQKQLLALA 488
|
170 180
....*....|....*....|
gi 1907081362 660 IAILGDPQIFLLDEPTAGLD 679
Cdd:PRK10790 489 RVLVQTPQILILDEATANID 508
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
530-679 |
1.13e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 60.96 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 530 LKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMtDLENISKLTGVCPQCNVQFDFLTVREn 609
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESW-SSKAFARKVAYLPQQLPAAEGMTVRE- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 610 lrLFAKIK----------GIQAHEvdnEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 679
Cdd:PRK10575 105 --LVAIGRypwhgalgrfGAADRE---KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1350-1539 |
1.17e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 61.27 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1350 VVGLLGHNGAGKSTSIKMITGETKPSAG-----QVLLKGSSTGDTPGFLGYCPQENALW-----LNLTVREHleIFAAIK 1419
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLEFRRRVGMLFqrpnpFPMSIMDN--VLAGVR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1420 GM----RKSDANVAIERLA-----DALKlqDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQ 1490
Cdd:PRK14271 127 AHklvpRKEFRGVAQARLTevglwDAVK--DRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEE 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907081362 1491 AIQATFSNTErgALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKS 1539
Cdd:PRK14271 205 FIRSLADRLT--VIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1337-1528 |
1.34e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 61.40 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGFLGYCPQ------ENALWLNLTV-- 1408
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNpyskkiKNFKELRRRVsm 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1409 ----------REHLE---IFAAIK-GMRKSDANVAIERLADALKLQDQL--KSPVKtLSEGVKRKLCF--VLSIlgNPSV 1470
Cdd:PRK13631 121 vfqfpeyqlfKDTIEkdiMFGPVAlGVKKSEAKKLAKFYLNKMGLDDSYleRSPFG-LSGGQKRRVAIagILAI--QPEI 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081362 1471 VLLDEPSTGMDPEGQQQMWQAIQATFSNtERGALLTTHYMAEAEAVCDRVAIMVSGRL 1528
Cdd:PRK13631 198 LIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1339-1528 |
1.56e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.38 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSS-TGDTPGF-----LGYCP---QENALWLN---- 1405
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEiNALSTAQrlargLVYLPedrQSSGLYLDapla 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1406 -----LTVREhLEIFaaikgMRKSDANVAIERLADALKLQ-DQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTG 1479
Cdd:PRK15439 360 wnvcaLTHNR-RGFW-----IKPARENAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 1480 MDPEGQQQMWQAIQatfSNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1528
Cdd:PRK15439 434 VDVSARNDIYQLIR---SIAAQNVavLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
508-700 |
1.61e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 62.73 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 508 KEAIRIRNLTKDYiqKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTdLENI 587
Cdd:PRK11176 339 KGDIEFRNVTFTY--PGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT-LASL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 588 SKltgvcpQCNVqfdfltVRENLRLFA-KIKGIQAHEVDNEVQRVLLE--------LD----MKNTQNILV-QN---LSG 650
Cdd:PRK11176 416 RN------QVAL------VSQNVHLFNdTIANNIAYARTEQYSREQIEeaarmayaMDfinkMDNGLDTVIgENgvlLSG 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907081362 651 GQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRVVL 700
Cdd:PRK11176 484 GQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSL 533
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1339-1546 |
1.82e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.04 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGEtkPS----AGQVLLKGSSTGDTPgflgycPQEnalwlnltvREHLEI 1414
Cdd:CHL00131 24 KGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PAykilEGDILFKGESILDLE------PEE---------RAHLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1415 FAA------IKGMRKSDanvaIERLADALKLQDQLKSPVKTLS--EGVKRKLCFV------LS----------------- 1463
Cdd:CHL00131 87 FLAfqypieIPGVSNAD----FLRLAYNSKRKFQGLPELDPLEflEIINEKLKLVgmdpsfLSrnvnegfsggekkrnei 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1464 ---ILGNPSVVLLDEPSTGMDPEGQQQMWQAIQaTFSNTERGALLTTHYMAEAEAVC-DRVAIMVSGRLRCIGSIQ--HL 1537
Cdd:CHL00131 163 lqmALLDSELAILDETDSGLDIDALKIIAEGIN-KLMTSENSIILITHYQRLLDYIKpDYVHVMQNGKIIKTGDAElaKE 241
|
....*....
gi 1907081362 1538 KSKFGKEYL 1546
Cdd:CHL00131 242 LEKKGYDWL 250
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1337-1537 |
1.85e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.41 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIK----MITGETKPSAGQVLL------KGSSTGD---TPGFLGYCPQENALW 1403
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELLgrtvqrEGRLARDirkSRANTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1404 LNLTVREHLEI------------FAAIKGMRKSDANVAIERLADALKLQDQlkspVKTLSEGVKRKLCFVLSILGNPSVV 1471
Cdd:PRK09984 99 NRLSVLENVLIgalgstpfwrtcFSWFTREQKQRALQALTRVGMVHFAHQR----VSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 1472 LLDEPSTGMDPEGQQQMWQAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1537
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1337-1526 |
1.96e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 60.28 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDT--PGFLGYCPQ-ENALWLNLTVREHLE 1413
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAlqKNLVAYVPQsEEVDWSFPVLVEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1414 IFAAIKGM------RKSDANVAIERLAdALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQ 1487
Cdd:PRK15056 102 MMGRYGHMgwlrraKKRDRQIVTAALA-RVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEAR 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907081362 1488 MWqAIQATFSNTERGALLTTHYMAEAEAVCDrVAIMVSG 1526
Cdd:PRK15056 181 II-SLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKG 217
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1340-1548 |
2.06e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 61.25 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1340 NISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSstgDTPGF------LGYCPQENALWLNLTVREHLE 1413
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT---DVSRLhardrkVGFVFQHYALFRHMTVFDNIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1414 IFAAIKGMRKSDANVAIERLADALKLQDQL-----KSPVKtLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQM 1488
Cdd:PRK10851 97 FGLTVLPRRERPNAAAIKAKVTQLLEMVQLahladRYPAQ-LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKEL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081362 1489 WQAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL----KSKFGKEYLLE 1548
Cdd:PRK10851 176 RRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVwrepATRFVLEFMGE 239
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1328-1548 |
2.09e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 60.58 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1328 FVLKSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGetkpsagqVLLKGSSTGDTPGFLGYCPQENALWlnlT 1407
Cdd:PRK13640 13 FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLING--------LLLPDDNPNSKITVDGITLTAKTVW---D 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1408 VREHLEIF-----AAIKGMRKSD------ANVAIER------LADALK---LQDQLKSPVKTLSEGVKRKLCfVLSILG- 1466
Cdd:PRK13640 82 IREKVGIVfqnpdNQFVGATVGDdvafglENRAVPRpemikiVRDVLAdvgMLDYIDSEPANLSGGQKQRVA-IAGILAv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1467 NPSVVLLDEPSTGMDPEGQQQMWQAIQATFSNTERGALLTTHYMAEAEaVCDRVAIMVSGRLRCIGSIQHLkskFGKEYL 1546
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEI---FSKVEM 236
|
..
gi 1907081362 1547 LE 1548
Cdd:PRK13640 237 LK 238
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
507-735 |
2.17e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.69 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 507 GKEAIRIRNltkDYIQKSKRTE--ALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGlcvptkgwvtihnnKLSEMTDL 584
Cdd:PLN03232 611 GAPAISIKN---GYFSWDSKTSkpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG--------------ELSHAETS 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 585 E-NISKLTGVCPQCNVQFDfLTVRENLRLFAKI------KGIQA----HEVDNEVQRVLLELDMKNTqnilvqNLSGGQK 653
Cdd:PLN03232 674 SvVIRGSVAYVPQVSWIFN-ATVRENILFGSDFeserywRAIDVtalqHDLDLLPGRDLTEIGERGV------NISGGQK 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 654 RKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWN--FLKERRADRVVLFSTQ--FMDeadiLADRKVFISKGKLKCAGS 729
Cdd:PLN03232 747 QRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDscMKDELKGKTRVLVTNQlhFLP----LMDRIILVSEGMIKEEGT 822
|
....*.
gi 1907081362 730 SLFLKK 735
Cdd:PLN03232 823 FAELSK 828
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1335-1492 |
2.19e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 62.11 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1335 KIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQV-LLKGSStgdtpgfLGYCPQenalwlnltvrEHLE 1413
Cdd:PRK10636 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIK-------LGYFAQ-----------HQLE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1414 IFAA----IKGMRKSDANVAIERLADAL---KLQ-DQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQ 1485
Cdd:PRK10636 387 FLRAdespLQHLARLAPQELEQKLRDYLggfGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
|
....*..
gi 1907081362 1486 QQMWQAI 1492
Cdd:PRK10636 467 QALTEAL 473
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1339-1542 |
2.26e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 62.43 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKG---------------SSTGDTPGFLGYCPQENALW 1403
Cdd:TIGR00958 498 KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylhrqvALVGQEPVLFSGSVRENIAY 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1404 lNLTVREHLEIFAAIKgmrKSDANVAIERLADALKLQDQLKSpvKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPE 1483
Cdd:TIGR00958 578 -GLTDTPDEEIMAAAK---AANAHDFIMEFPNGYDTEVGEKG--SQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE 651
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081362 1484 GQqqmwQAIQATFSNTERGALLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSKFG 1542
Cdd:TIGR00958 652 CE----QLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
511-717 |
2.80e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 60.09 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDY-----IQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMT--- 582
Cdd:PRK10419 4 LNVSGLSHHYahgglSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 583 ------DLENI--SKLTGVCPQCNVQFdflTVRENLR-LFAKIKGIQAHEVDnEVQRvLLELDMKNTQNiLVQNLSGGQK 653
Cdd:PRK10419 84 rkafrrDIQMVfqDSISAVNPRKTVRE---IIREPLRhLLSLDKAERLARAS-EMLR-AVDLDDSVLDK-RPPQLSGGQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 654 RKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLK--------------------ERRADRVVLfstqfMDEADILA 713
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKklqqqfgtaclfithdlrlvERFCQRVMV-----MDNGQIVE 232
|
....
gi 1907081362 714 DRKV 717
Cdd:PRK10419 233 TQPV 236
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1339-1540 |
3.47e-09 |
|
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: 59.87 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKST----SIKMITGEtkpsaGQVLLKGSSTGDTP-----GFLGYCPQENALWLNlTVR 1409
Cdd:cd03289 21 ENISFSISPGQRVGLLGRTGSGKSTllsaFLRLLNTE-----GDIQIDGVSWNSVPlqkwrKAFGVIPQKVFIFSG-TFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1410 EHLEIFAAIKG--MRKSDANVAIERLADAL--KLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQ 1485
Cdd:cd03289 95 KNLDPYGKWSDeeIWKVAEEVGLKSVIEQFpgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITY 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 1486 QQMWQAIQATFSNTErgALLTTHYMaEAEAVCDRVAIMVSGRLRCIGSIQHLKSK 1540
Cdd:cd03289 175 QVIRKTLKQAFADCT--VILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
506-724 |
3.48e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.22 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 506 HGKEAIRIRNLTKdyiqkskrtEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLE 585
Cdd:PRK15439 264 AGAPVLTVEDLTG---------EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 586 --------------------------NISKLTgvcpQCNVQFDFLTVRENLRL--FAKIKGIQAHEVDNEVQRvlleldm 637
Cdd:PRK15439 335 rlarglvylpedrqssglyldaplawNVCALT----HNRRGFWIKPARENAVLerYRRALNIKFNHAEQAART------- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 638 kntqnilvqnLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRADRV-VLFSTQFMDEADILADRK 716
Cdd:PRK15439 404 ----------LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVaVLFISSDLEEIEQMADRV 473
|
....*...
gi 1907081362 717 VFISKGKL 724
Cdd:PRK15439 474 LVMHQGEI 481
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
509-725 |
4.16e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 59.44 E-value: 4.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 509 EAIRIRNLTKDY----------------IQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVT 572
Cdd:PRK13546 3 VSVNIKNVTKEYriyrtnkermkdalipKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 573 IHNnklsemtDLENISKLTGVCPQcnvqfdfLTVRENLRLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQ 652
Cdd:PRK13546 83 RNG-------EVSVIAISAGLSGQ-------LTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081362 653 KRKLTFGIAILGDPQIFLLDEP-TAGLDPFSRHRVWNFLKERRADRVVLFSTQFMDEADILADRKVFISKGKLK 725
Cdd:PRK13546 149 RAKLGFSINITVNPDILVIDEAlSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLK 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
500-729 |
4.16e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.41 E-value: 4.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 500 PVSMEFHGKEAIRIRNLTKDYIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKST-------LLNVLSGLCVPTKGWVT 572
Cdd:PRK10261 2 PHSDELDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVQCDKMLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 573 IHNNK---LSEMTDL---------------ENISKLTGVCPQCNvqfdflTVRENLRLFakiKGIQAHEVDNEVQRVLLE 634
Cdd:PRK10261 82 RRSRQvieLSEQSAAqmrhvrgadmamifqEPMTSLNPVFTVGE------QIAESIRLH---QGASREEAMVEAKRMLDQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 635 LDMKNTQNILVQ---NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLK--ERRADRVVLFSTQFMDEA 709
Cdd:PRK10261 153 VRIPEAQTILSRyphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlQKEMSMGVIFITHDMGVV 232
|
250 260
....*....|....*....|
gi 1907081362 710 DILADRKVFISKGKLKCAGS 729
Cdd:PRK10261 233 AEIADRVLVMYQGEAVETGS 252
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1340-1528 |
4.61e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 58.95 E-value: 4.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1340 NISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGFL-------GYCPQENALWLNLTVREHL 1412
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlirqeaGMVFQQFYLFPHLTALENV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1413 eIFAAIK--GMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQ 1490
Cdd:PRK09493 99 -MFGPLRvrGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907081362 1491 AIQATfsnTERG--ALLTTHYMAEAEAVCDRVAIMVSGRL 1528
Cdd:PRK09493 178 VMQDL---AEEGmtMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
512-572 |
4.83e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.17 E-value: 4.83e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 512 RIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVT 572
Cdd:PRK11701 8 SVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH 64
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1326-1382 |
5.19e-09 |
|
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: 58.60 E-value: 5.19e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1326 KCFVLK---SKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLK 1382
Cdd:COG4778 12 KTFTLHlqgGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR 71
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1339-1528 |
5.73e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.07 E-value: 5.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGE-TKPSA-------GQVLLKGSSTGDTPGFLGYC-----PQENALWLN 1405
Cdd:PRK13547 18 RDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDlTGGGAprgarvtGDVTLNGEPLAAIDAPRLARlravlPQAAQPAFA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1406 LTVRE--------HLEIFAAIKGMRKSDANVAIERL-ADALKLQDqlkspVKTLSEGVKRKLCF--VLSIL-------GN 1467
Cdd:PRK13547 98 FSAREivllgrypHARRAGALTHRDGEIAWQALALAgATALVGRD-----VTTLSGGELARVQFarVLAQLwpphdaaQP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 1468 PSVVLLDEPSTGMDPEGQQQMWQAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1528
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAI 233
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1308-1527 |
6.31e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.78 E-value: 6.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1308 EKPAIIASCLRKEYKGKKKCfvlkskkkiatRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTG 1387
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGC-----------RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1388 DTPgfLGYCPQENALWLNLT----VREHleifaAIKGMRKS---DANVAiERLA-----------------------DAL 1437
Cdd:PRK11701 72 LRD--LYALSEAERRRLLRTewgfVHQH-----PRDGLRMQvsaGGNIG-ERLMavgarhygdiratagdwlerveiDAA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1438 KLQDQlksPvKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDpegqqqmwQAIQATFSNTERG--------ALLTTHY 1509
Cdd:PRK11701 144 RIDDL---P-TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD--------VSVQARLLDLLRGlvrelglaVVIVTHD 211
|
250
....*....|....*...
gi 1907081362 1510 MAEAEAVCDRVAIMVSGR 1527
Cdd:PRK11701 212 LAVARLLAHRLLVMKQGR 229
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1330-1531 |
6.74e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.51 E-value: 6.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1330 LKSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGD-------------------TP 1390
Cdd:PRK10982 256 LTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhnaneainhgfalvteerrST 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1391 GFLGYCPQE-NALWLNltVREHLEIFAAIKGMR-KSDANVAIerlaDALKLQD-QLKSPVKTLSEGVKRKLCFVLSILGN 1467
Cdd:PRK10982 336 GIYAYLDIGfNSLISN--IRNYKNKVGLLDNSRmKSDTQWVI----DSMRVKTpGHRTQIGSLSGGNQQKVIIGRWLLTQ 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081362 1468 PSVVLLDEPSTGMDPEGQQQMWQAIqATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCI 1531
Cdd:PRK10982 410 PEILMLDEPTRGIDVGAKFEIYQLI-AELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGI 472
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1317-1410 |
9.24e-09 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 58.17 E-value: 9.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1317 LRKEYKGKKkcfVLKskkkiatrNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPG----- 1391
Cdd:COG4604 7 VSKRYGGKV---VLD--------DVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSrelak 75
|
90
....*....|....*....
gi 1907081362 1392 FLGYCPQENALWLNLTVRE 1410
Cdd:COG4604 76 RLAILRQENHINSRLTVRE 94
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
528-729 |
9.45e-09 |
|
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: 57.15 E-value: 9.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 528 EALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGlcVP----TKGWVTIHNNKLSEMTDLENISKLTGVCPQCNVQFDF 603
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG--HPkyevTEGEILFKGEDITDLPPEERARLGIFLAFQYPPEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 604 LTVRENLRlfakikgiqahEVdNEvqrvlleldmkntqnilvqNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSR 683
Cdd:cd03217 92 VKNADFLR-----------YV-NE-------------------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDAL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907081362 684 HRVWNFLKE-RRADRVVLFSTQFMDEAD-ILADRKVFISKGKLKCAGS 729
Cdd:cd03217 141 RLVAEVINKlREEGKSVLIITHYQRLLDyIKPDRVHVLYDGRIVKSGD 188
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1334-1528 |
9.69e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 58.25 E-value: 9.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1334 KKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMIT--GETKPS---AGQVLLKGSSTgdtpgflgYCPQENALWLN--- 1405
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHNI--------YSPRTDTVDLRkei 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1406 -----------LTVREHLEIFAAIKGMR-KSDANVAIERladALK-------LQDQLKSPVKTLSEGVKRKLCFVLSILG 1466
Cdd:PRK14239 89 gmvfqqpnpfpMSIYENVVYGLRLKGIKdKQVLDEAVEK---SLKgasiwdeVKDRLHDSALGLSGGQQQRVCIARVLAT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081362 1467 NPSVVLLDEPSTGMDPEGQQQmwqaIQATFSNTERG--ALLTTHYMAEAEAVCDRVAIMVSGRL 1528
Cdd:PRK14239 166 SPKIILLDEPTSALDPISAGK----IEETLLGLKDDytMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
513-679 |
1.18e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.12 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 513 IRNLTKDyiQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVT--IHNNKLSemtdLENISK- 589
Cdd:TIGR00956 62 FRKLKKF--RDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEgvITYDGIT----PEEIKKh 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 LTG---VCPQCNVQFDFLTVRENLRLFAKIKGIQ------------AHEVDneVQRVLLELDM-KNTQ--NILVQNLSGG 651
Cdd:TIGR00956 136 YRGdvvYNAETDVHFPHLTVGETLDFAARCKTPQnrpdgvsreeyaKHIAD--VYMATYGLSHtRNTKvgNDFVRGVSGG 213
|
170 180
....*....|....*....|....*...
gi 1907081362 652 QKRKLTFGIAILGDPQIFLLDEPTAGLD 679
Cdd:TIGR00956 214 ERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
482-724 |
1.31e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.60 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 482 RTALDNETDYEFSDDSFE-PVSMEFHGKEAIRIRNLTKDYiqkSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVL 560
Cdd:PRK10522 293 QVAFNKLNKLALAPYKAEfPRPQAFPDWQTLELRNVTFAY---QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLL 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 561 SGLCVPTKGWVTIHNNKLSeMTDLENISKLtgvcpqcnvqfdFLTVRENLRLFAKIKGIQAHEVDNE-VQRVLLELDMKN 639
Cdd:PRK10522 370 TGLYQPQSGEILLDGKPVT-AEQPEDYRKL------------FSAVFTDFHLFDQLLGPEGKPANPAlVEKWLERLKMAH 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 640 TQN-----ILVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDP-FSRHRVWNFLKERRADRVVLFSTQFMDEADILA 713
Cdd:PRK10522 437 KLEledgrISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPhFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHA 516
|
250
....*....|.
gi 1907081362 714 DRKVFISKGKL 724
Cdd:PRK10522 517 DRLLEMRNGQL 527
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
506-724 |
1.39e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.54 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 506 HGKEAIRIRNLtkdyiqkskRTEALK-DLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDL 584
Cdd:PRK11288 253 LGEVRLRLDGL---------KGPGLRePISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPR 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 585 ENISKLTGVCPQcNVQFD----FLTVRENL-----RLFAKIKGI--QAHEVDN-EVQRVLLELDMKNTQNiLVQNLSGGQ 652
Cdd:PRK11288 324 DAIRAGIMLCPE-DRKAEgiipVHSVADNInisarRHHLRAGCLinNRWEAENaDRFIRSLNIKTPSREQ-LIMNLSGGN 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081362 653 KRKltfgiAILG-----DPQIFLLDEPTAGLDPFSRHRVWNFLKERRAD-RVVLFSTQFMDEADILADRKVFISKGKL 724
Cdd:PRK11288 402 QQK-----AILGrwlseDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQgVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
515-724 |
1.73e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 57.80 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 515 NLTKDYIQKSkrteALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGW-----VTIHNNKLSEMTDLENISK 589
Cdd:PRK14271 26 NLTLGFAGKT----VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYRDVLEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 590 LTGVCPQCNVQFDfLTVRENLrlfakIKGIQAH------EVDNEVQRVLLELDMKNTQNILVQN----LSGGQKRKLTFG 659
Cdd:PRK14271 102 RVGMLFQRPNPFP-MSIMDNV-----LAGVRAHklvprkEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 660 IAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKErRADRV-VLFSTQFMDEADILADRKVFISKGKL 724
Cdd:PRK14271 176 RTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRS-LADRLtVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1340-1483 |
1.98e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.98 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1340 NISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLkgsstGDTPGfLGYCPQEnalwlnltvREHLE----IF 1415
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-----GETVK-LAYVDQS---------RDALDpnktVW 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1416 AAIKG----MR------KSDANVAierlADALKLQDQLKsPVKTLSEGVKRK--LCFVLSILGNpsVVLLDEPSTGMDPE 1483
Cdd:PRK11819 407 EEISGgldiIKvgnreiPSRAYVG----RFNFKGGDQQK-KVGVLSGGERNRlhLAKTLKQGGN--VLLLDEPTNDLDVE 479
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1029-1205 |
2.43e-08 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 57.79 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1029 APSAHIQTDRSTFPEENDHrKFDYLAYFFLWVLLMAcVPPYISMTSIDDYKNRAQFQLWISGLSPSAYWFGQALFEVPVY 1108
Cdd:pfam12698 140 STSAPIPVESTPLFNPQSG-YAYYLVGLILMIIILI-GAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVG 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1109 CALILSIFIAFYASAppeskFTVGDLFIQILYVGGYAMSVIFMTYVISFIYRKGRKNSGLWSLCFYIVSFFSMCFMLIDY 1188
Cdd:pfam12698 218 LLQLLIILLLLFGIG-----IPFGNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLED 292
|
170
....*....|....*..
gi 1907081362 1189 FRDIslFVLIALVPPAT 1205
Cdd:pfam12698 293 PPSF--LQWIFSIIPFF 307
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
528-692 |
2.61e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 58.41 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 528 EALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGL-------CVPTKGwVTI----HNNKLSE-MTDLENISKltGVCP 595
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdkdfngeARPQPG-IKVgylpQEPQLDPtKTVRENVEE--GVAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 596 QCNVQ----------------FDFLtVRENLRLFAKIKGIQAHEVDNEVQRVLLEL-----DMKntqnilVQNLSGGQKR 654
Cdd:TIGR03719 96 IKDALdrfneisakyaepdadFDKL-AAEQAELQEIIDAADAWDLDSQLEIAMDALrcppwDAD------VTKLSGGERR 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907081362 655 KLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKE 692
Cdd:TIGR03719 169 RVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE 206
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
497-724 |
2.83e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 58.26 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 497 SFEPVSMEFHGKEAIRIRNLTkdyiqkSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNN 576
Cdd:PRK09700 252 AMKENVSNLAHETVFEVRNVT------SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 577 KLSEMTDLENISKLTGVCPQC---NVQFDFLTVRENLRLFAKIK--------GIqAHEVDN----EVQRVLLELDMKN-T 640
Cdd:PRK09700 326 DISPRSPLDAVKKGMAYITESrrdNGFFPNFSIAQNMAISRSLKdggykgamGL-FHEVDEqrtaENQRELLALKCHSvN 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 641 QNIlvQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRAD-RVVLFSTQFMDEADILADRKVFI 719
Cdd:PRK09700 405 QNI--TELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVF 482
|
....*
gi 1907081362 720 SKGKL 724
Cdd:PRK09700 483 CEGRL 487
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
539-700 |
3.31e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.28 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 539 KGQITAILGHSGAGKSTLLNVLSGLCVPTKGwvtIHNNKLS-----------EMTD-LENIS--KLTGVC-PQcnvQFDF 603
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLG---DYEEEPSwdevlkrfrgtELQNyFKKLYngEIKVVHkPQ---YVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 604 L------TVRENLrlfakiKGIQAHEVDNEvqrVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAG 677
Cdd:PRK13409 172 IpkvfkgKVRELL------KKVDERGKLDE---VVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180
....*....|....*....|...
gi 1907081362 678 LDPFSRHRVWNFLKERRADRVVL 700
Cdd:PRK13409 243 LDIRQRLNVARLIRELAEGKYVL 265
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1345-1481 |
3.49e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 56.61 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1345 VRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPGFLGYCPQEN-ALWLNLTVREHL------EIFAA 1417
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEFRGSELQNYfTKLLEGDVKVIVkpqyvdLIPKA 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081362 1418 IKG-----MRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMD 1481
Cdd:cd03236 103 VKGkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
530-730 |
4.26e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.64 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 530 LKDLTLDVYKGQITAILGHSGAGKSTLLNVL---------------SGLCVPTKGWV---TIHNNKLseMTDLENISKLT 591
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLlsqfeisegrvwaerSIAYVPQQAWImnaTVRGNIL--FFDEEDAARLA 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 592 GVCPQCNVQFDFLTVRENLRLFAKIKGIqahevdnevqrvlleldmkntqnilvqNLSGGQKRKLTFGIAILGDPQIFLL 671
Cdd:PTZ00243 754 DAVRVSQLEADLAQLGGGLETEIGEKGV---------------------------NLSGGQKARVSLARAVYANRDVYLL 806
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 672 DEPTAGLDPFSRHRVWN--FLKERRADRVVLFSTQFMDEAdiLADRKVFISKGKLKCAGSS 730
Cdd:PTZ00243 807 DDPLSALDAHVGERVVEecFLGALAGKTRVLATHQVHVVP--RADYVVALGDGRVEFSGSS 865
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
511-686 |
5.09e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.12 E-value: 5.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKsKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTI---HNNK---------- 577
Cdd:PTZ00265 383 IQFKNVRFHYDTR-KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIndsHNLKdinlkwwrsk 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 578 ----------------------LSEMTDLE---------------NISKLTGVCPQCNVQFDFL----TVRENLRLFAKI 616
Cdd:PTZ00265 462 igvvsqdpllfsnsiknnikysLYSLKDLEalsnyynedgndsqeNKNKRNSCRAKCAGDLNDMsnttDSNELIEMRKNY 541
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081362 617 KGIQAHEVDNEVQRVLLE---LDMKNTQNILV----QNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRV 686
Cdd:PTZ00265 542 QTIKDSEVVDVSKKVLIHdfvSALPDKYETLVgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
530-679 |
5.62e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.06 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 530 LKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMtDLENISKLTGVCPQCNVQFDFlTVREN 609
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKF-GLTDLRRVLSIIPQSPVLFSG-TVRFN 1329
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 610 LRLFAK------IKGIQAHEVDNEVQRVLLELDMKNTQNilVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 679
Cdd:PLN03232 1330 IDPFSEhndadlWEALERAHIKDVIDRNPFGLDAEVSEG--GENFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
527-679 |
7.64e-08 |
|
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: 57.61 E-value: 7.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 527 TEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTiHNNKLSemtdleniskltgVCPqcnvQFDFL-- 604
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK-HSGRIS-------------FSP----QTSWImp 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 605 -TVRENLRLFAKIKGIQAHEVDNEVQrvlLELDMK---NTQNILVQN----LSGGQKRKLTFGIAILGDPQIFLLDEPTA 676
Cdd:TIGR01271 501 gTIKDNIIFGLSYDEYRYTSVIKACQ---LEEDIAlfpEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
...
gi 1907081362 677 GLD 679
Cdd:TIGR01271 578 HLD 580
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1348-1481 |
8.61e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 57.20 E-value: 8.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1348 GEVVGLLGHNGAGKSTSIKMITGETKPS--AGQVLLKGSS-TGDTPGFLGYCPQENALWLNLTVREHLeIFAAIKGMRKS 1424
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKpTKQILKRTGFVTQDDILYPHLTVRETL-VFCSLLRLPKS 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 1425 DANVAIERLADAL-------KLQDQL--KSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMD 1481
Cdd:PLN03211 173 LTKQEKILVAESViselgltKCENTIigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
497-679 |
9.17e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.74 E-value: 9.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 497 SFE--PVSMEFHGKEAIRIRNLTKDYiqkskrtealKDLTLDV-----YKGQITAILGHSGAGKSTLLNVLSGLCVPTKG 569
Cdd:PRK13409 325 EFEerPPRDESERETLVEYPDLTKKL----------GDFSLEVeggeiYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEG 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 570 WVTihnnklsemTDLEnIS-KltgvcPQcNVQFDF-LTVRENLRlfaKIKG-IQAHEVDNEVQRVLleldmkNTQNIL-- 644
Cdd:PRK13409 395 EVD---------PELK-ISyK-----PQ-YIKPDYdGTVEDLLR---SITDdLGSSYYKSEIIKPL------QLERLLdk 449
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907081362 645 -VQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 679
Cdd:PRK13409 450 nVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1341-1542 |
9.63e-08 |
|
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: 57.26 E-value: 9.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1341 ISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSstgdtpgfLGYCPQEnaLWL-NLTVREHLEIFAAIK 1419
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------VAYVPQQ--AWIqNDSLRENILFGKALN 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1420 GMRKSDANVAIERLAD--ALKLQDQLKSPVK--TLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAI--- 1492
Cdd:TIGR00957 727 EKYYQQVLEACALLPDleILPSGDRTEIGEKgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigp 806
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1493 QATFSNTERgaLLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFG 1542
Cdd:TIGR00957 807 EGVLKNKTR--ILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDG 853
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
511-692 |
9.72e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.18 E-value: 9.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKS-----KRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLsEMTDLE 585
Cdd:PRK15112 5 LEVRNLSKTFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 586 NISKL---------TGVCPQCNVQ--FDFltvreNLRLFAKIKGIQAHEVDNEVQR-VLLELDMKntqNILVQNLSGGQK 653
Cdd:PRK15112 84 YRSQRirmifqdpsTSLNPRQRISqiLDF-----PLRLNTDLEPEQREKQIIETLRqVGLLPDHA---SYYPHMLAPGQK 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907081362 654 RKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKE 692
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLE 194
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1345-1529 |
1.02e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.79 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1345 VRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGS--STGDTPG-------FLGYCPQENALWLNLTVREHLEIF 1415
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQplHQMDEEAraklrakHVGFVFQSFMLIPTLNALENVELP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1416 AAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDpegQQQMWQAIQAT 1495
Cdd:PRK10584 113 ALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD---RQTGDKIADLL 189
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907081362 1496 FS-NTERGA--LLTTHYMAEAeAVCDRVAIMVSGRLR 1529
Cdd:PRK10584 190 FSlNREHGTtlILVTHDLQLA-ARCDRRLRLVNGQLQ 225
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
507-725 |
1.09e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.48 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 507 GKEAIRIRNLTKdYIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGlCVPTK--GWVTIHNNKLSEMTDL 584
Cdd:PRK13549 256 GEVILEVRNLTA-WDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPGRweGEIFIDGKPVKIRNPQ 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 585 ENIS----------KLTGVCPQCNVQFDFLTVreNLRLFAKIKGI-QAHEVDNeVQRVLLELDMKNTQNIL-VQNLSGGQ 652
Cdd:PRK13549 334 QAIAqgiamvpedrKRDGIVPVMGVGKNITLA--ALDRFTGGSRIdDAAELKT-ILESIQRLKVKTASPELaIARLSGGN 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 653 KRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKE--RRADRVVLFSTQfMDEADILADRKVFISKGKLK 725
Cdd:PRK13549 411 QQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQlvQQGVAIIVISSE-LPEVLGLSDRVLVMHEGKLK 484
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
539-692 |
1.16e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 56.72 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 539 KGQITAILGHSGAGKSTLLNVLSGLCVPTKGwvtIHNNKLS-----------EMTD-LENIS--KLTGVC-PQcnvQFDF 603
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLG---DYDEEPSwdevlkrfrgtELQDyFKKLAngEIKVAHkPQ---YVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 604 L------TVRENLrlfakiKGIQAHEVDNEVQRvllELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAG 677
Cdd:COG1245 172 IpkvfkgTVRELL------EKVDERGKLDELAE---KLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSY 242
|
170
....*....|....*
gi 1907081362 678 LDPFSRHRVWNFLKE 692
Cdd:COG1245 243 LDIYQRLNVARLIRE 257
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
522-692 |
1.23e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 55.48 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 522 QKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMTDLENISK-----------L 590
Cdd:PRK15079 29 QPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdiqmifqdpL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQCNVQfDFLTvrENLRLFAkiKGIQAHEVDNEVQRVLLELDM-KNTQNILVQNLSGGQKRKLtfGIA---ILgDP 666
Cdd:PRK15079 109 ASLNPRMTIG-EIIA--EPLRTYH--PKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRI--GIAralIL-EP 180
|
170 180
....*....|....*....|....*.
gi 1907081362 667 QIFLLDEPTAGLDPFSRHRVWNFLKE 692
Cdd:PRK15079 181 KLIICDEPVSALDVSIQAQVVNLLQQ 206
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1340-1508 |
1.28e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 54.33 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1340 NISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTP-----GFLGYCPQENALWLNlTVREHLEI 1414
Cdd:PRK10247 25 NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKpeiyrQQVSYCAQTPTLFGD-TVYDNLIF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1415 FAAIKGmRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQA 1494
Cdd:PRK10247 104 PWQIRN-QQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHR 182
|
170
....*....|....
gi 1907081362 1495 TFSNTERGALLTTH 1508
Cdd:PRK10247 183 YVREQNIAVLWVTH 196
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1339-1532 |
1.28e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 54.85 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITG--ETKPSA---GQVLLKGSSTgdtpgflgYCPQENAL----------- 1402
Cdd:PRK14267 21 KGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRllELNEEArveGEVRLFGRNI--------YSPDVDPIevrrevgmvfq 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1403 ----WLNLTVREHLEIFAAIKGMRKSDANVAiERLADALK-------LQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVV 1471
Cdd:PRK14267 93 ypnpFPHLTIYDNVAIGVKLNGLVKSKKELD-ERVEWALKkaalwdeVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 1472 LLDEPSTGMDPEGQQQMWQAIQATfsNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1532
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
530-687 |
1.50e-07 |
|
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: 54.86 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 530 LKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTiHNNKLSemtdleniskltgVCPqcnvQFDFL---TV 606
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-HSGRIS-------------FSS----QFSWImpgTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 607 RENLrlfakIKGIQAHE--VDNEVQRVLLELDM----KNTQNILVQ---NLSGGQKRKLTFGIAILGDPQIFLLDEPTAG 677
Cdd:cd03291 115 KENI-----IFGVSYDEyrYKSVVKACQLEEDItkfpEKDNTVLGEggiTLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170
....*....|
gi 1907081362 678 LDPFSRHRVW 687
Cdd:cd03291 190 LDVFTEKEIF 199
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
527-679 |
1.61e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.26 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 527 TEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLcvP----TKGWVTIHNNKLSEMtDLENISKL------------ 590
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PaykiLEGDILFKGESILDL-EPEERAHLgiflafqypiei 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 591 TGVCPQcnvqfDFLTVRENlrlfAKIKGIQAHEVDN----EVQRVLLEL-DMKntQNILVQNL----SGGQKRKLTFGIA 661
Cdd:CHL00131 97 PGVSNA-----DFLRLAYN----SKRKFQGLPELDPleflEIINEKLKLvGMD--PSFLSRNVnegfSGGEKKRNEILQM 165
|
170
....*....|....*...
gi 1907081362 662 ILGDPQIFLLDEPTAGLD 679
Cdd:CHL00131 166 ALLDSELAILDETDSGLD 183
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1339-1528 |
2.03e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 54.30 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQvLLKGSS-----TGDTPGFLgycpQENALWLNLTVREHLE 1413
Cdd:PRK11247 29 NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTAplaeaREDTRLMF----QDARLLPWKKVIDNVG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1414 IfaAIKGMRKSDANVAIErladALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDP----EGQQ--- 1486
Cdd:PRK11247 104 L--GLKGQWRDAALQALA----AVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAltriEMQDlie 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907081362 1487 QMWQaiQATFSntergALLTTHYMAEAEAVCDRVAIMVSGRL 1528
Cdd:PRK11247 178 SLWQ--QHGFT-----VLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1334-1505 |
2.07e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.22 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1334 KKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGS-----STGDTPGFLGYCPQENALWLNLTV 1408
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiqhyASKEVARRIGLLAQNATTPGDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1409 RE--------HLEIFAAikgMRKSDANvAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGM 1480
Cdd:PRK10253 99 QElvargrypHQPLFTR---WRKEDEE-AVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180
....*....|....*....|....*
gi 1907081362 1481 DPEGQQQMWQAIQATfsNTERGALL 1505
Cdd:PRK10253 175 DISHQIDLLELLSEL--NREKGYTL 197
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
530-679 |
2.15e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 56.28 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 530 LKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMtDLENISKLTGVCPQCNVQFDFlTVREN 609
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF-GLMDLRKVLGIIPQAPVLFSG-TVRFN 1332
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081362 610 LRLFAKIKGI-------QAHEVDnEVQRVLLELDMKNTQNilVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 679
Cdd:PLN03130 1333 LDPFNEHNDAdlwesleRAHLKD-VIRRNSLGLDAEVSEA--GENFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1307-1533 |
2.25e-07 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 54.04 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1307 QEKPAIIASCLRKEYKGKKkcfVLKSkkkiatrnISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVL------ 1380
Cdd:COG4598 4 TAPPALEVRDLHKSFGDLE---VLKG--------VSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRvggeei 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1381 -LKGSSTGDTPGF-----------LGYCPQENALWLNLTVREHLeIFAAI--KGMRKSDANVAIERLADALKLQDQLKSP 1446
Cdd:COG4598 73 rLKPDRDGELVPAdrrqlqrirtrLGMVFQSFNLWSHMTVLENV-IEAPVhvLGRPKAEAIERAEALLAKVGLADKRDAY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1447 VKTLSEG------VKRKLCFvlsilgNPSVVLLDEPSTGMDPEGQQQMWQAIQAtFSNTERGALLTTHYMAEAEAVCDRV 1520
Cdd:COG4598 152 PAHLSGGqqqraaIARALAM------EPEVMLFDEPTSALDPELVGEVLKVMRD-LAEEGRTMLVVTHEMGFARDVSSHV 224
|
250
....*....|...
gi 1907081362 1521 AIMVSGRLRCIGS 1533
Cdd:COG4598 225 VFLHQGRIEEQGP 237
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
498-679 |
2.29e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.56 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 498 FEPVSMEFHGKEAIRIRNlTKDYIQKSKRTEALKDLTLDV-----YKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVT 572
Cdd:COG1245 320 IRDEPIEFEVHAPRREKE-EETLVEYPDLTKSYGGFSLEVeggeiREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 573 ihnnklsemTDLEnIS-KltgvcPQcNVQFDF-LTVRENLRLFAKiKGIQAHEVDNEVQRVLleldmkNTQNIL---VQN 647
Cdd:COG1245 399 ---------EDLK-ISyK-----PQ-YISPDYdGTVEEFLRSANT-DDFGSSYYKTEIIKPL------GLEKLLdknVKD 455
|
170 180 190
....*....|....*....|....*....|..
gi 1907081362 648 LSGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 679
Cdd:COG1245 456 LSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1341-1529 |
2.50e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 53.89 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1341 ISFCVRKGEVVGLLGHNGAGKSTSIKMITgETKPSAGQVLLKGSSTgdtpgFLGYCPQENALWLN--------------- 1405
Cdd:PRK14258 26 VSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNELESEVRVEGRVE-----FFNQNIYERRVNLNrlrrqvsmvhpkpnl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1406 --LTVREHLEIFAAIKGMR-KSDANVAIERLADALKLQDQLKSPVKT----LSEGVKRKLCFVLSILGNPSVVLLDEPST 1478
Cdd:PRK14258 100 fpMSVYDNVAYGVKIVGWRpKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALAVKPKVLLMDEPCF 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 1479 GMDPEGQQQMWQAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLR 1529
Cdd:PRK14258 180 GLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENR 230
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
516-690 |
2.56e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.95 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 516 LTKDYIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSemtdleNISK--LTGV 593
Cdd:PRK13541 2 LSLHQLQFNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN------NIAKpyCTYI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 594 CPQCNVQFDfLTVRENLRLFAKIKGiQAHEVDNEVQRVLLE--LDMKntqnilVQNLSGGQKRKLTFGIAILGDPQIFLL 671
Cdd:PRK13541 76 GHNLGLKLE-MTVFENLKFWSEIYN-SAETLYAAIHYFKLHdlLDEK------CYSLSSGMQKIVAIARLIACQSDLWLL 147
|
170
....*....|....*....
gi 1907081362 672 DEPTAGLDPFSRHRVWNFL 690
Cdd:PRK13541 148 DEVETNLSKENRDLLNNLI 166
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1339-1607 |
3.20e-07 |
|
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: 55.69 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVllKGSstgdtpGFLGYCPQENalWLNL-TVREHLEIFAA 1417
Cdd:TIGR01271 443 KNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI--KHS------GRISFSPQTS--WIMPgTIKDNIIFGLS 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1418 IKGMRKSDANVAIERLADALKLQDQLKSPVK----TLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQA-I 1492
Cdd:TIGR01271 513 YDEYRYTSVIKACQLEEDIALFPEKDKTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEScL 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1493 QATFSNTERgaLLTTHYMaEAEAVCDRVAIMVSGRLRCIGSIQHLKSKfgkeyllemKVKTPSQVepLNTEIMRLFpqaa 1572
Cdd:TIGR01271 593 CKLMSNKTR--ILVTSKL-EHLKKADKILLLHEGVCYFYGTFSELQAK---------RPDFSSLL--LGLEAFDNF---- 654
|
250 260 270
....*....|....*....|....*....|....*
gi 1907081362 1573 RQERYSSLMVYKLPREDVQPLSQAFFKLETVKQSF 1607
Cdd:TIGR01271 655 SAERRNSILTETLRRVSIDGDSTVFSGPETIKQSF 689
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
545-679 |
3.34e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 545 ILGHSGAGKSTLLNVLSGLcvptkgwVTIHNNKLSEMTDLeNISKLTGVCPQcNVQ---FDFLT--VRE----------- 608
Cdd:PRK11147 34 LVGRNGAGKSTLMKILNGE-------VLLDDGRIIYEQDL-IVARLQQDPPR-NVEgtvYDFVAegIEEqaeylkryhdi 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 609 -----------NLRLFAKIKGIQAHE----VDNEVQRVL--LELDmkntQNILVQNLSGGQKRKLTFGIAILGDPQIFLL 671
Cdd:PRK11147 105 shlvetdpsekNLNELAKLQEQLDHHnlwqLENRINEVLaqLGLD----PDAALSSLSGGWLRKAALGRALVSNPDVLLL 180
|
....*...
gi 1907081362 672 DEPTAGLD 679
Cdd:PRK11147 181 DEPTNHLD 188
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1345-1522 |
3.73e-07 |
|
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: 51.80 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1345 VRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSStgdtpgfLGYCPQEnalwlnltvrehleifaaIKgmrks 1424
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGIT-------PVYKPQY------------------ID----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1425 danvaierladalklqdqlkspvktLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIQATFSNTERGAL 1504
Cdd:cd03222 72 -------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTAL 126
|
170
....*....|....*...
gi 1907081362 1505 LTTHYMAEAEAVCDRVAI 1522
Cdd:cd03222 127 VVEHDLAVLDYLSDRIHV 144
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1346-1481 |
3.79e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.79 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1346 RKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQ---------VL--LKGSSTGD--------------TPGFLGYCPQEn 1400
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDydeepswdeVLkrFRGTELQDyfkklangeikvahKPQYVDLIPKV- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1401 alwLNLTVREHLEifaaikgmrKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGM 1480
Cdd:COG1245 176 ---FKGTVRELLE---------KVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
.
gi 1907081362 1481 D 1481
Cdd:COG1245 244 D 244
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1339-1508 |
3.97e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.87 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTgdtpgfLGYCPQENALWLNLTVREHLEIFAAI 1418
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVR------MAVFSQHHVDGLDLSSNPLLYMMRCF 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1419 KGM--RKSDANVAIERLADALKLQdqlksPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQAIqATF 1496
Cdd:PLN03073 600 PGVpeQKLRAHLGSFGVTGNLALQ-----PMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGL-VLF 673
|
170
....*....|..
gi 1907081362 1497 sntERGALLTTH 1508
Cdd:PLN03073 674 ---QGGVLMVSH 682
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1331-1555 |
4.09e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.11 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1331 KSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTP--------GFLGYCPQENAL 1402
Cdd:TIGR00956 70 DTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEGVITYDGITPeeikkhyrGDVVYNAETDVH 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1403 WLNLTVREHLEIFAAIKGMRKSDANVA----IERLADAL------------KLQDQLkspVKTLSEGVKRKLCFVLSILG 1466
Cdd:TIGR00956 150 FPHLTVGETLDFAARCKTPQNRPDGVSreeyAKHIADVYmatyglshtrntKVGNDF---VRGVSGGERKRVSIAEASLG 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1467 NPSVVLLDEPSTGMDPEGQQQMWQAIQ--ATFSNTergALLTTHYMAEAEA--VCDRVAIMVSGRLRCIGSIQHlkskfG 1542
Cdd:TIGR00956 227 GAKIQCWDNATRGLDSATALEFIRALKtsANILDT---TPLVAIYQCSQDAyeLFDKVIVLYEGYQIYFGPADK-----A 298
|
250
....*....|...
gi 1907081362 1543 KEYLLEMKVKTPS 1555
Cdd:TIGR00956 299 KQYFEKMGFKCPD 311
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1340-1528 |
4.20e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 53.59 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1340 NISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTP------------GFLGYCPqENALWlNLT 1407
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdikqirkkvGLVFQFP-ESQLF-EET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1408 VREHLEIFAAIKGMRKSDAN-VAIERLAdALKLQDQL--KSPVKtLSEGVKRKLCfVLSILG-NPSVVLLDEPSTGMDPE 1483
Cdd:PRK13649 103 VLKDVAFGPQNFGVSQEEAEaLAREKLA-LVGISESLfeKNPFE-LSGGQMRRVA-IAGILAmEPKILVLDEPTAGLDPK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907081362 1484 GQQQMwqaiQATFSNTERGAL---LTTHYMAEAEAVCDRVAIMVSGRL 1528
Cdd:PRK13649 180 GRKEL----MTLFKKLHQSGMtivLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1334-1543 |
4.21e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 54.58 E-value: 4.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1334 KKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTP-----GFLGYCPQEnALWLNLTV 1408
Cdd:PRK13657 347 SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTraslrRNIAVVFQD-AGLFNRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1409 REHL----------EIFAAIKGMRKSDanvAIERLADalKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPST 1478
Cdd:PRK13657 426 EDNIrvgrpdatdeEMRAAAERAQAHD---FIERKPD--GYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATS 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 1479 GMDPEGQQQMWQAIQATFSNteRGALLTTHYMAE-AEAvcDRVAIMVSGRLRCIGSIQHLKSKFGK 1543
Cdd:PRK13657 501 ALDVETEAKVKAALDELMKG--RTTFIIAHRLSTvRNA--DRILVFDNGRVVESGSFDELVARGGR 562
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1337-1527 |
4.43e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 54.45 E-value: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGeTKPSA---GQVL-----LKGSSTGDTP-GFLGYCPQENALWLNLT 1407
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGtwdGEIYwsgspLKASNIRDTErAGIVIIHQELTLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1408 VREHL----EIfaAIKGMRKSDAnvAIERLADALKLQDQLKS-----PVKTLSEGVKRKLCFVLSILGNPSVVLLDEPST 1478
Cdd:TIGR02633 95 VAENIflgnEI--TLPGGRMAYN--AMYLRAKNLLRELQLDAdnvtrPVGDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907081362 1479 GMdPEGQQQMWQAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1527
Cdd:TIGR02633 171 SL-TEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1317-1533 |
4.84e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 53.69 E-value: 4.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1317 LRKEYKGKKkcFVLKSkkkiatrnISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGD-TPG---- 1391
Cdd:PRK11650 9 VRKSYDGKT--QVIKG--------IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNElEPAdrdi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1392 ---FLGYcpqenALWLNLTVREHLEIFAAIKGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNP 1468
Cdd:PRK11650 79 amvFQNY-----ALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081362 1469 SVVLLDEPSTGMDPEGQQQM---WQAIQATFSNTergALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1533
Cdd:PRK11650 154 AVFLFDEPLSNLDAKLRVQMrleIQRLHRRLKTT---SLYVTHDQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1341-1475 |
6.23e-07 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 54.03 E-value: 6.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1341 ISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDtpgflgycpqENALWLnltvREHleiFAAI-- 1418
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA----------DNREAY----RQL---FSAVfs 413
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 1419 --------KGMRKSDANVAIERLADALKLQDQLK------SPVKtLSEGVKRKLCFVLSILGNPSVVLLDE 1475
Cdd:COG4615 414 dfhlfdrlLGLDGEADPARARELLERLELDHKVSvedgrfSTTD-LSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
529-562 |
7.54e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 53.64 E-value: 7.54e-07
10 20 30
....*....|....*....|....*....|....
gi 1907081362 529 ALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSG 562
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
529-678 |
7.93e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.85 E-value: 7.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 529 ALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGW-------VTIHNNKLSEMTDLENISKLTGVCPQcnvqf 601
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSilylgkeVTFNGPKSSQEAGIGIIHQELNLIPQ----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 602 dfLTVRENL---RLFAKIKG-IQAHEVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAG 677
Cdd:PRK10762 94 --LTIAENIflgREFVNRFGrIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDA 171
|
.
gi 1907081362 678 L 678
Cdd:PRK10762 172 L 172
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
530-704 |
9.09e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.49 E-value: 9.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 530 LKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWV-----TIHNNKLSEMTDLENISKLTGVCPqcnvqfdFL 604
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIlferqSIKKDLCTYQKQLCFVGHRSGINP-------YL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 605 TVRENLrLFAKIKGIQAHEVDNEVQRVLLELDMKNTQNIlvqnLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRH 684
Cdd:PRK13540 90 TLRENC-LYDIHFSPGAVGITELCRLFSLEHLIDYPCGL----LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|..
gi 1907081362 685 RVWNFLKERRAD--RVVLFSTQ 704
Cdd:PRK13540 165 TIITKIQEHRAKggAVLLTSHQ 186
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1339-1539 |
1.08e-06 |
|
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: 52.17 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVllKGSstgdtpGFLGYCPQENalWLNL-TVREHLEIFAA 1417
Cdd:cd03291 54 KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI--KHS------GRISFSSQFS--WIMPgTIKENIIFGVS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1418 IKGMRKSDANVAIERLADALKLQDQLKSPVK----TLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQQMWQA-I 1492
Cdd:cd03291 124 YDEYRYKSVVKACQLEEDITKFPEKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEScV 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907081362 1493 QATFSNTERgaLLTTHYMaEAEAVCDRVAIMVSGRLRCIGSIQHLKS 1539
Cdd:cd03291 204 CKLMANKTR--ILVTSKM-EHLKKADKILILHEGSSYFYGTFSELQS 247
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1345-1481 |
1.18e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.27 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1345 VRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQ---------VL--LKGSSTGD--------------TPGFLGYCPQe 1399
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDyeeepswdeVLkrFRGTELQNyfkklyngeikvvhKPQYVDLIPK- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1400 nalWLNLTVREHLEifaaikgmrKSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTG 1479
Cdd:PRK13409 175 ---VFKGKVRELLK---------KVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
..
gi 1907081362 1480 MD 1481
Cdd:PRK13409 243 LD 244
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
514-678 |
1.44e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.01 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 514 RNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLcVPTKGW----------VTIHNNKLSEMTD 583
Cdd:PRK13549 9 KNITKTF----GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHGTYegeiifegeeLQASNIRDTERAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 584 LENI-SKLTGVcPQcnvqfdfLTVRENLRLFAKI--KGIQAH-EVDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFG 659
Cdd:PRK13549 84 IAIIhQELALV-KE-------LSVLENIFLGNEItpGGIMDYdAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIA 155
|
170
....*....|....*....
gi 1907081362 660 IAILGDPQIFLLDEPTAGL 678
Cdd:PRK13549 156 KALNKQARLLILDEPTASL 174
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
533-679 |
1.47e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 51.47 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 533 LTLDVYKGQITAILGHSGAGKSTLLNVLSGLcVPTKGWVTIHNNKLSEMTdLENISKLTG-VCPQCNVQFD-----FLTv 606
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWS-AAELARHRAyLSQQQTPPFAmpvfqYLT- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 607 renLRLFAKIKGIQAHEVDNEVQRvLLELDMKNTQNIlvQNLSGGQKRKLTFGIAIL-----GDP--QIFLLDEPTAGLD 679
Cdd:PRK03695 92 ---LHQPDKTRTEAVASALNEVAE-ALGLDDKLGRSV--NQLSGGEWQRVRLAAVVLqvwpdINPagQLLLLDEPMNSLD 165
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1337-1537 |
1.51e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 52.03 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETkpsAGQVLLKGSSTGDTPGFLGYcpQENAL-------------- 1402
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL---AANGRIGGSATFNGREILNL--PEKELnklraeqismifqd 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1403 ---WLN--LTVREHL-EIFAAIKGMRKSDANVAIERLADALKLQDQLKS----PvKTLSEGVKRKLCFVLSILGNPSVVL 1472
Cdd:PRK09473 106 pmtSLNpyMRVGEQLmEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRmkmyP-HEFSGGMRQRVMIAMALLCRPKLLI 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 1473 LDEPSTGMDPEGQQQMWQAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1537
Cdd:PRK09473 185 ADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
506-724 |
2.51e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.93 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 506 HGKEAIRIRNLTKdyiqkskrtEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKL---SEMT 582
Cdd:PRK10762 253 PGEVRLKVDNLSG---------PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtrSPQD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 583 DLEN----IS---KLTGVCPQcnvqfdfLTVREN-----LRLFAKIKGIQAHevDNEVQRVLLELDMKN----TQNILVQ 646
Cdd:PRK10762 324 GLANgivyISedrKRDGLVLG-------MSVKENmsltaLRYFSRAGGSLKH--ADEQQAVSDFIRLFNiktpSMEQAIG 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 647 NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRAD--RVVLFSTQfMDEADILADRKVFISKGKL 724
Cdd:PRK10762 395 LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEglSIILVSSE-MPEVLGMSDRILVMHEGRI 473
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1340-1482 |
3.02e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 50.53 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1340 NISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSstgDTPGF-----------LGYCPQENALWLNLTV 1408
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGE---NIPAMsrsrlytvrkrMSMLFQSGALFTDMNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1409 --------REHLEIFAAIkgMRKSdanVAIERLADALKLQDQLKSpvKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGM 1480
Cdd:PRK11831 102 fdnvayplREHTQLPAPL--LHST---VMMKLEAVGLRGAAKLMP--SELSGGMARRAALARAIALEPDLIMFDEPFVGQ 174
|
..
gi 1907081362 1481 DP 1482
Cdd:PRK11831 175 DP 176
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1335-1533 |
3.23e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 50.43 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1335 KIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITG-----ETKPSA-GQVLLKGSSTGDTPGF-----LGYCPQENALW 1403
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRlieiyDSKIKVdGKVLYFGKDIFQIDAIklrkeVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1404 LNLTVREHLEIFAAIKGMR-----KSDANVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPST 1478
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKekreiKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907081362 1479 GMDPEGQQQMWQAIqaTFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1533
Cdd:PRK14246 183 MIDIVNSQAIEKLI--TELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGS 235
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1302-1533 |
3.56e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.09 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1302 TSADFQEKPAIIASClRKEYKGKKKCFVLKSKKKIatRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLL 1381
Cdd:PTZ00243 643 TGGGHEATPTSERSA-KTPKMKTDDFFELEPKVLL--RDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1382 KGSstgdtpgfLGYCPQEnALWLNLTVREHLEIFAaikgmrKSDAnvaiERLADALKLQD------QLKSPVKT------ 1449
Cdd:PTZ00243 720 ERS--------IAYVPQQ-AWIMNATVRGNILFFD------EEDA----ARLADAVRVSQleadlaQLGGGLETeigekg 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1450 --LSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPE-GQQQMWQAIQATFSNTERgaLLTTHYMaEAEAVCDRVAIMVSG 1526
Cdd:PTZ00243 781 vnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECFLGALAGKTR--VLATHQV-HVVPRADYVVALGDG 857
|
....*..
gi 1907081362 1527 RLRCIGS 1533
Cdd:PTZ00243 858 RVEFSGS 864
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1341-1482 |
5.16e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.13 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1341 ISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSS-TGDTPgflgycpqenalwlnltvREHLEIFAAI- 1418
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPvTAEQP------------------EDYRKLFSAVf 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1419 ------------KGMRKSDANVA--IERL--ADALKLQDQLKSPVKtLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDP 1482
Cdd:PRK10522 404 tdfhlfdqllgpEGKPANPALVEkwLERLkmAHKLELEDGRISNLK-LSKGQKKRLALLLALAEERDILLLDEWAADQDP 482
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1337-1383 |
5.55e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 49.79 E-value: 5.55e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKG 1383
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD 74
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1339-1508 |
6.02e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.39 E-value: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPS--AGQVLLKG-SSTGDTPGFL-GYCPQENALWLNLTVREHLeI 1414
Cdd:PLN03140 897 REVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGfPKKQETFARIsGYCEQNDIHSPQVTVRESL-I 975
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1415 FAAI----KGMRKSDANVAIERLADALKLqDQLKSP------VKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEG 1484
Cdd:PLN03140 976 YSAFlrlpKEVSKEEKMMFVDEVMELVEL-DNLKDAivglpgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARA 1054
|
170 180
....*....|....*....|....
gi 1907081362 1485 QQQMWQAIQATFsNTERGALLTTH 1508
Cdd:PLN03140 1055 AAIVMRTVRNTV-DTGRTVVCTIH 1077
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1340-1527 |
6.79e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.86 E-value: 6.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1340 NISFCVRKGEVVGLLGHNGAGKS-TSIKMITGETKPSA----GQVLLKGSST--GDTPGFLG-------YCPQENALWLN 1405
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVvypsGDIRFHGESLlhASEQTLRGvrgnkiaMIFQEPMVSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1406 --LTVREHL-EIFAAIKGMRKSDANVAIERLADALKLQD---QLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTG 1479
Cdd:PRK15134 107 plHTLEKQLyEVLSLHRGMRREAARGEILNCLDRVGIRQaakRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTA 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907081362 1480 MDPEGQQQMWQAIQATFSNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1527
Cdd:PRK15134 187 LDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1330-1508 |
7.13e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.26 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1330 LKSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKP---SAGQVLLKGSSTGDT-PGFLGYCPQENALWLN 1405
Cdd:TIGR00956 771 IKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDSSfQRSIGYVQQQDLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1406 LTVREHLEIFAAI---KGMRKSDANVAIERLADALKLQDQLKSPVKTLSEGV----KRKLCFVLSILGNP-SVVLLDEPS 1477
Cdd:TIGR00956 851 STVRESLRFSAYLrqpKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPkLLLFLDEPT 930
|
170 180 190
....*....|....*....|....*....|...
gi 1907081362 1478 TGMDpegQQQMWQAIQA--TFSNTERGALLTTH 1508
Cdd:TIGR00956 931 SGLD---SQTAWSICKLmrKLADHGQAILCTIH 960
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
509-696 |
1.04e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 50.19 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 509 EAIRIRNLTkdyIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGwvTIHNNKLSEMTdlenis 588
Cdd:COG4178 361 GALALEDLT---LRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSG--RIARPAGARVL------ 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 589 kltgvcpqcnvqfdFL---------TVRENLrLFAKikgiQAHEVDNEV-----QRVLLE--LDMKNTQNILVQNLSGGQ 652
Cdd:COG4178 430 --------------FLpqrpylplgTLREAL-LYPA----TAEAFSDAElrealEAVGLGhlAERLDEEADWDQVLSLGE 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907081362 653 KRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRAD 696
Cdd:COG4178 491 QQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPG 534
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1337-1370 |
1.30e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.93 E-value: 1.30e-05
10 20 30
....*....|....*....|....*....|....
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITG 1370
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG 53
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
490-704 |
1.76e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 48.54 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 490 DYEFSDDSFEPVSMEFHGKEAIRIR-----NLTKDYIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLC 564
Cdd:pfam13304 73 RYGLDLEREDVEEKLSSKPTLLEKRlllreDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLS 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 565 vptkGWVTIHNNKLSEMTDLENISKLTGVCPQCNVQFDFLTVRENLRLFAKIKGIQAHEVDNEVQRVLLE-----LDMKN 639
Cdd:pfam13304 153 ----FLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRErglilLENGG 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081362 640 TQNILVQNLSGGQKRKLTFGIAILGDPQ---IFLLDEPTAGLDPFSRHRVWNFLKERRADRV-VLFSTQ 704
Cdd:pfam13304 229 GGELPAFELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKELSRNGAqLILTTH 297
|
|
| RsgA |
COG1162 |
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis]; |
528-562 |
1.94e-05 |
|
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440776 [Multi-domain] Cd Length: 300 Bit Score: 48.57 E-value: 1.94e-05
10 20 30
....*....|....*....|....*....|....*
gi 1907081362 528 EALKDLtLdvyKGQITAILGHSGAGKSTLLNVLSG 562
Cdd:COG1162 158 DELREL-L---KGKTSVLVGQSGVGKSTLINALLP 188
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
528-562 |
2.09e-05 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 47.39 E-value: 2.09e-05
10 20 30
....*....|....*....|....*....|....*
gi 1907081362 528 EALKDLtLdvyKGQITAILGHSGAGKSTLLNVLSG 562
Cdd:cd01854 77 DELREL-L---KGKTSVLVGQSGVGKSTLLNALLP 107
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
511-679 |
2.26e-05 |
|
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: 48.91 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKS---KRT----EALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLcVPTKGWVTIHNNKLSEMTD 583
Cdd:COG4172 276 LEARDLKVWFPIKRglfRRTvghvKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 584 leniSKLTGVCPQCNVQF-D-F------LTVR----ENLRLFAkiKGIQAHEVDNEVQRVLLE--LDmKNTQNILVQNLS 649
Cdd:COG4172 355 ----RALRPLRRRMQVVFqDpFgslsprMTVGqiiaEGLRVHG--PGLSAAERRARVAEALEEvgLD-PAARHRYPHEFS 427
|
170 180 190
....*....|....*....|....*....|...
gi 1907081362 650 GGQKRKLtfGIA---ILgDPQIFLLDEPTAGLD 679
Cdd:COG4172 428 GGQRQRI--AIAralIL-EPKLLVLDEPTSALD 457
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1336-1521 |
2.31e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 47.85 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1336 IATRNISFCVRKGEVVGLLGHNGAGKSTSIKMI--TGETKPSA---GQVLLKGSSTGDTpgflGYCPQENALWLNL---- 1406
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGFrveGKVTFHGKNLYAP----DVDPVEVRRRIGMvfqk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1407 ------TVREHLEIFAAIKGMrKSDANVAIER------LADALKlqDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLD 1474
Cdd:PRK14243 100 pnpfpkSIYDNIAYGARINGY-KGDMDELVERslrqaaLWDEVK--DKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907081362 1475 EPSTGMDPEGQQQMWQAIQATfsNTERGALLTTHYMAEAEAVCDRVA 1521
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHEL--KEQYTIIIVTHNMQQAARVSDMTA 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
511-679 |
2.36e-05 |
|
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: 48.91 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKS----TLLNVLSGLCVPTKGWVTIHN---NKLSE--- 580
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGqdlLGLSErel 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 581 ---------------MTDLeN----ISKltgvcpQcnvqfdfltVRENLRLFAKIKGIQAHevdnevQRV--LLEL-DMK 638
Cdd:COG4172 87 rrirgnriamifqepMTSL-NplhtIGK------Q---------IAEVLRLHRGLSGAAAR------ARAleLLERvGIP 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907081362 639 NTQNILVQ---NLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 679
Cdd:COG4172 145 DPERRLDAyphQLSGGQRQRVMIAMALANEPDLLIADEPTTALD 188
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1312-1488 |
2.44e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 48.16 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1312 IIASCLRKEYKgKKKCFVLKskkkiATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQV--LLKGSSTGDT 1389
Cdd:PRK13651 3 IKVKNIVKIFN-KKLPTELK-----ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1390 PGFLGYCPQENALWLNL----------------------------TVREHLeIFAAIK-GMRKSDANvaiERLADALKL- 1439
Cdd:PRK13651 77 TKEKEKVLEKLVIQKTRfkkikkikeirrrvgvvfqfaeyqlfeqTIEKDI-IFGPVSmGVSKEEAK---KRAAKYIELv 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907081362 1440 ---QDQL-KSPVKtLSEGVKRKLCFVlSILG-NPSVVLLDEPSTGMDPEGQQQM 1488
Cdd:PRK13651 153 gldESYLqRSPFE-LSGGQKRRVALA-GILAmEPDFLVFDEPTAGLDPQGVKEI 204
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
530-695 |
2.88e-05 |
|
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: 45.99 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 530 LKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLcvptkgWvTIHNNKLSemtdleniskltgvCPQCNVQFdFLTVRE- 608
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGL------W-PWGSGRIG--------------MPEGEDLL-FLPQRPy 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 609 ----NLRlfakikgiqahevdnevQRVLLELDmkntqnilvQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRH 684
Cdd:cd03223 75 lplgTLR-----------------EQLIYPWD---------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170
....*....|.
gi 1907081362 685 RVWNFLKERRA 695
Cdd:cd03223 129 RLYQLLKELGI 139
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1335-1640 |
3.25e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.79 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1335 KIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVllkgsSTGdTPGFLGYCPQENA-LWLNLTVREHLe 1413
Cdd:PRK11147 332 KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-----HCG-TKLEVAYFDQHRAeLDPEKTVMDNL- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1414 ifaaikGMRKSDANV-AIERlaDALK-LQDQL------KSPVKTLSEGVKRKLcFVLSILGNPSVVL-LDEPSTGMDPEG 1484
Cdd:PRK11147 405 ------AEGKQEVMVnGRPR--HVLGyLQDFLfhpkraMTPVKALSGGERNRL-LLARLFLKPSNLLiLDEPTNDLDVET 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1485 ---QQQMWQAIQATF----------SNTergalLTTHYMAEAEAVCDRVaimvsgrlrcIGSIQHLKSKFGKEYLLEMKV 1551
Cdd:PRK11147 476 lelLEELLDSYQGTVllvshdrqfvDNT-----VTECWIFEGNGKIGRY----------VGGYHDARQQQAQYLALKQPA 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1552 KTPSQVEPLnteimrlfPQAARQERYSSLMVYKLPREdvqpLSQAFFKLETVKQSF--------DLEEYSLSQSTLEQVF 1623
Cdd:PRK11147 541 VKKKEEAAA--------PKAETVKRSSKKLSYKLQRE----LEQLPQLLEDLEAEIealqaqvaDADFFSQPHEQTQKVL 608
|
330 340
....*....|....*....|.
gi 1907081362 1624 LELS-KEQELD-GFE--EELD 1640
Cdd:PRK11147 609 ADLAdAEQELEvAFErwEELE 629
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
507-573 |
3.83e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 48.39 E-value: 3.83e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081362 507 GKEAIRIRNLTKDYIQKSkrteALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTI 573
Cdd:TIGR03719 319 GDKVIEAENLTKAFGDKL----LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
524-562 |
5.19e-05 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 45.61 E-value: 5.19e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1907081362 524 SKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSG 562
Cdd:pfam03193 90 SAKTGEGIEALKELLKGKTTVLAGQSGVGKSTLLNALLP 128
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1340-1529 |
6.26e-05 |
|
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: 47.51 E-value: 6.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1340 NISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPS-AGQVLLKGSSTgDTPGFL-----GYC--PQEN---------AL 1402
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPV-DIRNPAqairaGIAmvPEDRkrhgivpilGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1403 WLNLTVREhLEIFAAIKGMRKSDANVAIERLADALKLQDQLKS-PVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMD 1481
Cdd:TIGR02633 357 GKNITLSV-LKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFlPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1482 PEGQQQMWQAIqatFSNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRLR 1529
Cdd:TIGR02633 436 VGAKYEIYKLI---NQLAQEGVaiIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1337-1551 |
1.06e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.92 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAG-------QVLLKGSSTGDTPGfLGYCPQENALWLNLTV- 1408
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGsilylgkEVTFNGPKSSQEAG-IGIIHQELNLIPQLTIa 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1409 ------REHLEIFAAI--KGM-RKSDanvaieRLADALKLQDQLKSPVKTLSEGVKR--KLCFVLSIlgNPSVVLLDEPS 1477
Cdd:PRK10762 98 eniflgREFVNRFGRIdwKKMyAEAD------KLLARLNLRFSSDKLVGELSIGEQQmvEIAKVLSF--ESKVIIMDEPT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081362 1478 TGMDPEGQQQMWQAIQaTFSNTERGALLTTHYMAEAEAVCDRVAIMVSGRLrcIGsiQHLKSKFGKEYLLEMKV 1551
Cdd:PRK10762 170 DALTDTETESLFRVIR-ELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQF--IA--EREVADLTEDSLIEMMV 238
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
512-562 |
1.39e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 45.97 E-value: 1.39e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1907081362 512 RIRNLTKDYIQKSKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSG 562
Cdd:PRK00098 136 LYRAIGYDVLELSAKEGEGLDELKPLLAGKVTVLAGQSGVGKSTLLNALAP 186
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
511-678 |
1.84e-04 |
|
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: 45.97 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 511 IRIRNLTKDYiqksKRTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLcVPTKGWV-TIHNN----KLSEMTDLE 585
Cdd:TIGR02633 2 LEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHGTWDgEIYWSgsplKASNIRDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 586 N-----ISKLTGVCPQcnvqfdfLTVRENLRLFAKI--KGIQAH--EVDNEVQRVLLELDMKNTQNIL-VQNLSGGQKRK 655
Cdd:TIGR02633 77 RagiviIHQELTLVPE-------LSVAENIFLGNEItlPGGRMAynAMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQL 149
|
170 180
....*....|....*....|...
gi 1907081362 656 LTFGIAILGDPQIFLLDEPTAGL 678
Cdd:TIGR02633 150 VEIAKALNKQARLLILDEPSSSL 172
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
530-679 |
1.85e-04 |
|
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: 46.48 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 530 LKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNNKLSEMtDLENI-SKLTgVCPQCNVQFDFlTVRE 608
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI-GLHDLrFKIT-IIPQDPVLFSG-SLRM 1378
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081362 609 NLRLFAKIK------GIQAHEVDNEVQRVLLELDMKNTQNilVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLD 679
Cdd:TIGR00957 1379 NLDPFSQYSdeevwwALELAHLKTFVSALPDKLDHECAEG--GENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1339-1481 |
1.86e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 46.26 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1339 RNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPG---------FLGYCPQENALWLNLTVR 1409
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdalaqlrreHFGFIFQRYHLLSHLTAA 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 1410 EHLEIFAAIKGM----RKSDANVAIERLAdalkLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMD 1481
Cdd:PRK10535 105 QNVEVPAVYAGLerkqRLLRAQELLQRLG----LEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALD 176
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1340-1481 |
1.96e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.04 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1340 NISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLkgsstgdTPGF-LGYCPQ-----ENALWLNLTVREHLE 1413
Cdd:PRK15064 19 NISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL-------DPNErLGKLRQdqfafEEFTVLDTVIMGHTE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1414 IFAAIK---------------GMRKSDANVAI--------ERLADALKLQ-----DQLKSPVKTLSEGVKRKLCFVLSIL 1465
Cdd:PRK15064 92 LWEVKQerdriyalpemseedGMKVADLEVKFaemdgytaEARAGELLLGvgipeEQHYGLMSEVAPGWKLRVLLAQALF 171
|
170
....*....|....*.
gi 1907081362 1466 GNPSVVLLDEPSTGMD 1481
Cdd:PRK15064 172 SNPDILLLDEPTNNLD 187
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
643-714 |
5.67e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 42.35 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 643 ILVQNLSGGQKRKLT----FGIAILGDPQIFLLDEPTAGLDPFSRHRVWNFLKERRA-DRVVLFST---QFMDEADILAD 714
Cdd:cd03227 73 FTRLQLSGGEKELSAlaliLALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVkGAQVIVIThlpELAELADKLIH 152
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1341-1562 |
6.19e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.58 E-value: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1341 ISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTG-----DTPGFLGYCPQENALWLNlTVREHLEIF 1415
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfgltDLRRVLSIIPQSPVLFSG-TVRFNIDPF 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1416 AaikgmRKSDANV--AIER--LADALK-----LQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDPEGQQ 1486
Cdd:PLN03232 1334 S-----EHNDADLweALERahIKDVIDrnpfgLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDS 1408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 1487 QMWQAIQATFSNTergALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKEYLLEMKVKTPSQVEPLNT 1562
Cdd:PLN03232 1409 LIQRTIREEFKSC---TMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPANAQYLSN 1481
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
539-722 |
9.04e-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: 41.59 E-value: 9.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 539 KGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTIHNnklsemtdleniskltgvcpqcnvqfdfltvrenlrlfakikg 618
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID------------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 619 iqahevDNEVQRVLLELDMKNTQNILVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSRHRVW-------NFLK 691
Cdd:smart00382 38 ------GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrlLLLL 111
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907081362 692 ERRADRVVLFSTQFMDEAD-----ILADRKVFISKG 722
Cdd:smart00382 112 KSEKNLTVILTTNDEKDLGpallrRRFDRRIVLLLI 147
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
508-702 |
1.20e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.86 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 508 KEAIRIRNLTKDYIQKSKrTEALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLC-VPTKGWVTIHNNKLSEMTD--- 583
Cdd:PTZ00265 1163 KGKIEIMDVNFRYISRPN-VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdLKNDHHIVFKNEHTNDMTNeqd 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 584 ----------LENISKLT----GVCPQCNVQFD-----------------------FLTVRE-----NLRLFAKIKGIQA 621
Cdd:PTZ00265 1242 yqgdeeqnvgMKNVNEFSltkeGGSGEDSTVFKnsgkilldgvdicdynlkdlrnlFSIVSQepmlfNMSIYENIKFGKE 1321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 622 HEVDNEVQRV---------LLELDMKNTQNI--LVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAGLDPFSR------- 683
Cdd:PTZ00265 1322 DATREDVKRAckfaaidefIESLPNKYDTNVgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEkliekti 1401
|
250 260 270
....*....|....*....|....*....|....
gi 1907081362 684 ---------------HRVWNFlkeRRADRVVLFS 702
Cdd:PTZ00265 1402 vdikdkadktiitiaHRIASI---KRSDKIVVFN 1432
|
|
| MnmE_helical |
pfam12631 |
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ... |
493-562 |
1.22e-03 |
|
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An N-terminal domain, a helical domain and a GTPase domain which is nested within the helical domain. This family represents the helical domain.
Pssm-ID: 463649 [Multi-domain] Cd Length: 326 Bit Score: 42.85 E-value: 1.22e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 493 FSDDSFEPVSMEFHGKEAIRIRNLTKDYIQKSKRTEALKDltldvykGQITAILGHSGAGKSTLLNVLSG 562
Cdd:pfam12631 54 FPEDDIEELTEEELLERLEELLAELEKLLATADRGRILRE-------GIKVVIVGKPNVGKSSLLNALLG 116
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1317-1383 |
1.45e-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: 43.13 E-value: 1.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081362 1317 LRKEYKGKKKCFVLKSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETkPSAGQVLLKG 1383
Cdd:COG4172 281 LKVWFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDG 346
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
605-679 |
2.36e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.47 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 605 TVRENLRLfAKIKGIQAHEVDNEVQRVLLELDMKNTQNI-------LVQNLSGGQKRKLTFGIAILGDPQIFLLDEPTAG 677
Cdd:NF040905 356 DIKRNITL-ANLGKVSRRGVIDENEEIKVAEEYRKKMNIktpsvfqKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRG 434
|
..
gi 1907081362 678 LD 679
Cdd:NF040905 435 ID 436
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1317-1364 |
2.79e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.38 E-value: 2.79e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1907081362 1317 LRKEYKGKKKCFVLKSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTS 1364
Cdd:PRK15134 281 LQVAFPIRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTT 328
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1350-1476 |
2.96e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 41.78 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1350 VVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPG--FL-------GYCPQENALWLNLTVREHLEIfaaikG 1420
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKgiCLppekrriGYVFQDARLFPHYKVRGNLRY-----G 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081362 1421 MRKSDaNVAIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEP 1476
Cdd:PRK11144 101 MAKSM-VAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1328-1494 |
2.98e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 42.31 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1328 FVLKSKKKIATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKGSSTGDTPgfLGYCPQENAL----- 1402
Cdd:PRK11176 349 FTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT--LASLRNQVALvsqnv 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1403 -WLNLTVREHLEIFAAIKGMRKSDANVAieRLADALKLQDQLKSPVKT--------LSEGVKRKLCFVLSILGNPSVVLL 1473
Cdd:PRK11176 427 hLFNDTIANNIAYARTEQYSREQIEEAA--RMAYAMDFINKMDNGLDTvigengvlLSGGQRQRIAIARALLRDSPILIL 504
|
170 180
....*....|....*....|.
gi 1907081362 1474 DEPSTGMDPEGQqqmwQAIQA 1494
Cdd:PRK11176 505 DEATSALDTESE----RAIQA 521
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1337-1370 |
3.98e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.70 E-value: 3.98e-03
10 20 30
....*....|....*....|....*....|....
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITG 1370
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
530-558 |
4.14e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.92 E-value: 4.14e-03
10 20
....*....|....*....|....*....
gi 1907081362 530 LKDLTLDVYKGQITAILGHSGAGKSTLLN 558
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLIN 652
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1307-1383 |
5.15e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 41.10 E-value: 5.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081362 1307 QEKPAIIASCLRKEYKGKKKCFVLKSKKKiATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKG 1383
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVKRGLFKPERLVK-ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQG 76
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1337-1527 |
5.27e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.25 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1337 ATRNISFCVRKGEVVGLLGHNGAGKSTSIKMITGETKPSAGQVLLKG------SSTGDTPGFLGYCPQENALWLNLTVRE 1410
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeidfkSSKEALENGISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081362 1411 HL--------EIFAAIKGMRKSdanvaIERLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSVVLLDEPSTGMDP 1482
Cdd:PRK10982 93 NMwlgryptkGMFVDQDKMYRD-----TKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907081362 1483 EGQQQMWQAIQATfsnTERGA--LLTTHYMAEAEAVCDRVAIMVSGR 1527
Cdd:PRK10982 168 KEVNHLFTIIRKL---KERGCgiVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
507-573 |
6.15e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.26 E-value: 6.15e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081362 507 GKEAIRIRNLTKDYIQKSkrteALKDLTLDVYKGQITAILGHSGAGKSTLLNVLSGLCVPTKGWVTI 573
Cdd:PRK11819 321 GDKVIEAENLSKSFGDRL----LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| |
