|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-1522 |
0e+00 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 2566.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 7 SGELGSKFWDSNLSIYTNTPDLTPCFQNSLLAWVPCIYLWAALPCYLFYLRHHQLGYIVLSWLSRLKTALGVLLWCVSWV 86
Cdd:TIGR00957 2 SADGSDPLWDWNVTWHTSNPDFTKCFQNTVLAWVPCFYLWVCFPCYFLYLSRHDRGYIQMTHLNKTKTALGFLLWIVCWA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 87 DLFYSFHGLIHGSSPAPVFFVTPLVVGITMLLATLLIQYERLRGVQSSGVLIIFWLLCVICAIIPFRSKILSALAEGKIL 166
Cdd:TIGR00957 82 DLFYSFWERSHGRAPAPVFLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALVCALAILRSKILLALKEDAIV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 167 DPFRFTTFYIYFALVFCALILSCFKEKPPLFSPENLDTNPCPEASAGFFSRLSFWWFTRLAILGYRRPLEDRDLWSLSEE 246
Cdd:TIGR00957 162 DPFRDTTFYIYFALVLSQLVLSCFSDKSPLFSETNHDPNPCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 247 DCSHKVVQRLLEAWQKQQNQASRSQTATA-EPKIP------------GEDAVLLKPRP-KSKQPSFLRALVRTFTSSLLM 312
Cdd:TIGR00957 242 DTSEMVVPVLVENWKKECKKTRKQPVSAVyGKKDPskpkgssqldanEEVEALIVKSPhKPRKPSLFKVLYKTFGPYFLM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 313 SACFNLIQNLLGFVNPQLLSILIRFISDPTAPTWWGFLLAGLMFLSSTMQTLILHQYYHCIFVMALRLRTAIIGVIYRKA 392
Cdd:TIGR00957 322 SFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 393 LVITNSVKRESTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNGAVSMKM 472
Cdd:TIGR00957 402 LVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKT 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 473 KTYQVKQMKFKDSRIKLMSEILNGIKVLKLYAWEPSFLEQVKGIRQSELQLLRKGAYLQAISTFIWICTPFLVTLITLGV 552
Cdd:TIGR00957 482 KTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAV 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 553 YVYVDESNVLDAEKAFVSLSLFNILKIPLNMLPQLISGLTQASVSLKRIQDFLNQNELDPQCVERKTISPG--YAITIHN 630
Cdd:TIGR00957 562 YVTVDENNILDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGegNSITVHN 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 631 GTFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSVAYVPQQAWIQNCTLQENVLF 710
Cdd:TIGR00957 642 ATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILF 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 711 GQPMNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFD 790
Cdd:TIGR00957 722 GKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 791 QVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLAGGQVSEMGHYSALLQHDGSFANFLRNYAPDEDQEDHE----AALQN 866
Cdd:TIGR00957 802 HVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQGHLEdswtALVSG 881
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 867 ANEEVLLLEDTLSThtdltdnepaIYEVRKQFMREMSSLSSEGEVQNRtmpkkHTNSLEKEALVTKTKETGALIKEEIAE 946
Cdd:TIGR00957 882 EGKEAKLIENGMLV----------TDVVGKQLQRQLSASSSDSGDQSR-----HHGSSAELQKAEAKEETWKLMEADKAQ 946
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 947 TGNVKLSVYWDYAKSMGLCTTLSICLLYGGQSAAAIGANVWLSAWSNDAEEHGQQNKTSVRLGVYAALGILQGLLVMLSA 1026
Cdd:TIGR00957 947 TGQVELSVYWDYMKAIGLFITFLSIFLFVCNHVSALASNYWLSLWTDDPMVNGTQNNTSLRLSVYGALGILQGFAVFGYS 1026
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1027 FTMVVGAIQAARLLHEALLHNKIRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLLNSFFTSISTIMVIVASTPL 1106
Cdd:TIGR00957 1027 MAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPI 1106
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1107 FMVVVLPLAVLYGFVQRFYVATSRQLKRLESISRSPIFSHFSETVTGTSVIRAYGRIQDFKVLSDTKVDNNQKSSYPYIA 1186
Cdd:TIGR00957 1107 AAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIV 1186
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1187 SNRWLGVHVEFVGNCVVLFAALFAVIGRNSLNPGLVGLSVSYALQVTMALNWMIRMISDLESNIIAVERVKEYSKTKTEA 1266
Cdd:TIGR00957 1187 ANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEA 1266
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1267 PWVVESNRAPEGWPTRGMVEFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVID 1346
Cdd:TIGR00957 1267 PWQIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIID 1346
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1347 GLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQ 1426
Cdd:TIGR00957 1347 GLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQ 1426
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1427 RQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNL 1506
Cdd:TIGR00957 1427 RQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNL 1506
|
1530
....*....|....*.
gi 1388591336 1507 IAAGGIFYGMAKDAGL 1522
Cdd:TIGR00957 1507 LQQRGIFYSMAKDAGL 1522
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
172-1523 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 1041.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 172 TTFYIYFALVFCALILSCFK-------EKPPLFSP---ENLDT----------NPCPEASAGFFSRLSFWWFTRLAILGY 231
Cdd:PLN03130 172 FVLYLYISEVAAQVLFGILLlvyfpnlDPYPGYTPigsESVDDyeyeelpggeQICPERHANIFSRIFFGWMTPLMQLGY 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 232 RRPLEDRDLWSLSEEDCSHKVVQRLLEAWQKQqnqasrsqtataepkipgedavLLKPRPKskqpsFLRALVRTFTSSLL 311
Cdd:PLN03130 252 KRPLTEKDVWKLDTWDQTETLYRSFQKCWDEE----------------------LKKPKPW-----LLRALNNSLGGRFW 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 312 MSACFNLIQNLLGFVNPQLLSILIRFISDpTAPTWWGFLLAGLMFLSSTMQTLILHQYYHCIFVMALRLRTAIIGVIYRK 391
Cdd:PLN03130 305 LGGFFKIGNDLSQFVGPLLLNLLLESMQN-GEPAWIGYIYAFSIFVGVVLGVLCEAQYFQNVMRVGFRLRSTLVAAVFRK 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 392 ALVITNSVKRESTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNGAVSMK 471
Cdd:PLN03130 384 SLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQTFIISK 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 472 MKTYQVKQMKFKDSRIKLMSEILNGIKVLKLYAWEPSFLEQVKGIRQSELQLLRKGAYLQAISTFIWICTPFLVTLITLG 551
Cdd:PLN03130 464 MQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNSIPVLVTVVSFG 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 552 VYVYVdeSNVLDAEKAFVSLSLFNILKIPLNMLPQLISGLTQASVSLKRIQDFLNQNE--LDPQcverKTISPGY-AITI 628
Cdd:PLN03130 544 VFTLL--GGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEErvLLPN----PPLEPGLpAISI 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 629 HNGTFTWAQDLP-PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLE-GVVSVKGSVAYVPQQAWIQNCTLQE 706
Cdd:PLN03130 618 KNGYFSWDSKAErPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTVAYVPQVSWIFNATVRD 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 707 NVLFGQPMNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAK 786
Cdd:PLN03130 698 NILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGR 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 787 HIFDQVIGPEgvLAGKTRVLVTHGISFLPQTDFIIVLAGGQVSEMGHYSALLQHDGSFANFLRNYAPDEDQEDheaalqn 866
Cdd:PLN03130 778 QVFDKCIKDE--LRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENAGKMEEYVE------- 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 867 aneevllledtlsthtdltdnEPAIYEVRKqfmremsslSSEGEVQNRTMPKKHTNSLEKealvTKTKETGA-LIKEEIA 945
Cdd:PLN03130 849 ---------------------ENGEEEDDQ---------TSSKPVANGNANNLKKDSSSK----KKSKEGKSvLIKQEER 894
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 946 ETGNVKLSVYWDYAKSMG---LCTTLSICllYGGQSAAAIGANVWLSAWSNDAEehGQQNKTSVRLGVYAALGILQGLLV 1022
Cdd:PLN03130 895 ETGVVSWKVLERYKNALGgawVVMILFLC--YVLTEVFRVSSSTWLSEWTDQGT--PKTHGPLFYNLIYALLSFGQVLVT 970
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1023 MLSAFTMVVGAIQAARLLHEALLHNKIRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLLNSFFTSISTIMVIVA 1102
Cdd:PLN03130 971 LLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGI 1050
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1103 STPLFMVVVLPLAVLYGFVQRFYVATSRQLKRLESISRSPIFSHFSETVTGTSVIRAYGRIQDFKVLSDTKVDNNQKSSY 1182
Cdd:PLN03130 1051 VSTISLWAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTL 1130
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1183 PYIASNRWLGVHVEFVGNCVVLFAALFAVIGR-NSLNP----GLVGLSVSYALQVTMALNWMIRMISDLESNIIAVERVK 1257
Cdd:PLN03130 1131 VNMSSNRWLAIRLETLGGLMIWLTASFAVMQNgRAENQaafaSTMGLLLSYALNITSLLTAVLRLASLAENSLNAVERVG 1210
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1258 EYSKTKTEAPWVVESNRAPEGWPTRGMVEFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILE 1337
Cdd:PLN03130 1211 TYIDLPSEAPLVIENNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVE 1290
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1338 AAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQPAGLDFQCAE 1417
Cdd:PLN03130 1291 LERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSE 1370
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1418 GGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVV 1497
Cdd:PLN03130 1371 AGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRV 1450
|
1370 1380
....*....|....*....|....*..
gi 1388591336 1498 AEFDSPVNLIA-AGGIFYGMAKDAGLA 1523
Cdd:PLN03130 1451 VEFDTPENLLSnEGSAFSKMVQSTGAA 1477
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
29-1523 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 987.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 29 TPCFQNSLLAWVPCIYLWAALPCYLFYLRHHQLGYIVLSWLSRLKTALGVLLWCVSWVDLFYSFHGL----IHGSSPAPV 104
Cdd:PLN03232 30 TPCAIDSLVMIVSHSVLLGLCFYRIWIILDNAKAQIYVLRKKYYNCVLGILACYCVVEPVLRLVMGIslfdMDEETDLPP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 105 FFVTPLVVGITMLLATL-LIQYERLRGVQSSGVLIIFWLLCVICAIIPFRSKILSalaegkILDPFRFTTFYIYFA---- 179
Cdd:PLN03232 110 FEVASLMVEAFAWFSMLvLIGLETKQYVKEFRWYVRFGVVYVLVADAVLLDLVLP------LKNSINRTALYLCISsrcc 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 180 -LVFCALILSCFKEKPP-----LFSPENLDT----------NPCPEASAGFFSRLSFWWFTRLAILGYRRPLEDRDLWSL 243
Cdd:PLN03232 184 qALFGILLLVYIPELDPypgyhILNNESLDNveydalrggeNICPERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 244 SEEDCSHKVVQRLLEAWQKQQNqasrsqtataepkipgedavllkpRPKskqPSFLRALVRTFTSSLLMSACFNLIQNLL 323
Cdd:PLN03232 264 DQWDQTETLIKRFQRCWTEESR------------------------RPK---PWLLRALNNSLGGRFWLGGIFKIGHDLS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 324 GFVNPQLLSILIRFISDPTaPTWWGFLLAGLMFLSSTMQTLILHQYYHCIFVMALRLRTAIIGVIYRKALVITNSVKRES 403
Cdd:PLN03232 317 QFVGPVILSHLLQSMQEGD-PAWVGYVYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAAIFHKSLRLTHEARKNF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 404 TVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNGAVSMKMKTYQVKQMKFK 483
Cdd:PLN03232 396 ASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 484 DSRIKLMSEILNGIKVLKLYAWEPSFLEQVKGIRQSELQLLRKGAYLQAISTFIWICTPFLVTLITLGVYVYVDESnvLD 563
Cdd:PLN03232 476 DKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGVFVLLGGD--LT 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 564 AEKAFVSLSLFNILKIPLNMLPQLISGLTQASVSLKRIQD-FLNQNELDPQcveRKTISPGY-AITIHNGTFTWAQDLP- 640
Cdd:PLN03232 554 PARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEElLLSEERILAQ---NPPLQPGApAISIKNGYFSWDSKTSk 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLE-GVVSVKGSVAYVPQQAWIQNCTLQENVLFGQPMNPKRY 719
Cdd:PLN03232 631 PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERY 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 720 QQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGPEgvL 799
Cdd:PLN03232 711 WRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDE--L 788
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 800 AGKTRVLVTHGISFLPQTDFIIVLAGGQVSEMGHYSALLQHDGSFANFLRNYAPDEDQEDheaalQNANEEVLLledtls 879
Cdd:PLN03232 789 KGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKMDATQE-----VNTNDENIL------ 857
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 880 thtdltdnepaiyevrkqfmremsslssegevqnRTMPKKHTNSLEKEALVTKTKETG--ALIKEEIAETGNVKLSVYWD 957
Cdd:PLN03232 858 ----------------------------------KLGPTVTIDVSERNLGSTKQGKRGrsVLVKQEERETGIISWNVLMR 903
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 958 YAKSMGLCTTLSICLL-YGGQSAAAIGANVWLSAWSNdaeehgQQNKTSVRLG----VYAALGILQGLLVMLSAFTMVVG 1032
Cdd:PLN03232 904 YNKAVGGLWVVMILLVcYLTTEVLRVSSSTWLSIWTD------QSTPKSYSPGfyivVYALLGFGQVAVTFTNSFWLISS 977
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1033 AIQAARLLHEALLHNKIRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLLNSFFTSISTIMVIVASTPLFMVVVL 1112
Cdd:PLN03232 978 SLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIM 1057
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1113 PLAVLYGFVQRFYVATSRQLKRLESISRSPIFSHFSETVTGTSVIRAYGRIQDFKVLSDTKVDNNQKSSYPYIASNRWLG 1192
Cdd:PLN03232 1058 PLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLT 1137
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1193 VHVEFVGNCVVLFAALFAVIGRNSLN-----PGLVGLSVSYALQVTMALNWMIRMISDLESNIIAVERVKEYSKTKTEAP 1267
Cdd:PLN03232 1138 IRLETLGGVMIWLTATFAVLRNGNAEnqagfASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEAT 1217
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1268 WVVESNRAPEGWPTRGMVEFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDG 1347
Cdd:PLN03232 1218 AIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD 1297
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1348 LNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQR 1427
Cdd:PLN03232 1298 CDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQR 1377
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1428 QLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLI 1507
Cdd:PLN03232 1378 QLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELL 1457
|
1530
....*....|....*..
gi 1388591336 1508 A-AGGIFYGMAKDAGLA 1523
Cdd:PLN03232 1458 SrDTSAFFRMVHSTGPA 1474
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
284-1521 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 827.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 284 AVLLKPRPKSKQPSFLRALVRTFTSSLLMSACFNLIQNLLGFVNPQLLSILIRFISDPTApTW-WGFLLAGLMFLSSTMQ 362
Cdd:PTZ00243 220 VVRPGPPPTPKRLSLLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFLDADNA-TWgRGLGLVLTLFLTQLIQ 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 363 TLILHQYYHCIFVMALRLRTAIIGVIYRKALVITN-SVKR-ESTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAI 440
Cdd:PTZ00243 299 SVCLHRFYYISIRCGLQYRSALNALIFEKCFTISSkSLAQpDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSI 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 441 YFLWQILGPSALAGVAVIVLLIPLNGAVSMKMKTYQVKQMKFKDSRIKLMSEILNGIKVLKLYAWEPSFLEQVKGIRQSE 520
Cdd:PTZ00243 379 LLLSRLVGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARE 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 521 LQLLRKGAYLQAISTFIWICTPFLVtlITLGVYVYVDESNVLDAEKAFVSLSLFNILKIPLNMLPQLISGLTQASVSLKR 600
Cdd:PTZ00243 459 LRYLRDVQLARVATSFVNNATPTLM--IAVVFTVYYLLGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKR 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 601 IQDFL------------------NQNELD----------------------PQCVERKT--------------------- 619
Cdd:PTZ00243 537 ISTFLecdnatcstvqdmeeywrEQREHStacqlaavlenvdvtafvpvklPRAPKVKTsllsralrmlcceqcrptkrh 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 620 -----------------------------------ISPGYAITIHNGTFTWAQDLPPTL-HSLNIQIPKGALVAVVGPVG 663
Cdd:PTZ00243 617 pspsvvvedtdygspssasrhiveggtgggheatpTSERSAKTPKMKTDDFFELEPKVLlRDVSVSVPRGKLTVVLGATG 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 664 CGKSSLVSALLGEMEKLEGVVSVKGSVAYVPQQAWIQNCTLQENVLFGQPMNPKRYQQALETCALLADLDVLPGGDQTEI 743
Cdd:PTZ00243 697 SGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEI 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 744 GEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIgpEGVLAGKTRVLVTHGISFLPQTDFIIVL 823
Cdd:PTZ00243 777 GEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECF--LGALAGKTRVLATHQVHVVPRADYVVAL 854
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 824 AGGQVSEMGHYSALLQhdGSFANFLRNyapdEDQEDHEAALQNANEEVLlledtlsthtdltdnepaiyevrkqfmrEMS 903
Cdd:PTZ00243 855 GDGRVEFSGSSADFMR--TSLYATLAA----ELKENKDSKEGDADAEVA----------------------------EVD 900
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 904 SLSSEGEVQNRTMPKKHTNSlEKEALVTKTKETGALIKEEIAETGNVKLSVYWDYAKSMG-LCTTLSICLLYGGQSAAAI 982
Cdd:PTZ00243 901 AAPGGAVDHEPPVAKQEGNA-EGGDGAALDAAAGRLMTREEKASGSVPWSTYVAYLRFCGgLHAAGFVLATFAVTELVTV 979
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 983 GANVWLSAWSNDAEEHGQQNKTSVRLGVYAALGILQGLLVMLSAFTMVVGAiqaaRLLHEALLHNKIRSPQSFFDTTPSG 1062
Cdd:PTZ00243 980 SSGVWLSMWSTRSFKLSAATYLYVYLGIVLLGTFSVPLRFFLSYEAMRRGS----RNMHRDLLRSVSRGTMSFFDTTPLG 1055
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1063 RILNRFSKDIYVIDEVLAPTILMLLNSFFTSISTIMVIVASTPLFMVVVLPLAVLYGFVQRFYVATSRQLKRLESISRSP 1142
Cdd:PTZ00243 1056 RILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSP 1135
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1143 IFSHFSETVTGTSVIRAYGRIQdfKVLSDT--KVDNNQKSSYPYIASNRWLGVHVEFVGNCVVLFAALFAVIGR----NS 1216
Cdd:PTZ00243 1136 VFTLLEEALQGSATITAYGKAH--LVMQEAlrRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIGVIGTmlraTS 1213
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1217 LNPGLVGLSVSYALQVTMALNWMIRMISDLESNIIAVERVKEYS--------------------KTKTEAP----WVVES 1272
Cdd:PTZ00243 1214 QEIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTdevphedmpeldeevdalerRTGMAADvtgtVVIEP 1293
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1273 NRAPEGWP---TRGMVEFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLN 1349
Cdd:PTZ00243 1294 ASPTSAAPhpvQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGRE 1373
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1350 VAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQL 1429
Cdd:PTZ00243 1374 IGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQL 1453
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1430 VCLARALLRK-SRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLI- 1507
Cdd:PTZ00243 1454 MCMARALLKKgSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVm 1533
|
1370
....*....|....
gi 1388591336 1508 AAGGIFYGMAKDAG 1521
Cdd:PTZ00243 1534 NRQSIFHSMVEALG 1547
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
208-1513 |
0e+00 |
|
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: 582.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 208 PEASAGFFSRLSFWWFTRLAILGYRRPLEDRDLWSLSEEDCSHKVVQRLLEAWQKQqnqasrsqTATAEpkipgedavll 287
Cdd:TIGR01271 5 PVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRE--------LASAK----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 288 kprpksKQPSFLRALVRTFTSSLLMSACFNLIQNLLGFVNPQLLS-ILIRFISDPTAPTWWGFLLAGLMFLSSTMQTLIL 366
Cdd:TIGR01271 66 ------KNPKLLNALRRCFFWRFVFYGILLYFGEATKAVQPLLLGrIIASYDPFNAPEREIAYYLALGLCLLFIVRTLLL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 367 HQYYHCIFVMALRLRTAIIGVIYRKALVITNSVKRESTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQI 446
Cdd:TIGR01271 140 HPAIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWEL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 447 LGPSALAGVAVIVLLIPLNGAVSMKMKTYQVKQMKFKDSRIKLMSEILNGIKVLKLYAWEPSFLEQVKGIRQSELQLLRK 526
Cdd:TIGR01271 220 LEVNGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 527 GAYLQAISTFIWICTPFLVTLITLGVYVYvdeSNVLDAEKAFVSLSLFNILKIPLN-MLPQLISGLTQASVSLKRIQDFL 605
Cdd:TIGR01271 300 IAYLRYFYSSAFFFSGFFVVFLSVVPYAL---IKGIILRRIFTTISYCIVLRMTVTrQFPGAIQTWYDSLGAITKIQDFL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 606 NQNELdpQCVERKTISPgyAITIHNGTFTWAQDL--------------------------------PPTLHSLNIQIPKG 653
Cdd:TIGR01271 377 CKEEY--KTLEYNLTTT--EVEMVNVTASWDEGIgelfekikqnnkarkqpngddglffsnfslyvTPVLKNISFKLEKG 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 654 ALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSVAYVPQQAWIQNCTLQENVLFGQPMNPKRYQQALETCALLADLD 733
Cdd:TIGR01271 453 QLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIA 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 734 VLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGPegVLAGKTRVLVTHGISF 813
Cdd:TIGR01271 533 LFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCK--LMSNKTRILVTSKLEH 610
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 814 LPQTDFIIVLAGGQVSEMGHYSAL--LQHDGS--------FANF------------LRNYAPDED--------------- 856
Cdd:TIGR01271 611 LKKADKILLLHEGVCYFYGTFSELqaKRPDFSslllgleaFDNFsaerrnsiltetLRRVSIDGDstvfsgpetikqsfk 690
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 857 QEDHEAALQNANEEVL------------------------------LLEDTLSTHTDLTDNEPAIYEV------------ 894
Cdd:TIGR01271 691 QPPPEFAEKRKQSIILnpiasarkfsfvqmgpqkaqattiedavrePSERKFSLVPEDEQGEESLPRGnqyhhglqhqaq 770
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 895 RKQFMREMSSLSSEGEVQNRtmpkKHTNSLEKEALVTKT---------------KETGALIKEEIAETG----------N 949
Cdd:TIGR01271 771 RRQSVLQLMTHSNRGENRRE----QLQTSFRKKSSITQQnelaseldiysrrlsKDSVYEISEEINEEDlkecfadereN 846
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 950 VKLSVYWD-YAKSM----GLCTTLSICLLYGGQSAAAIGANVWLsaWSNDAEEHGQQNK------------------TSV 1006
Cdd:TIGR01271 847 VFETTTWNtYLRYIttnrNLVFVLIFCLVIFLAEVAASLLGLWL--ITDNPSAPNYVDQqhanasspdvqkpviitpTSA 924
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1007 RLGVYAALGILQGLLVM--LSAFTMVVGAIQAARLLHEALLHNKIRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTIL 1084
Cdd:TIGR01271 925 YYIFYIYVGTADSVLALgfFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLF 1004
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1085 MLLNSFFTSISTIMVIVASTPLFMVVVLPLAVLYGFVQRFYVATSRQLKRLESISRSPIFSHFSETVTGTSVIRAYGRIQ 1164
Cdd:TIGR01271 1005 DFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQS 1084
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1165 DFKVLSDTKVDNNQKSSYPYIASNRWLGVHVEFVgncVVLF--AALFAVIGRNSLNPGLVGLSVSYALQVTMALNWMIRM 1242
Cdd:TIGR01271 1085 YFETLFHKALNLHTANWFLYLSTLRWFQMRIDII---FVFFfiAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNS 1161
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1243 ISDLESNIIAVERVKEYSKTKTEAP--------------WVVESNRAPEGWPTRGMVEFRNYSVRYRPGLELVLKNVTVH 1308
Cdd:TIGR01271 1162 SIDVDGLMRSVSRVFKFIDLPQEEPrpsggggkyqlstvLVIENPHAQKCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFS 1241
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1309 VQGGEKVGIVGRTGAGKSSMTLCLFRILeAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSE 1388
Cdd:TIGR01271 1242 VEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSD 1320
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1389 EDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQF 1468
Cdd:TIGR01271 1321 EEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSF 1400
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|....*
gi 1388591336 1469 EDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIF 1513
Cdd:TIGR01271 1401 SNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
313-601 |
3.97e-162 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350039 [Multi-domain] Cd Length: 290 Bit Score: 490.44 E-value: 3.97e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 313 SACFNLIQNLLGFVNPQLLSILIRFISDPTAPTWWGFLLAGLMFLSSTMQTLILHQYYHCIFVMALRLRTAIIGVIYRKA 392
Cdd:cd18595 2 AALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 393 LVITNSVKRESTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNGAVSMKM 472
Cdd:cd18595 82 LRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 473 KTYQVKQMKFKDSRIKLMSEILNGIKVLKLYAWEPSFLEQVKGIRQSELQLLRKGAYLQAISTFIWICTPFLVTLITLGV 552
Cdd:cd18595 162 KKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFAT 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1388591336 553 YVYVDESNVLDAEKAFVSLSLFNILKIPLNMLPQLISGLTQASVSLKRI 601
Cdd:cd18595 242 YVLSDPDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
967-1260 |
1.52e-160 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 486.60 E-value: 1.52e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 967 TLSICLLYGGQSAAAIGANVWLSAWSNDA--EEHGQQNKTSVRLGVYAALGILQGLLVMLSAFTMVVGAIQAARLLHEAL 1044
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPalNGTQDTEQRDYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1045 LHNKIRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLLNSFFTSISTIMVIVASTPLFMVVVLPLAVLYGFVQRF 1124
Cdd:cd18603 81 LHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1125 YVATSRQLKRLESISRSPIFSHFSETVTGTSVIRAYGRIQDFKVLSDTKVDNNQKSSYPYIASNRWLGVHVEFVGNCVVL 1204
Cdd:cd18603 161 YVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 1205 FAALFAVIGRNSLNPGLVGLSVSYALQVTMALNWMIRMISDLESNIIAVERVKEYS 1260
Cdd:cd18603 241 FAALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEYS 296
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1283-1503 |
7.91e-135 |
|
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: 414.97 E-value: 7.91e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1283 GMVEFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQL 1362
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1363 TIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRV 1442
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 1443 LVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSP 1503
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1008-1518 |
6.26e-118 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 382.98 E-value: 6.26e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1008 LGVYAALGILQGLLVMLSAFTMVVGAIQAARLLHEALLHNKIRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLL 1087
Cdd:COG1132 64 LLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1088 NSFFTSISTIMVIVASTPLFMVVVLPLAVLYGFVQRFYVATSRQLKRLESISRSPIFSHFSETVTGTSVIRAYGRIQDFK 1167
Cdd:COG1132 144 RSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREEREL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1168 VLSDTKVDNNQKSSYPYIASNRWLGVHVEFVGNCVVLFAALFAV--IGRNSLNPGLVGLSVSYALQVTMALNWMIRMISD 1245
Cdd:COG1132 224 ERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGllVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQ 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1246 LESNIIAVERVKEYSKTKTEapwVVESNRAPEGWPTRGMVEFRNYSVRYRPGlELVLKNVTVHVQGGEKVGIVGRTGAGK 1325
Cdd:COG1132 304 LQRALASAERIFELLDEPPE---IPDPPGAVPLPPVRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1326 SSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDpFGR--YSEEDIWRALELSHLNTF 1403
Cdd:COG1132 380 STLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIR-YGRpdATDEEVEEAAKAAQAHEF 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1404 VSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTI 1483
Cdd:COG1132 459 IEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTI 538
|
490 500 510
....*....|....*....|....*....|....*
gi 1388591336 1484 MDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGMAK 1518
Cdd:COG1132 539 RNADRILVLDDGRIVEQGTHEELLARGGLYARLYR 573
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
313-601 |
3.43e-117 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 369.89 E-value: 3.43e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 313 SACFNLIQNLLGFVNPQLLSILIRFISD-PTAPTWWGFLLAGLMFLSSTMQTLILHQYYHCIFVMALRLRTAIIGVIYRK 391
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSyPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 392 ALVITNSVKRESTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNGAVSMK 471
Cdd:cd18579 82 ALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 472 MKTYQVKQMKFKDSRIKLMSEILNGIKVLKLYAWEPSFLEQVKGIRQSELQLLRKGAYLQAISTFIWICTPFLVTLITLG 551
Cdd:cd18579 162 ISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1388591336 552 VYVYVDesNVLDAEKAFVSLSLFNILKIPLNMLPQLISGLTQASVSLKRI 601
Cdd:cd18579 242 TYVLLG--NPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
626-827 |
6.71e-113 |
|
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: 354.47 E-value: 6.71e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 626 ITIHNGTFTW---AQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSVAYVPQQAWIQNC 702
Cdd:cd03250 1 ISVEDASFTWdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 703 TLQENVLFGQPMNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDS 782
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1388591336 783 HVAKHIFDQVIGPEGvLAGKTRVLVTHGISFLPQTDFIIVLAGGQ 827
Cdd:cd03250 161 HVGRHIFENCILGLL-LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
968-1260 |
6.65e-107 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 341.79 E-value: 6.65e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 968 LSICLLYGGQSAAAIGANVWLSAWSNDAEEHGQQNkTSVRLGVYAALGIL-QGLLVMLSAFTMVVGAIQAARLLHEALLH 1046
Cdd:cd18580 2 LLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSS-SGYYLGVYAALLVLaSVLLVLLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1047 NKIRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLLNSFFTSISTIMVIVASTPLFMVVVLPLAVLYGFVQRFYV 1126
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1127 ATSRQLKRLESISRSPIFSHFSETVTGTSVIRAYGRIQDFKVLSDTKVDNNQKSSYPYIASNRWLGVHVEFVGNCVVLFA 1206
Cdd:cd18580 161 RTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALVV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1388591336 1207 ALFAVIGRNSLNPGLVGLSVSYALQVTMALNWMIRMISDLESNIIAVERVKEYS 1260
Cdd:cd18580 241 ALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1279-1503 |
8.48e-104 |
|
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: 329.37 E-value: 8.48e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1279 WPTRGMVEFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDL 1358
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1359 RSQLTIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELShlntfvssqpagldfqcaEGGDNLSVGQRQLVCLARALLR 1438
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALRVS------------------EGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388591336 1439 KSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSP 1503
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
979-1260 |
5.73e-98 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 316.72 E-value: 5.73e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 979 AAAIGANVWLSAWSNDaeEHGQQNKTSVrlGVYAALGILQGLLVMLSAFTMVVGAIQAARLLHEALLHNKIRSPQSFFDT 1058
Cdd:cd18606 13 FAQVFTNLWLSFWTED--FFGLSQGFYI--GIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1059 TPSGRILNRFSKDIYVIDEVLAPTILMLLNSFFTSISTIMVIVASTPLFMVVVLPLAVLYGFVQRFYVATSRQLKRLESI 1138
Cdd:cd18606 89 TPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRASSRELKRLESI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1139 SRSPIFSHFSETVTGTSVIRAYGRIQDFKVLSDTKVDNNQKSSYPYIASNRWLGVHVEFVGNCVVLFAALFAVIGRNSLN 1218
Cdd:cd18606 169 LRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLLVLIVALLCVTRRFSIS 248
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1388591336 1219 PGLVGLSVSYALQVTMALNWMIRMISDLESNIIAVERVKEYS 1260
Cdd:cd18606 249 PSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
968-1260 |
6.90e-94 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 305.55 E-value: 6.90e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 968 LSICLLYGGQSAAAIGANVWLSAWSNDAEEHGQQNKTSVR----LGVYAALGILQGLLVMLSAFTMVVGAIQAARLLHEA 1043
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEVSvlyyLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1044 LLHNKIRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLLNSFFTSISTIMVIVASTPLFMVVVLPLAVLYGFVQR 1123
Cdd:cd18604 82 LLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1124 FYVATSRQLKRLESISRSPIFSHFSETVTGTSVIRAYGRIQDFKVLSDTKVDNNQKSSYPYIASNRWLGVHVEFVGNCVV 1203
Cdd:cd18604 162 LYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFS 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1388591336 1204 LFAALFAVIGRnSLNPGLVGLSVSYALQVTMALNWMIRMISDLESNIIAVERVKEYS 1260
Cdd:cd18604 242 FATAALLVYGP-GIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
314-601 |
1.37e-89 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350040 [Multi-domain] Cd Length: 309 Bit Score: 293.63 E-value: 1.37e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 314 ACFNLIQNLLGFVNPQLLSILIRFISDPTA-PTWWGFLLAGLMFLSSTMQTLILHQYYHCIFVMALRLRTAIIGVIYRKA 392
Cdd:cd18596 3 ALLAVLSSVLSFAPPFFLNRLLRYLEDPGEdATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 393 LVI-------------------TNSVKRESTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSALA 453
Cdd:cd18596 83 LRRrdksgssksseskkkdkeeDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 454 GVAVIVLLIPLNGAVSMKMKTYQVKQMKFKDSRIKLMSEILNGIKVLKLYAWEPSFLEQVKGIRQSELQLLRKGAYLQAI 533
Cdd:cd18596 163 GLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591336 534 STFIWICTPFLVTLITLGVYVYVdESNVLDAEKAFVSLSLFNILKIPLNMLPQLISGLTQASVSLKRI 601
Cdd:cd18596 243 LSLLWFLIPILVTVVTFATYTLV-MGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1012-1518 |
1.91e-88 |
|
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: 304.45 E-value: 1.91e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1012 AALGILQGLLVMLSAFTMVVGAIQAARLLHEALLHNKIRSPQSFFDTTPSGRILNRFSkDIYVIDEVLA-PTILMLLNSF 1090
Cdd:COG2274 203 LLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTgSLLTALLDLL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1091 FTSISTIMVIVASTPLFMVVVL--PLAVLYGFV-QRFYVATSRQLKRLESISRSpifsHFSETVTGTSVIRAYG----RI 1163
Cdd:COG2274 282 FVLIFLIVLFFYSPPLALVVLLliPLYVLLGLLfQPRLRRLSREESEASAKRQS----LLVETLRGIETIKALGaesrFR 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1164 QDFKVLSDTKVDNNQKSSYPYIASNRWLGVhVEFVGNCVVLFAALFAVIGrNSLNPG-LVGlSVSYALQVTMALNWMIRM 1242
Cdd:COG2274 358 RRWENLLAKYLNARFKLRRLSNLLSTLSGL-LQQLATVALLWLGAYLVID-GQLTLGqLIA-FNILSGRFLAPVAQLIGL 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1243 ISDLESNIIAVERVKEYSKTKTEAPWVVESNRAPEgwpTRGMVEFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTG 1322
Cdd:COG2274 435 LQRFQDAKIALERLDDILDLPPEREEGRSKLSLPR---LKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSG 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1323 AGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNL---DPfgRYSEEDIWRALELSH 1399
Cdd:COG2274 512 SGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDP--DATDEEIIEAARLAG 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1400 LNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHR 1479
Cdd:COG2274 590 LHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHR 669
|
490 500 510
....*....|....*....|....*....|....*....
gi 1388591336 1480 LNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGMAK 1518
Cdd:COG2274 670 LSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
312-601 |
4.02e-88 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 288.73 E-value: 4.02e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 312 MSACFNLIQNLLGFVNPQLLSILIRFISDPTAPTWWGFLLAGLMFLSSTMQTLILHQYYHCIFVMALRLRTAIIGVIYRK 391
Cdd:cd18559 1 SFLLIKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 392 ALVITNSVKRESTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNGAVSMK 471
Cdd:cd18559 81 ALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 472 MKTYQVKQMKFKDSRIKLMSEILNGIKVLKLYAWEPSFLEQVKGIRQSELQLLRKGAYLQAISTFIWICTPFLVTLITLG 551
Cdd:cd18559 161 SRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1388591336 552 VYVYVDESNVLDAEKAFVSLSLFNILKIPLNMLPQLISGLTQASVSLKRI 601
Cdd:cd18559 241 AYVSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
971-1260 |
3.96e-84 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 277.95 E-value: 3.96e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 971 CLLYGGQSAAAIGANVWLSAWSNDAEEHGQQNKTSVR-----------LGVYAALGILQGLLVMLSAFTMVVGAIQAARL 1039
Cdd:cd18602 5 LALALLKQGLRVATDFWLADWTEANHDVASVVFNITSssleddevsyyISVYAGLSLGAVILSLVTNLAGELAGLRAARR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1040 LHEALLHNKIRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLLNSFFTSISTIMVIVASTPLFMVVVLPLAVLYG 1119
Cdd:cd18602 85 LHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIIIVYY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1120 FVQRFYVATSRQLKRLESISRSPIFSHFSETVTGTSVIRAYGRIQDFKVLSDTKVDNNQKSSYPYIASNRWLGVHVEFVG 1199
Cdd:cd18602 165 FLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRLDYLG 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388591336 1200 NCVVLFAALFAVIG--RNSLNPGLVGLSVSYALQVTMALNWMIRMISDLESNIIAVERVKEYS 1260
Cdd:cd18602 245 AVIVFLAALSSLTAalAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1283-1508 |
5.20e-81 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 267.16 E-value: 5.20e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1283 GMVEFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQL 1362
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1363 TIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRV 1442
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 1443 LVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIA 1508
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLA 243
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
979-1259 |
5.54e-79 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 263.24 E-value: 5.54e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 979 AAAIGANVWLSAW---SNDAEEHGQQNKTSVRLGVYAALGILQGLLVMLSAFTMVVGAIQAARLLHEALLHNKIRSPQSF 1055
Cdd:cd18605 13 ASRNLIDFWLSYWvshSNNSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFAKMSF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1056 FDTTPSGRILNRFSKDIYVIDEVLaPTILM-LLNSFFTSISTIMVIVASTPLFMVVVLPLAVLYGFVQRFYVATSRQLKR 1134
Cdd:cd18605 93 FDKTPVGRILNRFSSDVYTIDDSL-PFILNiLLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQRYYRATSRELKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1135 LESISRSPIFSHFSETVTGTSVIRAYGRIQDFKVLSDTKVDNNQKSSYPYIASNRWLGVHVEFVGNCVVLFAALFAVIGR 1214
Cdd:cd18605 172 LNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVLIVTFVALTAVVQH 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1388591336 1215 N---SLNPGLVGLSVSYALQVTMALNWMIRMISDLESNIIAVERVKEY 1259
Cdd:cd18605 252 FfglSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQY 299
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
318-601 |
9.19e-79 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350042 [Multi-domain] Cd Length: 288 Bit Score: 262.10 E-value: 9.19e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 318 LIQNLLGFVNPQLLSILIRFISDPTAPTWWGFLLAGLMFLSSTMQTLILHQYYHCIFVMALRLRTAIIGVIYRKALVITN 397
Cdd:cd18598 7 LLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYRKALRVRS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 398 SVKRESTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNGAVSMKMKTYQV 477
Cdd:cd18598 87 SSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRIGALSE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 478 KQMKFKDSRIKLMSEILNGIKVLKLYAWEPSFLEQVKGIRQSELQLLRKGAYLQAISTFIWICTPFLVTLITLGVYVYVd 557
Cdd:cd18598 167 KMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTPVLISILTFATYVLM- 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1388591336 558 eSNVLDAEKAFVSLSLFNILKIPLNMLPQLISGLTQASVSLKRI 601
Cdd:cd18598 246 -GNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
312-601 |
2.02e-76 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350041 [Multi-domain] Cd Length: 293 Bit Score: 255.46 E-value: 2.02e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 312 MSACFNLIQNLLGFVNPQLLSILIRFISD-----PTAPTWWGFLLAGLMFLSSTMQTLILHQYYHCIFVMALRLRTAIIG 386
Cdd:cd18597 1 LAGLLKLLADVLQVLSPLLLKYLINFVEDaylggPPPSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 387 VIYRKALVITNSVKRESTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNG 466
Cdd:cd18597 81 AIYRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 467 AVSMKMKTYQVKQMKFKDSRIKLMSEILNGIKVLKLYAWEPSFLEQVKGIRQSELQLLRKGAYLQAISTFIWICTPFLVT 546
Cdd:cd18597 161 FLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLAS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1388591336 547 LITLGVYVYVdeSNVLDAEKAFVSLSLFNILKIPLNMLPQLISGLTQASVSLKRI 601
Cdd:cd18597 241 MLSFITYYAT--GHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
313-601 |
5.43e-73 |
|
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 1 (TMD1) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and they belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350035 [Multi-domain] Cd Length: 309 Bit Score: 246.38 E-value: 5.43e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 313 SACFNLIQNLLGFVNPQLLSILIRFISDPTAPTWW------------------GFLLAGLMFLSSTMQTLILHQYYHCIF 374
Cdd:cd18591 2 GGILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNstdklsvsyvtveeffsnGYVLAVILFLALLLQATFSQASYHIVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 375 VMALRLRTAIIGVIYRKALVITNSVKRES--TVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSAL 452
Cdd:cd18591 82 REGIRLKTALQAMIYEKALRLSSWNLSSGsmTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 453 AGVAVIVLLIPLNGAVSMKMKTYQVKQMKFKDSRIKLMSEILNGIKVLKLYAWEPSFLEQVKGIRQSELQLLRKGAYLQA 532
Cdd:cd18591 162 IGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWS 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388591336 533 ISTFIWICTPFLVTLITLGVYVYVdESNVLDAEKAFVSLSLFNILKIPLNMLPQLISGLTQASVSLKRI 601
Cdd:cd18591 242 LMTFLTQASPILVTLVTFGLYPYL-EGEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
298-849 |
1.09e-72 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 254.70 E-value: 1.09e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 298 FLRALVRTFTSSLLMSACFNLIQNLLGFVNPQLLSILIRFI---SDPTAPTWWGFLLAGLMFLSSTMQTLilhqYYHCIF 374
Cdd:COG1132 11 RLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALlagGDLSALLLLLLLLLGLALLRALLSYL----QRYLLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 375 VMALRLRTAIIGVIYRKALVITNSVKRESTVGEMVNLMSVDAQRFMD-VSPFINLLWSAPLQVILAIYFLWQILGPSALA 453
Cdd:COG1132 87 RLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQfLAHGLPQLVRSVVTLIGALVVLFVIDWRLALI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 454 GVAVIVLLIPLNGAVSMKMKTYQVKQMKFKDSRIKLMSEILNGIKVLKLYAWEPSFLEQVKGIRQSELQLLRKGAYLQAI 533
Cdd:COG1132 167 VLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 534 STFI--WICTPFLVTLITLGVYVYVDESnvLDAEKAFVSLSLFNILKIPLNMLPQLISGLTQASVSLKRIQDFLNQNELD 611
Cdd:COG1132 247 FFPLmeLLGNLGLALVLLVGGLLVLSGS--LTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 612 PQCVERKTISP-GYAITIHNGTFTWAQDlPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-- 688
Cdd:COG1132 325 PDPPGAVPLPPvRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvd 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 689 -----------SVAYVPQQAWIQNCTLQENVLFGqpmNPKRYQQALETCALLADLDV----LPGGDQTEIGEKGINLSGG 753
Cdd:COG1132 404 irdltleslrrQIGVVPQDTFLFSGTIRENIRYG---RPDATDEEVEEAAKAAQAHEfieaLPDGYDTVVGERGVNLSGG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 754 QRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLAGGQVSEMGH 833
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTETEALIQEAL---ERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGT 557
|
570
....*....|....*.
gi 1388591336 834 YSALLQHDGSFANFLR 849
Cdd:COG1132 558 HEELLARGGLYARLYR 573
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
284-850 |
1.15e-70 |
|
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: 252.45 E-value: 1.15e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 284 AVLLKPRP----KSKQPSFLRALVRTFT---SSLLMSACFNLIQNLLGFVNPQLLSILI-RFISDPTAPTWW----GFLL 351
Cdd:COG2274 125 ALLLEPTPefdkRGEKPFGLRWFLRLLRryrRLLLQVLLASLLINLLALATPLFTQVVIdRVLPNQDLSTLWvlaiGLLL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 352 AGLM-FLSSTMQTLILhqyyhciFVMALRLRTAIIGVIYRKALVITNSVKRESTVGEMVN-LMSVDA-QRFMdVSPFINL 428
Cdd:COG2274 205 ALLFeGLLRLLRSYLL-------LRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASrFRDVESiREFL-TGSLLTA 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 429 LWSAPlQVILAIYFLWQILGPSALAGVAVIVLLIPLNGAVSMKMKTYQVKQMKFKDSRIKLMSEILNGIKVLKLYAWEPS 508
Cdd:COG2274 277 LLDLL-FVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESR 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 509 FLEQ----VKGIRQSELQLLRKGAYLQAISTFIwictPFLVTLITLGVYVYVdesnVLDAEkafvsLSL-----FNILKI 579
Cdd:COG2274 356 FRRRwenlLAKYLNARFKLRRLSNLLSTLSGLL----QQLATVALLWLGAYL----VIDGQ-----LTLgqliaFNILSG 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 580 ----PLNMLPQLISGLTQASVSLKRIQDFLNQ---NELDPQCVERKTISPgyAITIHNGTFTWAQDLPPTLHSLNIQIPK 652
Cdd:COG2274 423 rflaPVAQLIGLLQRFQDAKIALERLDDILDLppeREEGRSKLSLPRLKG--DIELENVSFRYPGDSPPVLDNISLTIKP 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 653 GALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-------------SVAYVPQQAWIQNCTLQENVLFGQP-MNPKR 718
Cdd:COG2274 501 GERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqidpaslrrQIGVVLQDVFLFSGTIRENITLGDPdATDEE 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 719 YQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVigpEGV 798
Cdd:COG2274 581 IIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENL---RRL 657
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1388591336 799 LAGKTRVLVTHGISFLPQTDFIIVLAGGQVSEMGHYSALLQHDGSFANFLRN 850
Cdd:COG2274 658 LKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
963-1260 |
7.56e-69 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 234.38 E-value: 7.56e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 963 GLCTTLSICLLYGGQSAAAIGANVWLSAW-----SNDAEEHGQQ--NKTSVR--------LGVYAALGILQGLLVMLSAF 1027
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWlkqgsGNTTNNVDNStvDSGNISdnpdlnfyQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1028 TMVVGAIQAARLLHEALLHNKIRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLLNSFFTSISTIMVIVASTPLF 1107
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1108 MVVVLPLAVLYGFVQRFYVATSRQLKRLESISRSPIFSHFSETVTGTSVIRAYGRIQDFKVLSDTKVDNNQKSSYPYIAS 1187
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388591336 1188 NRWLGVHVEFVGNCVVLFAALFAVIGRNSLNPGLVGLSVSYALQVTMALNWMIRMISDLESNIIAVERVKEYS 1260
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1265-1511 |
1.81e-68 |
|
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: 241.97 E-value: 1.81e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1265 EAPWVVESNRAPEGWPTRGMVEFRNYSVRYrPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIV 1344
Cdd:COG4988 317 APEPAAPAGTAPLPAAGPPSIELEDVSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1345 IDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDpFGR--YSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNL 1422
Cdd:COG4988 396 INGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLR-LGRpdASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGL 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1423 SVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDS 1502
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGT 554
|
....*....
gi 1388591336 1503 PVNLIAAGG 1511
Cdd:COG4988 555 HEELLAKNG 563
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
316-602 |
3.97e-68 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 231.75 E-value: 3.97e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 316 FNLIQNLLGFVNPQLLSILIR-FISDPTAPTWWGFLLAGLMFLSSTMQTLILHQYYHCIFVMALRLRTAIIGVIYRKALV 394
Cdd:cd18594 5 LLFLEESLKIVQPLLLGRLVAyFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTLK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 395 ITNSVKRESTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNGAVSMKMKT 474
Cdd:cd18594 85 LSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 475 YQVKQMKFKDSRIKLMSEILNGIKVLKLYAWEPSFLEQVKGIRQSELQLLRKGAYLQAISTFIWICTPFLVTLITLGVYV 554
Cdd:cd18594 165 YRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYV 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1388591336 555 YVDesNVLDAEKAFVSLSLFNILKIPLNM-LPQLISGLTQASVSLKRIQ 602
Cdd:cd18594 245 LTG--NTLTARKVFTVISLLNALRMTITRfFPESIQTLSESRVSLKRIQ 291
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1283-1511 |
4.01e-68 |
|
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: 229.03 E-value: 4.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1283 GMVEFRNYSVRYRPGlELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQL 1362
Cdd:cd03254 1 GEIEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1363 TIIPQDPILFSGTLRMNLDpFGR--YSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKS 1440
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIR-LGRpnATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 1441 RVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGG 1511
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
626-826 |
1.07e-67 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 227.60 E-value: 1.07e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 626 ITIHNGTFTWAQDLPpTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVV-----------------SVKG 688
Cdd:cd03290 1 VQVTNGYFSWGSGLA-TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 689 SVAYVPQQAWIQNCTLQENVLFGQPMNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDA 768
Cdd:cd03290 80 SVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388591336 769 NIFLLDDPLSAVDSHVAKHIFDqvigpEGVLA-----GKTRVLVTHGISFLPQTDFIIVLAGG 826
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQ-----EGILKflqddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1014-1513 |
1.26e-66 |
|
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: 236.92 E-value: 1.26e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1014 LGILQGLLVMLSAFTMVVGAIQAARLLHEALLHNKIRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLLNSFFTS 1093
Cdd:TIGR02203 63 LAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1094 IS-TIMVIVASTPLFMVVVLPLAVLYGFVQRFYvatsrqlKRLESISRSPIFSH------FSETVTGTSVIRAYG----R 1162
Cdd:TIGR02203 143 IGlFIVLLYYSWQLTLIVVVMLPVLSILMRRVS-------KRLRRISKEIQNSMgqvttvAEETLQGYRVVKLFGgqayE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1163 IQDFKVLSDTKVDNNQKSSYPYIASNRWLGVhVEFVGNCVVLFAALFAViGRNSLNPGLVGLSVSYALQVTMALNWMIRM 1242
Cdd:TIGR02203 216 TRRFDAVSNRNRRLAMKMTSAGSISSPITQL-IASLALAVVLFIALFQA-QAGSLTAGDFTAFITAMIALIRPLKSLTNV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1243 ISDLESNIIAVERVKEYSKTKTEAPwvvESNRAPEgwPTRGMVEFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTG 1322
Cdd:TIGR02203 294 NAPMQRGLAAAESLFTLLDSPPEKD---TGTRAIE--RARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSG 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1323 AGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLdPFGR---YSEEDIWRALELSH 1399
Cdd:TIGR02203 369 SGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNI-AYGRteqADRAEIERALAAAY 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1400 LNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHR 1479
Cdd:TIGR02203 448 AQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHR 527
|
490 500 510
....*....|....*....|....*....|....
gi 1388591336 1480 LNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIF 1513
Cdd:TIGR02203 528 LSTIEKADRIVVMDDGRIVERGTHNELLARNGLY 561
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
309-601 |
7.96e-66 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350037 [Multi-domain] Cd Length: 291 Bit Score: 224.79 E-value: 7.96e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 309 SLLMSACFNLIQnllgfvnPQLLSILIRFISDP--TAPTWWGFLLAGLMFLSSTMQTLILHQYYHCIFVMALRLRTAIIG 386
Cdd:cd18593 5 FLFLEEAIRVVQ-------PIFLGKLIRYFEGNgsSISLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 387 VIYRKALVITNSVKRESTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNG 466
Cdd:cd18593 78 LIYRKALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 467 AVSMKMKTYQVKQMKFKDSRIKLMSEILNGIKVLKLYAWEPSFLEQVKGIRQSELQLLRKGAYLQAISTFIWICTPFLVT 546
Cdd:cd18593 158 FFGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLIL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 547 LITLGVYVYVDesNVLDAEKAFVSLSLFNILKIPLNM-LPQLISGLTQASVSLKRI 601
Cdd:cd18593 238 FLTFLAYILLG--NILTAERVFVTMALYNAVRLTMTLfFPFAIQFGSELSVSIRRI 291
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1285-1516 |
3.47e-64 |
|
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: 217.87 E-value: 3.47e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTI 1364
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1365 IPQDPILFSGTLRMNLdPFGRY--SEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRV 1442
Cdd:cd03251 81 VSQDVFLFNDTVAENI-AYGRPgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388591336 1443 LVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGM 1516
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
963-1260 |
1.32e-63 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 219.50 E-value: 1.32e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 963 GLCTTLSICLLYGGQSAAAIGANVWLSAWSN-----DAEEHGQQNKTSVR-----------LGVYAALGILQGLLVMLSA 1026
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANleeklNDTTDRVQGENSTNvdiedldrdfnLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1027 FTMVVGAIQAARLLHEALLHNKIRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLLNSFFTSISTIMVIVASTPL 1106
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1107 FMVVVLPLAVLYGFVQRFYVATSRQLKRLESISRSPIFSHFSETVTGTSVIRAYGRIQDFKVLSDTKVDNNQKSSYPYIA 1186
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388591336 1187 SNRWLGVHVEFVGNCVVLFAALFAVIGRNSLNPGLVGLSVSYALQVTMALNWMIRMISDLESNIIAVERVKEYS 1260
Cdd:cd18601 241 TSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEYS 314
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1061-1518 |
1.90e-63 |
|
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: 227.34 E-value: 1.90e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1061 SGRILNRFSKDIYVIDE----VLAPTILMLLNSFFTSIST------IMVIVASTPLFMVVVLPLAVLygfvqRFYVATSR 1130
Cdd:COG4987 111 SGDLLNRLVADVDALDNlylrVLLPLLVALLVILAAVAFLaffspaLALVLALGLLLAGLLLPLLAA-----RLGRRAGR 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1131 QLKRLESISRSpifsHFSETVTGTSVIRAYGRIQDFKVLSDTKVDNNQKSSYpyiASNRWLGVHvEFVGNCVVLFAALFA 1210
Cdd:COG4987 186 RLAAARAALRA----RLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQR---RLARLSALA-QALLQLAAGLAVVAV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1211 VI------GRNSLNPGLVGLSVSYALQVTMALNWMIRMISDLESNIIAVERVKEYsktkTEAPWVVESNRAPEGWPTRGM 1284
Cdd:COG4987 258 LWlaaplvAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNEL----LDAPPAVTEPAEPAPAPGGPS 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTI 1364
Cdd:COG4987 334 LELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAV 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1365 IPQDPILFSGTLRMNL---DPfgRYSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSR 1441
Cdd:COG4987 414 VPQRPHLFDTTLRENLrlaRP--DATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAP 491
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388591336 1442 VLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGMAK 1518
Cdd:COG4987 492 ILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
973-1260 |
2.80e-62 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 214.77 E-value: 2.80e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 973 LYGGQSAAAIGANVWLSAWSNDaEEHGQQNKTSVRLGVYAALGILQGLLVMLSAFTMVVGAIQAARLLHEALLHNKIRSP 1052
Cdd:cd18559 7 LVLCNHVFSGPSNLWLLLWFDD-PVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1053 QSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLLNSFFTSISTIMVIVASTPLFmVVVLPLAVLYGFVQRFYVATSRQL 1132
Cdd:cd18559 86 ISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMA-AVGIPLGLLYVPVNRVYAASSRQL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1133 KRLESISRSPIFSHFSETVTGTSVIRAYGRIQDFKVLSDTKVDnNQKSSYPYIASNRWLGVHVEFVGNCVVLFAALFAVI 1212
Cdd:cd18559 165 KRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYV 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1388591336 1213 GRNSLNpGLVGLSVSYALQVTMALNWMIRMISDLESNIIAVERVKEYS 1260
Cdd:cd18559 244 SRHSLA-GLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1285-1495 |
4.35e-61 |
|
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: 206.47 E-value: 4.35e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTI 1364
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1365 IPQDPILFSGTLRMNLdpfgryseediwralelshlntfvssqpagldfqcaeggdnLSVGQRQLVCLARALLRKSRVLV 1444
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 1445 LDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKG 1495
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
312-601 |
1.79e-59 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350036 [Multi-domain] Cd Length: 287 Bit Score: 206.64 E-value: 1.79e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 312 MSACFNLIQNLLGFVNPQ-LLSILIRFISDPTAPTWWGFLLAGLMFLSSTMQTLILHQYYHCIFVMALRLRTAIIGVIYR 390
Cdd:cd18592 1 FSILLLLISLIFGFIGPTiLIRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 391 KALVItNSVKrESTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNGAVSM 470
Cdd:cd18592 81 KILRL-RSLG-DKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 471 KMKTYQVKQMKFKDSRIKLMSEILNGIKVLKLYAWEPSFLEQVKGIRQSELQLLRKGAYLQAISTFIWICTPFLVTLITL 550
Cdd:cd18592 159 LTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTF 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 551 GVYVYVDesNVLDAEKAFVSLSLFNILKIPLNMLPQLISGLTQASVSLKRI 601
Cdd:cd18592 239 LAHVALG--NDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1285-1516 |
3.45e-59 |
|
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: 203.62 E-value: 3.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYRPGLElVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTI 1364
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1365 IPQDPILFSGTLRMNLDpFGRY--SEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRV 1442
Cdd:cd03253 80 VPQDTVLFNDTIGYNIR-YGRPdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388591336 1443 LVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGM 1516
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1202-1516 |
9.37e-58 |
|
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: 211.60 E-value: 9.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1202 VVLFAALFAVIGRNSLnpGLVGLSVSYALQVTMALNWMIRMISDLESNIIAVERVKEYSKTKTEapwVVESNRAPEGWPT 1281
Cdd:COG5265 280 MMLMAAQGVVAGTMTV--GDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPE---VADAPDAPPLVVG 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1282 RGMVEFRNYSVRYRPGLElVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQ 1361
Cdd:COG5265 355 GGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAA 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1362 LTIIPQDPILFSGTLRMNLdpfgRY-----SEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARAL 1436
Cdd:COG5265 434 IGIVPQDTVLFNDTIAYNI----AYgrpdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTL 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1437 LRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGM 1516
Cdd:COG5265 510 LKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1285-1518 |
2.45e-56 |
|
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: 195.45 E-value: 2.45e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRY--RPGLElVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQL 1362
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1363 TIIPQDPILFSGTLRMNLDpFGRYS--EEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKS 1440
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIR-YGKPDatDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591336 1441 RVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGMAK 1518
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVK 236
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1283-1498 |
4.48e-56 |
|
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: 194.35 E-value: 4.48e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1283 GMVEFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQL 1362
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1363 TIIPQDPILFSGTLRMNLDPFGRY-SEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSR 1441
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591336 1442 VLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKG-VVA 1498
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGrIVA 218
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1283-1513 |
1.24e-55 |
|
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: 195.07 E-value: 1.24e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1283 GMVEFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAaEGEIVIDGLNVAHIGLHDLRSQL 1362
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1363 TIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRV 1442
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 1443 LVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIF 1513
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
422-849 |
2.88e-55 |
|
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: 203.07 E-value: 2.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 422 VSPFInllwSAPLQVILAIYFLWQILGPSAL---AGVAVIVLLIPLNGAVSMKMKTYQVKQMKfKDSRIKLMsEILNGIK 498
Cdd:COG4987 133 LLPLL----VALLVILAAVAFLAFFSPALALvlaLGLLLAGLLLPLLAARLGRRAGRRLAAAR-AALRARLT-DLLQGAA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 499 VLKLYAWEPSFLEQVKGIRQSELQLLRKGAYLQAISTFIWICTPFLVTLITLGVYVYVDESNVLDAEK----AFVSLSLF 574
Cdd:COG4987 207 ELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLlallVLAALALF 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 575 NILkiplNMLPQLISGLTQASVSLKRIQDFLNQNELDPQCVERKTISPGYAITIHNGTFTWAQDLPPTLHSLNIQIPKGA 654
Cdd:COG4987 287 EAL----APLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 655 LVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-------------SVAYVPQQAWIQNCTLQENVLFGQPM-NPKRYQ 720
Cdd:COG4987 363 RVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlrdldeddlrrRIAVVPQRPHLFDTTLRENLRLARPDaTDEELW 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 721 QALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIgpeGVLA 800
Cdd:COG4987 443 AALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLL---EALA 519
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1388591336 801 GKTRVLVTHGISFLPQTDFIIVLAGGQVSEMGHYSALLQHDGSFANFLR 849
Cdd:COG4987 520 GRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1012-1516 |
3.21e-52 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 194.94 E-value: 3.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1012 AALGILQGLLVMLSAftmvVGAIQAAR--LLHEALlhnkiRSPQSFFDTTPSGRILNRFSKDIYVIDEV---LAPTIL-- 1084
Cdd:PRK10790 79 AGLHYAQSLLFNRAA----VGVVQQLRtdVMDAAL-----RQPLSAFDTQPVGQLISRVTNDTEVIRDLyvtVVATVLrs 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1085 ------MLLNSFftSISTIMVIVASTpLFmVVVLPLAVLYgfvQRFYVATSRQLKR-LESISRSpifshFSETVTGTSVI 1157
Cdd:PRK10790 150 aaligaMLVAMF--SLDWRMALVAIM-IF-PAVLVVMVIY---QRYSTPIVRRVRAyLADINDG-----FNEVINGMSVI 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1158 RAYGRIQDF-KVLSDTkvdnnqkSSYPYIASNRWLGVHVEFVGNCVVLFAA-----LFAVIGRNSlnPGLVGLSVSYALq 1231
Cdd:PRK10790 218 QQFRQQARFgERMGEA-------SRSHYMARMQTLRLDGFLLRPLLSLFSAlilcgLLMLFGFSA--SGTIEVGVLYAF- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1232 vtmaLNWMIRM----------ISDLESNIIAVERVKEysktkteapwVVESNRAPEGWPTR----GMVEFRNYSVRYRPG 1297
Cdd:PRK10790 288 ----ISYLGRLneplielttqQSMLQQAVVAGERVFE----------LMDGPRQQYGNDDRplqsGRIDIDNVSFAYRDD 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1298 lELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLR 1377
Cdd:PRK10790 354 -NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFL 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1378 MNLDpFGR-YSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLET 1456
Cdd:PRK10790 433 ANVT-LGRdISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGT 511
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1457 DDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGM 1516
Cdd:PRK10790 512 EQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQM 571
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
299-842 |
6.74e-52 |
|
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: 193.05 E-value: 6.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 299 LRALVRTFTSSLLMSACFNLIQNLLG----FVNPQLLSILIRFISDPTAPTWWGFLLAGLMFLsstmQTLILHQYYHCIF 374
Cdd:COG4988 8 LKRLARGARRWLALAVLLGLLSGLLIiaqaWLLASLLAGLIIGGAPLSALLPLLGLLLAVLLL----RALLAWLRERAAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 375 VMALRLRTAIIGVIYRKALVI-TNSVKRESTvGEMVNLMS--VDAqrfMD--VSPFINLLWSA---PLQVILAIYFLwqi 446
Cdd:COG4988 84 RAAARVKRRLRRRLLEKLLALgPAWLRGKST-GELATLLTegVEA---LDgyFARYLPQLFLAalvPLLILVAVFPL--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 447 lgpSALAGV--AVIVLLIPLNGA-VSMKMKTYQVKQMKfkdsRIKLMS----EILNGIKVLKLYAWEPSFLEQVKGI--- 516
Cdd:COG4988 157 ---DWLSGLilLVTAPLIPLFMIlVGKGAAKASRRQWR----ALARLSghflDRLRGLTTLKLFGRAKAEAERIAEAsed 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 517 -RQSELQLLRkgayLQAISTFIwicTPFLVTL-ITLG-VYV---YVDESnvLDAEKAFVSLSL----FnilkIPLNMLpq 586
Cdd:COG4988 230 fRKRTMKVLR----VAFLSSAV---LEFFASLsIALVaVYIgfrLLGGS--LTLFAALFVLLLapefF----LPLRDL-- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 587 lisGL-----TQASVSLKRIQDFLNQNELDPQCVERKTISPGY-AITIHNGTFTWAQDlPPTLHSLNIQIPKGALVAVVG 660
Cdd:COG4988 295 ---GSfyharANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPpSIELEDVSFSYPGG-RPALDGLSLTIPPGERVALVG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 661 PVGCGKSSLVSALLGEMEKLEGVVSVKG-------------SVAYVPQQAWIQNCTLQENVLFGQP-MNPKRYQQALETC 726
Cdd:COG4988 371 PSGAGKSTLLNLLLGFLPPYSGSILINGvdlsdldpaswrrQIAWVPQNPYLFAGTIRENLRLGRPdASDEELEAALEAA 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 727 ALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVigpEGVLAGKTRVL 806
Cdd:COG4988 451 GLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQAL---RRLAKGRTVIL 527
|
570 580 590
....*....|....*....|....*....|....*.
gi 1388591336 807 VTHGISFLPQTDFIIVLAGGQVSEMGHYSALLQHDG 842
Cdd:COG4988 528 ITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1285-1514 |
1.58e-51 |
|
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: 181.92 E-value: 1.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTI 1364
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1365 IPQDPILFSGTLRMNL---DPfgRYSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSR 1441
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388591336 1442 VLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFY 1514
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1027-1516 |
3.44e-51 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 194.17 E-value: 3.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1027 FTMVVGAIQAArlLHEALLHNKIRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLLNSFFTSI-STIMVIVASTP 1105
Cdd:TIGR00958 225 FNYTMARINLR--IREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLgLLGFMLWLSPR 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1106 LFMV--VVLPLAVL----YGfvqRFYVATSRQLKrlESISRSPIFSHfsETVTGTSVIRAYG----RIQDFKV-LSDTKv 1174
Cdd:TIGR00958 303 LTMVtlINLPLVFLaekvFG---KRYQLLSEELQ--EAVAKANQVAE--EALSGMRTVRSFAaeegEASRFKEaLEETL- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1175 DNNQKSSYPYIA---SNRWLGVHVeFVGncvVLFAALFAVIgRNSLNPGLVGLSVSYALQVTMALNWMIRMISDLESNII 1251
Cdd:TIGR00958 375 QLNKRKALAYAGylwTTSVLGMLI-QVL---VLYYGGQLVL-TGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVG 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1252 AVERVKEYSKTKTEAPWVVEsnRAPEgwPTRGMVEFRNYSVRY--RPGLeLVLKNVTVHVQGGEKVGIVGRTGAGKSSMT 1329
Cdd:TIGR00958 450 ASEKVFEYLDRKPNIPLTGT--LAPL--NLEGLIEFQDVSFSYpnRPDV-PVLKGLTFTLHPGEVVALVGPSGSGKSTVA 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1330 LCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLdPFG--RYSEEDIWRALELSHLNTFVSSQ 1407
Cdd:TIGR00958 525 ALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENI-AYGltDTPDEEIMAAAKAANAHDFIMEF 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1408 PAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTirTQFEDCTVLTIAHRLNTIMDYN 1487
Cdd:TIGR00958 604 PNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERAD 681
|
490 500
....*....|....*....|....*....
gi 1388591336 1488 RVLVLDKGVVAEFDSPVNLIAAGGIFYGM 1516
Cdd:TIGR00958 682 QILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1008-1523 |
6.39e-50 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 187.86 E-value: 6.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1008 LGVYAALGIlqgllvmlsaFTMVVG---AIQAARLLHE---ALLHNK----IRSPQSFFDTTPSGRILNrfskdiyvide 1077
Cdd:PRK13657 59 LAAWAGFGL----------FNIIAGvlvARHADRLAHRrrlAVLTEYferiIQLPLAWHSQRGSGRALH----------- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1078 vlapTIL--------MLLNSFFTSISTIMVIVASTP--LFM-----VVVLPLAVLYGFVQRFYVATSRQLKRLESISRSP 1142
Cdd:PRK13657 118 ----TLLrgtdalfgLWLEFMREHLATLVALVVLLPlaLFMnwrlsLVLVVLGIVYTLITTLVMRKTKDGQAAVEEHYHD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1143 IFSHFSETVTGTSVIRAYGRIQDFKVLSDTKVDNNQKSSYPYIasNRWLGVHVefvGN-------CVVLFAALFAVIGRN 1215
Cdd:PRK13657 194 LFAHVSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQMPVL--SWWALASV---LNraastitMLAILVLGAALVQKG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1216 SLNPGLVGLSVSYAlqvTMALNWMIRMISDLESNIIAVERVKEYSKTKTEAPWVVESNRAPEGWPTRGMVEFRNYSVRY- 1294
Cdd:PRK13657 269 QLRVGEVVAFVGFA---TLLIGRLDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYd 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1295 --RPGLElvlkNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILF 1372
Cdd:PRK13657 346 nsRQGVE----DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLF 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1373 SGTLRMNLDpFGR--YSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATA 1450
Cdd:PRK13657 422 NRSIEDNIR-VGRpdATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATS 500
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388591336 1451 AIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGMAKDAGLA 1523
Cdd:PRK13657 501 ALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQGML 573
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1012-1518 |
1.99e-49 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 188.24 E-value: 1.99e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1012 AALGILQGLLVMLSAfTMVVGAIQAA---RLLheallhnkiRSPQSFFDTTPSGRILNRFSKdIYVIDEVLAPTIL-MLL 1087
Cdd:TIGR03797 190 AAFQLAQSLAVLRLE-TRMDASLQAAvwdRLL---------RLPVSFFRQYSTGDLASRAMG-ISQIRRILSGSTLtTLL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1088 NSFFTSISTIMVIVASTPLFMVVVLPLAVLY------GFVQRFYVatsRQLKRLESisrsPIFSHFSETVTGTSVIRAYG 1161
Cdd:TIGR03797 259 SGIFALLNLGLMFYYSWKLALVAVALALVAIavtlvlGLLQVRKE---RRLLELSG----KISGLTVQLINGISKLRVAG 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1162 RiqdfkvlsdtkvdnnQKSSYPYIASN----RWLGVHVEFVGNCVVLF---------AALFAVIGRNSLNPGL-VGLSVS 1227
Cdd:TIGR03797 332 A---------------ENRAFARWAKLfsrqRKLELSAQRIENLLTVFnavlpvltsAALFAAAISLLGGAGLsLGSFLA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1228 YALQVTMALNWMIRM---ISDLESNIIAVERVKEYSKTKTEapwvVESNRAPEGwPTRGMVEFRNYSVRYRPGLELVLKN 1304
Cdd:TIGR03797 397 FNTAFGSFSGAVTQLsntLISILAVIPLWERAKPILEALPE----VDEAKTDPG-KLSGAIEVDRVTFRYRPDGPLILDD 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1305 VTVHVQGGEKVGIVGRTGAGKSSmtlcLFRIL---EAAE-GEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNL 1380
Cdd:TIGR03797 472 VSLQIEPGEFVAIVGPSGSGKST----LLRLLlgfETPEsGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENI 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1381 DPFGRYSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLI 1460
Cdd:TIGR03797 548 AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIV 627
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591336 1461 QGTIRTQfeDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGMAK 1518
Cdd:TIGR03797 628 SESLERL--KVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLAR 683
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1052-1513 |
1.78e-47 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 180.21 E-value: 1.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1052 PQSFFDTTPSGRILNRFSKD------------IYVIDE---VLAPTILMLLNSFftSISTIMVIVAstPLfmvvvlpLAV 1116
Cdd:PRK11176 112 PVSFFDKQSTGTLLSRITYDseqvassssgalITVVREgasIIGLFIMMFYYSW--QLSLILIVIA--PI-------VSI 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1117 LYGFVQrfyvatsrqlKRLESISRSPIFSHFSETVT------GTSVIRAYGRiQDFKVLSDTKVDNN--QKSSYPYIASN 1188
Cdd:PRK11176 181 AIRVVS----------KRFRNISKNMQNTMGQVTTSaeqmlkGHKEVLIFGG-QEVETKRFDKVSNRmrQQGMKMVSASS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1189 RWLGVhVEFVGN---CVVLFAALFAVIgRNSLNPG--------LVGL--------SVSYALQVTMALNWMIRMISDLE-- 1247
Cdd:PRK11176 250 ISDPI-IQLIASlalAFVLYAASFPSV-MDTLTAGtitvvfssMIALmrplksltNVNAQFQRGMAACQTLFAILDLEqe 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1248 --SNIIAVERVKeysktkteapwvvesnrapegwptrGMVEFRNYSVRYrPGLE-LVLKNVTVHVQGGEKVGIVGRTGAG 1324
Cdd:PRK11176 328 kdEGKRVIERAK-------------------------GDIEFRNVTFTY-PGKEvPALRNINFKIPAGKTVALVGRSGSG 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1325 KSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLD--PFGRYSEEDIWRALELSHLNT 1402
Cdd:PRK11176 382 KSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAyaRTEQYSREQIEEAARMAYAMD 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1403 FVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNT 1482
Cdd:PRK11176 462 FINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLST 541
|
490 500 510
....*....|....*....|....*....|.
gi 1388591336 1483 IMDYNRVLVLDKGVVAEFDSPVNLIAAGGIF 1513
Cdd:PRK11176 542 IEKADEILVVEDGEIVERGTHAELLAQNGVY 572
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
641-851 |
7.10e-47 |
|
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: 170.04 E-value: 7.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSVAYVPQQAWIQNCTLQENVLFGQPMNPKRYQ 720
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 721 QALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGPegVLA 800
Cdd:cd03291 131 SVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCK--LMA 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 801 GKTRVLVTHGISFLPQTDFIIVLAGGQVSEMGHYSALLQHDGSFANFLRNY 851
Cdd:cd03291 209 NKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGY 259
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1264-1492 |
7.48e-46 |
|
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: 174.40 E-value: 7.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1264 TEAPWVVESNRAPEGWPTRGMVEFRNYSVRYrPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEI 1343
Cdd:TIGR02857 301 LDAAPRPLAGKAPVTAAPASSLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSI 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1344 VIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDpFGR--YSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDN 1421
Cdd:TIGR02857 380 AVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIR-LARpdASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAG 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 1422 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVL 1492
Cdd:TIGR02857 459 LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1016-1514 |
6.92e-45 |
|
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: 174.93 E-value: 6.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1016 ILQGLLVMLSAFTMVVGAIQAARLLHEALLHNKIRSPQSFFDTTPSGRILNRFSkDIYVIDEVLAPTILML-LNSFFTSI 1094
Cdd:TIGR01193 207 IIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFT-DASSIIDALASTILSLfLDMWILVI 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1095 STIMVIVASTPLFMV--VVLPL--AVLYGFVQRFYVATSRQLKRLESISRSPIfshfsETVTGTSVIRAYGRIQDFKVLS 1170
Cdd:TIGR01193 286 VGLFLVRQNMLLFLLslLSIPVyaVIIILFKRTFNKLNHDAMQANAVLNSSII-----EDLNGIETIKSLTSEAERYSKI 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1171 DTKVDNNQKSSYPYIASN---RWLGVHVEFVGNCVVLFAALFAVIgRNSLNpglVGLSVSYALQVTMALNWM---IRMIS 1244
Cdd:TIGR01193 361 DSEFGDYLNKSFKYQKADqgqQAIKAVTKLILNVVILWTGAYLVM-RGKLT---LGQLITFNALLSYFLTPLeniINLQP 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1245 DLESNIIAVERVKEYSKTKTEapwVVESNRAPEGWPTRGMVEFRNYSVRYRPGLElVLKNVTVHVQGGEKVGIVGRTGAG 1324
Cdd:TIGR01193 437 KLQAARVANNRLNEVYLVDSE---FINKKKRTELNNLNGDIVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSG 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1325 KSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGR--YSEEDIWRALELSHLNT 1402
Cdd:TIGR01193 513 KSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKenVSQDEIWAACEIAEIKD 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1403 FVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIrTQFEDCTVLTIAHRLNT 1482
Cdd:TIGR01193 593 DIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNL-LNLQDKTIIFVAHRLSV 671
|
490 500 510
....*....|....*....|....*....|..
gi 1388591336 1483 IMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFY 1514
Cdd:TIGR01193 672 AKQSDKIIVLDHGKIIEQGSHDELLDRNGFYA 703
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1282-1497 |
1.97e-42 |
|
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: 155.32 E-value: 1.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1282 RGMVEFRNYSVRY--RPGlELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLR 1359
Cdd:cd03248 9 KGIVKFQNVTFAYptRPD-TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1360 SQLTIIPQDPILFSGTLRMNLD-PFGRYSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLR 1438
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1388591336 1439 KSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVV 1497
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
968-1236 |
2.51e-42 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 156.65 E-value: 2.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 968 LSICLLYGGQSAAAIGAnVWLSAWSNDAEEHGQQN--KTSVRLGVYAALGILQGLLVMLSAFTMVVGAIQAARLLHEALL 1045
Cdd:pfam00664 3 LAILLAILSGAISPAFP-LVLGRILDVLLPDGDPEtqALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1046 HNKIRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLLNSFFTSISTIMVIVASTPLFMVVVLPLAVLYGFVQRFY 1125
Cdd:pfam00664 82 KKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1126 VATSRQLKRLESISRSPIFSHFSETVTGTSVIRAYGRIQDFKVLSDTKVDNNQKSSYPYIASNRWLGVHVEFVGNCVVLF 1205
Cdd:pfam00664 162 AKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYAL 241
|
250 260 270
....*....|....*....|....*....|...
gi 1388591336 1206 AALFAV--IGRNSLNPGLVGLSVSYALQVTMAL 1236
Cdd:pfam00664 242 ALWFGAylVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
626-846 |
3.53e-40 |
|
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: 148.92 E-value: 3.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 626 ITIHNGTFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-------------SVAY 692
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslrrQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 693 VPQQAWIQNCTLQENVLFGQP-MNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIF 771
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPgATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388591336 772 LLDDPLSAVDSHVAKHIFDQVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLAGGQVSEMGHYSALLQHDGSFAN 846
Cdd:cd03251 161 ILDEATSALDTESERLVQAAL---ERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAK 232
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
492-823 |
8.81e-40 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 156.29 E-value: 8.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 492 EILNGIKVLKLYAWEPSFLEQVKGI----RQSELQLLRKgAYLqaiSTFIwicTPFLVTLITLGVYVYVDESNV---LDA 564
Cdd:TIGR02857 188 DRLRGLPTLKLFGRAKAQAAAIRRSseeyRERTMRVLRI-AFL---SSAV---LELFATLSVALVAVYIGFRLLagdLDL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 565 EKAFVSLSLFNILKIPLNMLPQLISGLTQASVSLKRIQDFLNQNELDPQCVERKTISPGYAITIHNGTFTWAqDLPPTLH 644
Cdd:TIGR02857 261 ATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYP-GRRPALR 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 645 SLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-------------SVAYVPQQAWIQNCTLQENVLFG 711
Cdd:TIGR02857 340 PVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVPQHPFLFAGTIAENIRLA 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 712 QP-MNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFD 790
Cdd:TIGR02857 420 RPdASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLE 499
|
330 340 350
....*....|....*....|....*....|...
gi 1388591336 791 QVigpEGVLAGKTRVLVTHGISFLPQTDFIIVL 823
Cdd:TIGR02857 500 AL---RALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1061-1480 |
9.07e-40 |
|
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: 156.37 E-value: 9.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1061 SGRILNRFSKDIYVIDEVLAPTILMLLNSFFTSISTIMVIVASTPLFMVVVLPLAVLYGFV-QRFYVATSRQLKRLESIS 1139
Cdd:TIGR02868 109 RGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAGLLLAGFVaPLVSLRAARAAEQALARL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1140 RSPIFSHFSETVTGTSVIRAYGRIQDFKvlsdTKVDNNQKSSYPYIASNRWL-----GVHVEFVGNCVV--LFAALFAVI 1212
Cdd:TIGR02868 189 RGELAAQLTDALDGAAELVASGALPAAL----AQVEEADRELTRAERRAAAAtalgaALTLLAAGLAVLgaLWAGGPAVA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1213 GrNSLNPGLVGLSVSYALQVTMALNWMIRMISDLESNIIAVERVKEYSKTKTEAPwVVESNRAPEGWPTRGMVEFRNYSV 1292
Cdd:TIGR02868 265 D-GRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVA-EGSAPAAGAVGLGKPTLELRDLSA 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1293 RYrPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILF 1372
Cdd:TIGR02868 343 GY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLF 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1373 SGTLRMNLDpFGR--YSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATA 1450
Cdd:TIGR02868 422 DTTVRENLR-LARpdATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTE 500
|
410 420 430
....*....|....*....|....*....|
gi 1388591336 1451 AIDLETDDLIQGTIRTQFEDCTVLTIAHRL 1480
Cdd:TIGR02868 501 HLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1302-1516 |
8.62e-39 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 154.23 E-value: 8.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1302 LKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILeAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNL- 1380
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVl 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1381 --DPfgRYSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDD 1458
Cdd:PRK11174 445 lgNP--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQ 522
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591336 1459 LIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGM 1516
Cdd:PRK11174 523 LVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
641-845 |
5.37e-38 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 142.75 E-value: 5.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-------------SVAYVPQQAWIQNCTLQEN 707
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGVVPQDTVLFNDTIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 708 VLFGqpmNPKRYQQALETCALLADLD----VLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSH 783
Cdd:cd03253 95 IRYG---RPDATDEEVIEAAKAAQIHdkimRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTH 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388591336 784 VAKHIFDQVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLAGGQVSEMGHYSALLQHDGSFA 845
Cdd:cd03253 172 TEREIQAAL---RDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYA 230
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
601-850 |
5.55e-38 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 151.92 E-value: 5.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 601 IQDFLNQNELDPQcVERKTISPGYAITIHngtftwAQDLP-------PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSAL 673
Cdd:PRK11174 324 LVTFLETPLAHPQ-QGEKELASNDPVTIE------AEDLEilspdgkTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNAL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 674 LGEMeKLEGVVSVKG------SVAYVPQQ-AWI-QN-----CTLQENVLFGQP-MNPKRYQQALETCALLADLDVLPGGD 739
Cdd:PRK11174 397 LGFL-PYQGSLKINGielrelDPESWRKHlSWVgQNpqlphGTLRDNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGL 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 740 QTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVigpEGVLAGKTRVLVTHGISFLPQTDF 819
Cdd:PRK11174 476 DTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQAL---NAASRRQTTLMVTHQLEDLAQWDQ 552
|
250 260 270
....*....|....*....|....*....|.
gi 1388591336 820 IIVLAGGQVSEMGHYSALLQHDGSFANFLRN 850
Cdd:PRK11174 553 IWVMQDGQIVQQGDYAELSQAGGLFATLLAH 583
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
299-849 |
6.52e-38 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 153.19 E-value: 6.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 299 LRALVRTFTSSLLMSacfnLIQNLLGFVNPQLLSILI-RFISDPTAPTWWGflLAGLMFLSSTMQTLIlhQYYHCIFVma 377
Cdd:TIGR03797 131 LRGARRDLLAILAMG----LLGTLLGMLVPIATGILIgTAIPDADRSLLVQ--IALALLAAAVGAAAF--QLAQSLAV-- 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 378 LRLRTAIIGV----IYRKALVITNSVKRESTVGEMVN-LMSVDA-QRFMDVSPFINLLwsaplQVILAIYFLWQIL---G 448
Cdd:TIGR03797 201 LRLETRMDASlqaaVWDRLLRLPVSFFRQYSTGDLASrAMGISQiRRILSGSTLTTLL-----SGIFALLNLGLMFyysW 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 449 PSALAGVAVIVLLIPLNGAVSMKMKTYQVKQMKFKDSRIKLMSEILNGIKVLK--------LYAWEPSFLEQVK---GIR 517
Cdd:TIGR03797 276 KLALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRvagaenraFARWAKLFSRQRKlelSAQ 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 518 QSELQLLRKGAYLQAIST--FIWICTPFL-VTLITLGVYVyvdesnvldaekAFVSLslFNILKIPLNMLPQLISGLTQA 594
Cdd:TIGR03797 356 RIENLLTVFNAVLPVLTSaaLFAAAISLLgGAGLSLGSFL------------AFNTA--FGSFSGAVTQLSNTLISILAV 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 595 SVSLKRIQDFLnqnELDPQCVERKTiSPGY---AITIHNGTFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVS 671
Cdd:TIGR03797 422 IPLWERAKPIL---EALPEVDEAKT-DPGKlsgAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLR 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 672 ALLGeMEKLEgvvsvKGSVAY-------------------VPQQAWIQNCTLQENVLFGQPMNPKRYQQALETCALLADL 732
Cdd:TIGR03797 498 LLLG-FETPE-----SGSVFYdgqdlagldvqavrrqlgvVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDI 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 733 DVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVakhifdQVIGPEGVLAGK-TRVLVTHGI 811
Cdd:TIGR03797 572 RAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRT------QAIVSESLERLKvTRIVIAHRL 645
|
570 580 590
....*....|....*....|....*....|....*...
gi 1388591336 812 SFLPQTDFIIVLAGGQVSEMGHYSALLQHDGSFANFLR 849
Cdd:TIGR03797 646 STIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLAR 683
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
626-827 |
1.79e-37 |
|
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: 139.06 E-value: 1.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 626 ITIHNGTFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-------------SVAY 692
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 693 VPQQAWIQNCTLQENVLfgqpmnpkryqqaletcalladldvlpggdqteigekginlSGGQRQRVSLARAVYSDANIFL 772
Cdd:cd03228 81 VPQDPFLFSGTIRENIL-----------------------------------------SGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1388591336 773 LDDPLSAVDSHVAKHIFDQVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLAGGQ 827
Cdd:cd03228 120 LDEATSALDPETEALILEAL---RALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
375-845 |
1.75e-36 |
|
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: 147.17 E-value: 1.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 375 VMALRLRtaiigvIYRKALVITNSVKRESTVGEMVNLMSVDA-QRFMDVSPFINLLWSAPLQVILAIYFL----WQIlgp 449
Cdd:TIGR02203 86 VRDIRVR------MFEKLLGLPVSFFDRQPTGTLLSRITFDSeQVASAATDAFIVLVRETLTVIGLFIVLlyysWQL--- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 450 salaGVAVIVLLIPLNGAVSMKMKTYQVKQMKFKDSRIKLM---SEILNGIKVLKLYAWEPSFLEQVKGIRQSELQLLRK 526
Cdd:TIGR02203 157 ----TLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTtvaEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 527 GAYLQAISTfiwictPF--LVTLITLGVYVYVDESNVLDAEK------AFVS--LSLFNILKIPLNMLPQLISGLTQAsv 596
Cdd:TIGR02203 233 MTSAGSISS------PItqLIASLALAVVLFIALFQAQAGSLtagdftAFITamIALIRPLKSLTNVNAPMQRGLAAA-- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 597 slKRIQDFLNQneldPQCVERKTISPGYA---ITIHNGTFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSAL 673
Cdd:TIGR02203 305 --ESLFTLLDS----PPEKDTGTRAIERArgdVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLI 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 674 LGEMEKLEGVV-------------SVKGSVAYVPQQAWIQNCTLQENVLFGQP--MNPKRYQQALETCALLADLDVLPGG 738
Cdd:TIGR02203 379 PRFYEPDSGQIlldghdladytlaSLRRQVALVSQDVVLFNDTIANNIAYGRTeqADRAEIERALAAAYAQDFVDKLPLG 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 739 DQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVigpEGVLAGKTRVLVTHGISFLPQTD 818
Cdd:TIGR02203 459 LDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAAL---ERLMQGRTTLVIAHRLSTIEKAD 535
|
490 500
....*....|....*....|....*..
gi 1388591336 819 FIIVLAGGQVSEMGHYSALLQHDGSFA 845
Cdd:TIGR02203 536 RIVVMDDGRIVERGTHNELLARNGLYA 562
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
641-842 |
3.77e-36 |
|
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: 137.36 E-value: 3.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVV-------------SVKGSVAYVPQQAWIQNCTLQEN 707
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgidirdisrkSLRSMIGVVLQDTFLFSGTIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 708 VLFGQPMNP-KRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAK 786
Cdd:cd03254 97 IRLGRPNATdEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 787 HIFDQVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLAGGQVSEMGHYSALLQHDG 842
Cdd:cd03254 177 LIQEAL---EKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1285-1508 |
3.85e-36 |
|
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: 137.08 E-value: 3.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYRPGlELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTI 1364
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1365 IPQDPI--LFSGTLR-------MNLdpfgRYSEEDIWR----ALELSHLNTFVSSQPAgldfqcaeggdNLSVGQRQLVC 1431
Cdd:COG1122 80 VFQNPDdqLFAPTVEedvafgpENL----GLPREEIRErveeALELVGLEHLADRPPH-----------ELSGGQKQRVA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388591336 1432 LARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT-QFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSPVNLIA 1508
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAELaDRVIVLDDGRIVADGTPREVFS 223
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
625-828 |
1.62e-35 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 135.02 E-value: 1.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 625 AITIHNGTFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-------------SVA 691
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 692 YVPQQAWIQNCTLQENVLFGQPM-NPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANI 770
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591336 771 FLLDDPLSAVDSHVAKHIFDQVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLAGGQV 828
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERL---RQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
364-809 |
2.55e-35 |
|
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: 142.88 E-value: 2.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 364 LILHqyyHCIFVMALRLRTAIIGVIYRKALvitNSVKRESTvGEMVNLMSVDAQRFMD-----VSPFINLLWSAPLQVIL 438
Cdd:TIGR02868 75 LVGH---DAALRSLGALRVRVYERLARQAL---AGRRRLRR-GDLLGRLGADVDALQDlyvrvIVPAGVALVVGAAAVAA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 439 AIYFLWQiLGPSALAGVAVIVLLIPLNGAVSMKMKTYQVKQmkfkdSRIKLMSEI---LNGIKVLKLYAWEPSFLEQVKG 515
Cdd:TIGR02868 148 IAVLSVP-AALILAAGLLLAGFVAPLVSLRAARAAEQALAR-----LRGELAAQLtdaLDGAAELVASGALPAALAQVEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 516 IRQSELQLLRKGAYLQAIST--FIWICTPFLVTLITLGVYVYVDES--NVLDAEKAFVSLSLFNilkiPLNMLPQLISGL 591
Cdd:TIGR02868 222 ADRELTRAERRAAAATALGAalTLLAAGLAVLGALWAGGPAVADGRlaPVTLAVLVLLPLAAFE----AFAALPAAAQQL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 592 TQASVSLKRIQDFLNQNEL--DPQCVERKTISPGYA-ITIHNGTFTWAQDlPPTLHSLNIQIPKGALVAVVGPVGCGKSS 668
Cdd:TIGR02868 298 TRVRAAAERIVEVLDAAGPvaEGSAPAAGAVGLGKPtLELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKST 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 669 LVSALLGEMEKLEGVVSVKGS-------------VAYVPQQAWIQNCTLQENVLFGQP-MNPKRYQQALETCALLADLDV 734
Cdd:TIGR02868 377 LLATLAGLLDPLQGEVTLDGVpvssldqdevrrrVSVCAQDAHLFDTTVRENLRLARPdATDEELWAALERVGLADWLRA 456
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388591336 735 LPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIgpeGVLAGKTRVLVTH 809
Cdd:TIGR02868 457 LPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLL---AALSGRTVVLITH 528
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
641-850 |
4.11e-35 |
|
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: 134.59 E-value: 4.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGS-------------VAYVPQQAWIQNCTLQEN 707
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIGLVSQEPVLFDGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 708 VLFGQPmnpKRYQQALETCALLADLD----VLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSH 783
Cdd:cd03249 97 IRYGKP---DATDEEVEEAAKKANIHdfimSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 784 VAKHI---FDQVIGpegvlaGKTRVLVTHGISFLPQTDFIIVLAGGQVSEMGHYSALLQHDGSFANFLRN 850
Cdd:cd03249 174 SEKLVqeaLDRAMK------GRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
968-1256 |
6.95e-35 |
|
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350044 [Multi-domain] Cd Length: 324 Bit Score: 136.86 E-value: 6.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 968 LSICLLYGGQSAAAIGANVWLSAWSNDAEEHGQQNKTSVRLGV-----------YAALGILQGLLVM--LSAFTMVVGAI 1034
Cdd:cd18600 20 LILCLVIFAIEVAASLVGLWLLRSQADRVNTTRPESSSNTYAVivtftssyyvfYIYVGVADSLLAMgfFRGLPLVHTLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1035 QAARLLHEALLHNKIRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLLNSFFTSISTIMVIVASTPLFMVVVLPL 1114
Cdd:cd18600 100 TVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVVSILQPYIFLATVPV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1115 AVLYGFVQRFYVATSRQLKRLESISRSPIFSHFSETVTGTSVIRAYGRIQDFKVLSDTKVDNNQKSSYPYIASNRWLGVH 1194
Cdd:cd18600 180 IIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMR 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388591336 1195 VEFVgncVVLF--AALFAVIGRNSLNPGLVGLSVSYALQVTMALNWMIRMISDLESNIIAVERV 1256
Cdd:cd18600 260 IEMI---FVIFftAVTFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRI 320
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1286-1497 |
8.15e-35 |
|
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: 131.57 E-value: 8.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1286 EFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTII 1365
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1366 PQDPILFSGTLRMNLdpfgryseediwralelshlntfvssqpagldfqcaeggdnLSVGQRQLVCLARALLRKSRVLVL 1445
Cdd:cd03246 82 PQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1388591336 1446 DEATAAIDLETDDLIQGTI-RTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVV 1497
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIaALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
280-849 |
1.97e-33 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 139.31 E-value: 1.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 280 PGEDAvllkpRPKSKQPSFLRALVRTFTSS-----LLMSACFNLIqnLLGFVNPQLLSILIRFISDPTAPTWWGFLLAGl 354
Cdd:TIGR03796 128 PGPEF-----QKGGRKPSLLRALWRRLRGSrgallYLLLAGLLLV--LPGLVIPAFSQIFVDEILVQGRQDWLRPLLLG- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 355 MFLSSTMQTLIlhQYYHCIFVMALRLRTAI---IGVIYRK-ALVITNSVKREStvGEMVNLMSVDAQrfmdVSPFIN-LL 429
Cdd:TIGR03796 200 MGLTALLQGVL--TWLQLYYLRRLEIKLAVgmsARFLWHIlRLPVRFFAQRHA--GDIASRVQLNDQ----VAEFLSgQL 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 430 WSAPLQVILAI-YFLWQILGPSALAGVAVIVLLIPLnGAVSMKMKTYQVKQMKFKDSRIKLMSEILNGIKV---LKLYAW 505
Cdd:TIGR03796 272 ATTALDAVMLVfYALLMLLYDPVLTLIGIAFAAINV-LALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSietLKASGL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 506 EPSFLEQVKGIR----QSELQLLRKGAYLQAISTFIWICTPFLVTLI----------TLGVYVyvdesnvldaekAFVSL 571
Cdd:TIGR03796 351 ESDFFSRWAGYQakllNAQQELGVLTQILGVLPTLLTSLNSALILVVgglrvmegqlTIGMLV------------AFQSL 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 572 sLFNILKiPLNMLPQLISGLTQASVSLKRIQDFLNqNELDPQCVERKTISP---------GYaITIHNGTFTWAQDLPPT 642
Cdd:TIGR03796 419 -MSSFLE-PVNNLVGFGGTLQELEGDLNRLDDVLR-NPVDPLLEEPEGSAAtsepprrlsGY-VELRNITFGYSPLEPPL 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-------------SVAYVPQQAWIQNCTLQENV- 708
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGipreeiprevlanSVAMVDQDIFLFEGTVRDNLt 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 709 LFGQPMNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHI 788
Cdd:TIGR03796 575 LWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKII 654
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 789 fDQVIGPEGVlagkTRVLVTHGISFLPQTDFIIVLAGGQVSEMGHYSALLQHDGSFANFLR 849
Cdd:TIGR03796 655 -DDNLRRRGC----TCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARLIR 710
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1250-1514 |
5.43e-33 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 136.49 E-value: 5.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1250 IIAVERVKEYsktkTEAPWVVESNRAPEGWPTRGMVEFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMT 1329
Cdd:PRK11160 308 IASARRINEI----TEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1330 LCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNL---DPfgRYSEEDIWRALE---LSHLntf 1403
Cdd:PRK11160 384 QLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQqvgLEKL--- 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1404 vSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTI 1483
Cdd:PRK11160 459 -LEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGL 537
|
250 260 270
....*....|....*....|....*....|.
gi 1388591336 1484 MDYNRVLVLDKGVVAEFDSPVNLIAAGGIFY 1514
Cdd:PRK11160 538 EQFDRICVMDNGQIIEQGTHQELLAQQGRYY 568
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
489-845 |
6.05e-33 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 137.57 E-value: 6.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 489 LMSEILNGIKVLKLYAWEPSFL----EQVKGIRQSELQLLRKGAYL-QAIStfiwictpfLVTLITLGVYVYVDESNVLD 563
Cdd:TIGR01846 319 FLVESVTGIETIKATATEPQFQnrwdRQLAAYVAASFRVTNLGNIAgQAIE---------LIQKLTFAILLWFGAHLVIG 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 564 AEKAFVSLSLFNILK----IPLNMLPQLISGLTQASVSLKRIQDFLNQ-NELDPQCVERKTISPGyAITIHNGTFTWAQD 638
Cdd:TIGR01846 390 GALSPGQLVAFNMLAgrvtQPVLRLAQLWQDFQQTGIALERLGDILNSpTEPRSAGLAALPELRG-AITFENIRFRYAPD 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 639 LPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSVAYVPQQAWIQ---NCTLQENVLFGQPM- 714
Cdd:TIGR01846 469 SPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRrqmGVVLQENVLFSRSIr 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 715 ------NPKRYQQALETCALLAD----LDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHV 784
Cdd:TIGR01846 549 dnialcNPGAPFEHVIHAAKLAGahdfISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYES 628
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 785 AKHIFDQVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLAGGQVSEMGHYSALLQHDGSFA 845
Cdd:TIGR01846 629 EALIMRNM---REICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYA 686
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
626-833 |
7.72e-33 |
|
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: 127.61 E-value: 7.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 626 ITIHNGTFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-------------SVAY 692
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 693 VPQQAWIQNCTLQENV-LFGQpMNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIF 771
Cdd:cd03244 83 IPQDPVLFSGTIRSNLdPFGE-YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388591336 772 LLDDPLSAVDSHVAKHIFdQVIGPEgvLAGKTRVLVTHGISFLPQTDFIIVLAGGQVSEMGH 833
Cdd:cd03244 162 VLDEATASVDPETDALIQ-KTIREA--FKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
735-1493 |
2.37e-32 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 137.85 E-value: 2.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 735 LPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDS---HVAKHIFDQVIGPEGvlagKTRVLVTHGI 811
Cdd:PTZ00265 565 LPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNkseYLVQKTINNLKGNEN----RITIIIAHRL 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 812 SFLPQTDFIIVLAGGQVSEMGHYSALLQH--DGSFANFLRNYAPDEDQEDHEAALQNANEEVLLLEDtlSTHTDLTDNEP 889
Cdd:PTZ00265 641 STIRYANTIFVLSNRERGSTVDVDIIGEDptKDNKENNNKNNKDDNNNNNNNNNNKINNAGSYIIEQ--GTHDALMKNKN 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 890 AIY---------------------------EVRKQFMR-----EMSSLSSEGevqNRTMPKKHTNSLEKEALVTKTKETG 937
Cdd:PTZ00265 719 GIYytminnqkvsskkssnndndkdsdmksSAYKDSERgydpdEMNGNSKHE---NESASNKKSCKMSDENASENNAGGK 795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 938 A-----LIKEEIAETGNVKLsVY---WDYAKSMGLcTTLSICLLYGGQSAAAIGANVWLSAWSNDAEEHGQQNKTSVRLG 1009
Cdd:PTZ00265 796 LpflrnLFKRKPKAPNNLRI-VYreiFSYKKDVTI-IALSILVAGGLYPVFALLYAKYVSTLFDFANLEANSNKYSLYIL 873
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1010 VYA-ALGILQGLLvmlSAFTMVVGAiQAARLLHEALLHNKIRSPQSFFDT---TPsGRILNRFSKDIYVIDEVLAPTILM 1085
Cdd:PTZ00265 874 VIAiAMFISETLK---NYYNNVIGE-KVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHINRDVHLLKTGLVNNIVI 948
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1086 llnsfFTSIstIMVIVASTPL-FMVVVLPLAVLYG--------FVQRFYVATSRQLKRLESISRSPIFSHFS-------- 1148
Cdd:PTZ00265 949 -----FTHF--IVLFLVSMVMsFYFCPIVAAVLTGtyfifmrvFAIRARLTANKDVEKKEINQPGTVFAYNSddeifkdp 1021
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1149 -----ETVTGTSVIRAYGRIQDFKVLSDTKVDNNQKSSYPYIASNRWLGVHVE----FVGNCVVLFAALFAVIGRNSLNP 1219
Cdd:PTZ00265 1022 sfliqEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQsaqlFINSFAYWFGSFLIRRGTILVDD 1101
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1220 GLVGL-----SVSYALQVtMALNwmirmiSDLESNIIAVERVkeYSKTKTEAPWVVESN---RAPEGWPTRGMVEFRNYS 1291
Cdd:PTZ00265 1102 FMKSLftflfTGSYAGKL-MSLK------GDSENAKLSFEKY--YPLIIRKSNIDVRDNggiRIKNKNDIKGKIEIMDVN 1172
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1292 VRY--RPGLElVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFR---------ILEAAE-------------------- 1340
Cdd:PTZ00265 1173 FRYisRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydlkndhhIVFKNEhtndmtneqdyqgdeeqnvg 1251
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1341 -------------------------GEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDpFGR--YSEEDIWR 1393
Cdd:PTZ00265 1252 mknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FGKedATREDVKR 1330
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1394 ALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIR--TQFEDC 1471
Cdd:PTZ00265 1331 ACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdiKDKADK 1410
|
890 900
....*....|....*....|..
gi 1388591336 1472 TVLTIAHRLNTIMDYNRVLVLD 1493
Cdd:PTZ00265 1411 TIITIAHRIASIKRSDKIVVFN 1432
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
310-577 |
6.52e-32 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 126.60 E-value: 6.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 310 LLMSACFNLIQNLLGFVNPQLLSILIRFISDPTAPTWW--GFLLAGLMFLSSTMQTLILHQYYhCIFVMALRLRTAIIGV 387
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQalNVYSLALLLLGLAQFILSFLQSY-LLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 388 IYRKALVITNSVKRESTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPS-ALAGVAVIVLLIPLNG 466
Cdd:pfam00664 80 LFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKlTLVLLAVLPLYILVSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 467 AVSMKMKTYQVKQMKFKDSRIKLMSEILNGIKVLKLYAWEPSFLEQVKGIRQSELQLLRKGAYLQAIS-TFIWICTPFLV 545
Cdd:pfam00664 160 VFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSfGITQFIGYLSY 239
|
250 260 270
....*....|....*....|....*....|..
gi 1388591336 546 TLITLGVYVYVDeSNVLDAEKAFVSLSLFNIL 577
Cdd:pfam00664 240 ALALWFGAYLVI-SGELSVGDLVAFLSLFAQL 270
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
625-861 |
1.40e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 124.43 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 625 AITIHNGTFTWAQDlpPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG--------SVAYVPQQ 696
Cdd:COG1121 6 AIELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 697 A---WIQNCTLQENVLFG--------QPMNPKRYQQALEtcaLLADLDVLPGGDQTeIGEkginLSGGQRQRVSLARAVY 765
Cdd:COG1121 84 AevdWDFPITVRDVVLMGrygrrglfRRPSRADREAVDE---ALERVGLEDLADRP-IGE----LSGGQQQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 766 SDANIFLLDDPLSAVDSHVAKHIFDqvigpegVLA-----GKTRVLVTHGISFLPQ-TDFIIVLAGGQVSEmGHYSALLQ 839
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYE-------LLRelrreGKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPPEEVLT 227
|
250 260
....*....|....*....|..
gi 1388591336 840 HDgsfaNFLRNYAPDEDQEDHE 861
Cdd:COG1121 228 PE----NLSRAYGGPVALLAHG 245
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1234-1516 |
3.80e-31 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 130.60 E-value: 3.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1234 MALNWMIrmisdlesNIiaVER-VKEYSKTKT---EAPWVVESNRA-PEGwptRGMVEFRNYSVRYRPGLELVLKNVTVH 1308
Cdd:PRK10789 271 LALAWMF--------NI--VERgSAAYSRIRAmlaEAPVVKDGSEPvPEG---RGELDVNIRQFTYPQTDHPALENVNFT 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1309 VQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLdPFGR--Y 1386
Cdd:PRK10789 338 LKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNI-ALGRpdA 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1387 SEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT 1466
Cdd:PRK10789 417 TQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQ 496
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1467 QFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGM 1516
Cdd:PRK10789 497 WGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDM 546
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1284-1503 |
4.70e-31 |
|
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: 123.23 E-value: 4.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYRPGLelVLKNVTVHVQGGEKVGIVGRTGAGKSsmTL--CLFRILEAAEGEIVIDGLNVAHIGLHDLRSQ 1361
Cdd:COG1120 1 MLEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKS--TLlrALAGLLKPSSGEVLLDGRDLASLSRRELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1362 LTIIPQDPIL-FSGTLR----M----NLDPFGRYSEED---IWRALELSHLNTFvssqpAGLDFqcaeggDNLSVGQRQL 1429
Cdd:COG1120 77 IAYVPQEPPApFGLTVRelvaLgrypHLGLFGRPSAEDreaVEEALERTGLEHL-----ADRPV------DELSGGERQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388591336 1430 VCLARALLRKSRVLVLDEATAAIDL----ETDDLIQGTIRTQfeDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSP 1503
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARER--GRTVVMVLHDLNLAARYaDRLVLLKDGRIVAQGPP 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1285-1495 |
8.76e-31 |
|
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: 120.11 E-value: 8.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGlHDLRSQLTI 1364
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1365 IPQDPILFSGTLRMNLdpfgryseediwralelshlntfvssqpagldfqcaegGDNLSVGQRQLVCLARALLRKSRVLV 1444
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 1445 LDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKG 1495
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENG 172
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1284-1511 |
2.68e-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: 2.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSmtlcLFR----ILEAAEGEIVIDGLNVAHiglhdLR 1359
Cdd:COG1121 6 AIELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKST----LLKailgLLPPTSGTVRLFGKPPRR-----AR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1360 SQLTIIPQD-------PILFSGTLRMNLDP----FGRYSEED---IWRALE---LSHLntfvSSQPAGldfqcaeggdNL 1422
Cdd:COG1121 75 RRIGYVPQRaevdwdfPITVRDVVLMGRYGrrglFRRPSRADreaVDEALErvgLEDL----ADRPIG----------EL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1423 SVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT-QFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVA-- 1498
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREYfDRVLLLNRGLVAhg 220
|
250
....*....|....*.
gi 1388591336 1499 ---EFDSPVNLIAAGG 1511
Cdd:COG1121 221 ppeEVLTPENLSRAYG 236
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1286-1495 |
3.20e-30 |
|
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: 119.49 E-value: 3.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1286 EFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTII 1365
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1366 PQDP------------ILFSgtLRmNLdpfgRYSEEDIWR----ALELSHLNTFVSSQPagldfqcaeggDNLSVGQRQL 1429
Cdd:cd03225 81 FQNPddqffgptveeeVAFG--LE-NL----GLPEEEIEErveeALELVGLEGLRDRSP-----------FTLSGGQKQR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591336 1430 VCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT-QFEDCTVLTIAHRLNTIMDY-NRVLVLDKG 1495
Cdd:cd03225 143 VAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLELaDRVIVLEDG 210
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
486-849 |
4.14e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 127.63 E-value: 4.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 486 RIKLMsEILNGIKVLKLYAWEPSFLEQvkgIRQSELQLL---RKGAYLQAISTFIWI-CTPFLVTLITlgvyvYVDESNV 561
Cdd:PRK11160 200 RVQLT-EWLQGQAELTLFGAEDRYRQQ---LEQTEQQWLaaqRRQANLTGLSQALMIlANGLTVVLML-----WLAAGGV 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 562 LDAEK--AFVSLSLFNILKIPLNMLPqlISG----LTQASVSLKRIQDFLNQnELDPQCVERKTISPG-YAITIHNGTFT 634
Cdd:PRK11160 271 GGNAQpgALIALFVFAALAAFEALMP--VAGafqhLGQVIASARRINEITEQ-KPEVTFPTTSTAAADqVSLTLNNVSFT 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 635 WAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-------------SVAYVPQQAWIQN 701
Cdd:PRK11160 348 YPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqpiadyseaalrqAISVVSQRVHLFS 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 702 CTLQENVLFGQP-MNPKRYQQALETCALLADLDVLPGGDqTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAV 780
Cdd:PRK11160 428 ATLRDNLLLAAPnASDEALIEVLQQVGLEKLLEDDKGLN-AWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388591336 781 DSHVAKHIFDQVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLAGGQVSEMGHYSALLQHDGSFANFLR 849
Cdd:PRK11160 507 DAETERQILELL---AEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1286-1495 |
4.58e-30 |
|
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: 117.35 E-value: 4.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1286 EFRNYSVRYRPGLelVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTII 1365
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1366 PQdpilfsgtlrmnldpfgryseediwralelshlntfvssqpagldfqcaeggdnLSVGQRQLVCLARALLRKSRVLVL 1445
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1388591336 1446 DEATAAIDLETDDLIQGTIRTQFED-CTVLTIAHRLNTIMDY-NRVLVLDKG 1495
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
626-846 |
4.71e-30 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 119.90 E-value: 4.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 626 ITIHNGTFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSVAYVPQQAWIQ---NC 702
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRrqvGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 703 TLQENVLFGQPM-------NPKRYQQALETCALLAD----LDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIF 771
Cdd:cd03252 81 VLQENVLFNRSIrdnialaDPGMSMERVIEAAKLAGahdfISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388591336 772 LLDDPLSAVDSHvAKHIFDQVIgpEGVLAGKTRVLVTHGISFLPQTDFIIVLAGGQVSEMGHYSALLQHDGSFAN 846
Cdd:cd03252 161 IFDEATSALDYE-SEHAIMRNM--HDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAY 232
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1302-1450 |
5.67e-30 |
|
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: 116.59 E-value: 5.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1302 LKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGT-----L 1376
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLtvrenL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388591336 1377 RMNLDPFGRYSEEDIWRALE-LSHLNtfvssQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATA 1450
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEaLEKLG-----LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
632-869 |
2.34e-29 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 125.21 E-value: 2.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 632 TFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVV-------------SVKGSVAYVPQQAW 698
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhdipltklqldSWRSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 699 IQNCTLQENVLFGqpmNPKRYQQALETCALLA----DLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLD 774
Cdd:PRK10789 400 LFSDTVANNIALG---RPDATQQEIEHVARLAsvhdDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILD 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 775 DPLSAVDSHVAKHIFdQVIGPEGvlAGKTRVLVTHGISFLPQTDFIIVLAGGQVSEMGHYSALLQHDGSFANFLRnyapd 854
Cdd:PRK10789 477 DALSAVDGRTEHQIL-HNLRQWG--EGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYR----- 548
|
250
....*....|....*
gi 1388591336 855 edQEDHEAALQNANE 869
Cdd:PRK10789 549 --YQQLEAALDDAPE 561
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1284-1509 |
1.00e-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: 122.70 E-value: 1.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAA---EGEIVIDGLNVAHIGLHDLRS 1360
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1361 QLTIIPQDP------------ILFsgTLRmNLDPFGRYSEEDIWRALELSHLNTFVSSQPAgldfqcaeggdNLSVGQRQ 1428
Cdd:COG1123 84 RIGMVFQDPmtqlnpvtvgdqIAE--ALE-NLGLSRAEARARVLELLEAVGLERRLDRYPH-----------QLSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1429 LVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIR--TQFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSPVN 1505
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEE 229
|
....
gi 1388591336 1506 LIAA 1509
Cdd:COG1123 230 ILAA 233
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1286-1498 |
2.45e-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: 114.17 E-value: 2.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1286 EFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAhiglhDLRSQLTII 1365
Cdd:cd03235 1 EVEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE-----KERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1366 PQD-------PILFSGTLRMNLDP----FGRYSEED---IWRALELSHLNTFVSSQPagldfqcaeggDNLSVGQRQLVC 1431
Cdd:cd03235 74 PQRrsidrdfPISVRDVVLMGLYGhkglFRRLSKADkakVDEALERVGLSELADRQI-----------GELSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388591336 1432 LARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT-QFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVA 1498
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYfDRVLLLNRTVVA 211
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
586-840 |
5.34e-28 |
|
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: 120.92 E-value: 5.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 586 QLISGLTQ---ASVSLKRIQDFLNQNELDPQCVERKtiSPGYAITIHNGTFTWAQDLPPTLHSLNIQIPKGALVAVVGPV 662
Cdd:TIGR01842 276 GAIGGWKQfsgARQAYKRLNELLANYPSRDPAMPLP--EPEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 663 GCGKSSLVSALLGEMEKLEGVVSVKG-------------SVAYVPQQAWIQNCTLQENVL-FGQPMNPKRYQQAletcAL 728
Cdd:TIGR01842 354 GSGKSTLARLIVGIWPPTSGSVRLDGadlkqwdretfgkHIGYLPQDVELFPGTVAENIArFGENADPEKIIEA----AK 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 729 LADLD----VLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIgpEGVLAGKTR 804
Cdd:TIGR01842 430 LAGVHelilRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIK--ALKARGITV 507
|
250 260 270
....*....|....*....|....*....|....*.
gi 1388591336 805 VLVTHGISFLPQTDFIIVLAGGQVSEMGHYSALLQH 840
Cdd:TIGR01842 508 VVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1284-1499 |
5.97e-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: 114.13 E-value: 5.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYRPGLEL--VLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQ 1361
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1362 LTIIPQDPIlfsGTL--RMNLD-----PF----GRYSEEDIWRALELSHLN-TFVSSQPAgldfQcaeggdnLSVGQRQL 1429
Cdd:COG1124 81 VQMVFQDPY---ASLhpRHTVDrilaePLrihgLPDREERIAELLEQVGLPpSFLDRYPH----Q-------LSGGQRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 1430 VCLARALLRKSRVLVLDEATAAIDL----ETDDLIQgTIRTQfEDCTVLTIAHRLNTImDY--NRVLVLDKGVVAE 1499
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVsvqaEILNLLK-DLREE-RGLTYLFVSHDLAVV-AHlcDRVAVMQNGRIVE 219
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
626-828 |
6.24e-28 |
|
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: 111.54 E-value: 6.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 626 ITIHNGTFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGS-------------VAY 692
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 693 VPQQAWIQNCTLQENVLfgqpmnpkryqqaletcalladldvlpggdqteigekginlSGGQRQRVSLARAVYSDANIFL 772
Cdd:cd03246 81 LPQDDELFSGSIAENIL-----------------------------------------SGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 773 LDDPLSAVDSHVAKHIFDQVIGPEgvLAGKTRVLVTHGISFLPQTDFIIVLAGGQV 828
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALK--AAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1284-1500 |
8.71e-28 |
|
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: 112.98 E-value: 8.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYRPGLELV--LKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDL--- 1358
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1359 RSQLTIIPQDPILfsgtlrmNLDPfgRYS-EEDIWRALeLSHLNTFVSSQPAGLDFQCAEGGDN-----------LSVGQ 1426
Cdd:cd03257 81 RKEIQMVFQDPMS-------SLNP--RMTiGEQIAEPL-RIHGKLSKKEARKEAVLLLLVGVGLpeevlnrypheLSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388591336 1427 RQLVCLARALLRKSRVLVLDEATAAIDLETD----DLIQgTIRTQFeDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEF 1500
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQaqilDLLK-KLQEEL-GLTLLFITHDLGVVAKIaDRVAVMYAGKIVEE 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1284-1509 |
9.73e-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: 9.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRY---RPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIG---LHD 1357
Cdd:COG1123 260 LLEVRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1358 LRSQLTIIPQDPilfSGTL--RMN--------LDPFGRYSEEDIWR----ALELSHLNtfvssqPAGLD---FQcaeggd 1420
Cdd:COG1123 340 LRRRVQMVFQDP---YSSLnpRMTvgdiiaepLRLHGLLSRAERRErvaeLLERVGLP------PDLADrypHE------ 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1421 nLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLetddLIQGTIRTQFED------CTVLTIAHRLNTIMDY-NRVLVLD 1493
Cdd:COG1123 405 -LSGGQRQRVAIARALALEPKLLILDEPTSALDV----SVQAQILNLLRDlqrelgLTYLFISHDLAVVRYIaDRVAVMY 479
|
250
....*....|....*.
gi 1388591336 1494 KGVVAEFDSPVNLIAA 1509
Cdd:COG1123 480 DGRIVEDGPTEEVFAN 495
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1282-1500 |
1.42e-27 |
|
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: 119.47 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1282 RGMVEFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQ 1361
Cdd:COG4618 328 KGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1362 LTIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSR 1441
Cdd:COG4618 408 IGYLPQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPR 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1442 VLVLDEATAAIDLETDDLIQGTIRTQFED-CTVLTIAHRLNTIMDYNRVLVLDKGVVAEF 1500
Cdd:COG4618 488 LVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAF 547
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1286-1503 |
7.03e-27 |
|
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: 110.74 E-value: 7.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1286 EFRNYSVRYrPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVA---HIGLHDLRSQL 1362
Cdd:cd03256 2 EVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklkGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1363 TIIPQDPIL----------FSGTL-RMNLDP--FGRYSEEDIWRALELshLNTFvssqpaGLDFQCAEGGDNLSVGQRQL 1429
Cdd:cd03256 81 GMIFQQFNLierlsvlenvLSGRLgRRSTWRslFGLFPKEEKQRALAA--LERV------GLLDKAYQRADQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388591336 1430 VCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIR--TQFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAeFDSP 1503
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLKriNREEGITVIVSLHQVDLAREYaDRIVGLKDGRIV-FDGP 228
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1282-1500 |
7.96e-27 |
|
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: 117.06 E-value: 7.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1282 RGMVEFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQ 1361
Cdd:TIGR01842 314 EGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKH 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1362 LTIIPQDPILFSGTLRMNLDPFGRYSE-EDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKS 1440
Cdd:TIGR01842 394 IGYLPQDVELFPGTVAENIARFGENADpEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDP 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 1441 RVLVLDEATAAIDLETDD-LIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEF 1500
Cdd:TIGR01842 474 KLVVLDEPNSNLDEEGEQaLANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARF 534
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
641-826 |
9.36e-27 |
|
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: 109.55 E-value: 9.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG--------SVAYVPQQAWIQNC---TLQENVL 709
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQRRSIDRDfpiSVRDVVL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 710 FG--QPMNPKRYQQALETCALLADLDVLpggDQTEIGEKGI-NLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAK 786
Cdd:cd03235 93 MGlyGHKGLFRRLSKADKAKVDEALERV---GLSELADRQIgELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1388591336 787 HIFDQVIGpegvLA--GKTRVLVTHGI-SFLPQTDFIIVLAGG 826
Cdd:cd03235 170 DIYELLRE----LRreGMTILVVTHDLgLVLEYFDRVLLLNRT 208
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
586-832 |
1.05e-26 |
|
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: 116.77 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 586 QLISG---LTQASVSLKRIQDFLNQNELDPQCVErkTISPGYAITIHNGTFTWAQDLPPTLHSLNIQIPKGALVAVVGPV 662
Cdd:COG4618 290 QAIGGwkqFVSARQAYRRLNELLAAVPAEPERMP--LPRPKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPS 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 663 GCGKSSLVSALLGEMEKLEGVVSVKG-------------SVAYVPQQAWIQNCTLQENV-LFGQPmNPKRYQQAletcAL 728
Cdd:COG4618 368 GSGKSTLARLLVGVWPPTAGSVRLDGadlsqwdreelgrHIGYLPQDVELFDGTIAENIaRFGDA-DPEKVVAA----AK 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 729 LADL-DV---LPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDShvakhifdqvigpEGVLA---- 800
Cdd:COG4618 443 LAGVhEMilrLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD-------------EGEAAlaaa 509
|
250 260 270
....*....|....*....|....*....|....*....
gi 1388591336 801 -------GKTRVLVTHGISFLPQTDFIIVLAGGQVSEMG 832
Cdd:COG4618 510 iralkarGATVVVITHRPSLLAAVDKLLVLRDGRVQAFG 548
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1284-1503 |
3.80e-26 |
|
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: 108.79 E-value: 3.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHdLRSQLT 1363
Cdd:COG4555 1 MIEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1364 IIPQDPILFSG-TLRMNLDPFGR----YSEEDIWRALELSHLNTFVSSqpagLDFQCAEggdnLSVGQRQLVCLARALLR 1438
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRYFAElyglFDEELKKRIEELIELLGLEEF----LDRRVGE----LSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 1439 KSRVLVLDEATAAIDLETDDLIQGTIRTQF-EDCTVLTIAHrlntIMD-----YNRVLVLDKGVVAEFDSP 1503
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSH----IMQevealCDRVVILHKGKVVAQGSL 216
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
626-825 |
4.33e-26 |
|
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: 107.94 E-value: 4.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 626 ITIHNGTFTWAQDLPPT--LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG--------SVAYVPQ 695
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepvtgpgpDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 696 QA----WIqncTLQENVLFG---QPMNPK----RYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAV 764
Cdd:cd03293 81 QDallpWL---TVLDNVALGlelQGVPKAeareRAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALARAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388591336 765 YSDANIFLLDDPLSAVDSHVAKHIFDQVIGpegvL---AGKTRVLVTHGIS---FLpqTDFIIVLAG 825
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTREQLQEELLD----IwreTGKTVLLVTHDIDeavFL--ADRVVVLSA 207
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1286-1497 |
1.05e-25 |
|
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: 105.60 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1286 EFRNYSVRYRPGLelVLKNVTVHVQGGEKVGIVGRTGAGKSsmTL--CLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLT 1363
Cdd:cd03214 1 EVENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKS--TLlkTLAGLLKPSSGEILLDGKDLASLSPKELARKIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1364 IIPQdpILfsgtlrmnldpfgryseediwRALELSHLntfvssqpAGLDFqcaeggDNLSVGQRQLVCLARALLRKSRVL 1443
Cdd:cd03214 77 YVPQ--AL---------------------ELLGLAHL--------ADRPF------NELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1388591336 1444 VLDEATAAIDL----ETDDLIQGTIRTqfEDCTVLTIAHRLNTIMDY-NRVLVLDKGVV 1497
Cdd:cd03214 120 LLDEPTSHLDIahqiELLELLRRLARE--RGKTVVMVLHDLNLAARYaDRVILLKDGRI 176
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1284-1499 |
1.12e-25 |
|
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: 107.28 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRY--RPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLfRILEA-AEGEIVIDGLNVAHI---GLHD 1357
Cdd:cd03258 1 MIELKNVSKVFgdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCI-NGLERpTSGSVLVDGTDLTLLsgkELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1358 LRSQLTIIPQDPILFSG-TLRMNLD-PF------GRYSEEDIWRALELSHLNTFVSSQPAgldfqcaeggdNLSVGQRQL 1429
Cdd:cd03258 80 ARRRIGMIFQHFNLLSSrTVFENVAlPLeiagvpKAEIEERVLELLELVGLEDKADAYPA-----------QLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388591336 1430 VCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT--QFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAE 1499
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRIcDRVAVMEKGEVVE 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1231-1495 |
2.03e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 112.98 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1231 QVTMALNWMIRMISDLeSNIIA-VERVKEYS---KTKTEAPWVVESNRAPEGwptrGMVEFRNYSVRyRPGLELVLKNVT 1306
Cdd:COG4178 310 QVQGALSWFVDNYQSL-AEWRAtVDRLAGFEealEAADALPEAASRIETSED----GALALEDLTLR-TPDGRPLLEDLS 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1307 VHVQGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAEGEIVidglnvahigLHDLRSQLtIIPQDPILFSGTLRMNL-- 1380
Cdd:COG4178 384 LSLKPGERLLITGPSGSGKST----LLRAIaglwPYGSGRIA----------RPAGARVL-FLPQRPYLPLGTLREALly 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1381 -DPFGRYSEEDIWRALELSHLNTFVSSqpagLDfQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDL 1459
Cdd:COG4178 449 pATAEAFSDAELREALEAVGLGHLAER----LD-EEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAA 523
|
250 260 270
....*....|....*....|....*....|....*..
gi 1388591336 1460 IQGTIRTQFEDCTVLTIAHRlNTIMDY-NRVLVLDKG 1495
Cdd:COG4178 524 LYQLLREELPGTTVISVGHR-STLAAFhDRVLELTGD 559
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
567-849 |
2.33e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 113.13 E-value: 2.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 567 AFVSLSLFNILKiplnmLPQLISGLTQASVSLKRIQDFLNQNELDPQCVER-KTISPGY---AITIHNGTFTWAQDlPPT 642
Cdd:PRK13657 277 AFVGFATLLIGR-----LDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPpGAIDLGRvkgAVEFDDVSFSYDNS-RQG 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-------------SVAYVPQQAWIQNCTLQENVL 709
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirtvtraslrrNIAVVFQDAGLFNRSIEDNIR 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 710 FGQP-MNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHI 788
Cdd:PRK13657 431 VGRPdATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKV 510
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 789 FDQVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLAGGQVSEMGHYSALLQHDGSFANFLR 849
Cdd:PRK13657 511 KAAL---DELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLR 568
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
628-827 |
3.80e-25 |
|
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: 104.86 E-value: 3.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 628 IHNGTFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-------------SVAYVP 694
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkelrrKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 695 QQAWIQ--NCTLQENVLFGqPMN--------PKRYQQALETCALLADLDVLPggdqteigekgINLSGGQRQRVSLARAV 764
Cdd:cd03225 82 QNPDDQffGPTVEEEVAFG-LENlglpeeeiEERVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 765 YSDANIFLLDDPLSAVDSHVAKHIFDQVIGpegvL--AGKTRVLVTHGISFL-PQTDFIIVLAGGQ 827
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKK----LkaEGKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
625-826 |
4.51e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 106.33 E-value: 4.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 625 AITIHNGTFTWAQDLPPT--LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG--------SVAYVP 694
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvtgpgpDRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 695 QQA----WIqncTLQENVLFGQPMN--PKRY-----QQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARA 763
Cdd:COG1116 87 QEPallpWL---TVLDNVALGLELRgvPKAErreraRELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591336 764 VYSDANIFLLDDPLSAVDSHVAKHIFDQVIgpeGVLA--GKTRVLVTHGIS---FLpqTDFIIVLAGG 826
Cdd:COG1116 153 LANDPEVLLMDEPFGALDALTRERLQDELL---RLWQetGKTVLFVTHDVDeavFL--ADRVVVLSAR 215
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1285-1495 |
5.06e-25 |
|
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: 104.47 E-value: 5.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYRPG---LELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGlNVAhiglhdlrsq 1361
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-SIA---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1362 ltIIPQDPILFSGTLRMNLdPFGR-YSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKS 1440
Cdd:cd03250 70 --YVSQEPWIQNGTIRENI-LFGKpFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388591336 1441 RVLVLDEATAAIDLETDDLIqgtirtqFEDC---------TVLTIAHRLNTIMDYNRVLVLDKG 1495
Cdd:cd03250 147 DIYLLDDPLSAVDAHVGRHI-------FENCilglllnnkTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1285-1495 |
6.13e-25 |
|
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: 103.04 E-value: 6.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLH--DLRSQL 1362
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1363 TIIPQDPILFsgtlrmnldpfgryseediwralelSHLNTFvssqpagldfqcaeggDN----LSVGQRQLVCLARALLR 1438
Cdd:cd03229 79 GMVFQDFALF-------------------------PHLTVL----------------ENialgLSGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1439 KSRVLVLDEATAAIDLETDDLIQGTIRTQFED--CTVLTIAHRLNTIMDY-NRVLVLDKG 1495
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARLaDRVVVLRDG 177
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
626-845 |
1.88e-24 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 110.11 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 626 ITIHNGTFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALL-------GEMEkLEGV-------VSVKGSVA 691
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTrfydideGEIL-LDGHdlrdytlASLRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 692 YVPQQAWIQNCTLQENVLFGQPMNPKRYQqaLETCALLAD----LDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSD 767
Cdd:PRK11176 421 LVSQNVHLFNDTIANNIAYARTEQYSREQ--IEEAARMAYamdfINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRD 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591336 768 ANIFLLDDPLSAVDSHVAKHIFDQVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLAGGQVSEMGHYSALLQHDGSFA 845
Cdd:PRK11176 499 SPILILDEATSALDTESERAIQAAL---DELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYA 573
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
643-778 |
3.23e-24 |
|
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: 100.03 E-value: 3.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-------------SVAYVPQQAWIQN-CTLQENV 708
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslrkEIGYVFQDPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388591336 709 LFGQPMnpKRYQQALETCALLADLDVLPGGDQ--TEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLS 778
Cdd:pfam00005 81 RLGLLL--KGLSKREKDARAEEALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
641-863 |
3.56e-24 |
|
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: 109.52 E-value: 3.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVV-------------SVKGSVAYVPQQAWIQNCTLQEN 707
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIlidgqdirdvtqaSLRAAIGIVPQDTVLFNDTIAYN 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 708 VLFGQPMNPkryQQALETCALLADLD----VLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSH 783
Cdd:COG5265 452 IAYGRPDAS---EEEVEAAARAAQIHdfieSLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSR 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 784 VAKHIFDQVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLAGGQVSEMGHYSALLQHDGSFANFLRNYAPDEDQEDHEAA 863
Cdd:COG5265 529 TERAIQAAL---REVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEAEEALAA 605
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
646-832 |
6.48e-24 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 101.44 E-value: 6.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 646 LNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-----------SVAYVPQQ-AWIQNCTLQENVLFG-- 711
Cdd:cd03259 19 LSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvtgvpperrNIGMVFQDyALFPHLTVAENIAFGlk 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 712 --QPMNPKRYQQALETCALLADLDVLpggdQTEIGEkginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVA---- 785
Cdd:cd03259 99 lrGVPKAEIRARVRELLELVGLEGLL----NRYPHE----LSGGQQQRVALARALAREPSLLLLDEPLSALDAKLReelr 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 786 ---KHIFDQvigpegvlAGKTRVLVTHGIS-FLPQTDFIIVLAGGQVSEMG 832
Cdd:cd03259 171 eelKELQRE--------LGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1284-1499 |
8.04e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 101.28 E-value: 8.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYRPGLElVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHI---GLHDLRS 1360
Cdd:COG2884 1 MIRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1361 QLTIIPQD-PILFSGTLRMN----LDPFGRySEEDIWR----ALELSHLNTFVSSQPagldfqcaeggDNLSVGQRQLVC 1431
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENvalpLRVTGK-SRKEIRRrvreVLDLVGLSDKAKALP-----------HELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388591336 1432 LARALLRKSRVLVLDEATAAIDLET-DDLIQ--------GTirtqfedcTVLtIA-HRLNTIMDYN-RVLVLDKGVVAE 1499
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETsWEIMElleeinrrGT--------TVL-IAtHDLELVDRMPkRVLELEDGRLVR 217
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1285-1497 |
2.14e-23 |
|
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: 98.62 E-value: 2.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYRPGLelVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGlHDLRSQLTI 1364
Cdd:cd03230 1 IEVRNLSKRYGKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1365 IPQDPILFSG-TLRMNLDpfgryseediwralelshlntfvssqpagldfqcaeggdnLSVGQRQLVCLARALLRKSRVL 1443
Cdd:cd03230 78 LPEEPSLYENlTVRENLK----------------------------------------LSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 1444 VLDEATAAIDLETDDLIQGTIRT-QFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVV 1497
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
402-845 |
2.98e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 107.12 E-value: 2.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 402 ESTVGEMVNLMSVDAQRFMD-VSPFIN-LLWSAPLQVILAIYFLWqiLGPSaLAGVAVIvlLIPLNGAVSMKM-KTYQVK 478
Cdd:TIGR00958 254 ENKTGELTSRLSSDTQTMSRsLSLNVNvLLRNLVMLLGLLGFMLW--LSPR-LTMVTLI--NLPLVFLAEKVFgKRYQLL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 479 QMKFKDSRIKL---MSEILNGIKVLKLYAWEPSFLEQVKGIRQSELQLLRKGAYlqAISTFIWIcTPFLVTLITLGVyVY 555
Cdd:TIGR00958 329 SEELQEAVAKAnqvAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKAL--AYAGYLWT-TSVLGMLIQVLV-LY 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 556 VDESNVLDAEKAFVSLSLFNILKIPL-NMLPQLI---SGLTQASVSLKRIQDFLNQNeldPQCVERKTISPGY---AITI 628
Cdd:TIGR00958 405 YGGQLVLTGKVSSGNLVSFLLYQEQLgEAVRVLSyvySGMMQAVGASEKVFEYLDRK---PNIPLTGTLAPLNlegLIEF 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 629 HNGTFTW-AQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-------------SVAYVP 694
Cdd:TIGR00958 482 QDVSFSYpNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylhrQVALVG 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 695 QQAWIQNCTLQENVLFGQPMNPKRYQQALETCALLAD-LDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLL 773
Cdd:TIGR00958 562 QEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDfIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLIL 641
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388591336 774 DDPLSAVDSHVakhifDQVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLAGGQVSEMGHYSALLQHDGSFA 845
Cdd:TIGR00958 642 DEATSALDAEC-----EQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYK 708
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1284-1465 |
2.99e-23 |
|
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: 99.09 E-value: 2.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAEGEIVIDGLNVaHIGLHDLR 1359
Cdd:COG4133 2 MLEAENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTT----LLRILagllPPSAGEVLWNGEPI-RDAREDYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1360 SQLTIIPQDPILFSG-TLRMNLDpF------GRYSEEDIWRALE---LSHLntfvSSQPAGldfqcaeggdNLSVGQRQL 1429
Cdd:COG4133 75 RRLAYLGHADGLKPElTVRENLR-FwaalygLRADREAIDEALEavgLAGL----ADLPVR----------QLSAGQKRR 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 1388591336 1430 VCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIR 1465
Cdd:COG4133 140 VALARLLLSPAPLWLLDEPFTALDAAGVALLAELIA 175
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1285-1503 |
4.22e-23 |
|
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: 99.56 E-value: 4.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYRPGLelVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEA-----AEGEIVIDGLNVAHIGLHD-- 1357
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1358 LRSQLTIIPQDPILFSGTLRMNLDpFG---------RYSEEDIWRALELSHLNTFVSSQPAGLDfqcaeggdnLSVGQRQ 1428
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVA-YGlrlhgiklkEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591336 1429 LVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNT---IMDYnrVLVLDKGVVAEFDSP 1503
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQaarVADR--TAFLLNGRLVEFGPT 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1284-1511 |
4.81e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 100.96 E-value: 4.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYRPGLE-LVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQL 1362
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1363 TIIPQDPI-LFSGTLRMNLDPFG------RYSE--EDIWRALELSHLNTFVSSQPAgldfqcaeggdNLSVGQRQLVCLA 1433
Cdd:PRK13650 84 GMVFQNPDnQFVGATVEDDVAFGlenkgiPHEEmkERVNEALELVGMQDFKEREPA-----------RLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1434 RALLRKSRVLVLDEATAAIDLETD-DLIQgTIRTQFED--CTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAG 1510
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRlELIK-TIKGIRDDyqMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRG 231
|
.
gi 1388591336 1511 G 1511
Cdd:PRK13650 232 N 232
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
643-828 |
5.10e-23 |
|
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: 97.89 E-value: 5.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGS-------------VAYVPQqawiqnctlqenvl 709
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlaslspkelarkIAYVPQ-------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 710 fgqpmnpkryqqALETCALladldvlpggdqTEIGEKGIN-LSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHI 788
Cdd:cd03214 81 ------------ALELLGL------------AHLADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1388591336 789 FDQVIGpegvLA---GKTRVLVTHGISFLPQ-TDFIIVLAGGQV 828
Cdd:cd03214 137 LELLRR----LArerGKTVVMVLHDLNLAARyADRVILLKDGRI 176
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1014-1492 |
5.15e-23 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 107.42 E-value: 5.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1014 LGILQGLLVMLSAFTMVVGAIQAARLLHEALLHNKIRSPQSFFDTTPSGRIlnRFSKDIYvIDEVLAP------TILMLL 1087
Cdd:PTZ00265 106 IGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKL--TSDLDFY-LEQVNAGigtkfiTIFTYA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1088 NSFFTSISTIMVIVASTPLFMVVVLPLAVLYGFVQRFYVATSrqlKRLESISRSPIFSHFSETVTGTSVIRAYgrIQDFK 1167
Cdd:PTZ00265 183 SAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKIN---KKTSLLYNNNTMSIIEEALVGIRTVVSY--CGEKT 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1168 VLSDTKVDNNQKSSYpYIASNRWLGVHVEFVgNCVVLFAALFA-------VIG-------RNSLNPGLVglsVSYALQVT 1233
Cdd:PTZ00265 258 ILKKFNLSEKLYSKY-ILKANFMESLHIGMI-NGFILASYAFGfwygtriIISdlsnqqpNNDFHGGSV---ISILLGVL 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1234 MALNWMIRMISDLESNIIAVERVKEYSKTKTEAPwVVESNRAPEGWPTRGMVEFRNYSVRY--RPGLElVLKNVTVHVQG 1311
Cdd:PTZ00265 333 ISMFMLTIILPNITEYMKSLEATNSLYEIINRKP-LVENNDDGKKLKDIKKIQFKNVRFHYdtRKDVE-IYKDLNFTLTE 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1312 GEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVI-DGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMN----------L 1380
Cdd:PTZ00265 411 GKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNikyslyslkdL 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1381 DPFGRYSEED------------IWRALELSHLN------------------------------------TFVSSQPAGLD 1412
Cdd:PTZ00265 491 EALSNYYNEDgndsqenknkrnSCRAKCAGDLNdmsnttdsneliemrknyqtikdsevvdvskkvlihDFVSALPDKYE 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1413 FQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT--QFEDCTVLTIAHRLNTIMDYNRVL 1490
Cdd:PTZ00265 571 TLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNlkGNENRITIIIAHRLSTIRYANTIF 650
|
..
gi 1388591336 1491 VL 1492
Cdd:PTZ00265 651 VL 652
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1285-1498 |
6.09e-23 |
|
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: 97.11 E-value: 6.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHD-LRSQLT 1363
Cdd:cd03216 1 LELRGITKRF--GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1364 IIPQdpilfsgtlrmnldpfgryseediwralelshlntfvssqpagldfqcaeggdnLSVGQRQLVCLARALLRKSRVL 1443
Cdd:cd03216 79 MVYQ------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591336 1444 VLDEATAAIDL-ETDDLIQgTIRT-QFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVA 1498
Cdd:cd03216 105 ILDEPTAALTPaEVERLFK-VIRRlRAQGVAVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
641-809 |
6.75e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 97.69 E-value: 6.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG--SVAYVPQQ---AWIQNCTLQENVLFG--QP 713
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRsevPDSLPLTVRDLVAMGrwAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 714 MNPKRY---------QQALEtcAL-LADLDVLPggdqteIGEkginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSH 783
Cdd:NF040873 86 RGLWRRltrddraavDDALE--RVgLADLAGRQ------LGE----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
|
170 180
....*....|....*....|....*.
gi 1388591336 784 VAKHIFDqVIGpEGVLAGKTRVLVTH 809
Cdd:NF040873 154 SRERIIA-LLA-EEHARGATVVVVTH 177
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
626-854 |
9.72e-23 |
|
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: 98.91 E-value: 9.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 626 ITIHNGTFTWAqDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-------------SVAY 692
Cdd:cd03295 1 IEFENVTKRYG-GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 693 VPQQAWI-QNCTLQENV-----LFGQPmNPKRYQQALEtcaLLADLDVLPGG------DQteigekginLSGGQRQRVSL 760
Cdd:cd03295 80 VIQQIGLfPHMTVEENIalvpkLLKWP-KEKIRERADE---LLALVGLDPAEfadrypHE---------LSGGQQQRVGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 761 ARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGPEGVLaGKTRVLVTHGI-SFLPQTDFIIVLAGGQvsemghysalLQ 839
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQEL-GKTIVFVTHDIdEAFRLADRIAIMKNGE----------IV 215
|
250
....*....|....*
gi 1388591336 840 HDGSFANFLRNYAPD 854
Cdd:cd03295 216 QVGTPDEILRSPAND 230
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
626-832 |
1.85e-22 |
|
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: 96.23 E-value: 1.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 626 ITIHNGTFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGS------------VAYV 693
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 694 PQQAWIQNCTLQENVlfgqpmnpkryqqaletcalladldvlpggdqteigekGINLSGGQRQRVSLARAVYSDANIFLL 773
Cdd:cd03247 81 NQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1388591336 774 DDPLSAVDSHVAKHIFDQVIgpeGVLAGKTRVLVTHGISFLPQTDFIIVLAGGQVSEMG 832
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIF---EVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
580-844 |
2.78e-22 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 103.26 E-value: 2.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 580 PLNMLPQLISGLTQASVSLKRIQDFLNQNELDPQCVERkTISPGyAITIHNGTFTWAQDlPPTLHSLNIQIPKGALVAVV 659
Cdd:PRK10790 297 PLIELTTQQSMLQQAVVAGERVFELMDGPRQQYGNDDR-PLQSG-RIDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALV 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 660 GPVGCGKSSLVSALLGEMEKLEGVVSVKG-------------SVAYVPQQAWIQNCTLQENVLFGQPMNPKRYQQALETC 726
Cdd:PRK10790 374 GHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsslshsvlrqGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETV 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 727 ALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIfDQVIGpeGVLAGKTRVL 806
Cdd:PRK10790 454 QLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAI-QQALA--AVREHTTLVV 530
|
250 260 270
....*....|....*....|....*....|....*...
gi 1388591336 807 VTHGISFLPQTDFIIVLAGGQVSEMGHYSALLQHDGSF 844
Cdd:PRK10790 531 IAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRY 568
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1285-1501 |
3.67e-22 |
|
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: 96.43 E-value: 3.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHdlRSQLTI 1364
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1365 IPQDPILFSG-TLRMNLDpFG----RYSEEDIWR----ALELSHLNTFVSSQPAGldfqcaeggdnLSVGQRQLVCLARA 1435
Cdd:cd03259 77 VFQDYALFPHlTVAENIA-FGlklrGVPKAEIRArvreLLELVGLEGLLNRYPHE-----------LSGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388591336 1436 LLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFE--DCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFD 1501
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEEALALaDRIAVMNEGRIVQVG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1285-1497 |
6.21e-22 |
|
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: 96.02 E-value: 6.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYRPGLE--LVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDL---- 1358
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1359 RSQLTIIPQD----PILfsgTLRMN----LDPFGRYSEEDIWRALEL-------SHLNTFVSsqpagldfqcaeggdNLS 1423
Cdd:cd03255 81 RRHIGFVFQSfnllPDL---TALENvelpLLLAGVPKKERRERAEELlervglgDRLNHYPS---------------ELS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591336 1424 VGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIR--TQFEDCTVLTIAH--RLNTIMDynRVLVLDKGVV 1497
Cdd:cd03255 143 GGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHdpELAEYAD--RIIELRDGKI 218
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
641-828 |
9.55e-22 |
|
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: 95.25 E-value: 9.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSaLLGEMEKL-EGVVSVKG-----------------SVAYVPQQ-AWIQN 701
Cdd:cd03255 18 QALKGVSLSIEKGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVRVDGtdisklsekelaafrrrHIGFVFQSfNLLPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 702 CTLQENVLFGQPMNPK-------RYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLD 774
Cdd:cd03255 97 LTALENVELPLLLAGVpkkerreRAEELLERVGLGDRLNHYPS-----------ELSGGQQQRVAIARALANDPKIILAD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1388591336 775 DPLSAVDSHVAKHIFDqVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLAGGQV 828
Cdd:cd03255 166 EPTGNLDSETGKEVME-LLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
643-828 |
2.26e-21 |
|
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: 95.11 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-------------SVAYVPQQ---AWiqNCTLQE 706
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAYVPQEppaPF--GLTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 707 NVLFG--------QPMNPKRYQ---QALETCAL--LADLDVLpggdqteigekgiNLSGGQRQRVSLARAVYSDANIFLL 773
Cdd:COG1120 95 LVALGryphlglfGRPSAEDREaveEALERTGLehLADRPVD-------------ELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1388591336 774 DDPLSAVDSHVAKHIFDQVIGpegvLA---GKTRVLVTHGISF-LPQTDFIIVLAGGQV 828
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLRR----LArerGRTVVMVLHDLNLaARYADRLVLLKDGRI 216
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
627-827 |
6.90e-21 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 90.77 E-value: 6.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 627 TIHNGTFTWAQdlPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVsvkgsvayvpqqawiqnctlqe 706
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI---------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 707 nVLFGQPMNPKRYQQALETCALLadldvlpggDQteigekginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHvAK 786
Cdd:cd00267 57 -LIDGKDIAKLPLEELRRRIGYV---------PQ---------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA-SR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1388591336 787 HIFDQVIGpEGVLAGKTRVLVTHGISFL-PQTDFIIVLAGGQ 827
Cdd:cd00267 117 ERLLELLR-ELAEEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
643-832 |
8.03e-21 |
|
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: 93.01 E-value: 8.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSAL-----LGEMEKLEGVVSVKGS---------------VAYVPQQAWIQNC 702
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKdiydldvdvlelrrrVGMVFQKPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 703 TLQENVLFGQP---MNPKRY-----QQALETCALLADLDvlpggDQTeigeKGINLSGGQRQRVSLARAVYSDANIFLLD 774
Cdd:cd03260 96 SIYDNVAYGLRlhgIKLKEEldervEEALRKAALWDEVK-----DRL----HALGLSGGQQQRLCLARALANEPEVLLLD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388591336 775 DPLSAVDShVAKHIFDQVIGPegvLAGK-TRVLVTHGisfLPQ----TDFIIVLAGGQVSEMG 832
Cdd:cd03260 167 EPTSALDP-ISTAKIEELIAE---LKKEyTIVIVTHN---MQQaarvADRTAFLLNGRLVEFG 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
625-873 |
9.35e-21 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 98.05 E-value: 9.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 625 AITIHNGTFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLG---EMEKLEGVVSVKG------------- 688
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGrdllelsealrgr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 689 SVAYVPQQAWIQNC--TLQENVLFG---QPMNP----KRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVS 759
Cdd:COG1123 84 RIGMVFQDPMTQLNpvTVGDQIAEAlenLGLSRaearARVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 760 LARAVYSDANIFLLDDPLSAVDSHVAKHIFDqVIGPEGVLAGKTRVLVTHGISFLPQ-TDFIIVLAGGQVSEMGHYSALL 838
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILD-LLRELQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEIL 231
|
250 260 270
....*....|....*....|....*....|....*
gi 1388591336 839 QHDGSFANflrnyAPDEDQEDHEAALQNANEEVLL 873
Cdd:COG1123 232 AAPQALAA-----VPRLGAARGRAAPAAAAAEPLL 261
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
633-809 |
1.05e-20 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 92.19 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 633 FTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-------------SVAYVPQQ-AW 698
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppewrrQVAYVPQEpAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 699 IQNcTLQENVLF-----GQPMNPKRYQQALEtcALLADLDVLpggdQTEIGEkginLSGGQRQRVSLARAVYSDANIFLL 773
Cdd:COG4619 86 WGG-TVRDNLPFpfqlrERKFDRERALELLE--RLGLPPDIL----DKPVER----LSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1388591336 774 DDPLSAVDS----HVAKHIFDQVIGPegvlaGKTRVLVTH 809
Cdd:COG4619 155 DEPTSALDPentrRVEELLREYLAEE-----GRAVLWVSH 189
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
626-828 |
1.61e-20 |
|
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: 92.01 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 626 ITIHNGTFTWAQDlPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-------------SVAY 692
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkknlrelrrKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 693 VPQQAWIQ--NCTLQENVLFGqPMN--------PKRYQQALETCAL--LADLDVLpggdqteigekgiNLSGGQRQRVSL 760
Cdd:COG1122 80 VFQNPDDQlfAPTVEEDVAFG-PENlglpreeiRERVEEALELVGLehLADRPPH-------------ELSGGQKQRVAI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 761 ARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGpegvL--AGKTRVLVTHGISFLPQ-TDFIIVLAGGQV 828
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKR----LnkEGKTVIIVTHDLDLVAElADRVIVLDDGRI 212
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1284-1510 |
2.27e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 92.75 E-value: 2.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLT 1363
Cdd:PRK13632 7 MIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1364 IIPQDPIlfsgtlrmnlDPF-GRYSEEDIWRALE-----LSHLNTFV--SSQPAGLDFQCAEGGDNLSVGQRQLVCLARA 1435
Cdd:PRK13632 87 IIFQNPD----------NQFiGATVEDDIAFGLEnkkvpPKKMKDIIddLAKKVGMEDYLDKEPQNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591336 1436 LLRKSRVLVLDEATAAID-LETDDLIQ--GTIRTQfEDCTVLTIAHRLNTIMDYNRVLVLDKGvvaefdspvNLIAAG 1510
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDpKGKREIKKimVDLRKT-RKKTLISITHDMDEAILADKVIVFSEG---------KLIAQG 224
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
641-828 |
2.98e-20 |
|
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: 91.38 E-value: 2.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGS-------------VAYVPQQAWIQNCTLQEN 707
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhskVSLVGQEPVLFARSLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 708 VLFGQPMNP-KRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHvAK 786
Cdd:cd03248 108 IAYGLQSCSfECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE-SE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1388591336 787 HIFDQVI--GPEgvlaGKTRVLVTHGISFLPQTDFIIVLAGGQV 828
Cdd:cd03248 187 QQVQQALydWPE----RRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1285-1494 |
3.16e-20 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 89.14 E-value: 3.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVrYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAEGEIVIDGlnvahiglhdlRS 1360
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSS----LFRALaglwPWGSGRIGMPE-----------GE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1361 QLTIIPQDPILFSGTLRMNLdpfgRYSeediWralelshlntfvssqpagldfqcaegGDNLSVGQRQLVCLARALLRKS 1440
Cdd:cd03223 65 DLLFLPQRPYLPLGTLREQL----IYP----W--------------------------DDVLSGGEQQRLAFARLLLHKP 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 1441 RVLVLDEATAAIDLETDDLIQGTIRTQFedCTVLTIAHR--LNTImdYNRVLVLDK 1494
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKELG--ITVISVGHRpsLWKF--HDRVLDLDG 162
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
643-848 |
4.11e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 93.67 E-value: 4.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGemekLE----GVVSVKG------------SVAYVPQQ-AWIQNCTLQ 705
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAG----LEtpdsGRIVLNGrdlftnlpprerRVGFVFQHyALFPHMTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 706 ENVLFGQPMNPKRYQQALETCALLADL-------DVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLS 778
Cdd:COG1118 94 ENIAFGLRVRPPSKAEIRARVEELLELvqleglaDRYPS-----------QLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 779 AVDSHVAK-------HIFDQVigpegvlaGKTRVLVTH------GISflpqtDFIIVLAGGQVSEMGHYSALLQHDGSF- 844
Cdd:COG1118 163 ALDAKVRKelrrwlrRLHDEL--------GGTTVFVTHdqeealELA-----DRVVVMNQGRIEQVGTPDEVYDRPATPf 229
|
....*
gi 1388591336 845 -ANFL 848
Cdd:COG1118 230 vARFL 234
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
643-809 |
4.92e-20 |
|
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: 89.85 E-value: 4.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG------------SVAYVPQQ-AWIQNCTLQENVL 709
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLAYLGHAdGLKPELTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 710 F-----GQPMNPKRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHv 784
Cdd:COG4133 98 FwaalyGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA- 165
|
170 180
....*....|....*....|....*
gi 1388591336 785 AKHIFDQVIGpEGVLAGKTRVLVTH 809
Cdd:COG4133 166 GVALLAELIA-AHLARGGAVLLTTH 189
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
626-833 |
7.68e-20 |
|
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: 89.39 E-value: 7.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 626 ITIHNGTFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-------------SVAY 692
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 693 VPQQAWIQNCTLQENVlfgQPMNpkRYQQALETCALladldvlpggdqtEIGEKGINLSGGQRQRVSLARAVYSDANIFL 772
Cdd:cd03369 87 IPQDPTLFSGTIRSNL---DPFD--EYSDEEIYGAL-------------RVSEGGLNLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 773 LDDPLSAVDSHvAKHIFDQVIGPEgvLAGKTRVLVTHGISFLPQTDFIIVLAGGQVSEMGH 833
Cdd:cd03369 149 LDEATASIDYA-TDALIQKTIREE--FTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1288-1499 |
1.08e-19 |
|
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: 89.80 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1288 RNYSVRYRpGLeLVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDlRSQLTIIP- 1366
Cdd:cd03219 4 RGLTKRFG-GL-VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE-IARLGIGRt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1367 -QDPILFSG-TLRMNL-------------DPFGRYSEEDIW-RALELshLNTF----VSSQPAGldfqcaeggdNLSVGQ 1426
Cdd:cd03219 81 fQIPRLFPElTVLENVmvaaqartgsgllLARARREEREAReRAEEL--LERVgladLADRPAG----------ELSYGQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388591336 1427 RQLVCLARALLRKSRVLVLDEATAAIDL-ETDDLIQgTIRT-QFEDCTVLTIAHRLNTIMDY-NRVLVLDKG-VVAE 1499
Cdd:cd03219 149 QRRLEIARALATDPKLLLLDEPAAGLNPeETEELAE-LIRElRERGITVLLVEHDMDVVMSLaDRVTVLDQGrVIAE 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1285-1510 |
1.27e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 90.84 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTI 1364
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1365 IPQDPI-LFSGT-----LRMNLDPFGRYSEEDIWR---ALELSHLNTFVSSQPAgldfqcaeggdNLSVGQRQLVCLARA 1435
Cdd:PRK13635 86 VFQNPDnQFVGAtvqddVAFGLENIGVPREEMVERvdqALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388591336 1436 LLRKSRVLVLDEATAAIDLETDDLIQGTIRT--QFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAG 1510
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSG 231
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
643-828 |
1.37e-19 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 89.74 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG------------SVAYVPQQAWI-QNCTLQENV- 708
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEPALyPDLTVRENLr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 709 ----LFGQPMN--PKRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDS 782
Cdd:COG1131 96 ffarLYGLPRKeaRERIDELLELFGLTDAADRKVG-----------TLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1388591336 783 HVAKHIFDQVIGpegvLA--GKTRVLVTHGISFLPQT-DFIIVLAGGQV 828
Cdd:COG1131 165 EARRELWELLRE----LAaeGKTVLLSTHYLEEAERLcDRVAIIDKGRI 209
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
623-849 |
1.48e-19 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 89.97 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 623 GYAITIHNGTFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-SVAYVPQQAWIQN 701
Cdd:cd03288 17 GGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGiDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 702 CT--LQENVLFGQP----MNPK------RYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDAN 769
Cdd:cd03288 97 LSiiLQDPILFSGSirfnLDPEckctddRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 770 IFLLDDPLSAVDShVAKHIFDQVIgpEGVLAGKTRVLVTHGISFLPQTDFIIVLAGGQVSEMGHYSALL-QHDGSFANFL 848
Cdd:cd03288 177 ILIMDEATASIDM-ATENILQKVV--MTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLV 253
|
.
gi 1388591336 849 R 849
Cdd:cd03288 254 R 254
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1284-1503 |
1.72e-19 |
|
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: 89.27 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIG---LHDLRS 1360
Cdd:COG1127 5 MIEVRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1361 QLTIIPQDPILFSG-TLRMN----LDPFGRYSEEDI----WRALELSHLNTFVSSQPAgldfqcaEggdnLSVGQRQLVC 1431
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENvafpLREHTDLSEAEIrelvLEKLELVGLPGAADKMPS-------E----LSGGMRKRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388591336 1432 LARALLRKSRVLVLDEATAAID----LETDDLIQgTIRTQFeDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSP 1503
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDpitsAVIDELIR-ELRDEL-GLTSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTP 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
627-828 |
2.78e-19 |
|
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: 87.70 E-value: 2.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 627 TIHNGTFTWaQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG----------SVAYVPQQ 696
Cdd:cd03226 1 RIENISFSY-KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 697 AWIQ--NCTLQENVLFGQPMNPKRYQQA---LETCALLADLDVLPggdqteigekgINLSGGQRQRVSLARAVYSDANIF 771
Cdd:cd03226 80 VDYQlfTDSVREELLLGLKELDAGNEQAetvLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591336 772 LLDDPLSAVDSHVAKHIFDqVIGpEGVLAGKTRVLVTHGISFLPQT-DFIIVLAGGQV 828
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGE-LIR-ELAAQGKAVIVITHDYEFLAKVcDRVLLLANGAI 204
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1284-1501 |
3.26e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.77 E-value: 3.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYrPGLeLVLKNVTVHVQGGEKVGIVGRTGAGKSsmTL--CLFRILEAAEGEIVIDGLNVAHIGLHD-LRS 1360
Cdd:COG1129 4 LLEMRGISKSF-GGV-KALDGVSLELRPGEVHALLGENGAGKS--TLmkILSGVYQPDSGEILLDGEPVRFRSPRDaQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1361 QLTIIPQDPIL----------FSGTLRMNldpFGRYSeediWRALE------LSHLNTFVS-SQPAGldfqcaeggdNLS 1423
Cdd:COG1129 80 GIAIIHQELNLvpnlsvaeniFLGREPRR---GGLID----WRAMRrrarelLARLGLDIDpDTPVG----------DLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1424 VGQRQLVCLARALLRKSRVLVLDEATAAIDL-ETDDLIqGTIRT-QFEDCTVLTIAHRLNTIMDY-NRVLVL-DKGVVAE 1499
Cdd:COG1129 143 VAQQQLVEIARALSRDARVLILDEPTASLTErEVERLF-RIIRRlKAQGVAIIYISHRLDEVFEIaDRVTVLrDGRLVGT 221
|
..
gi 1388591336 1500 FD 1501
Cdd:COG1129 222 GP 223
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
643-841 |
3.32e-19 |
|
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: 88.33 E-value: 3.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGS----------------VAYVPQQ-AWIQNCTLQ 705
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrrrMGMLFQSgALFDSLTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 706 ENVLF--------GQPMNPKRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPL 777
Cdd:cd03261 96 ENVAFplrehtrlSEEEIREIVLEKLEAVGLRGAEDLYPA-----------ELSGGMKKRVALARALALDPELLLYDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388591336 778 SAVDShVAKHIFDQVIGPEGVLAGKTRVLVTHGISFLPQT-DFIIVLAGGQVSEMGHYSALLQHD 841
Cdd:cd03261 165 AGLDP-IASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEELRASD 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1285-1503 |
3.41e-19 |
|
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: 88.33 E-value: 3.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAH---IGLHDLRSQ 1361
Cdd:cd03261 1 IELRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1362 LTIIPQDPILFSG-TLRMN----LDPFGRYSEEDIwRALELSHLNTfvssqpAGLdfqcaEGGDN-----LSVGQRQLVC 1431
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENvafpLREHTRLSEEEI-REIVLEKLEA------VGL-----RGAEDlypaeLSGGMKKRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388591336 1432 LARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT--QFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSP 1503
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTP 221
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
643-830 |
7.35e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 87.02 E-value: 7.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSaLLGEMEKL-EGVVSVKG-----------------SVAYVPQQA-WIQNCT 703
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVLIDGqdisslserelarlrrrHIGFVFQFFnLLPELT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 704 LQENVLF-----GQP--MNPKRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDP 776
Cdd:COG1136 103 ALENVALplllaGVSrkERRERARELLERVGLGDRLDHRPS-----------QLSGGQQQRVAIARALVNRPKLILADEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 777 LSAVDSHVAKHIFDqvigpegVLA------GKTRVLVTHGISFLPQTDFIIVLAGGQVSE 830
Cdd:COG1136 172 TGNLDSKTGEEVLE-------LLRelnrelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1286-1508 |
9.27e-19 |
|
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: 86.72 E-value: 9.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1286 EFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHD-LRSQLTI 1364
Cdd:cd03224 2 EVENLNAGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1365 IPQDPILFSG-TLRMNLD-----PFGRYSEEDIWRALELshlntF-----VSSQPAGldfqcaeggdNLSVGQRQLVCLA 1433
Cdd:cd03224 80 VPEGRRIFPElTVEENLLlgayaRRRAKRKARLERVYEL-----FprlkeRRKQLAG----------TLSGGEQQMLAIA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1434 RALLRKSRVLVLDEATA----AIDLETDDLIQgTIRTqfEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSPVNLIA 1508
Cdd:cd03224 145 RALMSRPKLLLLDEPSEglapKIVEEIFEAIR-ELRD--EGVTILLVEQNARFALEIaDRAYVLERGRVVLEGTAAELLA 221
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
641-828 |
1.43e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 88.98 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGemekLE----GVVSVKG-----------SVAYVPQQ-AWIQNCTL 704
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG----LEdptsGEILIGGrdvtdlppkdrNIAMVFQSyALYPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 705 QENVLFGQPMN--PK-----RYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPL 777
Cdd:COG3839 93 YENIAFPLKLRkvPKaeidrRVREAAELLGLEDLLDRKPK-----------QLSGGQRQRVALGRALVREPKVFLLDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388591336 778 SAVDSHVA-------KHIFDQVigpegvlaGKTRVLVTHGisflpQT------DFIIVLAGGQV 828
Cdd:COG3839 162 SNLDAKLRvemraeiKRLHRRL--------GTTTIYVTHD-----QVeamtlaDRIAVMNDGRI 212
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
641-832 |
1.86e-18 |
|
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: 86.24 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-----------SVAYVPQQ-AWIQNCTLQENV 708
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedatdvpvqerNVGFVFQHyALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 709 LFGQPMNPK-----------RYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPL 777
Cdd:cd03296 96 AFGLRVKPRserppeaeiraKVHELLKLVQLDWLADRYPA-----------QLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388591336 778 SAVDSHVAKH-------IFDQVigpegvlaGKTRVLVTHGIS-FLPQTDFIIVLAGGQVSEMG 832
Cdd:cd03296 165 GALDAKVRKElrrwlrrLHDEL--------HVTTVFVTHDQEeALEVADRVVVMNKGRIEQVG 219
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
640-826 |
2.34e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 86.45 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 640 PPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSV--------AYVPQQ----AWIqncTLQEN 707
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVVFQKdallPWL---NVLDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 708 VLFGQPMN--PK--RYQQALETCALLAdldvLPGGDQTEIGEkginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSH 783
Cdd:COG4525 97 VAFGLRLRgvPKaeRRARAEELLALVG----LADFARRRIWQ----LSGGMRQRVGIARALAADPRFLLMDEPFGALDAL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 784 VAKHIfdQVIgpegVL-----AGKTRVLVTHGIS---FLpQTDfIIVLAGG 826
Cdd:COG4525 169 TREQM--QEL----LLdvwqrTGKGVFLITHSVEealFL-ATR-LVVMSPG 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
643-827 |
3.42e-18 |
|
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: 83.78 E-value: 3.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG---------------SVAYVPQQ-AWIQNCTLQE 706
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledelpplrrRIGMVFQDfALFPHLTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 707 NVLFGqpmnpkryqqaletcalladldvlpggdqteigekginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVA- 785
Cdd:cd03229 96 NIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRr 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1388591336 786 ------KHIFDQVigpegvlaGKTRVLVTHGISFLPQ-TDFIIVLAGGQ 827
Cdd:cd03229 138 evrallKSLQAQL--------GITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
443-857 |
3.88e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 91.19 E-value: 3.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 443 LWQILGPSALAGV-------AVIVLLIPLNGAVSMKMKTyqVKQMKFKDSRIK-----LMSEILNG---IKVLKLYAWep 507
Cdd:PLN03232 1035 LWQLLSTFALIGTvstislwAIMPLLILFYAAYLYYQST--SREVRRLDSVTRspiyaQFGEALNGlssIRAYKAYDR-- 1110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 508 sfLEQVKG------IRQSelqllrkgayLQAISTFIWICtpflVTLITLG-VYVYVDES-NVL---DAEKAFVSLSLFNI 576
Cdd:PLN03232 1111 --MAKINGksmdnnIRFT----------LANTSSNRWLT----IRLETLGgVMIWLTATfAVLrngNAENQAGFASTMGL 1174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 577 LKIPLNMLPQLISG-LTQASV------SLKRIQDFLNQNELDPQCVERKTISPGY----AITIHNGTFTWAQDLPPTLHS 645
Cdd:PLN03232 1175 LLSYTLNITTLLSGvLRQASKaenslnSVERVGNYIDLPSEATAIIENNRPVSGWpsrgSIKFEDVHLRYRPGLPPVLHG 1254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 646 LNIQIPKGALVAVVGPVGCGKSSLVSAL--LGEMEKLE-----------GVVSVKGSVAYVPQQAWIQNCTLQENVLFGQ 712
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALfrIVELEKGRimiddcdvakfGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFS 1334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 713 PMNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIfDQV 792
Cdd:PLN03232 1335 EHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLI-QRT 1413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 793 IGPEgvLAGKTRVLVTHGISFLPQTDFIIVLAGGQVSEMGHYSALLQHDGS-FANFLRNYAPDEDQ 857
Cdd:PLN03232 1414 IREE--FKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSaFFRMVHSTGPANAQ 1477
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1284-1499 |
4.68e-18 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 87.44 E-value: 4.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYRPGLELV--LKNVTVHVQGGEKVGIVGRTGAGKSsmTL--CLFRiLEAA-EGEIVIDGLNVAHI---GL 1355
Cdd:COG1135 1 MIELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKS--TLirCINL-LERPtSGSVLVDGVDLTALserEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1356 HDLRSQLTIIPQDPILFSG-T--------LRMNldpfgRYSEEDIW-RALELshLNtFVssqpaGLdfqcAEGGD----N 1421
Cdd:COG1135 78 RAARRKIGMIFQHFNLLSSrTvaenvalpLEIA-----GVPKAEIRkRVAEL--LE-LV-----GL----SDKADaypsQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1422 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETD----DLIQgTIRTQFeDCTVLTIAHRLNTIMDY-NRVLVLDKGV 1496
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTrsilDLLK-DINREL-GLTIVLITHEMDVVRRIcDRVAVLENGR 218
|
...
gi 1388591336 1497 VAE 1499
Cdd:COG1135 219 IVE 221
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
626-842 |
4.84e-18 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 85.29 E-value: 4.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 626 ITIHNGTFTWaqDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG------------SVAYV 693
Cdd:COG4555 2 IEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 694 PQQAWI-QNCTLQENVLF---GQPMNPKRYQQALEtcALLADLDVLPGGDQTeIGEkginLSGGQRQRVSLARAVYSDAN 769
Cdd:COG4555 80 PDERGLyDRLTVRENIRYfaeLYGLFDEELKKRIE--ELIELLGLEEFLDRR-VGE----LSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388591336 770 IFLLDDPLSAVDShVAKHIFDQVI---GPEgvlaGKTRVLVTHGISFLPQT-DFIIVLAGGQVSEMGHYSALLQHDG 842
Cdd:COG4555 153 VLLLDEPTNGLDV-MARRLLREILralKKE----GKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1284-1499 |
5.43e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 84.71 E-value: 5.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYRPGLELV--LKNVTVHVQGGEKVGIVGRTGAGKSsmTL--CLFRILEAAEGEIVIDGLNVAHIG---LH 1356
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKS--TLlnILGGLDRPTSGEVLIDGQDISSLSereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1357 DLRSQ-LTIIPQDPILFSGT-----LRMNLDPFGRYSEEDIWRALEL-------SHLNTFVSSqpagldfqcaeggdnLS 1423
Cdd:COG1136 82 RLRRRhIGFVFQFFNLLPELtalenVALPLLLAGVSRKERRERARELlervglgDRLDHRPSQ---------------LS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1424 VGQRQLVCLARALLRKSRVLVLDEATAAIDLETD----DLIQGTIRTQfeDCTVLTIAHRLNtIMDY-NRVLVLDKGVVA 1498
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGeevlELLRELNREL--GTTIVMVTHDPE-LAARaDRVIRLRDGRIV 223
|
.
gi 1388591336 1499 E 1499
Cdd:COG1136 224 S 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
643-828 |
1.47e-17 |
|
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: 81.68 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSV------------KGSVAYVPQQA-WIQNCTLQENvl 709
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlgkdikkepeevKRRIGYLPEEPsLYENLTVREN-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 710 fgqpmnpkryqqaletcalladldvlpggdqteigekgINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIF 789
Cdd:cd03230 94 --------------------------------------LKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFW 135
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1388591336 790 DQVIgpEGVLAGKTRVLVTHGISFLPQT-DFIIVLAGGQV 828
Cdd:cd03230 136 ELLR--ELKKEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
632-840 |
1.68e-17 |
|
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: 83.70 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 632 TFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSVAYVPQQAWiQNCTLQenVLFG 711
Cdd:COG1124 10 SYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA-FRRRVQ--MVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 712 QPM---NP-KRYQQALETCALLADLDvlpgGDQTEIGEK----GIN----------LSGGQRQRVSLARAVYSDANIFLL 773
Cdd:COG1124 87 DPYaslHPrHTVDRILAEPLRIHGLP----DREERIAELleqvGLPpsfldryphqLSGGQRQRVAIARALILEPELLLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 774 DDPLSAVDSHVAKHIFDqvigpegVLA------GKTRVLVTHG---ISFLpqTDFIIVLAGGQVSEMGHYSALLQH 840
Cdd:COG1124 163 DEPTSALDVSVQAEILN-------LLKdlreerGLTYLFVSHDlavVAHL--CDRVAVMQNGRIVEELTVADLLAG 229
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
642-832 |
1.87e-17 |
|
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: 82.69 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 642 TLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-----------SVAYVPQQ-AWIQNCTLQENVL 709
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppkdrDIAMVFQNyALYPHMTVYDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 710 FGQPMN-------PKRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDS 782
Cdd:cd03301 95 FGLKLRkvpkdeiDERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 783 HVAKHIFDQVIGPEGVLaGKTRVLVTHG-ISFLPQTDFIIVLAGGQVSEMG 832
Cdd:cd03301 164 KLRVQMRAELKRLQQRL-GTTTIYVTHDqVEAMTMADRIAVMNDGQIQQIG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1280-1501 |
1.97e-17 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 83.99 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1280 PTRGMVEFRNYSVRYRPGLE--LVLKNVTVHVQGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAEGEIVIDGLNVAHI 1353
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKST----LLRLIagleKPTSGEVLVDGKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1354 GlhdlrSQLTIIPQDPILFsgtlrmnldP---------FG--------RYSEEDIWRALELSHLNTFVSSQPAgldfqca 1416
Cdd:COG1116 79 G-----PDRGVVFQEPALL---------PwltvldnvaLGlelrgvpkAERRERARELLELVGLAGFEDAYPH------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1417 eggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLET-----DDLIQgtIRTQfEDCTVLTIAH------RLNtimd 1485
Cdd:COG1116 138 ----QLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTrerlqDELLR--LWQE-TGKTVLFVTHdvdeavFLA---- 206
|
250
....*....|....*....
gi 1388591336 1486 yNRVLVLDKG---VVAEFD 1501
Cdd:COG1116 207 -DRVVVLSARpgrIVEEID 224
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
643-832 |
2.20e-17 |
|
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: 82.94 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG----------------SVAYVPQQAwiQNC---- 702
Cdd:cd03257 21 LDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkirrkEIQMVFQDP--MSSlnpr 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 703 -TLQEnvLFGQPM---NPKRYQQALETCALLADLDVlpGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLS 778
Cdd:cd03257 99 mTIGE--QIAEPLrihGKLSKKEARKEAVLLLLVGV--GLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTS 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 779 AVDSHVAKHIFDqvigpegVLA------GKTRVLVTHGISFLPQ-TDFIIVLAGGQVSEMG 832
Cdd:cd03257 175 ALDVSVQAQILD-------LLKklqeelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1285-1497 |
2.64e-17 |
|
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: 82.19 E-value: 2.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNV--AHIGLHDLRSQL 1362
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1363 TIIPQDPILFSgtlRMN------LDP---FGRYSEEDIWRALELshLntfvssQPAGLDFQCAEGGDNLSVGQRQLVCLA 1433
Cdd:cd03262 79 GMVFQQFNLFP---HLTvlenitLAPikvKGMSKAEAEERALEL--L------EKVGLADKADAYPAQLSGGQQQRVAIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1434 RALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFED-CTVLTIAHRlntiMDY-----NRVLVLDKGVV 1497
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEgMTMVVVTHE----MGFarevaDRVIFMDDGRI 213
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1284-1501 |
3.87e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 86.62 E-value: 3.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYrPGLeLVLKNVTVHVQGGEKVGIVGRTGAGKSsmTL--CLFRILEAAEGEIVIDGLNV----------A 1351
Cdd:COG3845 5 ALELRGITKRF-GGV-VANDDVSLTVRPGEIHALLGENGAGKS--TLmkILYGLYQPDSGEILIDGKPVrirsprdaiaL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1352 HIGLhdlrsqltiIPQDPILFSG-TLRMNL------DPFGRYSEEDIWRAL-ELS-------HLNTFVSsqpagldfqca 1416
Cdd:COG3845 81 GIGM---------VHQHFMLVPNlTVAENIvlglepTKGGRLDRKAARARIrELSerygldvDPDAKVE----------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1417 eggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAI-DLETDDLIQgTIRtQF--EDCTVLTIAHRLNTIMDY-NRVLVL 1492
Cdd:COG3845 141 ----DLSVGEQQRVEILKALYRGARILILDEPTAVLtPQEADELFE-ILR-RLaaEGKSIIFITHKLREVMAIaDRVTVL 214
|
250
....*....|
gi 1388591336 1493 DKG-VVAEFD 1501
Cdd:COG3845 215 RRGkVVGTVD 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1285-1508 |
3.92e-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: 82.73 E-value: 3.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYrPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTI 1364
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1365 IPQDPILFSG-TLRMN--LDP-FGRYSEEDI-WRALELSHLntfVSSQPAGLdfqCAEGGDNLSVGQRQLVCLARALLRK 1439
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPkLLKWPKEKIrERADELLAL---VGLDPAEF---ADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388591336 1440 SRVLVLDEATAAIDLETDDLIQGTIRTQFEDC--TVLTIAHRLN-TIMDYNRVLVLDKGVVAEFDSPVNLIA 1508
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQELgkTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1285-1522 |
4.59e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 83.31 E-value: 4.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRIL---EAAEGEIVIDGLNVAHIGLHDLRSQ 1361
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1362 LTIIPQDPI-LFSGTLRMNLDPFGRYSeediwRALELSHLNTFVS---SQPAGLDFQCAEGGdNLSVGQRQLVCLARALL 1437
Cdd:PRK13640 86 VGIVFQNPDnQFVGATVGDDVAFGLEN-----RAVPRPEMIKIVRdvlADVGMLDYIDSEPA-NLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1438 RKSRVLVLDEATAAIDLETDDLIQGTIRTQFED--CTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNliaaggIFYG 1515
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnnLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVE------IFSK 233
|
....*....
gi 1388591336 1516 --MAKDAGL 1522
Cdd:PRK13640 234 veMLKEIGL 242
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1302-1498 |
4.86e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 83.17 E-value: 4.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1302 LKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVA--HIGLHDLRSQLTIIPQDP--ILFSGTLR 1377
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1378 MNLdPFG----RYSEEDI----WRALELshlntfvssqpAGLDFQCAEGGD--NLSVGQRQLVCLARALLRKSRVLVLDE 1447
Cdd:PRK13637 103 KDI-AFGpinlGLSEEEIenrvKRAMNI-----------VGLDYEDYKDKSpfELSGGQKRRVAIAGVVAMEPKILILDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1388591336 1448 ATAAIDLETDDLIQGTIRTQFE--DCTVLTIAHRLNTIMDY-NRVLVLDKGVVA 1498
Cdd:PRK13637 171 PTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKLaDRIIVMNKGKCE 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1284-1500 |
5.58e-17 |
|
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: 83.95 E-value: 5.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYRPGLELV--LKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEA---AEGEIVIDGLNVAHIGLHDL 1358
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1359 R----SQLTIIPQDPilfsgtlrMN-LDP--------------FGRYSEEDIW-RALEL----------SHLNTFvssqP 1408
Cdd:COG0444 81 RkirgREIQMIFQDP--------MTsLNPvmtvgdqiaeplriHGGLSKAEAReRAIELlervglpdpeRRLDRY----P 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1409 agldFQcaeggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLetddLIQGTI-------RTQFeDCTVLTIAHrln 1481
Cdd:COG0444 149 ----HE-------LSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQAQIlnllkdlQREL-GLAILFITH--- 209
|
250
....*....|....*....
gi 1388591336 1482 timdynrvlvlDKGVVAEF 1500
Cdd:COG0444 210 -----------DLGVVAEI 217
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
310-601 |
6.54e-17 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 82.98 E-value: 6.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 310 LLMSACFNLIQNLLGFVNPQLLSILI-RFISDPTAPT--WWGFLLAGLMFLSSTMQtlILHQYYHCIFV--MALRLRTAI 384
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIdDVIPAGDLSLllWIALLLLLLALLRALLS--YLRRYLAARLGqrVVFDLRRDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 385 igviYRKALVITNSVKRESTVGEMVNLMSVDAQRFMD-VSPFINLLWSAPLQVILAIYFL----WQIlgpsALAGVAVIV 459
Cdd:cd07346 79 ----FRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNlVSSGLLQLLSDVLTLIGALVILfylnWKL----TLVALLLLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 460 LLIPLNGAVSMKMKTYQVKQMKFKDSRIKLMSEILNGIKVLKLYAWEPS----FLEQVKGIRQSELQLLRKGAYLQAIST 535
Cdd:cd07346 151 LYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEReierFREANRDLRDANLRAARLSALFSPLIG 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 536 FIWICTPFLVTL----------ITLGVYVyvdesnvldaekAFvsLSLFNILKIPLNMLPQLISGLTQASVSLKRI 601
Cdd:cd07346 231 LLTALGTALVLLyggylvlqgsLTIGELV------------AF--LAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1284-1499 |
1.07e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 83.31 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYRPGLELV--LKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHI---GLHDL 1358
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1359 RSQLTIIPQDPILFSG-------TLRMNLDpfgRYSEEDIWRA----LELSHLNTFVSSQPAgldfqcaeggdNLSVGQR 1427
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSrtvfdnvALPLELA---GTPKAEIKARvtelLELVGLSDKADRYPA-----------QLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1428 QLVCLARALLRKSRVLVLDEATAAIDLETD----DLIQGTIRTQfeDCTVLTIAHRlntiMDY-----NRVLVLDKGVVA 1498
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPATTrsilELLKDINREL--GLTIVLITHE----MDVvkricDRVAVIDAGRLV 220
|
.
gi 1388591336 1499 E 1499
Cdd:PRK11153 221 E 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1284-1507 |
1.12e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 81.29 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNV--AHIGLHDLR-- 1359
Cdd:PRK09493 1 MIEFKNVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRqe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1360 -----SQLTIIPQ----DPILFsGTLRMNldpfGRYSEEDIWRALEL-------SHLNTFVSSqpagldfqcaeggdnLS 1423
Cdd:PRK09493 79 agmvfQQFYLFPHltalENVMF-GPLRVR----GASKEEAEKQARELlakvglaERAHHYPSE---------------LS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1424 VGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFED-CTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFD 1501
Cdd:PRK09493 139 GGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDG 218
|
....*.
gi 1388591336 1502 SPVNLI 1507
Cdd:PRK09493 219 DPQVLI 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1284-1499 |
1.26e-16 |
|
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: 81.24 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYRpGLElVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDlRSQLT 1363
Cdd:COG0411 4 LLEVRGLTKRFG-GLV-AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHR-IARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1364 I-----IPQdpiLFSG-TLRMNL------------------DPFGRYSEEDIW-RALELshLNTFvssqpaGLDFQCAEG 1418
Cdd:COG0411 81 IartfqNPR---LFPElTVLENVlvaaharlgrgllaallrLPRARREEREAReRAEEL--LERV------GLADRADEP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1419 GDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDL-ETDDLIQgTIRT--QFEDCTVLTIAHRLNTIMDY-NRVLVLDK 1494
Cdd:COG0411 150 AGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPeETEELAE-LIRRlrDERGITILLIEHDMDLVMGLaDRIVVLDF 228
|
....*.
gi 1388591336 1495 G-VVAE 1499
Cdd:COG0411 229 GrVIAE 234
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1284-1498 |
1.33e-16 |
|
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: 81.28 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSmtlcLFRILeAAE------GEIVI-----DGLNV-- 1350
Cdd:COG1119 3 LLELRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKST----LLSLI-TGDlpptygNDVRLfgerrGGEDVwe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1351 --AHIGL------HDLRSQLTIIpqDPIL--FSGTLrmnlDPFGRYSEEDIWRA------LELSHLntfvssqpAGLDFQ 1414
Cdd:COG1119 76 lrKRIGLvspalqLRFPRDETVL--DVVLsgFFDSI----GLYREPTDEQRERArellelLGLAHL--------ADRPFG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1415 caeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT--QFEDCTVLTIAHRLNTIMD-YNRVLV 1491
Cdd:COG1119 142 ------TLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPgITHVLL 215
|
....*...
gi 1388591336 1492 LDKG-VVA 1498
Cdd:COG1119 216 LKDGrVVA 223
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
643-828 |
1.43e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 81.21 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-------------SVAYVPQQAWI-QNCTLQENV 708
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLALLPQHHLTpEGITVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 709 LFGQ-PMNP----------KRYQQALEtcalladldvlpggdQTEIGE----KGINLSGGQRQRVSLARAVYSDANIFLL 773
Cdd:PRK11231 98 AYGRsPWLSlwgrlsaednARVNQAME---------------QTRINHladrRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388591336 774 DDPLSAVD-SHVAkhifdQVIGPEGVL--AGKTRVLVTHGISflpQT----DFIIVLAGGQV 828
Cdd:PRK11231 163 DEPTTYLDiNHQV-----ELMRLMRELntQGKTVVTVLHDLN---QAsrycDHLVVLANGHV 216
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1284-1508 |
1.47e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 80.57 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYrPGLELvlkNVTVHVQGGEKVGIVGRTGAGKSsmTLcLFRI---LEAAEGEIVIDGLNVAHIGLHDlRS 1360
Cdd:COG3840 1 MLRLDDLTYRY-GDFPL---RFDLTIAAGERVAILGPSGAGKS--TL-LNLIagfLPPDSGRILWNGQDLTALPPAE-RP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1361 qLTIIPQDPILFSG-TLRMN----LDPFGRYSEED---IWRALE---LSHLntfvssqpagLDFQCAEggdnLSVGQRQL 1429
Cdd:COG3840 73 -VSMLFQENNLFPHlTVAQNiglgLRPGLKLTAEQraqVEQALErvgLAGL----------LDRLPGQ----LSGGQRQR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1430 VCLARALLRKSRVLVLDEATAAID----LETDDLIQGTIRTQfeDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSPV 1504
Cdd:COG3840 138 VALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRER--GLTVLMVTHDPEDAARIaDRVLLVADGRIAADGPTA 215
|
....
gi 1388591336 1505 NLIA 1508
Cdd:COG3840 216 ALLD 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1285-1503 |
1.97e-16 |
|
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: 79.82 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYRPGLE--LVLKNVTVHVQGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAEGEIVIDGLNVAhiglhDL 1358
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKST----LLRIIagleRPTSGEVLVDGEPVT-----GP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1359 RSQLTIIPQDPILFS----------GtLRMNLDPFGRySEEDIWRALELSHLNTFVSSQPAgldfqcaeggdNLSVGQRQ 1428
Cdd:cd03293 72 GPDRGYVFQQDALLPwltvldnvalG-LELQGVPKAE-ARERAEELLELVGLSGFENAYPH-----------QLSGGMRQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1429 LVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTI-----RTQFedcTVLTIAHRLN-TIMDYNRVLVLDKG---VVAE 1499
Cdd:cd03293 139 RVALARALAVDPDVLLLDEPFSALDALTREQLQEELldiwrETGK---TVLLVTHDIDeAVFLADRVVVLSARpgrIVAE 215
|
....
gi 1388591336 1500 FDSP 1503
Cdd:cd03293 216 VEVD 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1284-1508 |
2.40e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.19 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYRPGLElVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIG-LHDLRSQL 1362
Cdd:PRK13644 1 MIRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1363 TIIPQDPilfsgtlrmNLDPFGRYSEEDIwrALELSHLNTFVSSQPAGLDFQCAEGG---------DNLSVGQRQLVCLA 1433
Cdd:PRK13644 80 GIVFQNP---------ETQFVGRTVEEDL--AFGPENLCLPPIEIRKRVDRALAEIGlekyrhrspKTLSGGQGQCVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 1434 RALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDC-TVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIA 1508
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
641-836 |
2.53e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 79.45 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEmekLEGVVSVKGSV-----------------AYVPQQAWI-QNC 702
Cdd:COG4136 15 PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGT---LSPAFSASGEVllngrrltalpaeqrriGILFQDDLLfPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 703 TLQENVLFGQPMNPKRYQQALETCALLADLDvLPGgdqteIGEKGIN-LSGGQRQRVSLARAVYSDANIFLLDDPLSAVD 781
Cdd:COG4136 92 SVGENLAFALPPTIGRAQRRARVEQALEEAG-LAG-----FADRDPAtLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388591336 782 SHVAKHI----FDQVigpegvlagKTR----VLVTHGISflpqtDfiiVLAGGQVSEMGHYSA 836
Cdd:COG4136 166 AALRAQFrefvFEQI---------RQRgipaLLVTHDEE-----D---APAAGRVLDLGNWQH 211
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
625-825 |
2.79e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 80.70 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 625 AITIHNGTFTWaQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGS----------VAYVP 694
Cdd:PRK15056 6 GIVVNDVTVTW-RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 695 QQA---WIQNCTLQENVLFGQPMN------PKRYQQALETCALlADLDVLPGgDQTEIGEkginLSGGQRQRVSLARAVY 765
Cdd:PRK15056 85 QSEevdWSFPVLVEDVVMMGRYGHmgwlrrAKKRDRQIVTAAL-ARVDMVEF-RHRQIGE----LSGGQKKRVFLARAIA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 766 SDANIFLLDDPLSAVDSHVAKHIFDQVigPEGVLAGKTRVLVTHGISFLPQ-TDFIIVLAG 825
Cdd:PRK15056 159 QQGQVILLDEPFTGVDVKTEARIISLL--RELRDEGKTMLVSTHNLGSVTEfCDYTVMVKG 217
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
1008-1256 |
3.34e-16 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 80.91 E-value: 3.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1008 LGVYAALGILQGLLVMLSAFTMVVGAIQAARLLHEALlHNKI-RSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILML 1086
Cdd:cd18547 48 LLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDL-FEKLqRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1087 LNSFFTSIST-IMVIVASTPLFMVVVLPLAVLYGFV-------QRFYVATSRQLKRLEsisrspifSHFSETVTGTSVIR 1158
Cdd:cd18547 127 ISSILTIVGTlIMMLYISPLLTLIVLVTVPLSLLVTkfiakrsQKYFRKQQKALGELN--------GYIEEMISGQKVVK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1159 AYGR----IQDFKVLSDTKVDNNQKSSypYIAS--NRWLGvhveFVGN----CVVLFAALFAVigRNSLNPGLVGLSVSY 1228
Cdd:cd18547 199 AFNReeeaIEEFDEINEELYKASFKAQ--FYSGllMPIMN----FINNlgyvLVAVVGGLLVI--NGALTVGVIQAFLQY 270
|
250 260
....*....|....*....|....*...
gi 1388591336 1229 ALQVTMALNWMIRMISDLESNIIAVERV 1256
Cdd:cd18547 271 SRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1302-1495 |
3.55e-16 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 79.30 E-value: 3.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1302 LKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQ----LTIIPQDPILFSGTLR 1377
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1378 MNLdPFGRYSEEDIWRAL-ELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLE- 1455
Cdd:cd03290 97 ENI-TFGSPFNKQRYKAVtDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHl 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1388591336 1456 TDDLIQGTIRTQFED--CTVLTIAHRLNTIMDYNRVLVLDKG 1495
Cdd:cd03290 176 SDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
1008-1256 |
3.64e-16 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 80.67 E-value: 3.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1008 LGVYAALGILQGLLVMLSAFTMVVGAIQAARLLHEALLHNKIRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLL 1087
Cdd:cd07346 42 ALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1088 NSFFTSI-STIMVIVASTPLFMVVVLPLAVLYGFVQRFYVATSRQLKRL-ESISRspIFSHFSETVTGTSVIRAYGR--- 1162
Cdd:cd07346 122 SDVLTLIgALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVrESLAE--LSAFLQESLSGIRVVKAFAAeer 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1163 -IQDFKVLSDTKVDNNQKSSYPYIASNRWLGVHVEFVGNCVVLFAALFavIGRNSLNPGLVGLSVSYALQVTMALNWMIR 1241
Cdd:cd07346 200 eIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYL--VLQGSLTIGELVAFLAYLGMLFGPIQRLAN 277
|
250
....*....|....*
gi 1388591336 1242 MISDLESNIIAVERV 1256
Cdd:cd07346 278 LYNQLQQALASLERI 292
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1302-1509 |
3.84e-16 |
|
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: 83.58 E-value: 3.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1302 LKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRiLEAAEGEIVIDGLNVAHIG---LHDLRSQLTIIPQDPilFsGTL-- 1376
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--F-GSLsp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1377 RMN---------------LDPFGRysEEDIWRALElshlntfvssqPAGLDFQCA-----EggdnLSVGQRQLVCLARAL 1436
Cdd:COG4172 378 RMTvgqiiaeglrvhgpgLSAAER--RARVAEALE-----------EVGLDPAARhryphE----FSGGQRQRIAIARAL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1437 LRKSRVLVLDEATAAIDLetddliqgTIRTQfedctVLT---------------IAHRLnTIMDY--NRVLVLDKGVVAE 1499
Cdd:COG4172 441 ILEPKLLVLDEPTSALDV--------SVQAQ-----ILDllrdlqrehglaylfISHDL-AVVRAlaHRVMVMKDGKVVE 506
|
250 260
....*....|....*....|..
gi 1388591336 1500 -------FDSPVN-----LIAA 1509
Cdd:COG4172 507 qgpteqvFDAPQHpytraLLAA 528
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1304-1503 |
3.96e-16 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 81.32 E-value: 3.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1304 NVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIG---LHDLRSQLTIIPQDPilfSGTL--RM 1378
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP---YASLnpRM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1379 N--------LDPFGRYSEEDIW-RALEL--------SHLNTFvssqPAgldfqcaEggdnLSVGQRQLVCLARALLRKSR 1441
Cdd:COG4608 113 TvgdiiaepLRIHGLASKAERReRVAELlelvglrpEHADRY----PH-------E----FSGGQRQRIGIARALALNPK 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591336 1442 VLVLDEATAAIDLEtddlIQGTIRTQFED------CTVLTIAHRLNT---IMDynRVLVLDKGVVAE-------FDSP 1503
Cdd:COG4608 178 LIVCDEPVSALDVS----IQAQVLNLLEDlqdelgLTYLFISHDLSVvrhISD--RVAVMYLGKIVEiaprdelYARP 249
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
626-781 |
4.79e-16 |
|
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: 79.53 E-value: 4.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 626 ITIHNGTFTWAQDLPpTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGS---------------- 689
Cdd:cd03256 1 IEVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 690 VAYVPQQ-AWIQNCTLQENVLFG------------QPMNPKRYQQALEtcaLLADLDVLPGGDQteigeKGINLSGGQRQ 756
Cdd:cd03256 80 IGMIFQQfNLIERLSVLENVLSGrlgrrstwrslfGLFPKEEKQRALA---ALERVGLLDKAYQ-----RADQLSGGQQQ 151
|
170 180
....*....|....*....|....*
gi 1388591336 757 RVSLARAVYSDANIFLLDDPLSAVD 781
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLD 176
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
625-790 |
6.18e-16 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 79.33 E-value: 6.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 625 AITIHNGTFTWAQDlPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG---------------- 688
Cdd:COG3638 2 MLELRNLSKRYPGG-TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGqdvtalrgralrrlrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 689 SVAYVPQQ-AWIQNCTLQENVLFGQ-----------PMNPKR-YQQALEtcaLLADLDVLPGGDQteigeKGINLSGGQR 755
Cdd:COG3638 81 RIGMIFQQfNLVPRLSVLTNVLAGRlgrtstwrsllGLFPPEdRERALE---ALERVGLADKAYQ-----RADQLSGGQQ 152
|
170 180 190
....*....|....*....|....*....|....*
gi 1388591336 756 QRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFD 790
Cdd:COG3638 153 QRVAIARALVQEPKLILADEPVASLDPKTARQVMD 187
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1284-1503 |
6.39e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 79.80 E-value: 6.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLT 1363
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1364 IIPQDPI-LFSGT---------LRMNLDPFGRYSEEdIWRALELSHLNTFVSSQPagldfqcaeggDNLSVGQRQLVCLA 1433
Cdd:PRK13648 87 IVFQNPDnQFVGSivkydvafgLENHAVPYDEMHRR-VSEALKQVDMLERADYEP-----------NALSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388591336 1434 RALLRKSRVLVLDEATAAIDLET-DDLIQGTIRTQFE-DCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSP 1503
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDArQNLLDLVRKVKSEhNITIISITHDLSEAMEADHVIVMNKGTVYKEGTP 226
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
641-809 |
9.33e-16 |
|
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: 77.83 E-value: 9.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-SVAYVPQQA----------------WIQNCT 703
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqDVSDLRGRAipylrrkigvvfqdfrLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 704 LQENVLF-----GQPMN--PKRYQQALETCALLADLDVLPGGdqteigekginLSGGQRQRVSLARAVYSDANIFLLDDP 776
Cdd:cd03292 95 VYENVAFalevtGVPPReiRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190
....*....|....*....|....*....|....
gi 1388591336 777 LSAVDSHVAKHIFDQVigpEGV-LAGKTRVLVTH 809
Cdd:cd03292 164 TGNLDPDTTWEIMNLL---KKInKAGTTVVVATH 194
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1285-1497 |
9.98e-16 |
|
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: 77.83 E-value: 9.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYrPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHigLHD-----LR 1359
Cdd:cd03292 1 IEFINVTKTY-PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSD--LRGraipyLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1360 SQLTIIPQDPILFSG---------TLRMNLDPfGRYSEEDIWRALELSHLNTFVSSQPAGldfqcaeggdnLSVGQRQLV 1430
Cdd:cd03292 78 RKIGVVFQDFRLLPDrnvyenvafALEVTGVP-PREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1431 CLARALLRKSRVLVLDEATAAIDLETDDLIQgTIRTQFED--CTVLTIAHRLNTIMDYN-RVLVLDKGVV 1497
Cdd:cd03292 146 AIARAIVNSPTILIADEPTGNLDPDTTWEIM-NLLKKINKagTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
646-836 |
1.24e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 80.46 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 646 LNIQIPKGALVAVVGPVGCGKSSLVSALLGemekLEGVVS---------------VKGSVAYVPQQ-AWIQNCTLQENVL 709
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAG----LEDITSgdlfigekrmndvppAERGVGMVFQSyALYPHLSVAENMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 710 FG-------QPMNPKRYQQALETCALLADLDVLPGGdqteigekginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD- 781
Cdd:PRK11000 98 FGlklagakKEEINQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDa 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388591336 782 ----------SHVAKHIfdqvigpegvlaGKTRVLVTHG-ISFLPQTDFIIVLAGGQVSEMG------HYSA 836
Cdd:PRK11000 167 alrvqmrieiSRLHKRL------------GRTMIYVTHDqVEAMTLADKIVVLDAGRVAQVGkplelyHYPA 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1287-1497 |
1.24e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 81.65 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1287 FRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAEGEIVID-GLNVAHiglhdlrsq 1361
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKST----LLKILagelEPDSGEVSIPkGLRIGY--------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1362 ltiIPQDPILFSG-----TLRMNLDPFGR-------------YSEEDIWRALELSH---------LNTFVSSQPAGLDFQ 1414
Cdd:COG0488 66 ---LPQEPPLDDDltvldTVLDGDAELRAleaeleeleaklaEPDEDLERLAELQEefealggweAEARAEEILSGLGFP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1415 CAEGG---DNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTqfEDCTVLTIAH-R--LNTIMdyNR 1488
Cdd:COG0488 143 EEDLDrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN--YPGTVLVVSHdRyfLDRVA--TR 218
|
....*....
gi 1388591336 1489 VLVLDKGVV 1497
Cdd:COG0488 219 ILELDRGKL 227
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1284-1495 |
1.25e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 78.59 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYRPGLEL---VLKNVTVHVQGGEKVGIVGRTGAGKSSmtlcLFRI----LEAAEGEIVIDGLNVAHIGLH 1356
Cdd:COG1101 1 MLELKNLSKTFNPGTVNekrALDGLNLTIEEGDFVTVIGSNGAGKST----LLNAiagsLPPDSGSILIDGKDVTKLPEY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1357 DlRSQLtI--IPQDPILfsGT---------------------LRMNLDPfgrySEEDIWRA----LELS---HLNTfvss 1406
Cdd:COG1101 77 K-RAKY-IgrVFQDPMM--GTapsmtieenlalayrrgkrrgLRRGLTK----KRRELFREllatLGLGlenRLDT---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1407 qPAGLdfqcaeggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAID-------LE-TDDLIQGtirtqfEDCTVLTIAH 1478
Cdd:COG1101 145 -KVGL----------LSGGQRQALSLLMATLTKPKLLLLDEHTAALDpktaalvLElTEKIVEE------NNLTTLMVTH 207
|
250
....*....|....*...
gi 1388591336 1479 RLNTIMDY-NRVLVLDKG 1495
Cdd:COG1101 208 NMEQALDYgNRLIMMHEG 225
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1284-1450 |
1.36e-15 |
|
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: 77.71 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDL-RSQL 1362
Cdd:COG0410 3 MLEVENLHAGY--GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1363 TIIPQDPILFSG-TLRMNLD------PFGRYSEEDIWRALELshlntF-----VSSQPAGldfqcaeggdNLSVGQRQLV 1430
Cdd:COG0410 81 GYVPEGRRIFPSlTVEENLLlgayarRDRAEVRADLERVYEL-----FprlkeRRRQRAG----------TLSGGEQQML 145
|
170 180
....*....|....*....|
gi 1388591336 1431 CLARALLRKSRVLVLDEATA 1450
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPSL 165
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1284-1503 |
2.26e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 77.89 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAEGEIVIDGLNVAHIGLHDLR 1359
Cdd:PRK13548 2 MLEARNLSVRL--GGRTLLDDVSLTLRPGEVVAILGPNGAGKST----LLRALsgelSPDSGEVRLNGRPLADWSPAELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1360 SQLTIIPQDPIL-FSGT----LRMNLDPFGRYSEED---IWRALE---LSHLntfvssqpAGLDFQcaeggdNLSVGQRQ 1428
Cdd:PRK13548 76 RRRAVLPQHSSLsFPFTveevVAMGRAPHGLSRAEDdalVAAALAqvdLAHL--------AGRDYP------QLSGGEQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1429 LVCLARALLR------KSRVLVLDEATAAIDL----ETDDLIQGtiRTQFEDCTVLTIAHRLN-TIMDYNRVLVLDKGVV 1497
Cdd:PRK13548 142 RVQLARVLAQlwepdgPPRWLLLDEPTSALDLahqhHVLRLARQ--LAHERGLAVIVVLHDLNlAARYADRIVLLHQGRL 219
|
....*.
gi 1388591336 1498 AEFDSP 1503
Cdd:PRK13548 220 VADGTP 225
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1301-1492 |
2.54e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 75.73 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1301 VLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGlnvaHIGLHDLRSQLTIIPQDPILFSGTLRMNL 1380
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVPQRSEVPDSLPLTVRDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1381 ----DPFGRYSEED---IWRALELSHLNTFvssqpAGLDFqcaeggDNLSVGQRQLVCLARALLRKSRVLVLDEATAAID 1453
Cdd:NF040873 83 warrGLWRRLTRDDraaVDDALERVGLADL-----AGRQL------GELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1388591336 1454 LETDDLIQGTIRTQFED-CTVLTIAHRLNTIMDYNRVLVL 1492
Cdd:NF040873 152 AESRERIIALLAEEHARgATVVVVTHDLELVRRADPCVLL 191
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1284-1512 |
3.06e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.89 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLT 1363
Cdd:PRK09536 3 MIDVSDLSVEF--GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1364 IIPQDPIL---FSG--TLRMNLDP----FGRYSEED---IWRALELSHLNTFVSsQPAgldfqcaeggDNLSVGQRQLVC 1431
Cdd:PRK09536 81 SVPQDTSLsfeFDVrqVVEMGRTPhrsrFDTWTETDraaVERAMERTGVAQFAD-RPV----------TSLSGGERQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1432 LARALLRKSRVLVLDEATAAIDL----ETDDLIQgtiRTQFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSPVNL 1506
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDInhqvRTLELVR---RLVDDGKTAVAAIHDLDLAARYcDELVLLADGRVRAAGPPADV 226
|
....*.
gi 1388591336 1507 IAAGGI 1512
Cdd:PRK09536 227 LTADTL 232
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1285-1503 |
3.31e-15 |
|
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: 76.99 E-value: 3.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSmtlcLFRI---LEAA-EGEIVIDGLNVAHIGLHDlrS 1360
Cdd:cd03296 3 IEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTT----LLRLiagLERPdSGTILFGGEDATDVPVQE--R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1361 QLTIIPQDPILFSG-TLRMNLdPFG--------RYSEEDIWRA----LELSHLNTFVSSQPAgldfqcaeggdNLSVGQR 1427
Cdd:cd03296 75 NVGFVFQHYALFRHmTVFDNV-AFGlrvkprseRPPEAEIRAKvhelLKLVQLDWLADRYPA-----------QLSGGQR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388591336 1428 QLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTI--AHRLNTIMDY-NRVLVLDKGVVAEFDSP 1503
Cdd:cd03296 143 QRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVfvTHDQEEALEVaDRVVVMNKGRIEQVGTP 221
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
625-832 |
3.41e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 77.38 E-value: 3.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 625 AITIHNGTFTWaqDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSAlLGEMEKLEGVVSVKGSVAYVPQQAWIQNCTL 704
Cdd:PRK14258 7 AIKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQNIYERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 705 Q---------------------ENVLFGQPM---NPK-RYQQALETCALLADL-DVLpggdQTEIGEKGINLSGGQRQRV 758
Cdd:PRK14258 84 NrlrrqvsmvhpkpnlfpmsvyDNVAYGVKIvgwRPKlEIDDIVESALKDADLwDEI----KHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 759 SLARAVYSDANIFLLDDPLSAVDShVAKHIFDQVIGPEGVLAGKTRVLVTHGisfLPQ----TDFIIVLAG-----GQVS 829
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDP-IASMKVESLIQSLRLRSELTMVIVSHN---LHQvsrlSDFTAFFKGnenriGQLV 235
|
...
gi 1388591336 830 EMG 832
Cdd:PRK14258 236 EFG 238
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
626-832 |
3.85e-15 |
|
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: 77.47 E-value: 3.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 626 ITIHNGTFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSVAYVPQQAW------- 698
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeirkkvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 699 --IQN-------CTLQENVLFGqPMN--------PKRYQQALETCALLADLDVLPggdqteigekgINLSGGQRQRVSLA 761
Cdd:TIGR04520 81 mvFQNpdnqfvgATVEDDVAFG-LENlgvpreemRKRVDEALKLVGMEDFRDREP-----------HLLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 762 RAVYSDANIFLLDDPLSAVDshvakhifdqvigPEG---VLA---------GKTRVLVTHGISFLPQTDFIIVLAGGQVS 829
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLD-------------PKGrkeVLEtirklnkeeGITVISITHDMEEAVLADRVIVMNKGKIV 215
|
...
gi 1388591336 830 EMG 832
Cdd:TIGR04520 216 AEG 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
626-833 |
4.65e-15 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 75.86 E-value: 4.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 626 ITIHNGTFTWAQDlPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEmEKL-EGVVSVKG---------SVAY--- 692
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGE-ERPtSGQVLVNGqdlsrlkrrEIPYlrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 693 ----VPQQAW-IQNCTLQENVLFgqPM-----NPKRYQQ----ALETCALLADLDVLPggdqteigekgINLSGGQRQRV 758
Cdd:COG2884 80 rigvVFQDFRlLPDRTVYENVAL--PLrvtgkSRKEIRRrvreVLDLVGLSDKAKALP-----------HELSGGEQQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 759 SLARAVYSDANIFLLDDPLSAVDSHVAKHIFDqvigpegVL-----AGKTRVLVTHGISFLPQTDF-IIVLAGGQVSEMG 832
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEIME-------LLeeinrRGTTVLIATHDLELVDRMPKrVLELEDGRLVRDE 219
|
.
gi 1388591336 833 H 833
Cdd:COG2884 220 A 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1284-1498 |
6.05e-15 |
|
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: 75.48 E-value: 6.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYRP--GLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLhDLRSQ 1361
Cdd:cd03266 1 MITADALTKRFRDvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPA-EARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1362 LTIIPQDPILFSG-TLRMNLDPFGRY----------SEEDIWRALELSHLntfvssqpagLDFQCAEggdnLSVGQRQLV 1430
Cdd:cd03266 80 LGFVSDSTGLYDRlTARENLEYFAGLyglkgdeltaRLEELADRLGMEEL----------LDRRVGG----FSTGMRQKV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1431 CLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFED-CTVLTIAHRLNTIMDY-NRVLVLDKGVVA 1498
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERLcDRVVVLHRGRVV 215
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
643-830 |
6.19e-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: 75.93 E-value: 6.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGemekLE----GVVSVKG-----------------SVAYVpQQAW--I 699
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAG----LDrptsGTVRLAGqdlfaldedararlrarHVGFV-FQSFqlL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 700 QNCTLQENV-----LFGQPMNPKRYQQALETCALLADLDVLPGGdqteigekginLSGGQRQRVSLARAVYSDANIFLLD 774
Cdd:COG4181 103 PTLTALENVmlpleLAGRRDARARARALLERVGLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAILFAD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388591336 775 DPLSAVDSHVAKHIFDqvigpegvL-------AGKTRVLVTHGISFLPQTDFIIVLAGGQVSE 830
Cdd:COG4181 172 EPTGNLDAATGEQIID--------LlfelnreRGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
644-785 |
7.73e-15 |
|
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: 75.02 E-value: 7.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 644 HSLNIQIP-KGALVAVVGPVGCGKSSLVSALLGeMEKLE-GVVSVKGS-----------------VAYVPQQ-AWIQNCT 703
Cdd:cd03297 13 FTLKIDFDlNEEVTGIFGASGAGKSTLLRCIAG-LEKPDgGTIVLNGTvlfdsrkkinlppqqrkIGLVFQQyALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 704 LQENVLFGQPMNPKRYQQALETcALLADLDVlpggdqTEIGEKGI-NLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDS 782
Cdd:cd03297 92 VRENLAFGLKRKRNREDRISVD-ELLDLLGL------DHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
...
gi 1388591336 783 HVA 785
Cdd:cd03297 165 ALR 167
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
643-841 |
7.73e-15 |
|
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: 75.80 E-value: 7.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG----------------SVAYVPQQ-AWIQNCTLQ 705
Cdd:TIGR02315 18 LKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGtditklrgkklrklrrRIGMIFQHyNLIERLTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 706 ENVLFG------------QPMNPKRYQQALEtcaLLADLDVLPGGDQteigeKGINLSGGQRQRVSLARAVYSDANIFLL 773
Cdd:TIGR02315 98 ENVLHGrlgykptwrsllGRFSEEDKERALS---ALERVGLADKAYQ-----RADQLSGGQQQRVAIARALAQQPDLILA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 774 DDPLSAVDSHVAKHIFDQV--IGPEgvlAGKTRVLVTHGISFLPQ-TDFIIVLAGGQVSEMGHYSALLQHD 841
Cdd:TIGR02315 170 DEPIASLDPKTSKQVMDYLkrINKE---DGITVIINLHQVDLAKKyADRIVGLKAGEIVFDGAPSELDDEV 237
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1295-1503 |
8.22e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 78.54 E-value: 8.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1295 RPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLR-----------SQLT 1363
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrkkiamvfQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1364 IIPQDPILFSGTLRMNLDpfGRYSEEDIWRALElshlntfvSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVL 1443
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELA--GINAEERREKALD--------ALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 1444 VLDEATAAID--LET---DDLIQGTIRTQFedcTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSP 1503
Cdd:PRK10070 187 LMDEAFSALDplIRTemqDELVKLQAKHQR---TIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTP 249
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1285-1507 |
8.70e-15 |
|
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: 75.45 E-value: 8.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYRpglELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAhiGLHDLRSQLTI 1364
Cdd:cd03299 1 LKVENLSKDWK---EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1365 IPQDPILFSGT---------LRMNLDPFGRYSEE--DIWRALELSHLntfVSSQPAgldfqcaeggdNLSVGQRQLVCLA 1433
Cdd:cd03299 76 VPQNYALFPHMtvykniaygLKKRKVDKKEIERKvlEIAEMLGIDHL---LNRKPE-----------TLSGGEQQRVAIA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591336 1434 RALLRKSRVLVLDEATAAIDLETDDLIQ---GTIRTQFeDCTVLTIAHRLNTI-MDYNRVLVLDKGVVAEFDSPVNLI 1507
Cdd:cd03299 142 RALVVNPKILLLDEPFSALDVRTKEKLReelKKIRKEF-GVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1284-1506 |
9.13e-15 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 77.45 E-value: 9.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSsmTLClfRIL----EAAEGEIVIDGLNVAHIGLHDlR 1359
Cdd:COG3842 5 ALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKT--TLL--RMIagfeTPDSGRILLDGRDVTGLPPEK-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1360 sQLTIIPQDPILFsgtlrmnldP---------FG----RYSEEDIWR----ALELSHLNTFVSSQPagldfqcaeggDNL 1422
Cdd:COG3842 78 -NVGMVFQDYALF---------PhltvaenvaFGlrmrGVPKAEIRArvaeLLELVGLEGLADRYP-----------HQL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1423 SVGQRQLVCLARALLRKSRVLVLDEATAAIDLETddliqgTIRTQFEdctVLTIAHRLN--TIM------------DynR 1488
Cdd:COG3842 137 SGGQQQRVALARALAPEPRVLLLDEPLSALDAKL------REEMREE---LRRLQRELGitFIYvthdqeealalaD--R 205
|
250
....*....|....*...
gi 1388591336 1489 VLVLDKGVVAEFDSPVNL 1506
Cdd:COG3842 206 IAVMNDGRIEQVGTPEEI 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1284-1497 |
9.22e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 76.43 E-value: 9.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYRPGLElVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDG--LNVAHIGLHDLRSQ 1361
Cdd:PRK13636 5 ILKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1362 LTIIPQDP--ILFSGTLR-------MNLDPFGRYSEEDIWRALE---LSHLNtfvsSQPAgldfQCaeggdnLSVGQRQL 1429
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYqdvsfgaVNLKLPEDEVRKRVDNALKrtgIEHLK----DKPT----HC------LSFGQKKR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 1430 VCLARALLRKSRVLVLDEATAAID-LETDDLIQGTIRTQFE-DCTVLTIAHRLNTIMDY-NRVLVLDKGVV 1497
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDpMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYcDNVFVMKEGRV 220
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
641-830 |
9.56e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 75.89 E-value: 9.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSVAYVP---------QQAWIQNCTLQENVLFG 711
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPgaergvvfqNEGLLPWRNVQDNVAFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 712 QPM----NPKRYQQALEtcaLLADLDvLPGGDQTEIGEkginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDShvakh 787
Cdd:PRK11248 95 LQLagveKMQRLEIAHQ---MLKKVG-LEGAEKRYIWQ----LSGGQRQRVGIARALAANPQLLLLDEPFGALDA----- 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1388591336 788 iFDQVIGPEGVL-----AGKTRVLVTHGIS---FLpQTDFIIVLAG-GQVSE 830
Cdd:PRK11248 162 -FTREQMQTLLLklwqeTGKQVLLITHDIEeavFM-ATELVLLSPGpGRVVE 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
647-848 |
1.42e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 74.79 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 647 NIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-SVAYVP----------QQawiQNC----TLQENVLFG 711
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqDLTALPpaerpvsmlfQE---NNLfphlTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 712 qpMNP---------KRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDS 782
Cdd:COG3840 96 --LRPglkltaeqrAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388591336 783 hvAK-----HIFDQVIGPEGVlagkTRVLVTHGIS-FLPQTDFIIVLAGGQVSEMGHYSALLQHDGS--FANFL 848
Cdd:COG3840 163 --ALrqemlDLVDELCRERGL----TVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALLDGEPPpaLAAYL 230
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
643-828 |
1.80e-14 |
|
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: 74.10 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSVAYVPQQAWIQ----------------NCTLQE 706
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElrqkvgmvfqqfnlfpHLTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 707 NVLFG----QPMNPK----RYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLS 778
Cdd:cd03262 96 NITLApikvKGMSKAeaeeRALELLEKVGLADKADAYPA-----------QLSGGQQQRVAIARALAMNPKVMLFDEPTS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1388591336 779 AVDSHVAKHIFDQVIGpegvLA--GKTRVLVTHGISFLPQ-TDFIIVLAGGQV 828
Cdd:cd03262 165 ALDPELVGEVLDVMKD----LAeeGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
643-809 |
2.05e-14 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 76.68 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGeMEKL-EGVVSVKG-----------SVAYVPQQ-AWIQNCTLQENVL 709
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAG-FETPdSGRILLDGrdvtglppekrNVGMVFQDyALFPHLTVAENVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 710 FG---QPMNP----KRYQQALETCALLADLDVLPggDQteigekginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDS 782
Cdd:COG3842 100 FGlrmRGVPKaeirARVAELLELVGLEGLADRYP--HQ---------LSGGQQQRVALARALAPEPRVLLLDEPLSALDA 168
|
170 180 190
....*....|....*....|....*....|....
gi 1388591336 783 HVA-------KHIFDQVigpegvlaGKTRVLVTH 809
Cdd:COG3842 169 KLReemreelRRLQREL--------GITFIYVTH 194
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1284-1447 |
2.10e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 74.73 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLT 1363
Cdd:COG4604 1 MIEIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1364 IIPQDPILfsgTLRM---NLDPFGRY-------SEED---IWRA---LELSHL-NTFVssqpagldfqcaeggDNLSVGQ 1426
Cdd:COG4604 79 ILRQENHI---NSRLtvrELVAFGRFpyskgrlTAEDreiIDEAiayLDLEDLaDRYL---------------DELSGGQ 140
|
170 180
....*....|....*....|.
gi 1388591336 1427 RQLVCLARALLRKSRVLVLDE 1447
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDE 161
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1284-1499 |
2.25e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 74.67 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLT 1363
Cdd:PRK11231 2 TLRTENLTVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1364 IIPQDPILFSG-TLR----------MNLdpFGRYSEED---IWRALELSHLNTFVsSQPAgldfqcaeggDNLSVGQRQL 1429
Cdd:PRK11231 80 LLPQHHLTPEGiTVRelvaygrspwLSL--WGRLSAEDnarVNQAMEQTRINHLA-DRRL----------TDLSGGQRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 1430 VCLARALLRKSRVLVLDEATAAIDL----ETDDLIQgtiRTQFEDCTVLTIAHRLNTIMDY-NRVLVLDKG-VVAE 1499
Cdd:PRK11231 147 AFLAMVLAQDTPVVLLDEPTTYLDInhqvELMRLMR---ELNTQGKTVVTVLHDLNQASRYcDHLVVLANGhVMAQ 219
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
658-832 |
2.26e-14 |
|
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: 75.99 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 658 VVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-SVAYVPQQ-----------AWIQNCTLQENVLFGQPMN--PK-----R 718
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGeDVTNVPPHlrhinmvfqsyALFPHMTVEENVAFGLKMRkvPRaeikpR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 719 YQQALETCALladldvlpggdQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGPEGV 798
Cdd:TIGR01187 81 VLEALRLVQL-----------EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQ 149
|
170 180 190
....*....|....*....|....*....|....*
gi 1388591336 799 LaGKTRVLVTHGIS-FLPQTDFIIVLAGGQVSEMG 832
Cdd:TIGR01187 150 L-GITFVFVTHDQEeAMTMSDRIAIMRKGKIAQIG 183
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
643-832 |
2.53e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 74.49 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSAL-----LGEMEKLEGVVSVKGSVAYVPQQAWIQ----------------N 701
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPIEvrrevgmvfqypnpfpH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 702 CTLQENVLFGQPMN---------PKRYQQALETCALLADLdvlpggdQTEIGEKGINLSGGQRQRVSLARAVYSDANIFL 772
Cdd:PRK14267 100 LTIYDNVAIGVKLNglvkskkelDERVEWALKKAALWDEV-------KDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388591336 773 LDDPLSAVDSHVAKHIfdqvigPEGVLAGK---TRVLVTHGISFLPQ-TDFIIVLAGGQVSEMG 832
Cdd:PRK14267 173 MDEPTANIDPVGTAKI------EELLFELKkeyTIVLVTHSPAQAARvSDYVAFLYLGKLIEVG 230
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1301-1465 |
3.52e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 72.78 E-value: 3.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1301 VLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAhiglhdlrsQLTIIPQDPILFSG------ 1374
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA---------EQRDEPHENILYLGhlpglk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1375 ---TLRMNLD---PFGRYSEEDIWRALELSHLNTFvSSQPAGldfqcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEA 1448
Cdd:TIGR01189 86 pelSALENLHfwaAIHGGAQRTIEDALAAVGLTGF-EDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170
....*....|....*..
gi 1388591336 1449 TAAIDLETDDLIQGTIR 1465
Cdd:TIGR01189 155 TTALDKAGVALLAGLLR 171
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
643-832 |
5.88e-14 |
|
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: 76.48 E-value: 5.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG----------------SVAYVPQQAWIQ-NC--T 703
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkdltklsrrslrelrrRVQMVFQDPYSSlNPrmT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 704 LQENVLFG----QPMNPK----RYQQALETCALLAD-LDVLPGGdqteigekginLSGGQRQRVSLARAVYSDANIFLLD 774
Cdd:COG1123 361 VGDIIAEPlrlhGLLSRAerreRVAELLERVGLPPDlADRYPHE-----------LSGGQRQRVAIARALALEPKLLILD 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388591336 775 DPLSAVDSHVAKHIFDqvigpegVLA------GKTRVLVTHGISFLPQ-TDFIIVLAGGQVSEMG 832
Cdd:COG1123 430 EPTSALDVSVQAQILN-------LLRdlqrelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDG 487
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
643-786 |
6.41e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 75.12 E-value: 6.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGS-----------VAYVPQQ-AWIQNCTLQENVLF 710
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQHyALFRHMTVFDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 711 GQPMNPKRYQ-----------QALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSA 779
Cdd:PRK10851 98 GLTVLPRRERpnaaaikakvtQLLEMVQLAHLADRYPA-----------QLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
....*..
gi 1388591336 780 VDSHVAK 786
Cdd:PRK10851 167 LDAQVRK 173
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
641-840 |
6.60e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 73.20 E-value: 6.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSAlLGEMEKLEG---VV---SVKGSVA----------YVPQQAWI-QNCT 703
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRC-INKLEEITSgdlIVdglKVNDPKVderlirqeagMVFQQFYLfPHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 704 LQENVLFGqpmnPKR---------YQQALEtcaLLADLdvlpgGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLD 774
Cdd:PRK09493 94 ALENVMFG----PLRvrgaskeeaEKQARE---LLAKV-----GLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388591336 775 DPLSAVDSHVAKHIFD--QVIGPEGVlagkTRVLVTHGISFLPQT-DFIIVLAGGQVSEMGHYSALLQH 840
Cdd:PRK09493 162 EPTSALDPELRHEVLKvmQDLAEEGM----TMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1255-1501 |
7.83e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.26 E-value: 7.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1255 RVKEYSKTKTEAPWVVESN---RAPEGwPTRG--MVEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSmt 1329
Cdd:COG0488 282 RIKALEKLEREEPPRRDKTveiRFPPP-ERLGkkVLELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKST-- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1330 lcLFRIL----EAAEGEIVIdGLNVaHIG-----LHDLRSQLTII-------PQDPILFSGTL--RMNLDPfgryseEDI 1391
Cdd:COG0488 357 --LLKLLagelEPDSGTVKL-GETV-KIGyfdqhQEELDPDKTVLdelrdgaPGGTEQEVRGYlgRFLFSG------DDA 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1392 WralelshlnTFVSSqpagldfqcaeggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETddliqgtiRTQFEDC 1471
Cdd:COG0488 427 F---------KPVGV---------------LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET--------LEALEEA 474
|
250 260 270
....*....|....*....|....*....|....*....
gi 1388591336 1472 ------TVLTIAH-R--LNTIMDynRVLVLDKGVVAEFD 1501
Cdd:COG0488 475 lddfpgTVLLVSHdRyfLDRVAT--RILEFEDGGVREYP 511
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1307-1498 |
8.81e-14 |
|
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: 72.14 E-value: 8.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1307 VHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDlrSQLTIIPQDPILFSG-TLRMNLD---- 1381
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFAHlTVEQNVGlgls 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1382 PFGRYSEED---IWRALELSHLNTFVSSQPagldfqcaeggDNLSVGQRQLVCLARALLRKSRVLVLDEATAAID----L 1454
Cdd:cd03298 97 PGLKLTAEDrqaIEVALARVGLAGLEKRLP-----------GELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1388591336 1455 ETDDLIQGTIRTQfeDCTVLTIAHRLNTIMD-YNRVLVLDKGVVA 1498
Cdd:cd03298 166 EMLDLVLDLHAET--KMTVLMVTHQPEDAKRlAQRVVFLDNGRIA 208
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1296-1495 |
1.18e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.43 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1296 PGLElVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDlrSQ----------LTII 1365
Cdd:PRK10762 15 PGVK-ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKS--SQeagigiihqeLNLI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1366 PQDPI---LFSGtlRMNLDPFGR------YSEEDiwrALeLSHLN-TFVSSQPAGldfqcaeggdNLSVGQRQLVCLARA 1435
Cdd:PRK10762 92 PQLTIaenIFLG--REFVNRFGRidwkkmYAEAD---KL-LARLNlRFSSDKLVG----------ELSIGEQQMVEIAKV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388591336 1436 LLRKSRVLVLDEATAAI-DLETDDLIQgTIRT-QFEDCTVLTIAHRLNTIMDY-NRVLVLDKG 1495
Cdd:PRK10762 156 LSFESKVIIMDEPTDALtDTETESLFR-VIRElKSQGRGIVYISHRLKEIFEIcDDVTVFRDG 217
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
641-841 |
1.18e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.88 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-------------SVAYVPQQAWIQ-NCTLQE 706
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVASVPQDTSLSfEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 707 NVLFGQPMNPKRYQQALETCALLADlDVLPGGDQTEIGEKGI-NLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVA 785
Cdd:PRK09536 97 VVEMGRTPHRSRFDTWTETDRAAVE-RAMERTGVAQFADRPVtSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1388591336 786 KHIFDQVigPEGVLAGKTRVLVTHGISFLPQ-TDFIIVLAGGQVSEMGHYSALLQHD 841
Cdd:PRK09536 176 VRTLELV--RRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
643-848 |
1.20e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 72.35 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSAL-LGEMEKlEGVVSVKGS-------------------VAYVPQQ--AWiQ 700
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMPR-SGTLNIAGNhfdfsktpsdkairelrrnVGMVFQQynLW-P 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 701 NCTLQENvLFGQPMN------PKRYQQALEtcaLLADLDVLPGGDQTEIgekgiNLSGGQRQRVSLARAVYSDANIFLLD 774
Cdd:PRK11124 96 HLTVQQN-LIEAPCRvlglskDQALARAEK---LLERLRLKPYADRFPL-----HLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 775 DPLSAVDSHVAKHIFDqvIGPEGVLAGKTRVLVTHGISFLPQT-DFIIVLAGGQVSEMGHYSALLQ-HDGSFANFL 848
Cdd:PRK11124 167 EPTAALDPEITAQIVS--IIRELAETGITQVIVTHEVEVARKTaSRVVYMENGHIVEQGDASCFTQpQTEAFKNYL 240
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
646-832 |
1.24e-13 |
|
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: 71.76 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 646 LNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-SVAYVPQQAWIQNCTLQENVLF---------GQPMN 715
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvDVTAAPPADRPVSMLFQENNLFahltveqnvGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 716 PKRY-----QQALETCAL---LADLDV-LPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAK 786
Cdd:cd03298 97 PGLKltaedRQAIEVALArvgLAGLEKrLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1388591336 787 HIFDQVIGPEGVlAGKTRVLVTHGIS-FLPQTDFIIVLAGGQVSEMG 832
Cdd:cd03298 166 EMLDLVLDLHAE-TKMTVLMVTHQPEdAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
643-828 |
1.46e-13 |
|
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: 70.15 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGsvayvpqqawiqnctlqENVLFGqpmNPKRYQQA 722
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG-----------------KEVSFA---SPRDARRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 723 letcalladldvlpggdqteigekGIN----LSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVigpeGV 798
Cdd:cd03216 76 ------------------------GIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVI----RR 127
|
170 180 190
....*....|....*....|....*....|...
gi 1388591336 799 LA--GKTRVLVTHGISFLPQT-DFIIVLAGGQV 828
Cdd:cd03216 128 LRaqGVAVIFISHRLDEVFEIaDRVTVLRDGRV 160
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
643-832 |
1.87e-13 |
|
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: 70.66 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLG--EMEKLEGVV----------SVKGSVAYVPqqawiqnctlQENVLF 710
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVlingrpldkrSFRKIIGYVP----------QDDILH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 711 GQpmnpKRYQQALETCALLadldvlpggdqteigeKGInlSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFD 790
Cdd:cd03213 95 PT----LTVRETLMFAAKL----------------RGL--SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1388591336 791 QVIGpegvLA--GKTRVLVTHGIS------FlpqtDFIIVLAGGQVSEMG 832
Cdd:cd03213 153 LLRR----LAdtGRTIICSIHQPSseifelF----DKLLLLSQGRVIYFG 194
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
612-809 |
2.21e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 73.72 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 612 PQCVERKTISPgyAITIHNGTFTWaqDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-SV 690
Cdd:PRK11607 8 PQAKTRKALTP--LLEIRNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 691 AYVP-----------QQAWIQNCTLQENVLFG--QPMNPK-----RYQQALETCALladldvlpggdQTEIGEKGINLSG 752
Cdd:PRK11607 84 SHVPpyqrpinmmfqSYALFPHMTVEQNIAFGlkQDKLPKaeiasRVNEMLGLVHM-----------QEFAKRKPHQLSG 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591336 753 GQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGP-EGVlaGKTRVLVTH 809
Cdd:PRK11607 153 GQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDIlERV--GVTCVMVTH 208
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
643-781 |
2.28e-13 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 71.69 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-------------SVAYVPQQAWIQ-NCTLQENV 708
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplaawspwelarRRAVLPQHSSLAfPFTVEEVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 709 LFG---QPMNPKRYQQALETCALLADLDVLPGGDQTEigekginLSGGQRQRVSLARA-------VYSDANIFLLDDPLS 778
Cdd:COG4559 97 ALGrapHGSSAAQDRQIVREALALVGLAHLAGRSYQT-------LSGGEQQRVQLARVlaqlwepVDGGPRWLFLDEPTS 169
|
...
gi 1388591336 779 AVD 781
Cdd:COG4559 170 ALD 172
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
647-832 |
2.45e-13 |
|
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: 70.66 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 647 NIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-SVAYVPQQAWIQNCTLQENVLF---------GQPMNP 716
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDqSHTGLAPYQRPVSMLFQENNLFahltvrqniGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 717 -----KRYQQALETCAL---LAD-LDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKH 787
Cdd:TIGR01277 98 glklnAEQQEKVVDAAQqvgIADyLDRLPE-----------QLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1388591336 788 IFdQVIGPEGVLAGKTRVLVTHGISFLPQT-DFIIVLAGGQVSEMG 832
Cdd:TIGR01277 167 ML-ALVKQLCSERQRTLLMVTHHLSDARAIaSQIAVVSQGKIKVVS 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1285-1506 |
2.76e-13 |
|
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: 71.11 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAEGEIVIDGLNVAHIGLHdlRS 1360
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTT----LLRLIagfeTPTSGEILLDGKDITNLPPH--KR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1361 QLTIIPQDPILFSG-TLRMNLdPFG----RYSEEDIWR----ALELSHLNTFVSSQPagldfqcaeggDNLSVGQRQLVC 1431
Cdd:cd03300 73 PVNTVFQNYALFPHlTVFENI-AFGlrlkKLPKAEIKErvaeALDLVQLEGYANRKP-----------SQLSGGQQQRVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1432 LARALLRKSRVLVLDEATAAID--------LETDDLiQGTIRTQFEDCT-----VLTIAhrlntimdyNRVLVLDKGVVA 1498
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDlklrkdmqLELKRL-QKELGITFVFVThdqeeALTMS---------DRIAVMNKGKIQ 210
|
....*...
gi 1388591336 1499 EFDSPVNL 1506
Cdd:cd03300 211 QIGTPEEI 218
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
643-781 |
2.93e-13 |
|
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: 71.21 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGS-----------VAYVPQQ-AWIQNCTLQENVLF 710
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNyALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388591336 711 G----QPMNPKRYQQALETCALLADLDVLpggdqteiGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD 781
Cdd:cd03299 95 GlkkrKVDKKEIERKVLEIAEMLGIDHLL--------NRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1285-1508 |
2.97e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 72.17 E-value: 2.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYRPGLELV---LKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDG----LNVAHIGLHD 1357
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEkkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1358 LRSQLTIIPQDP--ILFsgtlrmnldpfgrysEEDIWRALELSHLNTFVSSQPA-----------GLDFQCAEGGD-NLS 1423
Cdd:PRK13641 83 LRKKVSLVFQFPeaQLF---------------ENTVLKDVEFGPKNFGFSEDEAkekalkwlkkvGLSEDLISKSPfELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1424 VGQRQLVCLARALLRKSRVLVLDEATAAIDLET-DDLIQGTIRTQFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFD 1501
Cdd:PRK13641 148 GGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEYaDDVLVLEHGKLIKHA 227
|
....*..
gi 1388591336 1502 SPVNLIA 1508
Cdd:PRK13641 228 SPKEIFS 234
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
643-832 |
3.01e-13 |
|
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: 71.11 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-SVAYVP----------QQ-AWIQNCTLQENVLF 710
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkDITNLPphkrpvntvfQNyALFPHLTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 711 GQPMNPKRYQQALETCALLADLDVLPGGDQTEIGEkginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKH--- 787
Cdd:cd03300 96 GLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQ----LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDmql 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1388591336 788 ----IFDQVigpegvlaGKTRVLVTHGIS-FLPQTDFIIVLAGGQVSEMG 832
Cdd:cd03300 172 elkrLQKEL--------GITFVFVTHDQEeALTMSDRIAVMNKGKIQQIG 213
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1280-1501 |
3.16e-13 |
|
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: 70.64 E-value: 3.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1280 PTRGMVEFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGL-HDL 1358
Cdd:cd03220 16 GSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLgGGF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1359 RSQLTIIpqDPILFSGTLrMNLDP-FGRYSEEDIWralELSHLNTFVsSQPAGldfqcaeggdNLSVGQRQLVCLARALL 1437
Cdd:cd03220 96 NPELTGR--ENIYLNGRL-LGLSRkEIDEKIDEII---EFSELGDFI-DLPVK----------TYSSGMKARLAFAIATA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 1438 RKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDC-TVLTIAHRLNTIMDY-NRVLVLDKGVVAEFD 1501
Cdd:cd03220 159 LEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGkTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1287-1504 |
3.60e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 71.64 E-value: 3.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1287 FRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHI---GLHDLRSQLT 1363
Cdd:PRK10419 13 YAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1364 IIPQDPI-----------LFSGTLR--MNLDPFGRYSeediwRALELSHLntfVSSQPAGLDFQCAEggdnLSVGQRQLV 1430
Cdd:PRK10419 93 MVFQDSIsavnprktvreIIREPLRhlLSLDKAERLA-----RASEMLRA---VDLDDSVLDKRPPQ----LSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1431 CLARALLRKSRVLVLDEATAAIDLetddLIQGTI-------RTQFeDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAE--- 1499
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDL----VLQAGVirllkklQQQF-GTACLFITHDLRLVERFcQRVMVMDNGQIVEtqp 235
|
250
....*....|.
gi 1388591336 1500 ------FDSPV 1504
Cdd:PRK10419 236 vgdkltFSSPA 246
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
1000-1179 |
3.74e-13 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 71.67 E-value: 3.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1000 QQNKTSVRLGVYAALGILQGLLVMLSAFTMVVGAIQAARLLhEALLHNKI-----RSPQSFFDTTPSGRILNRFSKDIYV 1074
Cdd:cd18541 31 AGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRI-EYDLRNDLfahllTLSPSFYQKNRTGDLMARATNDLNA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1075 IDEVLAPTILMLLNSFFTSISTI-MVIVASTPLFMVVVLPLAVLYGFVQRFyvatSRQL-KRLESISRSpiFSHFS---- 1148
Cdd:cd18541 110 VRMALGPGILYLVDALFLGVLVLvMMFTISPKLTLIALLPLPLLALLVYRL----GKKIhKRFRKVQEA--FSDLSdrvq 183
|
170 180 190
....*....|....*....|....*....|....*
gi 1388591336 1149 ETVTGTSVIRAYGR----IQDFKVLSDTKVDNNQK 1179
Cdd:cd18541 184 ESFSGIRVIKAFVQeeaeIERFDKLNEEYVEKNLR 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1291-1506 |
3.94e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 71.25 E-value: 3.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1291 SVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMtLCLFRILEAAEGEIVIDGlnvaHIGLHDLRSQLTIIPQDPI 1370
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTL-LRLLAGLETPSAGELLAG----TAPLAEAREDTRLMFQDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1371 LFSgtLRMNLDPFGRYSEEDiWRALELSHLNTfvssqpAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATA 1450
Cdd:PRK11247 92 LLP--WKKVIDNVGLGLKGQ-WRDAALQALAA------VGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388591336 1451 AID----LETDDLIQGTIRTQ-FedcTVLTIAHRLN---TIMDynRVLVLDKGVVAeFDSPVNL 1506
Cdd:PRK11247 163 ALDaltrIEMQDLIESLWQQHgF---TVLLVTHDVSeavAMAD--RVLLIEEGKIG-LDLTVDL 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1301-1465 |
4.26e-13 |
|
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: 70.65 E-value: 4.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1301 VLKNVTVHVQGGEKVGIVGRTGAGKSS---MTLCLFRileAAEGEIVIDGLNVAHIGLHDlRSQLTII--PQDPILFSG- 1374
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTtfyMIVGLVK---PDSGKILLDGQDITKLPMHK-RARLGIGylPQEASIFRKl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1375 TLRMNLDPF--GRYSEEDIWRA-----LELSHLnTFVSSQPAgldfqcaeggDNLSVGQRQLVCLARALLRKSRVLVLDE 1447
Cdd:cd03218 91 TVEENILAVleIRGLSKKEREEkleelLEEFHI-THLRKSKA----------SSLSGGERRRVEIARALATNPKFLLLDE 159
|
170
....*....|....*...
gi 1388591336 1448 ATAAIDLETDDLIQGTIR 1465
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIK 177
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
622-850 |
6.10e-13 |
|
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: 70.75 E-value: 6.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 622 PGYAITIHNGTFTWAQDLPPT-----LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-------- 688
Cdd:cd03294 14 PQKAFKLLAKGKSKEEILKKTgqtvgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 689 ---------SVAYVPQQ-AWIQNCTLQENVLFG---QPMNPK----RYQQALETCALLADLDVLPGgdqteigekgiNLS 751
Cdd:cd03294 94 kelrelrrkKISMVFQSfALLPHRTVLENVAFGlevQGVPRAereeRAAEALELVGLEGWEHKYPD-----------ELS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 752 GGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGPEGVLaGKTRVLVTHG-ISFLPQTDFIIVLAGGQVSE 830
Cdd:cd03294 163 GGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAEL-QKTIVFITHDlDEALRLGDRIAIMKDGRLVQ 241
|
250 260
....*....|....*....|..
gi 1388591336 831 MGHYSALLQH--DGSFANFLRN 850
Cdd:cd03294 242 VGTPEEILTNpaNDYVREFFRG 263
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1289-1500 |
6.10e-13 |
|
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: 69.53 E-value: 6.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1289 NYSVRYRPGLelVLKNVTVHVQGGeKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAhIGLHDLRSQLTIIPQD 1368
Cdd:cd03264 5 NLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL-KQPQKLRRRIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1369 PILFSG-TLRMNLDPFG-------RYSEEDIWRALELSHLNTFVSSQPAGLdfqcaeggdnlSVGQRQLVCLARALLRKS 1440
Cdd:cd03264 81 FGVYPNfTVREFLDYIAwlkgipsKEVKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 1441 RVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMD-YNRVLVLDKGVVAEF 1500
Cdd:cd03264 150 SILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFE 210
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1301-1498 |
6.68e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.16 E-value: 6.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1301 VLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGlHDLRSQLTI--IPQDPILFSG-TLR 1377
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT-PAKAHQLGIylVPQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1378 MNLdPFGRYSEEDIWRALE--LSHLNTFVSsqpagLDFQCAeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAID-L 1454
Cdd:PRK15439 105 ENI-LFGLPKRQASMQKMKqlLAALGCQLD-----LDSSAG----SLEVADRQIVEILRGLMRDSRILILDEPTASLTpA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1388591336 1455 ETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVA 1498
Cdd:PRK15439 175 ETERLFSRIRELLAQGVGIVFISHKLPEIRQLaDRISVMRDGTIA 219
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1284-1453 |
7.40e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 70.49 E-value: 7.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYRPGLElVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDG--LNVAHIGLHDLRSQ 1361
Cdd:PRK13639 1 ILETRDLKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1362 LTIIPQDP--ILFSGTLR-------MNLdpfgRYSEEDIWR----ALELSHLNTFVSSQPagldfqcaeggDNLSVGQRQ 1428
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEedvafgpLNL----GLSKEEVEKrvkeALKAVGMEGFENKPP-----------HHLSGGQKK 144
|
170 180
....*....|....*....|....*
gi 1388591336 1429 LVCLARALLRKSRVLVLDEATAAID 1453
Cdd:PRK13639 145 RVAIAGILAMKPEIIVLDEPTSGLD 169
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1284-1454 |
8.94e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 70.20 E-value: 8.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYS--VRYRPGL------ELVlKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVaHIGL 1355
Cdd:PRK15112 4 LLEVRNLSktFRYRTGWfrrqtvEAV-KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1356 HDLRSQ-LTIIPQDPI-----------LFSGTLRMNLDPFGRYSEEDIWRAL-ELSHLNTFVSSQPagldfqcaeggDNL 1422
Cdd:PRK15112 82 YSYRSQrIRMIFQDPStslnprqrisqILDFPLRLNTDLEPEQREKQIIETLrQVGLLPDHASYYP-----------HML 150
|
170 180 190
....*....|....*....|....*....|..
gi 1388591336 1423 SVGQRQLVCLARALLRKSRVLVLDEATAAIDL 1454
Cdd:PRK15112 151 APGQKQRLGLARALILRPKVIIADEALASLDM 182
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
641-828 |
1.03e-12 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 69.00 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGS--------------VAYVPQ-QAWIQNCTLQ 705
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEgRRIFPELTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 706 ENVLFG-QPMNPKRYQQALEtcALLADLDVLpggdQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDP---LSAVd 781
Cdd:cd03224 94 ENLLLGaYARRRAKRKARLE--RVYELFPRL----KERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPsegLAPK- 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1388591336 782 shVAKHIFDQV--IGPEGVlagkTRVLVTHGISF-LPQTDFIIVLAGGQV 828
Cdd:cd03224 167 --IVEEIFEAIreLRDEGV----TILLVEQNARFaLEIADRAYVLERGRV 210
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
647-781 |
1.22e-12 |
|
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: 71.29 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 647 NIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSV-----------------AYVPQQAwiqncTL----- 704
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargiflpphrrriGYVFQEA-----RLfphls 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 705 -QENVLFGQPMNPK-----RYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLS 778
Cdd:COG4148 94 vRGNLLYGRKRAPRaerriSFDEVVELLGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
...
gi 1388591336 779 AVD 781
Cdd:COG4148 163 ALD 165
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1283-1510 |
1.28e-12 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 70.87 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1283 GMVEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSmTLclfRIL----EAAEGEIVIDGLNVAHIGLHDl 1358
Cdd:COG3839 2 ASLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKST-LL---RMIagleDPTSGEILIGGRDVTDLPPKD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1359 RSqLTIIPQDPILF-SGTLRMNLDpFG----RYSEEDIWRA-------LELSHLntfvssqpagLDFQCAEggdnLSVGQ 1426
Cdd:COG3839 75 RN-IAMVFQSYALYpHMTVYENIA-FPlklrKVPKAEIDRRvreaaelLGLEDL----------LDRKPKQ----LSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1427 RQLVCLARALLRKSRVLVLDEATAAID----LETddliqgtiRTQfedctvltIA---HRLNTIMDY------------N 1487
Cdd:COG3839 139 RQRVALGRALVREPKVFLLDEPLSNLDaklrVEM--------RAE--------IKrlhRRLGTTTIYvthdqveamtlaD 202
|
250 260 270
....*....|....*....|....*....|
gi 1388591336 1488 RVLVLDKGVVAEFDS-------PVNLIAAG 1510
Cdd:COG3839 203 RIAVMNDGRIQQVGTpeelydrPANLFVAG 232
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
632-832 |
1.33e-12 |
|
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: 69.15 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 632 TFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGeMEK-LEGVVSVKG----------------SVAYVP 694
Cdd:cd03258 10 VFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING-LERpTSGSVLVDGtdltllsgkelrkarrRIGMIF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 695 QQ-AWIQNCTLQENVLF-----GQPMNpKRYQQALETCAL--LADL-DVLPGgdqteigekgiNLSGGQRQRVSLARAVY 765
Cdd:cd03258 89 QHfNLLSSRTVFENVALpleiaGVPKA-EIEERVLELLELvgLEDKaDAYPA-----------QLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388591336 766 SDANIFLLDDPLSAVDSHVAKHIFD------QVIGPegvlagkTRVLVTHGISFLPQ-TDFIIVLAGGQVSEMG 832
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILAllrdinRELGL-------TIVLITHEMEVVKRiCDRVAVMEKGEVVEEG 223
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
645-848 |
1.59e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 70.90 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 645 SLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSvaYVPQQAwIQN---C------------TLQENVL 709
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE--DVTHRS-IQQrdiCmvfqsyalfphmSLGENVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 710 FGQPMN--PK-----RYQQALEtcalLADLDvlpgG------DQteigekginLSGGQRQRVSLARAVYSDANIFLLDDP 776
Cdd:PRK11432 101 YGLKMLgvPKeerkqRVKEALE----LVDLA----GfedryvDQ---------ISGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388591336 777 LSAVDSHVAKHIFDQVIGPEGVLaGKTRVLVTHGIS-FLPQTDFIIVLAGGQVSEMGHYSALLQHDGS--FANFL 848
Cdd:PRK11432 164 LSNLDANLRRSMREKIRELQQQF-NITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQPASrfMASFM 237
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
642-809 |
1.86e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 69.03 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 642 TLHSLNIQIPKGALVAVVGPVGCGKSSLVSALlGEMEKLEGVVSVKGSVAY---------------------VPQQAWIQ 700
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRMNDLNPEVTITGSIVYnghniysprtdtvdlrkeigmVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 701 NCTLQENVLFGQPMN----PKRYQQALETCALLADL--DVlpggdQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLD 774
Cdd:PRK14239 99 PMSIYENVVYGLRLKgikdKQVLDEAVEKSLKGASIwdEV-----KDRLHDSALGLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 1388591336 775 DPLSAVDSHVAKHIFDQVIGpegvLAGK-TRVLVTH 809
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLG----LKDDyTMLLVTR 205
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1287-1494 |
2.22e-12 |
|
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: 69.50 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1287 FRNYSVRYRPglelVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIvidglnvAHIGlhdlrsQLTIIP 1366
Cdd:cd03291 42 FSNLCLVGAP----VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-------KHSG------RISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1367 QDPILFSGTLRMNLdPFG-RYSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVL 1445
Cdd:cd03291 105 QFSWIMPGTIKENI-IFGvSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1388591336 1446 DEATAAIDLETDDLIqgtirtqFEDCTVLTIAHRlntimdyNRVLVLDK 1494
Cdd:cd03291 184 DSPFGYLDVFTEKEI-------FESCVCKLMANK-------TRILVTSK 218
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
643-860 |
2.24e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 68.89 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLG----------EMEKLEGVVSVKGSVA-----------YVPQQAWIQN 701
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdksagsHIELLGRTVQREGRLArdirksrantgYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 702 -CTLQENVLFG----QPM--------NPKRYQQALEtcALladldvlpggdqTEIG------EKGINLSGGQRQRVSLAR 762
Cdd:PRK09984 100 rLSVLENVLIGalgsTPFwrtcfswfTREQKQRALQ--AL------------TRVGmvhfahQRVSTLSGGQQQRVAIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 763 AVYSDANIFLLDDPLSAVDSHVAKHIFDQV--IGPEGvlaGKTRVLVTHGISF-LPQTDFIIVLAGGQVSemghysallq 839
Cdd:PRK09984 166 ALMQQAKVILADEPIASLDPESARIVMDTLrdINQND---GITVVVTLHQVDYaLRYCERIVALRQGHVF---------- 232
|
250 260
....*....|....*....|.
gi 1388591336 840 HDGSFANFlrnyapDEDQEDH 860
Cdd:PRK09984 233 YDGSSQQF------DNERFDH 247
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1297-1466 |
2.25e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.59 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1297 GLELVLKNVTVHVQGGEKVGIVGRTGAGKSSmtlcLFRI----LEAAEGEIVIDGLNvahIGLHDLRSQLTII-PQDPIL 1371
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTT----LLRLiaglLPPAAGTIKLDGGD---IDDPDVAEACHYLgHRNAMK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1372 FSGTLRMNLDPFGRY---SEEDIWRALE---LSHLntfvssqpAGLDFQcaeggdNLSVGQRQLVCLARALLRKSRVLVL 1445
Cdd:PRK13539 86 PALTVAENLEFWAAFlggEELDIAAALEavgLAPL--------AHLPFG------YLSAGQKRRVALARLLVSNRPIWIL 151
|
170 180
....*....|....*....|.
gi 1388591336 1446 DEATAAIDLETDDLIQGTIRT 1466
Cdd:PRK13539 152 DEPTAALDAAAVALFAELIRA 172
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
625-849 |
2.33e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 68.50 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 625 AITIHNGTFTWAQDlpPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSAL-LGEMEKlEGVVSVKGS-------------- 689
Cdd:COG4161 2 SIQLKNINCFYGSH--QALFDINLECPSGETLVLLGPSGAGKSSLLRVLnLLETPD-SGQLNIAGHqfdfsqkpsekair 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 690 -----VAYVPQQ--AWiQNCTLQENvLFGQPMN---------PKRYQQALETCALLADLDVLPggdqteigekgINLSGG 753
Cdd:COG4161 79 llrqkVGMVFQQynLW-PHLTVMEN-LIEAPCKvlglskeqaREKAMKLLARLRLTDKADRFP-----------LHLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 754 QRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDqvIGPEGVLAGKTRVLVTHGISFLPQT-DFIIVLAGGQVSEMG 832
Cdd:COG4161 146 QQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVE--IIRELSQTGITQVIVTHEVEFARKVaSQVVYMEKGRIIEQG 223
|
250
....*....|....*...
gi 1388591336 833 HYSALLQ-HDGSFANFLR 849
Cdd:COG4161 224 DASHFTQpQTEAFAHYLS 241
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
641-833 |
2.54e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.20 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGS-VAYVPQQAWIQN---CTlQENVLFGQPMN- 715
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdISTLKPEIYRQQvsyCA-QTPTLFGDTVYd 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 716 ----PkrYQ---QALETCALLADLDV--LPggdqTEIGEKGIN-LSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHvA 785
Cdd:PRK10247 100 nlifP--WQirnQQPDPAIFLDDLERfaLP----DTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDES-N 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 786 KHIFDQVIgPEGVLAGKTRVL-VTHGISFLPQTDFIIVL--AGGQVSEMGH 833
Cdd:PRK10247 173 KHNVNEII-HRYVREQNIAVLwVTHDKDEINHADKVITLqpHAGEMQEARY 222
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1284-1508 |
2.75e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 68.97 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYRPGLEL-VLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQL 1362
Cdd:PRK13642 4 ILEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1363 TIIPQDPI-LFSGTLRMNLDPFGRYS-----EEDIWRALE-LSHLNTfvssqpagLDFQCAEGGdNLSVGQRQLVCLARA 1435
Cdd:PRK13642 84 GMVFQNPDnQFVGATVEDDVAFGMENqgiprEEMIKRVDEaLLAVNM--------LDFKTREPA-RLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 1436 LLRKSRVLVLDEATAAIDLETDDLIQGTIRtQFED---CTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIA 1508
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIH-EIKEkyqLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
643-788 |
2.95e-12 |
|
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: 68.07 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEK---LEGVVSVKG----------SVAYVPQQ-AWIQNCTLQENV 708
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGqprkpdqfqkCVAYVRQDdILLPGLTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 709 LFGQPM-----NPKRYQQALETCALLADLDVLPGGdqteiGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSH 783
Cdd:cd03234 103 TYTAILrlprkSSDAIRKKRVEDVLLRDLALTRIG-----GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
....*
gi 1388591336 784 VAKHI 788
Cdd:cd03234 178 TALNL 182
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1295-1503 |
3.46e-12 |
|
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: 68.44 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1295 RPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIG---LHDLRSQ--------LT 1363
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKkismvfqsFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1364 IIPQDPILFSGTLRMNLDpfGRYSEEDIWRA---LELSHLNTFVSSQPagldfqcaeggDNLSVGQRQLVCLARALLRKS 1440
Cdd:cd03294 113 LLPHRTVLENVAFGLEVQ--GVPRAEREERAaeaLELVGLEGWEHKYP-----------DELSGGMQQRVGLARALAVDP 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1441 RVLVLDEATAAIdletDDLIQGTIRTQFEDC------TVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSP 1503
Cdd:cd03294 180 DILLMDEAFSAL----DPLIRREMQDELLRLqaelqkTIVFITHDLDEALRLgDRIAIMKDGRLVQVGTP 245
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
626-832 |
4.02e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 68.19 E-value: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 626 ITIHNGTFTWAQDlpPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-SVAYVPQQAWIQNCTL 704
Cdd:COG4604 2 IEIKNVSKRYGGK--VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGlDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 705 --QEN-----------VLFGqpmnpkRY---------------QQALETCAL--LAD--LDvlpggdqteigekgiNLSG 752
Cdd:COG4604 80 lrQENhinsrltvrelVAFG------RFpyskgrltaedreiiDEAIAYLDLedLADryLD---------------ELSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 753 GQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGpegvLA---GKTRVLVTHGISFLPQ-TDFIIVLAGGQV 828
Cdd:COG4604 139 GQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRR----LAdelGKTVVIVLHDINFASCyADHIVAMKDGRV 214
|
....
gi 1388591336 829 SEMG 832
Cdd:COG4604 215 VAQG 218
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
1010-1256 |
4.27e-12 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 68.74 E-value: 4.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1010 VYAALGILQGLLVMLSAFTMVVGAIQAARLLHEALLHNKIRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLLNS 1089
Cdd:cd18557 41 ILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1090 FFTSI-STIMVIVAS---TPLFMVVVLPLAVLYGFVQRFYVATSRQLkrLESISRSPifSHFSETVTGTSVIRAYGR--- 1162
Cdd:cd18557 121 ILQVIgGLIILFILSwklTLVLLLVIPLLLIASKIYGRYIRKLSKEV--QDALAKAG--QVAEESLSNIRTVRSFSAeek 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1163 -IQDFKVLSDTKVDNNQKSSypyiasnRWLGVHvEFVGNCVVlFAALFAV-------IGRNSLNPGLVGLSVSYALQVTM 1234
Cdd:cd18557 197 eIRRYSEALDRSYRLARKKA-------LANALF-QGITSLLI-YLSLLLVlwyggylVLSGQLTVGELTSFILYTIMVAS 267
|
250 260
....*....|....*....|..
gi 1388591336 1235 ALNWMIRMISDLESNIIAVERV 1256
Cdd:cd18557 268 SVGGLSSLLADIMKALGASERV 289
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
645-789 |
4.70e-12 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 70.93 E-value: 4.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 645 SLNIQIPKGALVAVVGPVGCGKSSLVSaLLGEMEKLEG---VVSVKGSVAYVPQQAWIQNCTLQENVLFgqPMNPKRYQ- 720
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGgrlTKPAKGKLFYVPQRPYMTLGTLRDQIIY--PDSSEDMKr 546
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 721 QALETCALLADLDVLPGGD--QTEIGEKGIN-----LSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIF 789
Cdd:TIGR00954 547 RGLSDKDLEQILDNVQLTHilEREGGWSAVQdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMY 622
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1297-1453 |
4.76e-12 |
|
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: 67.46 E-value: 4.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1297 GLEL-VLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVID----GLNVAHIG---LHDLR-------SQ 1361
Cdd:COG4778 21 GKRLpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASpreILALRrrtigyvSQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1362 -LTIIPQ--------DPILFSGTLRmnldpfgrysEEDIWRALE-LSHLN-----------TFvssqpagldfqcaeggd 1420
Cdd:COG4778 101 fLRVIPRvsaldvvaEPLLERGVDR----------EEARARARElLARLNlperlwdlppaTF----------------- 153
|
170 180 190
....*....|....*....|....*....|...
gi 1388591336 1421 nlSVGQRQLVCLARALLRKSRVLVLDEATAAID 1453
Cdd:COG4778 154 --SGGEQQRVNIARGFIADPPLLLLDEPTASLD 184
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
626-832 |
4.96e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 68.12 E-value: 4.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 626 ITIHNGTFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSVaYVPQQAW------- 698
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV-LSEETVWdvrrqvg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 699 --IQN-------CTLQENVLFGQPMN--P-----KRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLAR 762
Cdd:PRK13635 85 mvFQNpdnqfvgATVQDDVAFGLENIgvPreemvERVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388591336 763 AVYSDANIFLLDDPLSAVDShvakhifdqvIGPEGVLA---------GKTRVLVTHGISFLPQTDFIIVLAGGQVSEMG 832
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDP----------RGRREVLEtvrqlkeqkGITVLSITHDLDEAAQADRVIVMNKGEILEEG 222
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1297-1516 |
5.43e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.09 E-value: 5.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1297 GLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTL 1376
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1377 RMNLDPFGRYSEEDI---WRALELSHLNTfvSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAID 1453
Cdd:PRK10253 98 VQELVARGRYPHQPLftrWRKEDEEAVTK--AMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1454 LETD----DLIQGTIRTQfeDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSPVNLIAAGGI--FYGM 1516
Cdd:PRK10253 176 ISHQidllELLSELNREK--GYTLAAVLHDLNQACRYaSHLIALREGKIVAQGAPKEIVTAELIerIYGL 243
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1291-1497 |
5.97e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.99 E-value: 5.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1291 SVRYRPGlELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIglhdLRSQL-TIIPQD- 1368
Cdd:PRK15056 13 TVTWRNG-HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA----LQKNLvAYVPQSe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1369 ------PILFSGTLRMnldpfGRYSEEDiWRALELSHLNTFVSSQPAG---LDFQCAEGGDnLSVGQRQLVCLARALLRK 1439
Cdd:PRK15056 88 evdwsfPVLVEDVVMM-----GRYGHMG-WLRRAKKRDRQIVTAALARvdmVEFRHRQIGE-LSGGQKKRVFLARAIAQQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1388591336 1440 SRVLVLDEATAAIDLETDDLIQGTIRT-QFEDCTVLTIAHRLNTIMDYNRVLVLDKGVV 1497
Cdd:PRK15056 161 GQVILLDEPFTGVDVKTEARIISLLRElRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTV 219
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
693-849 |
6.17e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.83 E-value: 6.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 693 VPQQAWIQNCTLQENVLFG-QPMNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIF 771
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGkEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKIL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 772 LLDDPLSAVDSHVAKHIFDQVIGPEGVlAGKTRVLVTHGISFLPQTDFIIVL-----AGGQVSEMGHYSALLQ-HDGSFA 845
Cdd:PTZ00265 1381 LLDEATSSLDSNSEKLIEKTIVDIKDK-ADKTIITIAHRIASIKRSDKIVVFnnpdrTGSFVQAHGTHEELLSvQDGVYK 1459
|
....
gi 1388591336 846 NFLR 849
Cdd:PTZ00265 1460 KYVK 1463
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1285-1498 |
6.24e-12 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 66.04 E-value: 6.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRN--YSVRYRPGL--ELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCL--FRILEAAEGEIVIDGLNvahIGLHDL 1358
Cdd:cd03213 4 LSFRNltVTVKSSPSKsgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRP---LDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1359 RSQLTIIPQDPILFsGTLRMnldpfgrysEEDIWRALELShlntfvssqpagldfqcaeggdNLSVGQRQLVCLARALLR 1438
Cdd:cd03213 81 RKIIGYVPQDDILH-PTLTV---------RETLMFAAKLR----------------------GLSGGERKRVSIALELVS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388591336 1439 KSRVLVLDEATAAIDLETDDLIQGTIRtQFED--CTVLTIAHRLNTIM--DYNRVLVLDKGVVA 1498
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMSLLR-RLADtgRTIICSIHQPSSEIfeLFDKLLLLSQGRVI 191
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1312-1498 |
6.24e-12 |
|
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: 66.55 E-value: 6.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1312 GEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGlnvahIGLHDLRSQLTIIPQD---PILFSG-------TLRMNLD 1381
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG-----TVLFDSRKKINLPPQQrkiGLVFQQyalfphlNVRENLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1382 pFG---------RYSEEDIWRALELSHLntfVSSQPAGLdfqcaeggdnlSVGQRQLVCLARALLRKSRVLVLDEATAAI 1452
Cdd:cd03297 98 -FGlkrkrnredRISVDELLDLLGLDHL---LNRYPAQL-----------SGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1388591336 1453 DLETDDLIQGTIRTQFED--CTVLTIAHRLNTI-MDYNRVLVLDKGVVA 1498
Cdd:cd03297 163 DRALRLQLLPELKQIKKNlnIPVIFVTHDLSEAeYLADRIVVMEDGRLQ 211
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
643-840 |
6.61e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 67.47 E-value: 6.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALlGEMEKLE------GVVSVKGSVAYVPQQAWIQNC-------------- 702
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI-NLLEQPEagtirvGDITIDTARSLSQQKGLIRQLrqhvgfvfqnfnlf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 703 ---TLQENVLFGQPMNPKRYQQALETCA--LLADLDVlpGGDQTEIGEKginLSGGQRQRVSLARAVYSDANIFLLDDPL 777
Cdd:PRK11264 98 phrTVLENIIEGPVIVKGEPKEEATARAreLLAKVGL--AGKETSYPRR---LSGGQQQRVAIARALAMRPEVILFDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 778 SAVDSHVAKHIFDQVIGpegvLA--GKTRVLVTHGISFLPQ-TDFIIVLAGGQVSEMGHYSALLQH 840
Cdd:PRK11264 173 SALDPELVGEVLNTIRQ----LAqeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1301-1499 |
6.93e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 67.47 E-value: 6.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1301 VLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLfRILEAAE------GEIVIDG---LNVAHIGLHDLRSQLTIIPQDPIL 1371
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI-NLLEQPEagtirvGDITIDTarsLSQQKGLIRQLRQHVGFVFQNFNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1372 FSGtlRMNLD-----PF---GRYSEEDIWRALELShlntfvssQPAGLdfqcaEGGDN-----LSVGQRQLVCLARALLR 1438
Cdd:PRK11264 97 FPH--RTVLEniiegPVivkGEPKEEATARARELL--------AKVGL-----AGKETsyprrLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388591336 1439 KSRVLVLDEATAAIDLETDDLIQGTIRTQFEDC-TVLTIAHRLNTIMDY-NRVLVLDKGVVAE 1499
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDVaDRAIFMDQGRIVE 224
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
643-832 |
7.37e-12 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 66.94 E-value: 7.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGemekLE----GVVSVKG---------------SVAYVPQQ------- 696
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINL----LEepdsGTITVDGedltdskkdinklrrKVGMVFQQfnlfphl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 697 -AwIQNCTL-QENVLfGQPmnpkrYQQALETcAL-------LAD-LDVLPGgdqteigekgiNLSGGQRQRVSLARAVYS 766
Cdd:COG1126 93 tV-LENVTLaPIKVK-KMS-----KAEAEER-AMellervgLADkADAYPA-----------QLSGGQQQRVAIARALAM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591336 767 DANIFLLDDPLSAVDshvakhifdqvigPE---GVLA--------GKTRVLVTHGISFLPQT-DFIIVLAGGQVSEMG 832
Cdd:COG1126 154 EPKVMLFDEPTSALD-------------PElvgEVLDvmrdlakeGMTMVVVTHEMGFAREVaDRVVFMDGGRIVEEG 218
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1284-1509 |
7.70e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 67.03 E-value: 7.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYRPGLE--------------------LVLKNVTVHVQGGEKVGIVGRTGAGKSsmTLC--LFRILEAAEG 1341
Cdd:COG1134 4 MIEVENVSKSYRLYHEpsrslkelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKS--TLLklIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1342 EIVIDG-----LNVAHiGLHdlrSQLTIIpqDPILFSGTLrMNLdpfgrySEEDIWRALElshlntFVssqpagLDFqcA 1416
Cdd:COG1134 82 RVEVNGrvsalLELGA-GFH---PELTGR--ENIYLNGRL-LGL------SRKEIDEKFD------EI------VEF--A 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1417 EGGD-------NLSVGQRqlvclAR-----ALLRKSRVLVLDEATAAIDLE----TDDLIQGTIRtqfEDCTVLTIAHRL 1480
Cdd:COG1134 135 ELGDfidqpvkTYSSGMR-----ARlafavATAVDPDILLVDEVLAVGDAAfqkkCLARIRELRE---SGRTVIFVSHSM 206
|
250 260 270
....*....|....*....|....*....|
gi 1388591336 1481 NTIMDY-NRVLVLDKGVVAEFDSPVNLIAA 1509
Cdd:COG1134 207 GAVRRLcDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
597-781 |
7.71e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 69.84 E-value: 7.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 597 SLKRIQDF---LNQNELDPQCVERKTISPGYAITIHNGTFTwaqdLP---PTLHSLNIQIPKGALVAVVGPVGCGKSSLV 670
Cdd:COG4178 331 TVDRLAGFeeaLEAADALPEAASRIETSEDGALALEDLTLR----TPdgrPLLEDLSLSLKPGERLLITGPSGSGKSTLL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 671 SALLGemekL----EGVVSV--KGSVAYVPQQAWIQNCTLQENVLFGQP---MNPKRYQQALETCAL--LAD-LDVLPGG 738
Cdd:COG4178 407 RAIAG----LwpygSGRIARpaGARVLFLPQRPYLPLGTLREALLYPATaeaFSDAELREALEAVGLghLAErLDEEADW 482
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1388591336 739 DQTeigekginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD 781
Cdd:COG4178 483 DQV--------LSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
626-776 |
8.10e-12 |
|
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: 64.39 E-value: 8.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 626 ITIHNGTFTWAQDlpPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSV--KGSVAYVPQqawiqnct 703
Cdd:cd03221 1 IELENLSKTYGGK--LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWgsTVKIGYFEQ-------- 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388591336 704 lqenvlfgqpmnpkryqqaletcalladldvlpggdqteigekginLSGGQRQRVSLARAVYSDANIFLLDDP 776
Cdd:cd03221 71 ----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEP 97
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
643-781 |
8.18e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 67.10 E-value: 8.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-------------SVAYVPQQAWIQ-NCTLQENV 708
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHSSLSfPFTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 709 LFGQ---PMNPKRYQQALETCALLADLDVLPGGDQTEigekginLSGGQRQRVSLARA------VYSDANIFLLDDPLSA 779
Cdd:PRK13548 98 AMGRaphGLSRAEDDALVAAALAQVDLAHLAGRDYPQ-------LSGGEQQRVQLARVlaqlwePDGPPRWLLLDEPTSA 170
|
..
gi 1388591336 780 VD 781
Cdd:PRK13548 171 LD 172
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
643-812 |
8.39e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.01 E-value: 8.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGeMEKLEGVVSVKGSVayvPQQAWIQNCTL--QE-----------NVL 709
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG-LETPSAGELLAGTA---PLAEAREDTRLmfQDarllpwkkvidNVG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 710 FGQPMNPK-RYQQALETCALlADldvlpggdqtEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDShVAKHI 788
Cdd:PRK11247 104 LGLKGQWRdAALQALAAVGL-AD----------RANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA-LTRIE 171
|
170 180
....*....|....*....|....
gi 1388591336 789 FDQVIGPEGVLAGKTRVLVTHGIS 812
Cdd:PRK11247 172 MQDLIESLWQQHGFTVLLVTHDVS 195
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1282-1499 |
8.58e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 66.86 E-value: 8.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1282 RGMVEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILE-----AAEGEIVIDGLNVAHIGLH 1356
Cdd:PRK14247 1 MNKIEIRDLKVSF--GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1357 DLRSQLTIIPQ--DPI----LFSGT---LRMN-LDPFGRYSEEDIWRALELSHLNTFVSSQ---PAGldfqcaeggdNLS 1423
Cdd:PRK14247 79 ELRRRVQMVFQipNPIpnlsIFENValgLKLNrLVKSKKELQERVRWALEKAQLWDEVKDRldaPAG----------KLS 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388591336 1424 VGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAH---RLNTIMDYnrVLVLDKGVVAE 1499
Cdd:PRK14247 149 GGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqQAARISDY--VAFLYKGQIVE 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
643-776 |
9.20e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 69.32 E-value: 9.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVV----SVKgsVAYVPQQawiQ-----NCTLQENVlfgQP 713
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVklgeTVK--IGYFDQH---QeeldpDKTVLDEL---RD 402
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388591336 714 MNPKRYQQALEtcALLADLDvLPGGDQ-TEIGekgiNLSGGQRQRVSLARAVYSDANIFLLDDP 776
Cdd:COG0488 403 GAPGGTEQEVR--GYLGRFL-FSGDDAfKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEP 459
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
623-783 |
9.22e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 67.32 E-value: 9.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 623 GYAITIHNGTFTWAQDLpptlhslNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGsvAYVPQQA----- 697
Cdd:PRK10253 10 GEQLTLGYGKYTVAENL-------TVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDG--EHIQHYAskeva 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 698 -----WIQNCTLQENVLFGQPMNPKRY-QQALETCALLADLDVLPGGDQ----TEIGEKGIN-LSGGQRQRVSLARAVYS 766
Cdd:PRK10253 81 rriglLAQNATTPGDITVQELVARGRYpHQPLFTRWRKEDEEAVTKAMQatgiTHLADQSVDtLSGGQRQRAWIAMVLAQ 160
|
170
....*....|....*...
gi 1388591336 767 DANIFLLDDPLSAVD-SH 783
Cdd:PRK10253 161 ETAIMLLDEPTTWLDiSH 178
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
626-781 |
1.35e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.14 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 626 ITIHNGTFTWaQDLPptlHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGsvayvpqqawiQNCT-- 703
Cdd:PRK10771 2 LKLTDITWLY-HHLP---MRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG-----------QDHTtt 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 704 ----------LQENVLF---------GQPMNP---------KRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQR 755
Cdd:PRK10771 67 ppsrrpvsmlFQENNLFshltvaqniGLGLNPglklnaaqrEKLHAIARQMGIEDLLARLPG-----------QLSGGQR 135
|
170 180
....*....|....*....|....*.
gi 1388591336 756 QRVSLARAVYSDANIFLLDDPLSAVD 781
Cdd:PRK10771 136 QRVALARCLVREQPILLLDEPFSALD 161
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1293-1510 |
1.36e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.95 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1293 RYRPglELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDG--LNVAHIGLHDLRSQLTIIPQDP- 1369
Cdd:PRK13638 10 RYQD--EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDPe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1370 --ILFS---GTLRMNLDPFGrYSEEDIWR----ALELSHLNTFvSSQPagldFQCaeggdnLSVGQRQLVCLARALLRKS 1440
Cdd:PRK13638 88 qqIFYTdidSDIAFSLRNLG-VPEAEITRrvdeALTLVDAQHF-RHQP----IQC------LSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388591336 1441 RVLVLDEATAAIDLE-TDDLIQGTIRTQFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSPVNLIAAG 1510
Cdd:PRK13638 156 RYLLLDEPTAGLDPAgRTQMIAIIRRIVAQGNHVIISSHDIDLIYEIsDAVYVLRQGQILTHGAPGEVFACT 227
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1292-1492 |
1.52e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.89 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1292 VRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPIL 1371
Cdd:PRK10247 13 VGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1372 FSGTLRMNLD-PF---GRYSEEDIWRAlelsHLNTFvssqpaGLDFQCAEGGDN-LSVGQRQLVCLARALLRKSRVLVLD 1446
Cdd:PRK10247 93 FGDTVYDNLIfPWqirNQQPDPAIFLD----DLERF------ALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1447 EATAAID----LETDDLIQGTIRTQfeDCTVLTIAHRLNTIMDYNRVLVL 1492
Cdd:PRK10247 163 EITSALDesnkHNVNEIIHRYVREQ--NIAVLWVTHDKDEINHADKVITL 210
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
641-809 |
1.59e-11 |
|
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: 69.66 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG------------SVAYVPQQAWI-QNCTLQEN 707
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnldavrqSLGMCPQHNILfHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 708 VLFGQPMNPKRYQQA-LETCALLADLdvlpgGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAK 786
Cdd:TIGR01257 1024 ILFYAQLKGRSWEEAqLEMEAMLEDT-----GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180
....*....|....*....|...
gi 1388591336 787 HIFDQVIGPEgvlAGKTRVLVTH 809
Cdd:TIGR01257 1099 SIWDLLLKYR---SGRTIIMSTH 1118
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1255-1499 |
1.69e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.55 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1255 RVKEYSKTKTEAPWVVESNRAPEGWPTRGMVEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFR 1334
Cdd:PRK13536 12 RRLELSPIERKHQGISEAKASIPGSMSTVAIDLAGVSKSY--GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1335 ILEAAEGEIVIDGLNV---AHIGlhdlRSQLTIIPQ-DPILFSGTLRMNLDPFGRY-------SEEDIWRALELSHLNTF 1403
Cdd:PRK13536 90 MTSPDAGKITVLGVPVparARLA----RARIGVVPQfDNLDLEFTVRENLLVFGRYfgmstreIEAVIPSLLEFARLESK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1404 VSSQPAgldfqcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQF-EDCTVLTIAHrlnt 1482
Cdd:PRK13536 166 ADARVS-----------DLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTH---- 230
|
250 260
....*....|....*....|...
gi 1388591336 1483 IMDY-----NRVLVLDKGV-VAE 1499
Cdd:PRK13536 231 FMEEaerlcDRLCVLEAGRkIAE 253
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
643-832 |
1.70e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 67.66 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-SVAYVPQQAWIQNCTLQ-----------ENVLF 710
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqDITHVPAENRHVNTVFQsyalfphmtvfENVAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 711 GQPMN--PK-----RYQQALETCAL--LADldvlpggdqteigEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD 781
Cdd:PRK09452 110 GLRMQktPAaeitpRVMEALRMVQLeeFAQ-------------RKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1388591336 782 SHVAKHIFDQVIGPEGVLaGKTRVLVTHGI-SFLPQTDFIIVLAGGQVSEMG 832
Cdd:PRK09452 177 YKLRKQMQNELKALQRKL-GITFVFVTHDQeEALTMSDRIVVMRDGRIEQDG 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1301-1503 |
1.75e-11 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 67.48 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1301 VLKNVTVHVQGGEKVGIVGRTGAGKSsMTLclfRI---LEAA-EGEIVIDGlNVAHIGLHDLRSQLTIIPQDPILFsgtl 1376
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKT-TLL---RIiagLETPdSGRIVLNG-RDLFTNLPPRERRVGFVFQHYALF---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1377 rmnldP---------FG----RYSEEDIwRA-----LELSHLNTFVSSQPAgldfqcaeggdNLSVGQRQLVCLARALLR 1438
Cdd:COG1118 88 -----PhmtvaeniaFGlrvrPPSKAEI-RArveelLELVQLEGLADRYPS-----------QLSGGQRQRVALARALAV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591336 1439 KSRVLVLDEATAAID------LET------DDLiqgtirtqfeDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSP 1503
Cdd:COG1118 151 EPEVLLLDEPFGALDakvrkeLRRwlrrlhDEL----------GGTTVFVTHDQEEALELaDRVVVMNQGRIEQVGTP 218
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
643-832 |
1.99e-11 |
|
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: 65.56 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSVAYVP---QQAWIQNCTLQenvlfgqPMNPKRY 719
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgpdRMVVFQNYSLL-------PWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 720 QQALETCALLADLdvlPGGDQTEIGEKGINL--------------SGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVA 785
Cdd:TIGR01184 74 NIALAVDRVLPDL---SKSERRAIVEEHIALvglteaadkrpgqlSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1388591336 786 KHIFDQV--IGPEgvlAGKTRVLVTHGIS---FLpqTDFIIVLAGGQVSEMG 832
Cdd:TIGR01184 151 GNLQEELmqIWEE---HRVTVLMVTHDVDealLL--SDRVVMLTNGPAANIG 197
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
643-776 |
2.11e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.17 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG--SVAYVPQQAWI-QNCTLQENVLFGqpmNPKRY 719
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLdDDLTVLDTVLDG---DAELR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 720 QQALETCALLADLDVlPGGDQTEIGEK-----------------------GI----------NLSGGQRQRVSLARAVYS 766
Cdd:COG0488 91 ALEAELEELEAKLAE-PDEDLERLAELqeefealggweaearaeeilsglGFpeedldrpvsELSGGWRRRVALARALLS 169
|
170
....*....|
gi 1388591336 767 DANIFLLDDP 776
Cdd:COG0488 170 EPDLLLLDEP 179
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1301-1499 |
2.29e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.19 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1301 VLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILeAAEGEIVIDGLNVAHIG---LHDLRSQLTIIPQDPilfSGTL- 1376
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDP---NSSLn 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1377 -RMNLdpfgrysEEDIWRALELSHLNTFVSSQPA---------GLDFQC-----AEggdnLSVGQRQLVCLARALLRKSR 1441
Cdd:PRK15134 377 pRLNV-------LQIIEEGLRVHQPTLSAAQREQqviavmeevGLDPETrhrypAE----FSGGQRQRIAIARALILKPS 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 1442 VLVLDEATAAIDLETDDLIQGTIRT--QFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAE 1499
Cdd:PRK15134 446 LIILDEPTSSLDKTVQAQILALLKSlqQKHQLAYLFISHDLHVVRALcHQVIVLRQGEVVE 506
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1285-1466 |
2.43e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 66.75 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNysVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHdLRSQLTI 1364
Cdd:PRK13537 8 IDFRN--VEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH-ARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1365 IPQ----DPILfsgTLRMNLDPFGRY-------SEEDIWRALELSHLNTfvssqpaGLDFQCAEggdnLSVGQRQLVCLA 1433
Cdd:PRK13537 85 VPQfdnlDPDF---TVRENLLVFGRYfglsaaaARALVPPLLEFAKLEN-------KADAKVGE----LSGGMKRRLTLA 150
|
170 180 190
....*....|....*....|....*....|...
gi 1388591336 1434 RALLRKSRVLVLDEATAAIDLETDDLIQGTIRT 1466
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRS 183
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1286-1502 |
2.71e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.01 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1286 EFRNYSVRYrPGLeLVLKNVTVHVQGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAEGEIVIDGLNVAHIGLHD-LRS 1360
Cdd:PRK11288 6 SFDGIGKTF-PGV-KALDDISFDCRAGQVHALMGENGAGKST----LLKILsgnyQPDAGSILIDGQEMRFASTTAaLAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1361 QLTIIPQD----PILfsgTLRMNL------DPFG--RYSEEDIWRALELSHLntfvssqpaGLDFQCAEGGDNLSVGQRQ 1428
Cdd:PRK11288 80 GVAIIYQElhlvPEM---TVAENLylgqlpHKGGivNRRLLNYEAREQLEHL---------GVDIDPDTPLKYLSIGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388591336 1429 LVCLARALLRKSRVLVLDEATAAIDL-ETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDY-NRVLVLDKG-VVAEFDS 1502
Cdd:PRK11288 148 MVEIAKALARNARVIAFDEPTSSLSArEIEQLFRVIRELRAEGRVILYVSHRMEEIFALcDAITVFKDGrYVATFDD 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
643-832 |
3.22e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 65.32 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSAL-----LGEMEKLEGVVSVKGS----------------VAYVPQQawIQN 701
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQdifkmdvielrrrvqmVFQIPNP--IPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 702 CTLQENVLFGQPMN---------PKRYQQALETCALLADLdvlpggdQTEIGEKGINLSGGQRQRVSLARAVYSDANIFL 772
Cdd:PRK14247 97 LSIFENVALGLKLNrlvkskkelQERVRWALEKAQLWDEV-------KDRLDAPAGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388591336 773 LDDPLSAVDSHVAKHIFDQVIGPEGVLagkTRVLVTHgisFLPQ----TDFIIVLAGGQVSEMG 832
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLELKKDM---TIVLVTH---FPQQaariSDYVAFLYKGQIVEWG 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
653-783 |
3.68e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.12 E-value: 3.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 653 GALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG----------SVAYV-PQQAWIQNCTLQENVLF-----GQpmNP 716
Cdd:PRK13539 28 GEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddpdvaeACHYLgHRNAMKPALTVAENLEFwaaflGG--EE 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388591336 717 KRYQQALETCALlADLDVLPGGdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSH 783
Cdd:PRK13539 106 LDIAAALEAVGL-APLAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1284-1495 |
4.15e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 64.51 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYRPGLElVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHD---LRS 1360
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQ-ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1361 QLTIIPQD-PILFSGTLRMNLD-PF--GRYSEEDIWR----ALELSHLNTFVSSQPAgldfqcaeggdNLSVGQRQLVCL 1432
Cdd:PRK10908 80 QIGMIFQDhHLLMDRTVYDNVAiPLiiAGASGDDIRRrvsaALDKVGLLDKAKNFPI-----------QLSGGEQQRVGI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388591336 1433 ARALLRKSRVLVLDEATAAIDletDDLIQGTIRTqFED-----CTVLTIAHRLNTIMDYN-RVLVLDKG 1495
Cdd:PRK10908 149 ARAVVNKPAVLLADEPTGNLD---DALSEGILRL-FEEfnrvgVTVLMATHDIGLISRRSyRMLTLSDG 213
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1302-1484 |
4.29e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.26 E-value: 4.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1302 LKNVTVHVQGGEKVGIVGRTGAGKSSmtlcLFRILEAA------EGEIVIDG--LNVAHI------GLHDLRSQLTIIPQ 1367
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKST----LMKVLSGVyphgtyEGEIIFEGeeLQASNIrdteraGIAIIHQELALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1368 DPILFSGTLRMNLDPFGR------YSEEDIWraleLSHLNTFVS-SQPAGldfqcaeggdNLSVGQRQLVCLARALLRKS 1440
Cdd:PRK13549 97 LSVLENIFLGNEITPGGImdydamYLRAQKL----LAQLKLDINpATPVG----------NLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1388591336 1441 RVLVLDEATAAI-DLETDDLIQGTIRTQFEDCTVLTIAHRLNTIM 1484
Cdd:PRK13549 163 RLLILDEPTASLtESETAVLLDIIRDLKAHGIACIYISHKLNEVK 207
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1304-1493 |
4.34e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.05 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1304 NVTVHVQGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAEGEIVIDGLNVAHIGlHDLRSQLtiipqdpiLFSG----- 1374
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTS----LLRILaglaRPDAGEVLWQGEPIRRQR-DEYHQDL--------LYLGhqpgi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1375 --------TLRMNLDPFGRYSEEDIWRALELshlntfvssqpAGL----DFQCAeggdNLSVGQRQLVCLARALLRKSRV 1442
Cdd:PRK13538 86 kteltaleNLRFYQRLHGPGDDEALWEALAQ-----------VGLagfeDVPVR----QLSAGQQRRVALARLWLTRAPL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1388591336 1443 LVLDEATAAIDLETDDLIQGTIRTQFED--CTVLTIAHRLNTIMDYNRVLVLD 1493
Cdd:PRK13538 151 WILDEPFTAIDKQGVARLEALLAQHAEQggMVILTTHQDLPVASDKVRKLRLG 203
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
643-828 |
5.40e-11 |
|
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: 63.78 E-value: 5.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSV------------AYVPQQAWIQNCTLQENVLF 710
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSyqkniealrrigALIEAPGFYPNLTARENLRL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 711 GQPMNPKRYQQALETcalladLDVLpgGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDshvakhifd 790
Cdd:cd03268 96 LARLLGIRKKRIDEV------LDVV--GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD--------- 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1388591336 791 qvigPEGVLA-----------GKTRVLVTHGISFLPQT-DFIIVLAGGQV 828
Cdd:cd03268 159 ----PDGIKElrelilslrdqGITVLISSHLLSEIQKVaDRIGIINKGKL 204
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
624-849 |
6.11e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 64.76 E-value: 6.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 624 YAITIHNGTFTWaQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSVAYVPQQAWIQN-- 701
Cdd:PRK13647 3 NIIEVEDLHFRY-KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSkv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 702 -------------CTLQENVLFGqPMN--------PKRYQQALETCALLADLDVLPggdqteigekgINLSGGQRQRVSL 760
Cdd:PRK13647 82 glvfqdpddqvfsSTVWDDVAFG-PVNmgldkdevERRVEEALKAVRMWDFRDKPP-----------YHLSYGQKKRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 761 ARAVYSDANIFLLDDPLSAVDSHvakhifdqviGPEGVLA--------GKTRVLVTHGISFLPQ-TDFIIVLAGGQVSEM 831
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPR----------GQETLMEildrlhnqGKTVIVATHDVDLAAEwADQVIVLKEGRVLAE 219
|
250
....*....|....*...
gi 1388591336 832 GHYSALLQHDGSFANFLR 849
Cdd:PRK13647 220 GDKSLLTDEDIVEQAGLR 237
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1306-1510 |
6.33e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 64.22 E-value: 6.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1306 TVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNvaHIGLHDLRSQLTIIPQDPILFSG-TLRMN----- 1379
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD--HTTTPPSRRPVSMLFQENNLFSHlTVAQNiglgl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1380 -----LDPFGRYSEEDIWRALELSHLNTFVSSQpagldfqcaeggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAID- 1453
Cdd:PRK10771 97 npglkLNAAQREKLHAIARQMGIEDLLARLPGQ--------------LSGGQRQRVALARCLVREQPILLLDEPFSALDp 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 1454 ---LETDDLIQGTIRTQfeDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAeFDSPVNLIAAG 1510
Cdd:PRK10771 163 alrQEMLTLVSQVCQER--QLTLLMVSHSLEDAARIaPRSLVVADGRIA-WDGPTDELLSG 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
626-832 |
7.34e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 64.77 E-value: 7.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 626 ITIHNGTFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVV-------------SVKGSVAY 692
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddnfeKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 693 VPQQAWIQ--NCTLQENVLFGQPMNPKRYQQALETCA-LLADLDVLPGGDqteigEKGINLSGGQRQRVSLARAVYSDAN 769
Cdd:PRK13648 88 VFQNPDNQfvGSIVKYDVAFGLENHAVPYDEMHRRVSeALKQVDMLERAD-----YEPNALSGGQKQRVAIAGVLALNPS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388591336 770 IFLLDDPLSAVDSHVAKHIFDQVigpEGVLAGK--TRVLVTHGISFLPQTDFIIVLAGGQVSEMG 832
Cdd:PRK13648 163 VIILDEATSMLDPDARQNLLDLV---RKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEG 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
643-838 |
7.53e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 64.22 E-value: 7.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSVAY----------VPQQAWIQNCTLQENVLFgQ 712
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkVADKNQLRLLRTRLTMVF-Q 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 713 PMNPKRYQQALETcALLADLDVLP-----------------GGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDD 775
Cdd:PRK10619 100 HFNLWSHMTVLEN-VMEAPIQVLGlskqeareravkylakvGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 776 PLSAVDSHVAKHIFD--QVIGPEgvlaGKTRVLVTHGISFLPQ-TDFIIVLAGGQVSEMGHYSALL 838
Cdd:PRK10619 179 PTSALDPELVGEVLRimQQLAEE----GKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1284-1508 |
8.48e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 63.74 E-value: 8.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHD-LRSQL 1362
Cdd:PRK11614 5 MLSFDKVSAHY--GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1363 TIIPQDPILFSG-TLRMNLDPFGRYSEED-----IWRALELSHLNTFVSSQPAGldfqcaeggdNLSVGQRQLVCLARAL 1436
Cdd:PRK11614 83 AIVPEGRRVFSRmTVEENLAMGGFFAERDqfqerIKWVYELFPRLHERRIQRAG----------TMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388591336 1437 LRKSRVLVLDEATAA----IDLETDDLIQgtiRTQFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSPVNLIA 1508
Cdd:PRK11614 153 MSQPRLLLLDEPSLGlapiIIQQIFDTIE---QLREQGMTIFLVEQNANQALKLaDRGYVLENGHVVLEDTGDALLA 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
643-841 |
8.58e-11 |
|
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: 63.85 E-value: 8.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-SVAYVPQQAWIQnctLQEN--VLFgqpmnpkry 719
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqDITGLSEKELYE---LRRRigMLF--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 720 QQAletcALLADLDV-----LPGGDQTEIGEKGIN----------------------LSGGQRQRVSLARAVYSDANIFL 772
Cdd:COG1127 89 QGG----ALFDSLTVfenvaFPLREHTDLSEAEIRelvleklelvglpgaadkmpseLSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388591336 773 LDDPLSAVDShVAKHIFDQVIgpegvLA-----GKTRVLVTHGISFLPQT-DFIIVLAGGQVSEMGHYSALLQHD 841
Cdd:COG1127 165 YDEPTAGLDP-ITSAVIDELI-----RElrdelGLTSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTPEELLASD 233
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
609-809 |
9.07e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 65.24 E-value: 9.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 609 ELDPQCVERKTISPGYAITIHNGTF-TWAQDL---------PPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEME 678
Cdd:PRK13536 13 RLELSPIERKHQGISEAKASIPGSMsTVAIDLagvsksygdKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 679 KLEGVVSVKGsvAYVPQQAWI---------------QNCTLQENVL-FGQ--PMNPKRYQQALETcalLADLDVLPGGDQ 740
Cdd:PRK13536 93 PDAGKITVLG--VPVPARARLararigvvpqfdnldLEFTVRENLLvFGRyfGMSTREIEAVIPS---LLEFARLESKAD 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 741 TEIGEkginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHvAKH-IFDQVigpEGVLA-GKTRVLVTH 809
Cdd:PRK13536 168 ARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-ARHlIWERL---RSLLArGKTILLTTH 230
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1285-1497 |
9.79e-11 |
|
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: 63.07 E-value: 9.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYRPglELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHD------- 1357
Cdd:cd03269 1 LEVENVTKRFGR--VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRigylpee 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1358 --LRSQLTIIPQdpILFSGTLR-MNLDPFGRYSEEDIWRaLELS-HLNTFVssqpagldfqcaeggDNLSVGQRQLVCLA 1433
Cdd:cd03269 79 rgLYPKMKVIDQ--LVYLAQLKgLKKEEARRRIDEWLER-LELSeYANKRV---------------EELSKGNQQKVQFI 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 1434 RALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFED-CTVLTIAHRLNTIMDY-NRVLVLDKGVV 1497
Cdd:cd03269 141 AAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELcDRVLLLNKGRA 206
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1285-1453 |
1.12e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 63.90 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSsmTL--CLFRILE-----AAEGEIVIDGLNV--AHIGL 1355
Cdd:COG1117 12 IEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKS--TLlrCLNRMNDlipgaRVEGEILLDGEDIydPDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1356 HDLRSQLTIIPQDPILFSGT--------LRMNldpfGRYSEEDI----WRALELSHLNTFVS---SQPAGldfqcaeggd 1420
Cdd:COG1117 88 VELRRRVGMVFQKPNPFPKSiydnvaygLRLH----GIKSKSELdeivEESLRKAALWDEVKdrlKKSAL---------- 153
|
170 180 190
....*....|....*....|....*....|...
gi 1388591336 1421 NLSVGQRQLVCLARALLRKSRVLVLDEATAAID 1453
Cdd:COG1117 154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
1013-1162 |
1.22e-10 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 64.37 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1013 ALGILQGLLVMLSAFTMVVGAIQAARLLHEALLHNKIRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLLNSFFT 1092
Cdd:cd18552 47 GLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLT 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591336 1093 SISTIMVIVASTP---LFMVVVLPLAVLygFVQRFyvatSRQLKRL-----ESISRspIFSHFSETVTGTSVIRAYGR 1162
Cdd:cd18552 127 VIGLLGVLFYLDWkltLIALVVLPLAAL--PIRRI----GKRLRKIsrrsqESMGD--LTSVLQETLSGIRVVKAFGA 196
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1292-1508 |
1.47e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.45 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1292 VRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIglHDLRSQLTIIPQDPI- 1370
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLV--RDKDGQLKVADKNQLr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1371 LFSGTLRMNLDPFGRYSE----EDIWRA-LELSHLNTFVSSQPA-------GLDfQCAEGG--DNLSVGQRQLVCLARAL 1436
Cdd:PRK10619 89 LLRTRLTMVFQHFNLWSHmtvlENVMEApIQVLGLSKQEARERAvkylakvGID-ERAQGKypVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591336 1437 LRKSRVLVLDEATAAIDLE-TDDLIQGTIRTQFEDCTVLTIAHRlntiMDYNR-----VLVLDKGVVAEFDSPVNLIA 1508
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPElVGEVLRIMQQLAEEGKTMVVVTHE----MGFARhvsshVIFLHQGKIEEEGAPEQLFG 241
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1301-1495 |
1.61e-10 |
|
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: 61.68 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1301 VLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQ-LTIIPQDPilfsgtLRMN 1379
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDR------KREG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1380 LdpFGRYSEEDiwralelshlNTFVSSQpagldfqcaeggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDL 1459
Cdd:cd03215 89 L--VLDLSVAE----------NIALSSL--------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190
....*....|....*....|....*....|....*...
gi 1388591336 1460 IQGTIRTQFED-CTVLTIAHRLNTIMDY-NRVLVLDKG 1495
Cdd:cd03215 143 IYRLIRELADAgKAVLLISSELDELLGLcDRILVMYEG 180
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1285-1501 |
1.74e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 63.60 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYRPGLElVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTI 1364
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1365 IPQDP--ILFSGT---------LRMNLDPfgRYSEEDIWRALELSHLNTFVSSQPAgldfqcaeggdNLSVGQRQLVCLA 1433
Cdd:PRK13647 84 VFQDPddQVFSSTvwddvafgpVNMGLDK--DEVERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 1434 RALLRKSRVLVLDEATAAIDLETDDLIQGTI-RTQFEDCTVLTIAHRLNTIMDY-NRVLVLDKG-VVAEFD 1501
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILdRLHNQGKTVIVATHDVDLAAEWaDQVIVLKEGrVLAEGD 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1284-1497 |
1.78e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 63.57 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYRPGLE----LVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIG-LHDL 1358
Cdd:PRK13633 4 MIKCKNVSYKYESNEEstekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1359 RSQLTIIPQDP------------ILFsGTLRMNLDPfgryseEDIWRALE--LSHLNTF-VSSQPAGLdfqcaeggdnLS 1423
Cdd:PRK13633 84 RNKAGMVFQNPdnqivativeedVAF-GPENLGIPP------EEIRERVDesLKKVGMYeYRRHAPHL----------LS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 1424 VGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIR--TQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVV 1497
Cdd:PRK13633 147 GGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKelNKKYGITIILITHYMEEAVEADRIIVMDSGKV 222
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
646-781 |
1.91e-10 |
|
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: 64.36 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 646 LNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-----------------SVAYVPQQAWI-QNCTLQEN 707
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrkgiflppekrRIGYVFQEARLfPHLSVRGN 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388591336 708 VLFGQ-----PMNPKRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD 781
Cdd:TIGR02142 96 LRYGMkrarpSERRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
643-781 |
1.94e-10 |
|
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: 62.56 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG--------------SVAYVPQQAWI-QNCTLQEN 707
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklpmhkrarlGIGYLPQEASIfRKLTVEEN 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388591336 708 ---VLFGQPMNPKRYQQALEtcALLADLDVLPGGDQteigeKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD 781
Cdd:cd03218 96 ilaVLEIRGLSKKEREEKLE--ELLEEFHITHLRKS-----KASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1284-1484 |
2.15e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.82 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVidglnvahiglHDLRSQLT 1363
Cdd:PRK09544 4 LVSLENVSVSF--GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKLRIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1364 IIPQ----DPILFSGTLR-MNLDPFGRysEEDIWRALELSHLNTFVSsQPAgldfqcaeggDNLSVGQRQLVCLARALLR 1438
Cdd:PRK09544 71 YVPQklylDTTLPLTVNRfLRLRPGTK--KEDILPALKRVQAGHLID-APM----------QKLSGGETQRVLLARALLN 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1439 KSRVLVLDEATAAID----LETDDLIQgTIRTQFeDCTVLTIAHRLNTIM 1484
Cdd:PRK09544 138 RPQLLVLDEPTQGVDvngqVALYDLID-QLRREL-DCAVLMVSHDLHLVM 185
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1297-1492 |
2.26e-10 |
|
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: 61.74 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1297 GLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTL 1376
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1377 RMNLDPFGRY-SEEDIWRALELSHLNTFVssqpaglDFQCAEggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLE 1455
Cdd:cd03231 91 LENLRFWHADhSDEQVEEALARVGLNGFE-------DRPVAQ----LSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 1388591336 1456 TDDLIQGTIRTQFED--CTVLTIAHRLNTIMDYNRVLVL 1492
Cdd:cd03231 160 GVARFAEAMAGHCARggMVVLTTHQDLGLSEAGARELDL 198
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1301-1495 |
2.73e-10 |
|
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: 62.35 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1301 VLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGL--------NVAHIGL-HDLRSQL--TIIPQDp 1369
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvpwkrrkkFLRRIGVvFGQKTQLwwDLPVID- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1370 ilfsgTLRMN-----LDPFgRYSE--EDIWRALELSHLntfvSSQPAgldfqcaeggDNLSVGQRQLVCLARALLRKSRV 1442
Cdd:cd03267 115 -----SFYLLaaiydLPPA-RFKKrlDELSELLDLEEL----LDTPV----------RQLSLGQRMRAEIAAALLHEPEI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 1443 LVLDEATAAIDLETDDLIQGTIRTQFED--CTVLTIAHRLNTIMDY-NRVLVLDKG 1495
Cdd:cd03267 175 LFLDEPTIGLDVVAQENIRNFLKEYNRErgTTVLLTSHYMKDIEALaRRVLVIDKG 230
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
643-781 |
2.81e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 62.75 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSAL--LGEME---KLEG---------------VVSVKGSVAYVPQQAwiqN- 701
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIpgaRVEGeilldgediydpdvdVVELRRRVGMVFQKP---Np 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 702 --CTLQENVLFG---QPMNPKRY-----QQALETCALLADL-DVLpggdqteiGEKGINLSGGQRQRVSLARAVYSDANI 770
Cdd:COG1117 104 fpKSIYDNVAYGlrlHGIKSKSEldeivEESLRKAALWDEVkDRL--------KKSALGLSGGQQQRLCIARALAVEPEV 175
|
170
....*....|.
gi 1388591336 771 FLLDDPLSAVD 781
Cdd:COG1117 176 LLMDEPTSALD 186
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
644-791 |
3.13e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 61.36 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 644 HSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG------------SVAYVPQQAWIQN-CTLQENVLF 710
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGepirrqrdeyhqDLLYLGHQPGIKTeLTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 711 GQPM----NPKRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSH-VA 785
Cdd:PRK13538 98 YQRLhgpgDDEALWEALAQVGLAGFEDVPVR-----------QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQgVA 166
|
....*...
gi 1388591336 786 --KHIFDQ 791
Cdd:PRK13538 167 rlEALLAQ 174
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1284-1453 |
3.41e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 61.34 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRyRPGLELVlKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEA---AEGEIVIDGLNVAHIGLHdlRS 1360
Cdd:COG4136 1 MLSLENLTIT-LGGRPLL-APLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1361 QLTIIPQDPILFS-----GTLRMNLDP-FGRYSEED-IWRALELSHLNTFVSSQPAgldfqcaeggdNLSVGQRQLVCLA 1433
Cdd:COG4136 77 RIGILFQDDLLFPhlsvgENLAFALPPtIGRAQRRArVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALL 145
|
170 180
....*....|....*....|
gi 1388591336 1434 RALLRKSRVLVLDEATAAID 1453
Cdd:COG4136 146 RALLAEPRALLLDEPFSKLD 165
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
626-844 |
4.15e-10 |
|
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: 62.56 E-value: 4.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 626 ITIHNGTFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLgEMEKLEGVVSVKG-------------SVAY 692
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwrkAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 693 VPQQAWIQNCTLQENV-LFGQPMNPKRYQQAlETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIF 771
Cdd:cd03289 82 IPQKVFIFSGTFRKNLdPYGKWSDEEIWKVA-EEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 772 LLDDP---LSAVDSHVAKHIFDQvigpegVLAGKTRVLVTHGISFLPQTDFIIVLAGGQVSEMGHYSALLQHDGSF 844
Cdd:cd03289 161 LLDEPsahLDPITYQVIRKTLKQ------AFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1281-1495 |
4.47e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 61.93 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1281 TRGMVEFRNYSVRYrPGLeLVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHD--- 1357
Cdd:PRK11300 2 SQPLLSVSGLMMRF-GGL-LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiar 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1358 -----------LRSQLTII-----PQDPILFSGTLR--MNLDPFGRYSEEDIWRA---LELSHLnTFVSSQPAGldfqca 1416
Cdd:PRK11300 80 mgvvrtfqhvrLFREMTVIenllvAQHQQLKTGLFSglLKTPAFRRAESEALDRAatwLERVGL-LEHANRQAG------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1417 eggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAID-LETDDLIQ--GTIRTQFeDCTVLTIAHRLNTIMDY-NRVLVL 1492
Cdd:PRK11300 153 ----NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNpKETKELDEliAELRNEH-NVTVLLIEHDMKLVMGIsDRIYVV 227
|
...
gi 1388591336 1493 DKG 1495
Cdd:PRK11300 228 NQG 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1284-1508 |
4.81e-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: 64.05 E-value: 4.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRY---RPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIV-------ID------- 1346
Cdd:TIGR03269 279 IIKVRNVSKRYisvDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDmtkpgpd 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1347 --GLNVAHIGLhdLRSQLTIIPQDPILFSGTLRMNLD-PFgryseediwralELSHLNTFVSSQPAGLDFQCAEG----- 1418
Cdd:TIGR03269 359 grGRAKRYIGI--LHQEYDLYPHRTVLDNLTEAIGLElPD------------ELARMKAVITLKMVGFDEEKAEEildky 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1419 GDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTI---RTQFEDcTVLTIAHRLNTIMDY-NRVLVLDK 1494
Cdd:TIGR03269 425 PDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkaREEMEQ-TFIIVSHDMDFVLDVcDRAALMRD 503
|
250
....*....|....
gi 1388591336 1495 GVVAEFDSPVNLIA 1508
Cdd:TIGR03269 504 GKIVKIGDPEEIVE 517
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1285-1483 |
4.81e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.98 E-value: 4.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAaEGEIVIDG--------LNVAHIGLH 1356
Cdd:PRK14258 8 IKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGrveffnqnIYERRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1357 DLRSQLTIIPQDPILFSGTLRMNLdpfgRYSEEDI-WR-ALELshlNTFVSSQPAGLDF------QCAEGGDNLSVGQRQ 1428
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNV----AYGVKIVgWRpKLEI---DDIVESALKDADLwdeikhKIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1429 LVCLARALLRKSRVLVLDEATAAID----LETDDLIQG-TIRTQFedcTVLTIAHRLNTI 1483
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSlRLRSEL---TMVIVSHNLHQV 214
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
625-828 |
5.06e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 61.93 E-value: 5.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 625 AITIHNGTFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG------SVAYVPQQAW 698
Cdd:PRK13632 7 MIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskeNLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 699 I--QN-------CTLQENVLFG---QPMNPKRYQQALETCALLADLDVLpggdqteIGEKGINLSGGQRQRVSLARAVYS 766
Cdd:PRK13632 87 IifQNpdnqfigATVEDDIAFGlenKKVPPKKMKDIIDDLAKKVGMEDY-------LDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388591336 767 DANIFLLDDPLSAVDSHvAKHIFDQVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLAGGQV 828
Cdd:PRK13632 160 NPEIIIFDESTSMLDPK-GKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKL 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1286-1501 |
5.32e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.88 E-value: 5.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1286 EFRNYSVRYRpglelvLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNV----------AHIGL 1355
Cdd:COG1129 258 EVEGLSVGGV------VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVrirsprdairAGIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1356 --HDlRSQLTIIPQDPILFSGTLrMNLDPFGRYSEedIWRALELSHLNTFVSS---------QPAGldfqcaeggdNLSV 1424
Cdd:COG1129 332 vpED-RKGEGLVLDLSIRENITL-ASLDRLSRGGL--LDRRRERALAEEYIKRlriktpspeQPVG----------NLSG 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1425 GQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFED-CTVLTIAHRLNTIMDY-NRVLVLDKG-VVAEFD 1501
Cdd:COG1129 398 GNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEgKAVIVISSELPELLGLsDRILVMREGrIVGELD 477
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1271-1479 |
5.53e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 64.00 E-value: 5.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1271 ESNRAPEGWPTRGMVEFRNYSVRYR------PGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSmtlcLFRILeaaeGEI- 1343
Cdd:TIGR00954 431 EGGRNSNLVPGRGIVEYQDNGIKFEniplvtPNGDVLIESLSFEVPSGNNLLICGPNGCGKSS----LFRIL----GELw 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1344 -VIDGLNVAhiglhDLRSQLTIIPQDPILFSGTLR------MNLDPFGR--YSEEDIWRALELSHLnTFVSSQPAGLDFQ 1414
Cdd:TIGR00954 503 pVYGGRLTK-----PAKGKLFYVPQRPYMTLGTLRdqiiypDSSEDMKRrgLSDKDLEQILDNVQL-THILEREGGWSAV 576
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1415 CaEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIqgtirtqFEDC-----TVLTIAHR 1479
Cdd:TIGR00954 577 Q-DWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYM-------YRLCrefgiTLFSVSHR 638
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1301-1505 |
6.11e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 61.60 E-value: 6.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1301 VLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVID------GLNVAHIGLHDLRSQLTIIPQDPILFS- 1373
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfGKDIFQIDAIKLRKEVGMVFQQPNPFPh 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1374 ----GTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQpagLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEAT 1449
Cdd:PRK14246 105 lsiyDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKE---VYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 1450 AAIDLETDDLIQGTIRTQFEDCTVLTIAH---RLNTIMDYnrVLVLDKGVVAE-------FDSPVN 1505
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHnpqQVARVADY--VAFLYNGELVEwgssneiFTSPKN 245
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
626-809 |
6.79e-10 |
|
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: 60.60 E-value: 6.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 626 ITIHNGTFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG------------SVAYV 693
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 694 PQqawiqnctlqENVLFGQpMNPKryqQALETCALL-------ADLDVLPGGDQTEIGEKG----INLSGGQRQRVSLAR 762
Cdd:cd03263 81 PQ----------FDALFDE-LTVR---EHLRFYARLkglpkseIKEEVELLLRVLGLTDKAnkraRTLSGGMKRKLSLAI 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1388591336 763 AVYSDANIFLLDDPLSAVDsHVAKHIFDQVIgpEGVLAGKTRVLVTH 809
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLD-PASRRAIWDLI--LEVRKGRSIILTTH 190
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
643-832 |
7.59e-10 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 60.28 E-value: 7.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGaLVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGS------------VAYVPQQ-AWIQNCTLQENV- 708
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrrIGYLPQEfGVYPNFTVREFLd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 709 ----LFGqpMNPKRYQQALetCALLADLDVLPGGDQtEIGEkginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDShV 784
Cdd:cd03264 95 yiawLKG--IPSKEVKARV--DEVLELVNLGDRAKK-KIGS----LSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP-E 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1388591336 785 AKHIFDQVIGpeGVLAGKTRVLVTHGISFLPQT-DFIIVLAGGQVSEMG 832
Cdd:cd03264 165 ERIRFRNLLS--ELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1304-1495 |
7.88e-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: 63.31 E-value: 7.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1304 NVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAA-EGEIVIDGLNVA-HIGLHDLRSQLTIIPQD-------PILFSG 1374
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDiRNPAQAIRAGIAMVPEDrkrhgivPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1375 ---TLRMnLDPFGRYSEED-------IWRALELSHLNTFVSSQPAGldfqcaeggdNLSVGQRQLVCLARALLRKSRVLV 1444
Cdd:TIGR02633 358 kniTLSV-LKSFCFKMRIDaaaelqiIGSAIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 1445 LDEATAAIDL----ETDDLIQGTIRtqfEDCTVLTIAHRLNTIMDY-NRVLVLDKG 1495
Cdd:TIGR02633 427 LDEPTRGVDVgakyEIYKLINQLAQ---EGVAIIVVSSELAEVLGLsDRVLVIGEG 479
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
626-832 |
8.14e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 61.56 E-value: 8.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 626 ITIHNGTFTWAQDLPPTLHSLN---IQIPKGALVAVVGPVGCGKSSLVS------------------ALLGEMEKLEGVV 684
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEFKALNntsLTFKKNKVTCVIGTTGSGKSTMIQltngliisetgqtivgdyAIPANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 685 SVKGSVAYV---PQQAWIQNcTLQENVLFGqPMN-PKRYQQALETCALLADLDVLPggdQTEIGEKGINLSGGQRQRVSL 760
Cdd:PRK13645 87 RLRKEIGLVfqfPEYQLFQE-TIEKDIAFG-PVNlGENKQEAYKKVPELLKLVQLP---EDYVKRSPFELSGGQKRRVAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388591336 761 ARAVYSDANIFLLDDPLSAVDSHvAKHIFDQVIGPEGVLAGKTRVLVTHGI-SFLPQTDFIIVLAGGQVSEMG 832
Cdd:PRK13645 162 AGIIAMDGNTLVLDEPTGGLDPK-GEEDFINLFERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIG 233
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1284-1503 |
8.71e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 62.55 E-value: 8.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYRPglELVLKNVTVHVQGGEKVGIVGRTGAGKSSmtlcLFRILEAAE----GEIVIDGLNVAHIGLHdlR 1359
Cdd:PRK11607 19 LLEIRNLTKSFDG--QHAVDDVSLTIYKGEIFALLGASGCGKST----LLRMLAGFEqptaGQIMLDGVDLSHVPPY--Q 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1360 SQLTIIPQDPILFSG-TLRMNLdPFG----RYSEEDI----WRALELSHLNTFVSSQPagldfqcaeggDNLSVGQRQLV 1430
Cdd:PRK11607 91 RPINMMFQSYALFPHmTVEQNI-AFGlkqdKLPKAEIasrvNEMLGLVHMQEFAKRKP-----------HQLSGGQRQRV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 1431 CLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFE--DCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSP 1503
Cdd:PRK11607 159 ALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHDQEEAMTMaGRIAIMNRGKFVQIGEP 234
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
646-776 |
9.33e-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: 63.03 E-value: 9.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 646 LNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSV--AYVPQQ--AWIQNCTLQENVLFGQ--------P 713
Cdd:TIGR03719 341 LSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVklAYVDQSrdALDPNKTVWEEISGGLdiiklgkrE 420
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388591336 714 MNPKRYqqaletCALLAdldvLPGGDQTE-IGEkginLSGGQRQRVSLARAVYSDANIFLLDDP 776
Cdd:TIGR03719 421 IPSRAY------VGRFN----FKGSDQQKkVGQ----LSGGERNRVHLAKTLKSGGNVLLLDEP 470
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
646-828 |
1.32e-09 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 60.14 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 646 LNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-SVAYVP-------------QQAWI-QNCTLQENVL- 709
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeDITGLPpheiarlgigrtfQIPRLfPELTVLENVMv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 710 ---------FGQPMNPKRYQQA-------LETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLL 773
Cdd:cd03219 99 aaqartgsgLLLARARREEREAreraeelLERVGLADLADRPAG-----------ELSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1388591336 774 DDP---LSAVDSHVAKHIFDQVigpegVLAGKTRVLVTHGISFLPQ-TDFIIVLAGGQV 828
Cdd:cd03219 168 DEPaagLNPEETEELAELIREL-----RERGITVLLVEHDMDVVMSlADRVTVLDQGRV 221
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
1009-1256 |
1.43e-09 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 60.86 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1009 GVYAALGILQGLLVMLSAFTMVVGAIQAARLLHEALLHNKIRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLLN 1088
Cdd:cd18544 45 LLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1089 SFFTsISTIMVIVAST----PLFMVVVLPLAVLygfVQRFYVATSRQLKRLESISRSPIFSHFSETVTGTSVIRAYGR-- 1162
Cdd:cd18544 125 DLLL-LIGILIAMFLLnwrlALISLLVLPLLLL---ATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNRek 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1163 --IQDFKVLSDTKVDNNQKSSYpYIASNRWLgvhVEFVGNcvVLFAALFAVIGRNSLNpGLVGLSVSYALqvtmaLNWM- 1239
Cdd:cd18544 201 reFEEFDEINQEYRKANLKSIK-LFALFRPL---VELLSS--LALALVLWYGGGQVLS-GAVTLGVLYAF-----IQYIq 268
|
250 260
....*....|....*....|....*.
gi 1388591336 1240 -----IRMISD----LESNIIAVERV 1256
Cdd:cd18544 269 rffrpIRDLAEkfniLQSAMASAERI 294
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
643-828 |
1.45e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 60.86 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG--------SVAYVPQQAWI--QNC-------TLQ 705
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikydkkSLLEVRKTVGIvfQNPddqlfapTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 706 ENVLFGqPMN--------PKRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPL 777
Cdd:PRK13639 98 EDVAFG-PLNlglskeevEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 778 SAVD----SHVAKHIFDqvIGPEGVlagkTRVLVTHGISFLP-QTDFIIVLAGGQV 828
Cdd:PRK13639 166 SGLDpmgaSQIMKLLYD--LNKEGI----TIIISTHDVDLVPvYADKVYVMSDGKI 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
643-809 |
1.69e-09 |
|
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: 59.60 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGS---------VAYVPQQAWI-QNCTLQENVL-FG 711
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaarnrIGYLPEERGLyPKMKVIDQLVyLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 712 QPMNPKRYQQALETCALLADLDVlpggdqTEIGEKGIN-LSGGQRQRVSLARAVYSDANIFLLDDPLSAVDShVAKHIFD 790
Cdd:cd03269 96 QLKGLKKEEARRRIDEWLERLEL------SEYANKRVEeLSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VNVELLK 168
|
170
....*....|....*....
gi 1388591336 791 QVIGpEGVLAGKTRVLVTH 809
Cdd:cd03269 169 DVIR-ELARAGKTVILSTH 186
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
653-809 |
1.97e-09 |
|
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: 59.04 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 653 GALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSVAYVPQQAWIQNC-------------TLQENVLFGQPMNPK-R 718
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLlylghapgikttlSVLENLRFWHADHSDeQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 719 YQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGPEGv 798
Cdd:cd03231 106 VEEALARVGLNGFEDRPVA-----------QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCA- 173
|
170
....*....|.
gi 1388591336 799 lAGKTRVLVTH 809
Cdd:cd03231 174 -RGGMVVLTTH 183
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
646-809 |
2.14e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.20 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 646 LNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKgsvayVPQQAWIQNCTLQENVLFGQPMNPKRYqqALET 725
Cdd:COG2401 49 LNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----VPDNQFGREASLIDAIGRKGDFKDAVE--LLNA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 726 CALladldvlpgGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKhifdqvIGPEGVL-----A 800
Cdd:COG2401 122 VGL---------SDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK------RVARNLQklarrA 186
|
....*....
gi 1388591336 801 GKTRVLVTH 809
Cdd:COG2401 187 GITLVVATH 195
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1285-1495 |
2.22e-09 |
|
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: 57.46 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAEGEI-VIDGLNVAHIglhdlr 1359
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKST----LLKLIagelEPDEGIVtWGSTVKIGYF------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1360 SQLtiipqdpilfSGtlrmnldpfgryseediwralelshlntfvssqpagldfqcaeggdnlsvGQRQLVCLARALLRK 1439
Cdd:cd03221 69 EQL----------SG--------------------------------------------------GEKMRLALAKLLLEN 88
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1388591336 1440 SRVLVLDEATAAIDLETDDLIQGTIRTQfeDCTVLTIAH-R--LNTIMdyNRVLVLDKG 1495
Cdd:cd03221 89 PNLLLLDEPTNHLDLESIEALEEALKEY--PGTVILVSHdRyfLDQVA--TKIIELEDG 143
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1285-1453 |
2.35e-09 |
|
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: 59.19 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHD------- 1357
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDrdiamvf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1358 ----LRSQLTIIpqDPILFSGTLRmnldpfgRYSEEDIWR----ALELSHLNTFVSSQPAgldfqcaeggdNLSVGQRQL 1429
Cdd:cd03301 79 qnyaLYPHMTVY--DNIAFGLKLR-------KVPKDEIDErvreVAELLQIEHLLDRKPK-----------QLSGGQRQR 138
|
170 180
....*....|....*....|....
gi 1388591336 1430 VCLARALLRKSRVLVLDEATAAID 1453
Cdd:cd03301 139 VALGRAIVREPKVFLMDEPLSNLD 162
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
643-792 |
2.43e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 59.51 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG--------------SVAYVPQQAWI-QNCTLQEN 707
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkditdwqtakimreAVAIVPEGRRVfSRMTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 708 VLFGQPM-NPKRYQQALETCalladLDVLPGGDQTEIGEKGiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAK 786
Cdd:PRK11614 101 LAMGGFFaERDQFQERIKWV-----YELFPRLHERRIQRAG-TMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
....*.
gi 1388591336 787 HIFDQV 792
Cdd:PRK11614 175 QIFDTI 180
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1285-1510 |
2.59e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 60.18 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYRPGLEL---VLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIG----LHD 1357
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1358 LRSQLTIIPQDP------------ILFS-GTLRMNLDPFGRYSEEDIwraLELSHLNTFVSSQPagldFQcaeggdnLSV 1424
Cdd:PRK13646 83 VRKRIGMVFQFPesqlfedtvereIIFGpKNFKMNLDEVKNYAHRLL---MDLGFSRDVMSQSP----FQ-------MSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1425 GQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT-QFEDC-TVLTIAHRLNTIMDY-NRVLVLDKGVVAEFD 1501
Cdd:PRK13646 149 GQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlQTDENkTIILVSHDMNEVARYaDEVIVMKEGSIVSQT 228
|
....*....
gi 1388591336 1502 SPVNLIAAG 1510
Cdd:PRK13646 229 SPKELFKDK 237
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
625-828 |
2.84e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 59.81 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 625 AITIHNGTFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSS---LVSALLGEMEKLEGVVSVKGsVAYVPQQAW--- 698
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDG-ITLTAKTVWdir 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 699 ------IQN-------CTLQENVLFG-------QPMNPKRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRV 758
Cdd:PRK13640 84 ekvgivFQNpdnqfvgATVGDDVAFGlenravpRPEMIKIVRDVLADVGMLDYIDSEPA-----------NLSGGQKQRV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 759 SLARAVYSDANIFLLDDPLSAVDSHVAKHIFDqVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLAGGQV 828
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILK-LIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
1008-1213 |
3.48e-09 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 59.81 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1008 LGVYAALGILQGLLVMLSAFTMVVGAIQAARLLHEALLHNKIRS-------PQSFFDTTPSGRILNRFSKDIYVIDEVLA 1080
Cdd:cd18546 35 LGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVfahlqrlSLDFHERETSGRIMTRMTSDIDALSELLQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1081 PTILMLLNSFFTSIS-TIMVIVASTPLFMVVVLPLAVLYGFVQRFYVATSRQLKRL-ESISRspIFSHFSETVTGTSVIR 1158
Cdd:cd18546 115 TGLVQLVVSLLTLVGiAVVLLVLDPRLALVALAALPPLALATRWFRRRSSRAYRRArERIAA--VNADLQETLAGIRVVQ 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388591336 1159 AYGR----IQDFKVLSDTKVDNNQKSSYpYIAsnrWLGVHVEFVGNC---VVLFAALFAVIG 1213
Cdd:cd18546 193 AFRRerrnAERFAELSDDYRDARLRAQR-LVA---IYFPGVELLGNLataAVLLVGAWRVAA 250
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
643-832 |
3.61e-09 |
|
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: 59.33 E-value: 3.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEM------------EKLeGVVSV---KGSVAYV-P--QQAWIQNCTL 704
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpptygndvrlfgERR-GGEDVwelRKRIGLVsPalQLRFPRDETV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 705 QENVL---FGQPMNPKRY--QQALETCALLADLDVLPGGDQTeIGEkginLSGGQRQRVSLARAVYSDANIFLLDDPLSA 779
Cdd:COG1119 98 LDVVLsgfFDSIGLYREPtdEQRERARELLELLGLAHLADRP-FGT----LSQGEQRRVLIARALVKDPELLILDEPTAG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1388591336 780 VDSHvAKHIFDQVIgpeGVLAG---KTRVLVTHGISFLPQ-TDFIIVLAGGQVSEMG 832
Cdd:COG1119 173 LDLG-ARELLLALL---DKLAAegaPTLVLVTHHVEEIPPgITHVLLLKDGRVVAAG 225
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
626-828 |
3.90e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 59.62 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 626 ITIHNGTFTWAqDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSL---VSALL--------------GEMEKLEGVVSVKG 688
Cdd:PRK13644 2 IRLENVSYSYP-DGTPALENINLVIKKGEYIGIIGKNGSGKSTLalhLNGLLrpqkgkvlvsgidtGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 689 SVAYVPQQAWIQNcTLQENVLFGqPMN--------PKRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSL 760
Cdd:PRK13644 81 IVFQNPETQFVGR-TVEEDLAFG-PENlclppieiRKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591336 761 ARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGPEGvlAGKTRVLVTHGISFLPQTDFIIVLAGGQV 828
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHE--KGKTIVYITHNLEELHDADRIIVMDRGKI 213
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
626-837 |
4.27e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 59.71 E-value: 4.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 626 ITIHNGTFTWAQDLP---PTLHSLNIQIPKGALVAVVGPVGCGKSSLV---SALL----GEME----------------- 678
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtelKALDNVSVEINQGEFIAIIGQTGSGKTTFIehlNALLlpdtGTIEwifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 679 -------------KLEGVVSVKGSVAYVPQQAWIQ--NCTLQENVLFGqPMN---PKryQQALEtcaLLADLDVLPGGDQ 740
Cdd:PRK13651 83 vleklviqktrfkKIKKIKEIRRRVGVVFQFAEYQlfEQTIEKDIIFG-PVSmgvSK--EEAKK---RAAKYIELVGLDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 741 TEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDqvIGPEGVLAGKTRVLVTHGI-SFLPQTDF 819
Cdd:PRK13651 157 SYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKQGKTIILVTHDLdNVLEWTKR 234
|
250
....*....|....*....
gi 1388591336 820 IIVLAGGQVSEMGH-YSAL 837
Cdd:PRK13651 235 TIFFKDGKIIKDGDtYDIL 253
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1302-1483 |
4.35e-09 |
|
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: 60.99 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1302 LKNVTVHVQGGEKVGIVGRTGAGKSSmtlcLFRILEAA------EGEIVIDG--LNVAHI------GLHDLRSQLTIIPQ 1367
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKST----LMKILSGVyphgtwDGEIYWSGspLKASNIrdteraGIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1368 DPIL---FSG---TL---RMNLDPFGRYSEEdIWRALELSHLNTfvsSQPAGldfqcaeggdNLSVGQRQLVCLARALLR 1438
Cdd:TIGR02633 93 LSVAeniFLGneiTLpggRMAYNAMYLRAKN-LLRELQLDADNV---TRPVG----------DYGGGQQQLVEIAKALNK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1388591336 1439 KSRVLVLDEATAAI-DLETDDLIQGTIRTQFEDCTVLTIAHRLNTI 1483
Cdd:TIGR02633 159 QARLLILDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEV 204
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
618-841 |
4.58e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.03 E-value: 4.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 618 KTISPGYAITIHNGTFTWAQDLppTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGS-------- 689
Cdd:PRK10575 4 YTNHSDTTFALRNVSFRVPGRT--LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswssk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 690 -----VAYVPQQ-AWIQNCTLQENVLFGQ-PMNPK--RYQQA----LETCALLADLdvlpggdqTEIGEKGIN-LSGGQR 755
Cdd:PRK10575 82 afarkVAYLPQQlPAAEGMTVRELVAIGRyPWHGAlgRFGAAdrekVEEAISLVGL--------KPLAHRLVDsLSGGER 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 756 QRVSLARAVYSDANIFLLDDPLSAVDshvakhIFDQVigpeGVLA---------GKTRVLVTHGISFLPQ-TDFIIVLAG 825
Cdd:PRK10575 154 QRAWIAMLVAQDSRCLLLDEPTSALD------IAHQV----DVLAlvhrlsqerGLTVIAVLHDINMAARyCDYLVALRG 223
|
250
....*....|....*.
gi 1388591336 826 GQVSEMGHYSALLQHD 841
Cdd:PRK10575 224 GEMIAQGTPAELMRGE 239
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
643-832 |
5.66e-09 |
|
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: 58.15 E-value: 5.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-SVAYVPQQA---------------WIqncTLQE 706
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEArrrlgfvsdstglydRL---TARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 707 NVLFGQPMnpkryqQALETCALLADLDVLpgGDQTEIGE----KGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDS 782
Cdd:cd03266 98 NLEYFAGL------YGLKGDELTARLEEL--ADRLGMEElldrRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 783 HVAKHIFDQVigPEGVLAGKTRVLVTHGISFLPQ-TDFIIVLAGGQVSEMG 832
Cdd:cd03266 170 MATRALREFI--RQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1295-1508 |
6.00e-09 |
|
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: 59.73 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1295 RPGLELvlkNVTVHVQGGEKVGIVGRTGAGKSSmtlcLFRI---LE-AAEGEIVIDG---------LNVA----HIGLhd 1357
Cdd:COG4148 11 RGGFTL---DVDFTLPGRGVTALFGPSGSGKTT----LLRAiagLErPDSGRIRLGGevlqdsargIFLPphrrRIGY-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1358 lrsqltiIPQDPILFSG-TLRMNLDpFG---------RYSEEDIWRALELSHLntfVSSQPAgldfqcaeggdNLSVGQR 1427
Cdd:COG4148 82 -------VFQEARLFPHlSVRGNLL-YGrkrapraerRISFDEVVELLGIGHL---LDRRPA-----------TLSGGER 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1428 QLVCLARALLRKSRVLVLDEATAAIDLETDDLIQ---GTIRTQFeDCTVLTIAHRLNTIM---DynRVLVLDKGVVAEFD 1501
Cdd:COG4148 140 QRVAIGRALLSSPRLLLMDEPLAALDLARKAEILpylERLRDEL-DIPILYVSHSLDEVArlaD--HVVLLEQGRVVASG 216
|
....*..
gi 1388591336 1502 SPVNLIA 1508
Cdd:COG4148 217 PLAEVLS 223
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
643-839 |
6.05e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.98 E-value: 6.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVK--------------------GSVAYVPQQAWIQNC 702
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGdivvsstskqkeikpvrkkvGVVFQFPESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 703 TLQEnVLFGqpmnPKRYQQALETCALLADLDVLPGGDQTEIGEKG-INLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD 781
Cdd:PRK13643 102 VLKD-VAFG----PQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSpFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388591336 782 SHV---AKHIFDQVIGpegvlAGKTRVLVTHGISFLPQ-TDFIIVLAGGQVSEMGHYSALLQ 839
Cdd:PRK13643 177 PKArieMMQLFESIHQ-----SGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
649-779 |
6.29e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.59 E-value: 6.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 649 QIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSVAYVPQ----------QAWIQNCT--LQENVLFGQPMNP 716
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQyikpdydgtvEDLLRSITddLGSSYYKSEIIKP 440
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388591336 717 KRYQQALEtcallADLDvlpggdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPlSA 779
Cdd:PRK13409 441 LQLERLLD-----KNVK---------------DLSGGELQRVAIAACLSRDADLYLLDEP-SA 482
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1281-1509 |
6.68e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.49 E-value: 6.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1281 TRGMVEFRNYSVRYRPGLEL--VLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAA-----EGEIVIDGLNVAHI 1353
Cdd:PRK15134 2 TQPLLAIENLSVAFRQQQTVrtVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1354 GLHDLR----SQLTIIPQDPILfsgtlrmNLDPFG-------------RYSEEDIWRALELSHLNTFVSSQPAGldfQCA 1416
Cdd:PRK15134 82 SEQTLRgvrgNKIAMIFQEPMV-------SLNPLHtlekqlyevlslhRGMRREAARGEILNCLDRVGIRQAAK---RLT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1417 EGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIR--TQFEDCTVLTIAHRLNTIMDY-NRVLVLD 1493
Cdd:PRK15134 152 DYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKLaDRVAVMQ 231
|
250
....*....|....*.
gi 1388591336 1494 KGVVAEFDSPVNLIAA 1509
Cdd:PRK15134 232 NGRCVEQNRAATLFSA 247
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1288-1460 |
6.75e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 58.29 E-value: 6.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1288 RNYSVRYRPG--LELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDG--LN-VAHIGLHDLRSQ- 1361
Cdd:PRK11629 9 DNLCKRYQEGsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpMSkLSSAAKAELRNQk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1362 LTIIPQDPIL---FSG--TLRMNLDPFGRYSEEDIWRALELshlntfvsSQPAGLDFQCAEGGDNLSVGQRQLVCLARAL 1436
Cdd:PRK11629 89 LGFIYQFHHLlpdFTAleNVAMPLLIGKKKPAEINSRALEM--------LAAVGLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180
....*....|....*....|....
gi 1388591336 1437 LRKSRVLVLDEATAAIDLETDDLI 1460
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSI 184
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
653-832 |
6.93e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 60.45 E-value: 6.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 653 GALVAVVGPVGCGKSSLVSALLGEMEK---LEGVVSVKGSV----------AYVPQQ-AWIQNCTLQENVLF------GQ 712
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPidakemraisAYVQQDdLFIPTLTVREHLMFqahlrmPR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 713 PMNPKRYQQALEtcALLADLDVLPGGDqTEIGEKGI--NLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFD 790
Cdd:TIGR00955 131 RVTKKEKRERVD--EVLQALGLRKCAN-TRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQ 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1388591336 791 QVIGpegvLA--GKTRVLVTHGIS--FLPQTDFIIVLAGGQVSEMG 832
Cdd:TIGR00955 208 VLKG----LAqkGKTIICTIHQPSseLFELFDKIILMAEGRVAYLG 249
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1301-1453 |
7.38e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 57.98 E-value: 7.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1301 VLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHD-LRSQLTIIPQDPILFS------ 1373
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFRrlsvyd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1374 ---GTLRMNLDpfgRYSEEDIWRALEL------SHLNTFVssqpagldfqcaegGDNLSVGQRQLVCLARALLRKSRVLV 1444
Cdd:PRK10895 98 nlmAVLQIRDD---LSAEQREDRANELmeefhiEHLRDSM--------------GQSLSGGERRRVEIARALAANPKFIL 160
|
....*....
gi 1388591336 1445 LDEATAAID 1453
Cdd:PRK10895 161 LDEPFAGVD 169
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1286-1453 |
8.30e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.94 E-value: 8.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1286 EFRNYSVRY--RPGLELVlKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAA-EGEIVIDGLNVA-HIGLHDLRSQ 1361
Cdd:PRK13549 261 EVRNLTAWDpvNPHIKRV-DDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVKiRNPQQAIAQG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1362 LTIIPQD-------PILFSG---TLrMNLDPFGRYSEEDiwRALELSHLNTFVSS---QPAGLDFQCAeggdNLSVGQRQ 1428
Cdd:PRK13549 340 IAMVPEDrkrdgivPVMGVGkniTL-AALDRFTGGSRID--DAAELKTILESIQRlkvKTASPELAIA----RLSGGNQQ 412
|
170 180
....*....|....*....|....*
gi 1388591336 1429 LVCLARALLRKSRVLVLDEATAAID 1453
Cdd:PRK13549 413 KAVLAKCLLLNPKILILDEPTRGID 437
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
650-788 |
8.42e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 58.19 E-value: 8.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 650 IPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-SVAYVPQQAWIQNCTLQENVLFGqpMNPKRYQQALETCAL 728
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYIKADYEGTVRDLLSS--ITKDFYTHPYFKTEI 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388591336 729 LADLDVLPGGDQtEIGEkginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDS----HVAKHI 788
Cdd:cd03237 100 AKPLQIEQILDR-EVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrlMASKVI 158
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1285-1506 |
8.42e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 59.35 E-value: 8.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMtLCLFRILEA-AEGEIVIDGLNVAHIGLHdlRSQLT 1363
Cdd:PRK11432 7 VVLKNITKRF--GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTV-LRLVAGLEKpTEGQIFIDGEDVTHRSIQ--QRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1364 IIPQDPILFSGT---------LRMnldpFGRYSEEDIWR---ALELSHL----NTFVssqpagldfqcaeggDNLSVGQR 1427
Cdd:PRK11432 82 MVFQSYALFPHMslgenvgygLKM----LGVPKEERKQRvkeALELVDLagfeDRYV---------------DQISGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1428 QLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIR---TQFeDCTVLTIAH-RLNTIMDYNRVLVLDKGVVAEFDSP 1503
Cdd:PRK11432 143 QRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRelqQQF-NITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSP 221
|
...
gi 1388591336 1504 VNL 1506
Cdd:PRK11432 222 QEL 224
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1302-1505 |
8.46e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 58.95 E-value: 8.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1302 LKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGL--------NVAHIGL---HdlRSQL--TIIPQD 1368
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYvpfkrrkeFARRIGVvfgQ--RSQLwwDLPAID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1369 pilfsgTLRMN-----LDP------FGRYSEEdiwraLELSH-LNTFVSsqpagldfqcaeggdNLSVGQRQLVCLARAL 1436
Cdd:COG4586 116 ------SFRLLkaiyrIPDaeykkrLDELVEL-----LDLGElLDTPVR---------------QLSLGQRMRCELAAAL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388591336 1437 LRKSRVLVLDEATaaIDLetDDLIQGTIRtQF-------EDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAeFDSPVN 1505
Cdd:COG4586 170 LHRPKILFLDEPT--IGL--DVVSKEAIR-EFlkeynreRGTTILLTSHDMDDIEALcDRVIVIDHGRII-YDGSLE 240
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1301-1499 |
9.69e-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: 56.77 E-value: 9.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1301 VLKNVTVHVQGGEKVGIVGRTGAGKS--SMTLCLFRILEAAEGEIVIDGLNVAHIGLHDlRSQ--LTIIPQDPILFSGtl 1376
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKStlAKTIMGHPKYEVTEGEILFKGEDITDLPPEE-RARlgIFLAFQYPPEIPG-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1377 rMNLDPFGRYseediwralelshLNtfvssqpagldfqcaeggDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLET 1456
Cdd:cd03217 92 -VKNADFLRY-------------VN------------------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1388591336 1457 DDLIQGTIRT-QFEDCTVLTIAHRLNtIMDY---NRVLVLDKGVVAE 1499
Cdd:cd03217 140 LRLVAEVINKlREEGKSVLIITHYQR-LLDYikpDRVHVLYDGRIVK 185
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
647-781 |
1.00e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 57.73 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 647 NIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGS--------------VAYVPQQAWI-QNCTLQEN---V 708
Cdd:COG1137 23 SLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmhkrarlgIGYLPQEASIfRKLTVEDNilaV 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388591336 709 LFGQPMNPKRYQQALEtcALLADLDVLPGGDQteigeKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD 781
Cdd:COG1137 103 LELRKLSKKEREERLE--ELLEEFGITHLRKS-----KAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1285-1508 |
1.01e-08 |
|
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: 59.82 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYRpGLElVLKNVTVHVQGGEKVGIVGRTGAGKSSMtLCLFRIL---EAAEGEIV----------------- 1344
Cdd:TIGR03269 1 IEVKNLTKKFD-GKE-VLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMdqyEPTSGRIIyhvalcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1345 ----------------IDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRM------NLDPFGRYSEEDIWRALEL----- 1397
Cdd:TIGR03269 78 vgepcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTVldnvleALEEIGYEGKEAVGRAVDLiemvq 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1398 -SHLNTFVSSqpagldfqcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIR--TQFEDCTVL 1474
Cdd:TIGR03269 158 lSHRITHIAR--------------DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEeaVKASGISMV 223
|
250 260 270
....*....|....*....|....*....|....*
gi 1388591336 1475 TIAHRLNTIMDY-NRVLVLDKGVVAEFDSPVNLIA 1508
Cdd:TIGR03269 224 LTSHWPEVIEDLsDKAIWLENGEIKEEGTPDEVVA 258
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
626-828 |
1.04e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 58.20 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 626 ITIHNGTFTWAQDLP-PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSvAYVPQQAW------ 698
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD-LLTEENVWdirhki 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 699 ---IQN-------CTLQENVLFG--------QPMNpKRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSL 760
Cdd:PRK13650 84 gmvFQNpdnqfvgATVEDDVAFGlenkgiphEEMK-ERVNEALELVGMQDFKEREPA-----------RLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 761 ARAVYSDANIFLLDDPLSAVDshvakhifdqvigPEGVLA------------GKTRVLVTHGISFLPQTDFIIVLAGGQV 828
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLD-------------PEGRLEliktikgirddyQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
648-781 |
1.15e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 57.87 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 648 IQIPKGALVAVVGPVGCGKSSLVSAL-----LGEMEKLEGVVSVKGSVAYVP---------------QQAWIQNCTLQEN 707
Cdd:PRK14243 31 LDIPKNQITAFIGPSGCGKSTILRCFnrlndLIPGFRVEGKVTFHGKNLYAPdvdpvevrrrigmvfQKPNPFPKSIYDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 708 VLFGQPMNPKR------YQQALETCALLADLdvlpggdQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD 781
Cdd:PRK14243 111 IAYGARINGYKgdmdelVERSLRQAALWDEV-------KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALD 183
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
653-810 |
1.20e-08 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 56.60 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 653 GALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSVAYVPQQAWIQNC-------------TLQENVLFGQPMNpkRY 719
Cdd:TIGR01189 26 GEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENIlylghlpglkpelSALENLHFWAAIH--GG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 720 QQ-----ALETCALlADLDVLPGGdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD-SHVAK--HIFDQ 791
Cdd:TIGR01189 104 AQrtiedALAAVGL-TGFEDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPTTALDkAGVALlaGLLRA 172
|
170
....*....|....*....
gi 1388591336 792 VIGPEGVLagktrVLVTHG 810
Cdd:TIGR01189 173 HLARGGIV-----LLTTHQ 186
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
643-809 |
1.32e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 57.13 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG---SVAYVPQQAWIQNCTLQ-------------- 705
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmSKLSSAAKAELRNQKLGfiyqfhhllpdfta 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 706 -ENV----LFGQpMNPKRYQQ-ALETCALLadldvlpgGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSA 779
Cdd:PRK11629 105 lENVamplLIGK-KKPAEINSrALEMLAAV--------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190
....*....|....*....|....*....|
gi 1388591336 780 VDSHVAKHIFdQVIGPEGVLAGKTRVLVTH 809
Cdd:PRK11629 176 LDARNADSIF-QLLGELNRLQGTAFLVVTH 204
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1286-1503 |
1.91e-08 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 58.93 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1286 EFRNYSVRYRPGLEL--VLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEA----AEGEIVIDGLNVAHIGLHDLR 1359
Cdd:COG4172 8 SVEDLSVAFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSILFDGQDLLGLSERELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1360 ----SQLTIIPQDPilfsgtlrMN-LDPF--------------GRYSEEDIW-RALEL----------SHLNTFvssqPa 1409
Cdd:COG4172 88 rirgNRIAMIFQEP--------MTsLNPLhtigkqiaevlrlhRGLSGAAARaRALELlervgipdpeRRLDAY----P- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1410 gldFQcaeggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLetddliqgTIRTQF----------EDCTVLTIAHR 1479
Cdd:COG4172 155 ---HQ-------LSGGQRQRVMIAMALANEPDLLIADEPTTALDV--------TVQAQIldllkdlqreLGMALLLITHD 216
|
250 260 270
....*....|....*....|....*....|..
gi 1388591336 1480 LNTIMDY-NRVLVLDKGVVAE-------FDSP 1503
Cdd:COG4172 217 LGVVRRFaDRVAVMRQGEIVEqgptaelFAAP 248
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
641-809 |
1.93e-08 |
|
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: 56.96 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSVAYVPQQAWIQNCTlqenVLFGQ-------- 712
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIG----VVFGQktqlwwdl 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 713 -PMN------------PKRYQQALETCALLADLdvlpggdqTEIGEKGI-NLSGGQRQRVSLARAVYSDANIFLLDDPLS 778
Cdd:cd03267 111 pVIDsfyllaaiydlpPARFKKRLDELSELLDL--------EELLDTPVrQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190
....*....|....*....|....*....|.
gi 1388591336 779 AVDShVAKHIFDQVIGPEGVLAGKTRVLVTH 809
Cdd:cd03267 183 GLDV-VAQENIRNFLKEYNRERGTTVLLTSH 212
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
649-788 |
2.22e-08 |
|
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: 58.64 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 649 QIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSVAYVPQQAWIQNCTLQENVLFGqpMNPKRYQQALEtcal 728
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQYISPDYDGTVEEFLRS--ANTDDFGSSYY---- 435
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388591336 729 ladldvlpggdQTEIGEK-GI---------NLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDS----HVAKHI 788
Cdd:COG1245 436 -----------KTEIIKPlGLeklldknvkDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVAKAI 498
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1302-1497 |
3.18e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 56.56 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1302 LKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRIL---EAAEGEIVIDGLNV--------------AHIGL----HDLRS 1360
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVqregrlardirksrANTGYifqqFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1361 QLTIIPQDPILFSGTL---RMNLDPFGRYSEEDIWRALELSHLNTFVSSQPAgldfqcaeggdNLSVGQRQLVCLARALL 1437
Cdd:PRK09984 100 RLSVLENVLIGALGSTpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVS-----------TLSGGQQQRVAIARALM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388591336 1438 RKSRVLVLDEATAAIDLETDDLIQGTIR--TQFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVV 1497
Cdd:PRK09984 169 QQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDYALRYcERIVALRQGHV 231
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
643-828 |
3.32e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 58.20 E-value: 3.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSaLLGEMEK-LEGVVSVKGS-VAYVPQQAWIQ-----------------NCT 703
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDKpTSGTYRVAGQdVATLDADALAQlrrehfgfifqryhllsHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 704 LQENV----LFGQPMNPKRYQQALEtcaLLADLdvlpgGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSA 779
Cdd:PRK10535 103 AAQNVevpaVYAGLERKQRLLRAQE---LLQRL-----GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 780 VDSH-------VAKHIFDQvigpegvlaGKTRVLVTHGISFLPQTDFIIVLAGGQV 828
Cdd:PRK10535 175 LDSHsgeevmaILHQLRDR---------GHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
643-898 |
3.93e-08 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 57.01 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGemekLE----GVVSVKG----------------SVAYVPQQ-AWIQN 701
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL----LErptsGSVLVDGvdltalserelraarrKIGMIFQHfNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 702 CTLQENVLFgqPM------NPKRYQQALETCAL--LADL-DVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFL 772
Cdd:COG1135 97 RTVAENVAL--PLeiagvpKAEIRKRVAELLELvgLSDKaDAYPS-----------QLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 773 LDDPLSAVDshvakhifdqvigPE---GVLA---------GKTRVLVTHgisflpQTDFI--I-----VLAGGQVSEMGH 833
Cdd:COG1135 164 CDEATSALD-------------PEttrSILDllkdinrelGLTIVLITH------EMDVVrrIcdrvaVLENGRIVEQGP 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388591336 834 YSALLQHDGSFA--NFLRNYAPDEDQEDHEAALQNANEEVLLLEDTLsthTDLTDNEPAIYEVRKQF 898
Cdd:COG1135 225 VLDVFANPQSELtrRFLPTVLNDELPEELLARLREAAGGGRLVRLTF---VGESADEPLLSELARRF 288
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
643-948 |
5.27e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.49 E-value: 5.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSV-KG-SVAYVPQQAwIQNCTLQENVLfgQPMN---PK 717
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGiKLGYFAQHQ-LEFLRADESPL--QHLArlaPQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 718 RYQQALEtcalladlDVLPG----GDQ-TEIGEKginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQV 792
Cdd:PRK10636 405 ELEQKLR--------DYLGGfgfqGDKvTEETRR---FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 793 IGPEGVLagktrVLVTHGISFLPQT--DFIIVlaggqvsemghysallqHDGSFANFlrnyapDEDQEDHEAALQNANEE 870
Cdd:PRK10636 474 IDFEGAL-----VVVSHDRHLLRSTtdDLYLV-----------------HDGKVEPF------DGDLEDYQQWLSDVQKQ 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 871 vllledtlSTHTDLTDNEPAIY--EVRKQFMREmsslssEGEVQNRTMP-KKHTNSLEKEalVTKTKETGALIKEEIAET 947
Cdd:PRK10636 526 --------ENQTDEAPKENNANsaQARKDQKRR------EAELRTQTQPlRKEIARLEKE--MEKLNAQLAQAEEKLGDS 589
|
.
gi 1388591336 948 G 948
Cdd:PRK10636 590 E 590
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1273-1450 |
6.00e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 57.29 E-value: 6.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1273 NRAPEGWPTrgmVEFRNYSVRYR-PGLELVLKNVTVHvqGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVA 1351
Cdd:PRK10522 314 PQAFPDWQT---LELRNVTFAYQdNGFSVGPINLTIK--RGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1352 HIGLHDLRSQLTIIPQDPILFSGTlrmnLDPFGRYSEE---DIWRA-LELSHLNTFVSSQPAGLdfqcaeggdNLSVGQR 1427
Cdd:PRK10522 389 AEQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPalvEKWLErLKMAHKLELEDGRISNL---------KLSKGQK 455
|
170 180
....*....|....*....|...
gi 1388591336 1428 QLVCLARALLRKSRVLVLDEATA 1450
Cdd:PRK10522 456 KRLALLLALAEERDILLLDEWAA 478
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1284-1499 |
6.02e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 55.96 E-value: 6.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYRPGLElVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLT 1363
Cdd:PRK13652 3 LIETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1364 IIPQDP--ILFSGTLRMNLdPFG-----------RYSEEDIWRALELSHLNTFVSSqpagldfqcaeggdNLSVGQRQLV 1430
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDI-AFGpinlgldeetvAHRVSSALHMLGLEELRDRVPH--------------HLSGGEKKRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388591336 1431 CLARALLRKSRVLVLDEATAAIDLE-TDDLIQGTIRTQFE-DCTVLTIAHRLNTI---MDYnrVLVLDKG-VVAE 1499
Cdd:PRK13652 147 AIAGVIAMEPQVLVLDEPTAGLDPQgVKELIDFLNDLPETyGMTVIFSTHQLDLVpemADY--IYVMDKGrIVAY 219
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
643-825 |
6.12e-08 |
|
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: 53.70 E-value: 6.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSAL-------LGEMEKLEGvvsvkGSVAYVPQQAWIQNCTLQENVLFgqpmn 715
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALaglwpwgSGRIGMPEG-----EDLLFLPQRPYLPLGTLREQLIY----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 716 pkryqqaletcalladldvlPGGDqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVigp 795
Cdd:cd03223 87 --------------------PWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL--- 134
|
170 180 190
....*....|....*....|....*....|
gi 1388591336 796 egVLAGKTRVLVTHGISFLPQTDFIIVLAG 825
Cdd:cd03223 135 --KELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1285-1453 |
6.38e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 56.49 E-value: 6.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAEGEIVIDGLNVAHIGLHD--- 1357
Cdd:PRK09452 15 VELRGISKSF--DGKEVISNLDLTINNGEFLTLLGPSGCGKTT----VLRLIagfeTPDSGRIMLDGQDITHVPAENrhv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1358 --------LRSQLTIIpqDPILFSgtLRMNLDPfgrysEEDIWR----ALELSHLNTFVSSQPAgldfqcaeggdNLSVG 1425
Cdd:PRK09452 89 ntvfqsyaLFPHMTVF--ENVAFG--LRMQKTP-----AAEITPrvmeALRMVQLEEFAQRKPH-----------QLSGG 148
|
170 180
....*....|....*....|....*...
gi 1388591336 1426 QRQLVCLARALLRKSRVLVLDEATAAID 1453
Cdd:PRK09452 149 QQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
643-832 |
6.71e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 55.58 E-value: 6.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGS-------------VAYVPQQA--WIQNCTLQEN 707
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfVGLVFQNPddQIFSPTVEQD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 708 VLFGqPMN--------PKRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSA 779
Cdd:PRK13652 100 IAFG-PINlgldeetvAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1388591336 780 VDSHVAKHIFDqVIGPEGVLAGKTRVLVTHGISFLPQ-TDFIIVLAGGQVSEMG 832
Cdd:PRK13652 168 LDPQGVKELID-FLNDLPETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYG 220
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1284-1453 |
6.80e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 57.43 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYRPGLEL--VLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDL--- 1358
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1359 -RSQLTIIPQDPILFSG-TLRMNLDPFGRYS----EEDIWRALELSH---LNTFVSSQPAgldfqcaeggdNLSVGQRQL 1429
Cdd:PRK10535 84 rREHFGFIFQRYHLLSHlTAAQNVEVPAVYAglerKQRLLRAQELLQrlgLEDRVEYQPS-----------QLSGGQQQR 152
|
170 180
....*....|....*....|....
gi 1388591336 1430 VCLARALLRKSRVLVLDEATAAID 1453
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALD 176
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1296-1483 |
7.52e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.66 E-value: 7.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1296 PGLElVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVA-HIGLHDLRSQLTIIPQDPILFSG 1374
Cdd:PRK10982 9 PGVK-ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1375 TLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAI-D 1453
Cdd:PRK10982 88 RSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtE 167
|
170 180 190
....*....|....*....|....*....|
gi 1388591336 1454 LETDDLIQGTIRTQFEDCTVLTIAHRLNTI 1483
Cdd:PRK10982 168 KEVNHLFTIIRKLKERGCGIVYISHKMEEI 197
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1280-1456 |
7.63e-08 |
|
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: 54.75 E-value: 7.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1280 PTRGMVEFRNYSVRY-RPGLEL-VLKNVTVHVQGGEKVGIVGRTGAGKSSmtlcLFRI---LEAA-EGEIVIDGLNVAHI 1353
Cdd:COG4181 4 SSAPIIELRGLTKTVgTGAGELtILKGISLEVEAGESVAIVGASGSGKST----LLGLlagLDRPtSGTVRLAGQDLFAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1354 ---GLHDLRSQLT-IIPQD-PILFSGT----------LRMNLDPFGRYSEEdiwraLE---LSHLNTFVSSQpagldfqc 1415
Cdd:COG4181 80 dedARARLRARHVgFVFQSfQLLPTLTalenvmlpleLAGRRDARARARAL-----LErvgLGHRLDHYPAQ-------- 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1388591336 1416 aeggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLET 1456
Cdd:COG4181 147 ------LSGGEQQRVALARAFATEPAILFADEPTGNLDAAT 181
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
639-828 |
7.84e-08 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 53.98 E-value: 7.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 639 LPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGS--------------VAYVP----QQAWIQ 700
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdairagIAYVPedrkREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 701 NCTLQENVLFGQPmnpkryqqaletcalladldvlpggdqteigekginLSGGQRQRVSLARAVYSDANIFLLDDPLSAV 780
Cdd:cd03215 92 DLSVAENIALSSL------------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1388591336 781 DSHVAKHIFDQVIgpEGVLAGKTRVLVThgiSFLPQ----TDFIIVLAGGQV 828
Cdd:cd03215 136 DVGAKAEIYRLIR--ELADAGKAVLLIS---SELDEllglCDRILVMYEGRI 182
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
643-832 |
7.85e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.44 E-value: 7.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSVAYVPQQAW-IQNCTLQENV--LFGQPmNPKRY 719
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFqIDAIKLRKEVgmVFQQP-NPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 720 QQALETCAL-LADLDVLPGGDQTEIGEKGI------------------NLSGGQRQRVSLARAVYSDANIFLLDDPLSAV 780
Cdd:PRK14246 105 LSIYDNIAYpLKSHGIKEKREIKKIVEECLrkvglwkevydrlnspasQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1388591336 781 DShVAKHIFDQVIGPegVLAGKTRVLVTHGisflPQ-----TDFIIVLAGGQVSEMG 832
Cdd:PRK14246 185 DI-VNSQAIEKLITE--LKNEIAIVIVSHN----PQqvarvADYVAFLYNGELVEWG 234
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
643-781 |
8.37e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 55.12 E-value: 8.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVV--SVKGSVAYVPQQAWIqNCTLqenvlfgqPMNPKRYQ 720
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIkrNGKLRIGYVPQKLYL-DTTL--------PLTVNRFL 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591336 721 QALETcalLADLDVLPGGDQTEIG-------EKginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD 781
Cdd:PRK09544 91 RLRPG---TKKEDILPALKRVQAGhlidapmQK---LSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
646-809 |
8.53e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 55.58 E-value: 8.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 646 LNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGS------------VAYVPQQAWIQ-NCTLQENVL-FG 711
Cdd:PRK13537 26 LSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarharqrVGVVPQFDNLDpDFTVRENLLvFG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 712 qpmnpkRY-----QQALETCALLADLDVLPGGDQTEIGEkginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHvAK 786
Cdd:PRK13537 106 ------RYfglsaAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ-AR 174
|
170 180
....*....|....*....|....
gi 1388591336 787 HIFDQVIgpEGVLA-GKTRVLVTH 809
Cdd:PRK13537 175 HLMWERL--RSLLArGKTILLTTH 196
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1285-1503 |
8.74e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 55.41 E-value: 8.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYRPGL---ELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIdGLNVAHIG-----LH 1356
Cdd:PRK13634 3 ITFQKVEHRYQYKTpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGkknkkLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1357 DLRSQLTIIPQDP--ILFSGTLR-------MNldpFGRYSEEDIWRALELSHLntfVSSQPAGLDFQCAEggdnLSVGQR 1427
Cdd:PRK13634 82 PLRKKVGIVFQFPehQLFEETVEkdicfgpMN---FGVSEEDAKQKAREMIEL---VGLPEELLARSPFE----LSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1428 QLVCLARALLRKSRVLVLDEATAAID----LETDDLIQGTIRTQfeDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDS 1502
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLDpkgrKEMMEMFYKLHKEK--GLTTVLVTHSMEDAARYaDQIVVMHKGTVFLQGT 229
|
.
gi 1388591336 1503 P 1503
Cdd:PRK13634 230 P 230
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
643-841 |
9.69e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.22 E-value: 9.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-----------------SVAYV---PQQAWIQNc 702
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkKVSLVfqfPEAQLFEN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 703 TLQENVLFGqPMNPKRYQQALETCALLADLDVlpgGDQTEIGEKG-INLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD 781
Cdd:PRK13641 102 TVLKDVEFG-PKNFGFSEDEAKEKALKWLKKV---GLSEDLISKSpFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 782 SHVAKHIFDqvIGPEGVLAGKTRVLVTHGISFLPQ-TDFIIVLaggqvsEMGHysaLLQHD 841
Cdd:PRK13641 178 PEGRKEMMQ--LFKDYQKAGHTVILVTHNMDDVAEyADDVLVL------EHGK---LIKHA 227
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1009-1256 |
1.09e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 55.18 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1009 GVYAALGILQGLLVMLsaFTMVVGAIQA--ARLLHEALLHNKIRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILML 1086
Cdd:cd18540 46 LLYLGLILIQALSVFL--FIRLAGKIEMgvSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1087 LNSFF--TSISTIMVIV-ASTPLFMVVVLP-LAVLYGFVQRFYVATSRQLKRLESIsrspIFSHFSETVTGTSVIRAYGR 1162
Cdd:cd18540 124 VWGITymIGILIVMLILnWKLALIVLAVVPvLAVVSIYFQKKILKAYRKVRKINSR----ITGAFNEGITGAKTTKTLVR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1163 ----IQDFKVLSdtkvDNNQKSSypyIASNRWLGVHVEFVGNCVVLFAALFAVIGRNSLNPGLV---GLSV--SYALQVT 1233
Cdd:cd18540 200 eeknLREFKELT----EEMRRAS---VRAARLSALFLPIVLFLGSIATALVLWYGGILVLAGAItigTLVAfiSYATQFF 272
|
250 260
....*....|....*....|...
gi 1388591336 1234 MALNWMIRMISDLESNIIAVERV 1256
Cdd:cd18540 273 EPIQQLARVLAELQSAQASAERV 295
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
643-809 |
1.09e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 54.71 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-SVAYVPQQ---AWI----QN-----C---TLQE 706
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkDVTKLPEYkraKYIgrvfQDpmmgtApsmTIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 707 NVL----------FGQPMNPKRYQQALEtcaLLADLDV-LPGGDQTEIGekgiNLSGGQRQRVSLARAVYSDANIFLLDD 775
Cdd:COG1101 102 NLAlayrrgkrrgLRRGLTKKRRELFRE---LLATLGLgLENRLDTKVG----LLSGGQRQALSLLMATLTKPKLLLLDE 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1388591336 776 PLSAVDSHVAKHIF---DQVIGPEGVlagkTRVLVTH 809
Cdd:COG1101 175 HTAALDPKTAALVLeltEKIVEENNL----TTLMVTH 207
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
639-776 |
1.12e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.18 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 639 LPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGS--------------VAYVP----QQAWIQ 700
Cdd:COG1129 264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAYVPedrkGEGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 701 NCTLQENVLF--------GQPMNPKRYQQALEtcALLADLDVLPGGDQTEIGekgiNLSGGQRQRVSLARAVYSDANIFL 772
Cdd:COG1129 344 DLSIRENITLasldrlsrGGLLDRRRERALAE--EYIKRLRIKTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLI 417
|
....
gi 1388591336 773 LDDP 776
Cdd:COG1129 418 LDEP 421
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
643-814 |
1.15e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.18 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGS--------------VAYVPQQ-AWIQNCTLQEN 707
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvrfrsprdaqaagIAIIHQElNLVPNLSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 708 VLFGQP------MNPKR-YQQALETCALL-ADLDVlpggdQTEIGEkginLSGGQRQRVSLARAVYSDANIFLLDDPLSA 779
Cdd:COG1129 100 IFLGREprrgglIDWRAmRRRARELLARLgLDIDP-----DTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190
....*....|....*....|....*....|....*
gi 1388591336 780 VDSHVAKHIFDQVigpegvlagktRVLVTHGISFL 814
Cdd:COG1129 171 LTEREVERLFRII-----------RRLKAQGVAII 194
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1305-1492 |
1.16e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 55.48 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1305 VTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDG---LNVAHIGLHDLRSQLTIIPQDPiLFSGTLRMNL- 1380
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkdlLGMKDDEWRAVRSDIQMIFQDP-LASLNPRMTIg 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1381 ----DPFGRYSEE-------DIWRA--LELSHLNTFVSSQPagldfqcaeggDNLSVGQRQLVCLARALLRKSRVLVLDE 1447
Cdd:PRK15079 119 eiiaEPLRTYHPKlsrqevkDRVKAmmLKVGLLPNLINRYP-----------HEFSGGQCQRIGIARALILEPKLIICDE 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1388591336 1448 ATAAIDLEtddlIQGTI-----RTQFE-DCTVLTIAHRLNT---IMDynRVLVL 1492
Cdd:PRK15079 188 PVSALDVS----IQAQVvnllqQLQREmGLSLIFIAHDLAVvkhISD--RVLVM 235
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1285-1480 |
1.41e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 54.79 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILE-----AAEGEIVIDGLNV--AHIGLHD 1357
Cdd:PRK14243 11 LRTENLNVYY--GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1358 LRSQLTIIPQDPILFSGTLRMNLDPFGRYS------EEDIWRALELSHLNTFVSSQpagldfqCAEGGDNLSVGQRQLVC 1431
Cdd:PRK14243 89 VRRRIGMVFQKPNPFPKSIYDNIAYGARINgykgdmDELVERSLRQAALWDEVKDK-------LKQSGLSLSGGQQQRLC 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1388591336 1432 LARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRL 1480
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1302-1454 |
1.80e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.02 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1302 LKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIG---LHDLRSQLTIIPQDPIlfsgtlrM 1378
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPY-------A 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1379 NLDPFGR--YSEEDIWRALELSHLNTFVSS-----QPAGLDFQCA-EGGDNLSVGQRQLVCLARALLRKSRVLVLDEATA 1450
Cdd:PRK10261 413 SLDPRQTvgDSIMEPLRVHGLLPGKAAAARvawllERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVS 492
|
....
gi 1388591336 1451 AIDL 1454
Cdd:PRK10261 493 ALDV 496
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1301-1507 |
1.86e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.45 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1301 VLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAA--------EGEIVIDGLNVAHIG---LHDLRSQLTIIPQDP 1369
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDaprLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1370 ILFSGTLRMNLdpfGRYSEEDiwRALELSHLNTFVSSQP---AGLDFQCAEGGDNLSVGQRQLVCLARAL---------L 1437
Cdd:PRK13547 96 FAFSAREIVLL---GRYPHAR--RAGALTHRDGEIAWQAlalAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388591336 1438 RKSRVLVLDEATAAIDLETDDLIQGTIRTQFED--CTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSPVNLI 1507
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwnLGVLAIVHDPNLAARHaDRIAMLADGAIVAHGAPADVL 243
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1284-1506 |
1.92e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 54.35 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYRPGLELV---LKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIG----LH 1356
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFAsraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1357 DLRSQLTIIPQDP--ILFSGTLRMNL----DPFGRYSEEDIWRALELSHLntfvssqpAGLDFQCAEGGD-NLSVGQRQL 1429
Cdd:PRK13643 81 PVRKKVGVVFQFPesQLFEETVLKDVafgpQNFGIPKEKAEKIAAEKLEM--------VGLADEFWEKSPfELSGGQMRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1430 VCLARALLRKSRVLVLDEATAAID----LETDDLIQGTIRTqfeDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSPV 1504
Cdd:PRK13643 153 VAIAGILAMEPEVLVLDEPTAGLDpkarIEMMQLFESIHQS---GQTVVLVTHLMDDVADYaDYVYLLEKGHIISCGTPS 229
|
..
gi 1388591336 1505 NL 1506
Cdd:PRK13643 230 DV 231
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
646-776 |
2.02e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.51 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 646 LNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSV--AYVPQQ--AWIQNCTLQENVLFGQ--------P 713
Cdd:PRK11819 343 LSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVklAYVDQSrdALDPNKTVWEEISGGLdiikvgnrE 422
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388591336 714 MNPKRYqqaletCALLAdldvLPGGDQteigEKGI-NLSGGQRQRVSLARAVYSDANIFLLDDP 776
Cdd:PRK11819 423 IPSRAY------VGRFN----FKGGDQ----QKKVgVLSGGERNRLHLAKTLKQGGNVLLLDEP 472
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1301-1503 |
2.19e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 54.70 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1301 VLKNVTVHVQGGEKVGIVGRTGAGKSSmtlcLFRILEAAE----GEIVIDGLNVAHigLHDLRSQLTIIPQDPILFSGTL 1376
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTT----LLRIIAGLEhqtsGHIRFHGTDVSR--LHARDRKVGFVFQHYALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1377 RMNLDPFG--------RYSEEDIWRA-------LELSHLNTFVSSQpagldfqcaeggdnLSVGQRQLVCLARALLRKSR 1441
Cdd:PRK10851 91 VFDNIAFGltvlprreRPNAAAIKAKvtqllemVQLAHLADRYPAQ--------------LSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388591336 1442 VLVLDEATAAIDLETDDLIQGTIRTQFEDC--TVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSP 1503
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEAMEVaDRVVVMSQGNIEQAGTP 221
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
978-1447 |
2.25e-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: 55.57 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 978 SAAAIGANVWLSAWSNDAEEHGQQNKTSVrLGVYAALGilqgLLVMLSAFTMVVGAiqaARLLHEALLH------NKIR- 1050
Cdd:COG4615 22 GLLSGLANAGLIALINQALNATGAALARL-LLLFAGLL----VLLLLSRLASQLLL---TRLGQHAVARlrlrlsRRILa 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1051 SPQSFFDTTPSGRILNRFSKDIYVIDEVlAPTILMLLnsfftsISTIMVIVA-------STPLFMVVVLPLAVLyGFVQR 1123
Cdd:COG4615 94 APLERLERIGAARLLAALTEDVRTISQA-FVRLPELL------QSVALVLGClaylawlSPPLFLLTLVLLGLG-VAGYR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1124 FYVATSRQLKRLESISRSPIFSHFSETVTGTSVI------RAYGRIQDFKVLSDTKVDNNQKSSYPYIASNRWlgvhvef 1197
Cdd:COG4615 166 LLVRRARRHLRRAREAEDRLFKHFRALLEGFKELklnrrrRRAFFDEDLQPTAERYRDLRIRADTIFALANNW------- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1198 vGNCVVLFA---ALFAVIGRNSLNPGLVGLSVSYALQVTMALNWMIRMISDLESNIIAVERVKEYSKTKTEAPWVVESNR 1274
Cdd:COG4615 239 -GNLLFFALiglILFLLPALGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKIEELELALAAAEPAAADAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1275 APEGWPTRGMVEFRNYSVRYRPGLE---LVLKNVTVHVQGGEKVGIVGRTGAGKS--SMTLC-LFRileAAEGEIVIDGL 1348
Cdd:COG4615 318 APPAPADFQTLELRGVTYRYPGEDGdegFTLGPIDLTIRRGELVFIVGGNGSGKStlAKLLTgLYR---PESGEILLDGQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1349 NVAHIGLHDLRSQLTIIPQDPILFSGtlrmNLDPFGRYSEEDI--W-RALELSHLNTFvssqpagldfqcaEGGD----N 1421
Cdd:COG4615 395 PVTADNREAYRQLFSAVFSDFHLFDR----LLGLDGEADPARAreLlERLELDHKVSV-------------EDGRfsttD 457
|
490 500
....*....|....*....|....*.
gi 1388591336 1422 LSVGQRQLVCLARALLRKSRVLVLDE 1447
Cdd:COG4615 458 LSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1302-1484 |
2.36e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.18 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1302 LKNVTVHVQGGEKVGIVGRTGAGKSSmtlcLFRILEAA------EGEIVIDGlNVAHigLHDLRS-----------QLTI 1364
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKST----LMKVLSGVyphgsyEGEILFDG-EVCR--FKDIRDsealgiviihqELAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1365 IPQDPI---LFSGTLRmnldpfGRYS----EEDIWRALELshLNTfvssqpAGLDFQCAEGGDNLSVGQRQLVCLARALL 1437
Cdd:NF040905 90 IPYLSIaenIFLGNER------AKRGvidwNETNRRAREL--LAK------VGLDESPDTLVTDIGVGKQQLVEIAKALS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1388591336 1438 RKSRVLVLDEATAAIDlETD-----DLIQGtIRTQfeDCTVLTIAHRLNTIM 1484
Cdd:NF040905 156 KDVKLLILDEPTAALN-EEDsaallDLLLE-LKAQ--GITSIIISHKLNEIR 203
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
1008-1256 |
2.43e-07 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 53.97 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1008 LGVYAALGILQGLLVMLSAFTMVVGAIQAARLLHEALlHNKI-RSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILML 1086
Cdd:cd18542 42 ALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDL-YDHLqRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1087 LNSFFT-SISTIMVIVASTPL--FMVVVLPLAVLYGF-----VQRFYVATSRQLKRLESIsrspifshFSETVTGTSVIR 1158
Cdd:cd18542 121 VRAVLLfIGALIIMFSINWKLtlISLAIIPFIALFSYvffkkVRPAFEEIREQEGELNTV--------LQENLTGVRVVK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1159 AYGR----IQDFKVLSDTKVDNNQKSS------YPYIasnrwlgvhvEFVGNC----VVLFAALFAVigRNSLNPG-LVG 1223
Cdd:cd18542 193 AFARedyeIEKFDKENEEYRDLNIKLAkllakyWPLM----------DFLSGLqivlVLWVGGYLVI--NGEITLGeLVA 260
|
250 260 270
....*....|....*....|....*....|....*..
gi 1388591336 1224 LSvSYalqvTMALNWMIRM----ISDLESNIIAVERV 1256
Cdd:cd18542 261 FI-SY----LWMLIWPVRQlgrlINDMSRASASAERI 292
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1285-1478 |
2.63e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 53.69 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILE-----AAEGEIVIDGLNVAHIGLH--D 1357
Cdd:PRK14267 5 IETVNLRVYY--GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDpiE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1358 LRSQLTIIPQDPILFSGT---------LRMN--LDPFGRYSEEDIWrALELSHLNTFVSSQpagldfqCAEGGDNLSVGQ 1426
Cdd:PRK14267 83 VRREVGMVFQYPNPFPHLtiydnvaigVKLNglVKSKKELDERVEW-ALKKAALWDEVKDR-------LNDYPSNLSGGQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1388591336 1427 RQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAH 1478
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1281-1480 |
3.04e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 53.24 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1281 TRGMVEFRNYSVRYrpGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILE-----AAEGEIVIDGLNV--AHI 1353
Cdd:PRK14239 2 TEPILQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysPRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1354 GLHDLRSQLTIIPQDPILFSGT--------LRMNldpfGRYSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGgdnLSVG 1425
Cdd:PRK14239 80 DTVDLRKEIGMVFQQPNPFPMSiyenvvygLRLK----GIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSALG---LSGG 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1388591336 1426 QRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRL 1480
Cdd:PRK14239 153 QQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1280-1499 |
3.05e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.25 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1280 PTRGMVEFRNYSVRYRPGLELV--LKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEI-------------V 1344
Cdd:PRK10261 8 DARDVLAVENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1345 IDGLNVAHIGLHDLR-SQLTIIPQDPIL-----------FSGTLRMNLDPFGRYSEEDIWRALELSHL---NTFVSSQPa 1409
Cdd:PRK10261 88 IELSEQSAAQMRHVRgADMAMIFQEPMTslnpvftvgeqIAESIRLHQGASREEAMVEAKRMLDQVRIpeaQTILSRYP- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1410 gldfqcaeggDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCT--VLTIAHRLNTIMDY- 1486
Cdd:PRK10261 167 ----------HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIa 236
|
250
....*....|...
gi 1388591336 1487 NRVLVLDKGVVAE 1499
Cdd:PRK10261 237 DRVLVMYQGEAVE 249
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
643-832 |
3.46e-07 |
|
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: 52.92 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSVAYVPQ-QAWIQ-NCTLQENVLF-----GqpMN 715
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGlGGGFNpELTGRENIYLngrllG--LS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 716 PKRYQQALETCAlladldvlpggDQTEIGE------KgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSH----VA 785
Cdd:cd03220 116 RKEIDEKIDEII-----------EFSELGDfidlpvK--TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfqekCQ 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1388591336 786 KHIFDQVIGpegvlaGKTRVLVTHGISFLPQT-DFIIVLAGGQVSEMG 832
Cdd:cd03220 183 RRLRELLKQ------GKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
625-781 |
3.48e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 54.08 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 625 AITIHNGTFTWAQDLPpTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSV-----------AYV 693
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQ-VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVvnelepadrdiAMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 694 pqqawIQN------CTLQENVLFG---QPMnPK--RYQQALETCALLadldvlpggdqtEIGE----KGINLSGGQRQRV 758
Cdd:PRK11650 82 -----FQNyalyphMSVRENMAYGlkiRGM-PKaeIEERVAEAARIL------------ELEPlldrKPRELSGGQRQRV 143
|
170 180
....*....|....*....|...
gi 1388591336 759 SLARAVYSDANIFLLDDPLSAVD 781
Cdd:PRK11650 144 AMGRAIVREPAVFLFDEPLSNLD 166
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1302-1495 |
3.67e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.79 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1302 LKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGlHDLRSQL--TIIPQD-PILFSGTLRM 1378
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQLgiGIIYQElSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1379 NLdPFGRYSEEDIW------------RALELS-------HLNTFVSsqpagldfqcaeggdNLSVGQRQLVCLARALLRK 1439
Cdd:PRK09700 100 NL-YIGRHLTKKVCgvniidwremrvRAAMMLlrvglkvDLDEKVA---------------NLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591336 1440 SRVLVLDEATAAI-DLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDY-NRVLVLDKG 1495
Cdd:PRK09700 164 AKVIIMDEPTSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRIcDRYTVMKDG 221
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1049-1256 |
3.82e-07 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 53.64 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1049 IRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLLNSFFTSISTIMVIVASTP---LFMVVVLPL----AVLYG-F 1120
Cdd:cd18576 80 QRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWkltLLMLATVPVvvlvAVLFGrR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1121 VQRFyvatSRQlkRLESISRSpiFSHFSETVTGTSVIRAYGR----IQDFKVLSDTKVDNNQKSSypyiasnRWLGVHVE 1196
Cdd:cd18576 160 IRKL----SKK--VQDELAEA--NTIVEETLQGIRVVKAFTRedyeIERYRKALERVVKLALKRA-------RIRALFSS 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591336 1197 FVGncVVLFAALFAVI---GR----NSLNPG-LVGLsVSYALQVTMALNWMIRMISDLESNIIAVERV 1256
Cdd:cd18576 225 FII--FLLFGAIVAVLwygGRlvlaGELTAGdLVAF-LLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1295-1509 |
4.14e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 53.25 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1295 RPGLELVLKNVTVHVQG-------------GEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQ 1361
Cdd:PRK10575 7 HSDTTFALRNVSFRVPGrtllhplsltfpaGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1362 LTIIPQD-PILFSGTLR----MNLDPF----GRYSEED---IWRALELSHLNTFVSSQPagldfqcaeggDNLSVGQRQL 1429
Cdd:PRK10575 87 VAYLPQQlPAAEGMTVRelvaIGRYPWhgalGRFGAADrekVEEAISLVGLKPLAHRLV-----------DSLSGGERQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1430 VCLARALLRKSRVLVLDEATAAIDL----ETDDLIQGTirTQFEDCTVLTIAHRLNTIMDYNRVLVLDKG--VVAEfDSP 1503
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDIahqvDVLALVHRL--SQERGLTVIAVLHDINMAARYCDYLVALRGgeMIAQ-GTP 232
|
....*.
gi 1388591336 1504 VNLIAA 1509
Cdd:PRK10575 233 AELMRG 238
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
625-840 |
4.76e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 53.21 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 625 AITIHNGTFTWAQDLP---PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVV----------------- 684
Cdd:PRK13649 2 GINLQNVSYTYQAGTPfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVrvddtlitstsknkdik 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 685 SVKGSVAYVPQQAWIQ--NCTLQENVLFGqPMNPKRYQQALETCAL--LAdldvLPGGDQTEIGEKGINLSGGQRQRVSL 760
Cdd:PRK13649 82 QIRKKVGLVFQFPESQlfEETVLKDVAFG-PQNFGVSQEEAEALARekLA----LVGISESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 761 ARAVYSDANIFLLDDPLSAVDSHVAKHIFDqvIGPEGVLAGKTRVLVTHGISFLPQ-TDFIIVLAGGQVSEMGHYSALLQ 839
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMT--LFKKLHQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDIFQ 234
|
.
gi 1388591336 840 H 840
Cdd:PRK13649 235 D 235
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1312-1493 |
4.88e-07 |
|
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: 52.80 E-value: 4.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1312 GEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHiglhdlRSQlTIIPQDP-----ILFSGTLRMNLDPfgrY 1386
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY------KPQ-YIKADYEgtvrdLLSSITKDFYTHP---Y 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1387 SEEDIWRALELSHLntfvssqpagLDFQCAEggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT 1466
Cdd:cd03237 95 FKTEIAKPLQIEQI----------LDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170 180 190
....*....|....*....|....*....|..
gi 1388591336 1467 QFE--DCTVLTIAHrlNTIM-DY--NRVLVLD 1493
Cdd:cd03237 161 FAEnnEKTAFVVEH--DIIMiDYlaDRLIVFE 190
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
646-781 |
5.15e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 53.72 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 646 LNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSV-----------------AYVPQQAWI-QNCTLQEN 707
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgiclppekrriGYVFQDARLfPHYKVRGN 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388591336 708 VLFGqpMNPKRYQQALETCALLAD---LDVLPggdqteigekgINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD 781
Cdd:PRK11144 97 LRYG--MAKSMVAQFDKIVALLGIeplLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
650-855 |
5.53e-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: 51.42 E-value: 5.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 650 IPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-SVAYVPQQawiqnctlqenvlfgqpmnpkryqqaletcal 728
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQY-------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 729 ladldvlpggdqteigekgINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDS----HVAKhifdqVIGPEGVLAGKTR 804
Cdd:cd03222 70 -------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrlNAAR-----AIRRLSEEGKKTA 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1388591336 805 VLVTHGISFLPQ-TDFIIVLAGgqvsEMGHYSALLQHDGS---FANFLRNYAPDE 855
Cdd:cd03222 126 LVVEHDLAVLDYlSDRIHVFEG----EPGVYGIASQPKGTregINRFLRGYLITF 176
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1301-1455 |
5.64e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 52.32 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1301 VLKNVTVHVQGGEKVGIVGRTGAGKSSmtlcLFRILEAAE----GEIVIDGLNV---AHIG---LHDLRSQLTIIPQD-- 1368
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSS----LLRVLNLLEmprsGTLNIAGNHFdfsKTPSdkaIRELRRNVGMVFQQyn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1369 --PILfsgTLRMNL--DP---FGRYSEEDIWRALELS---HLNTFVSSQPAgldfqcaeggdNLSVGQRQLVCLARALLR 1438
Cdd:PRK11124 93 lwPHL---TVQQNLieAPcrvLGLSKDQALARAEKLLerlRLKPYADRFPL-----------HLSGGQQQRVAIARALMM 158
|
170
....*....|....*..
gi 1388591336 1439 KSRVLVLDEATAAIDLE 1455
Cdd:PRK11124 159 EPQVLLFDEPTAALDPE 175
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
1052-1182 |
5.99e-07 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 52.83 E-value: 5.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1052 PQSFFDTTPSGRILNRFSkDIYVIDEVLAPTIL-MLLNSFFTSISTIMVIVASTPLFMVVVLPLaVLYGFVQRFYVATSR 1130
Cdd:cd18570 89 PLSFFETRKTGEIISRFN-DANKIREAISSTTIsLFLDLLMVIISGIILFFYNWKLFLITLLII-PLYILIILLFNKPFK 166
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1388591336 1131 QLKRLESISRSPIFSHFSETVTGTSVIRAYGRIQDFKVLSDTKVDNNQKSSY 1182
Cdd:cd18570 167 KKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSF 218
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1288-1485 |
9.11e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 52.66 E-value: 9.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1288 RNYSVR----YRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVA---HIGLHDLRS 1360
Cdd:PRK11308 13 KHYPVKrglfKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1361 QLTIIPQDPIlfsgtlrMNLDPfgRYSEEDIwraLELSHL-NTFVSSQP-----------AGLDfqcAEGGDN----LSV 1424
Cdd:PRK11308 93 KIQIVFQNPY-------GSLNP--RKKVGQI---LEEPLLiNTSLSAAErrekalammakVGLR---PEHYDRyphmFSG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388591336 1425 GQRQLVCLARALLRKSRVLVLDEATAAIDLetddliqgTIRTQFedctvltiahrLNTIMD 1485
Cdd:PRK11308 158 GQRQRIAIARALMLDPDVVVADEPVSALDV--------SVQAQV-----------LNLMMD 199
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
646-809 |
1.04e-06 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 51.22 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 646 LNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEG--------VVS----VKGSVAYVPQQAWIQN-CTLQENV---- 708
Cdd:cd03265 19 VSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGratvaghdVVRepreVRRRIGIVFQDLSVDDeLTGWENLyiha 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 709 -LFGQPmNPKRYQQALEtcaLLADLDVLPGGDqteigEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKH 787
Cdd:cd03265 99 rLYGVP-GAERRERIDE---LLDFVGLLEAAD-----RLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAH 169
|
170 180
....*....|....*....|....
gi 1388591336 788 IFDQVigpEGVLA--GKTRVLVTH 809
Cdd:cd03265 170 VWEYI---EKLKEefGMTILLTTH 190
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
630-946 |
1.08e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 53.36 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 630 NGTFTWAqdlpptLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSVAYVPQQAWIQN-CTLQENV 708
Cdd:PRK13545 33 DGEYHYA------LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGqLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 709 -LFGQPMNPKRyQQALETCALLADLdvlpggdqTEIGeKGIN-----LSGGQRQRVSLARAVYSDANIFLLDDPLSAVDS 782
Cdd:PRK13545 107 eLKGLMMGLTK-EKIKEIIPEIIEF--------ADIG-KFIYqpvktYSSGMKSRLGFAISVHINPDILVIDEALSVGDQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 783 HVAKHIFDQVigPEGVLAGKTRVLVTHGI----SFLPQTdfiIVLAGGQVSEMGHYSALLQHdgsFANFLRNY--APDED 856
Cdd:PRK13545 177 TFTKKCLDKM--NEFKEQGKTIFFISHSLsqvkSFCTKA---LWLHYGQVKEYGDIKEVVDH---YDEFLKKYnqMSVEE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 857 QEDHEAALQNANEEVLLLEDT--LSTHTDLTDNEPAIYEVRKQFMRE-----MSSLSSEGEVQNRTMPKKHTNSLEKEAL 929
Cdd:PRK13545 249 RKDFREEQISQFQHGLLQEDQtgRERKRKKGKKTSRKFKKKRVLITGvcialLTGIISTGYYYKNLLPFNSENKYAEKVA 328
|
330
....*....|....*...
gi 1388591336 930 VTK-TKETGALIKEEIAE 946
Cdd:PRK13545 329 SKEnVTESKQMVKKEKGA 346
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
643-828 |
1.11e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 52.02 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSvAYVPQQAW---------IQN-------CTLQE 706
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-LLTAENVWnlrrkigmvFQNpdnqfvgATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 707 NVLFGQ-----PMNP--KRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSA 779
Cdd:PRK13642 102 DVAFGMenqgiPREEmiKRVDEALLAVNMLDFKTREPA-----------RLSGGQKQRVAVAGIIALRPEIIILDESTSM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1388591336 780 VDSHVAKHIFdQVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLAGGQV 828
Cdd:PRK13642 171 LDPTGRQEIM-RVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
647-851 |
1.23e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 52.73 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 647 NIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-----------------SVAYVPQQ-AWIQNCTLQENV 708
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrkKIAMVFQSfALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 709 LFGQPMN----PKRYQQALETCALLAdLDVLPGGDQTEigekginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHV 784
Cdd:PRK10070 128 AFGMELAginaEERREKALDALRQVG-LENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591336 785 AKHIFDQVIGPEGVlAGKTRVLVTHGI-SFLPQTDFIIVLAGGQVSEMGHYSALLQHDGSfaNFLRNY 851
Cdd:PRK10070 200 RTEMQDELVKLQAK-HQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAN--DYVRTF 264
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1422-1480 |
1.35e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 51.64 E-value: 1.35e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1388591336 1422 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRL 1480
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNL 222
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
643-828 |
1.49e-06 |
|
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: 51.19 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-SVAYVPQQAwI---------QN------CTLQE 706
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGrDITGLPPHR-IarlgiartfQNprlfpeLTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 707 NVLFGQPMNPKRY----------------------QQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAV 764
Cdd:COG0411 99 NVLVAAHARLGRGllaallrlprarreereareraEELLERVGLADRADEPAG-----------NLSYGQQRRLEIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388591336 765 YSDANIFLLDDP---LSAVDSHVAKHIFDQVIGPEGVlagkTRVLVTH------GISflpqtDFIIVLAGGQV 828
Cdd:COG0411 168 ATEPKLLLLDEPaagLNPEETEELAELIRRLRDERGI----TILLIEHdmdlvmGLA-----DRIVVLDFGRV 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
641-776 |
1.59e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 52.72 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGS--------------VAYVPQ----QAWIQNC 702
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditglsprerrrlgVAYIPEdrlgRGLVPDM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 703 TLQENVLFGQPMNPK-------RYQQALETCA-LLADLDVLPGGDQTEIGekgiNLSGGQRQRVSLARAVYSDANIFLLD 774
Cdd:COG3845 352 SVAENLILGRYRRPPfsrggflDRKAIRAFAEeLIEEFDVRTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAA 427
|
..
gi 1388591336 775 DP 776
Cdd:COG3845 428 QP 429
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
625-776 |
2.07e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.20 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 625 AITIHNGTFTWaqDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVV--SVKGSVAYVPQ---QAWI 699
Cdd:PRK15064 319 ALEVENLTKGF--DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwSENANIGYYAQdhaYDFE 396
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388591336 700 QNCTLQEnvLFGQPMNPKRYQQALEtcALLADLdvLPGGDqtEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDP 776
Cdd:PRK15064 397 NDLTLFD--WMSQWRQEGDDEQAVR--GTLGRL--LFSQD--DIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1302-1500 |
2.40e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.26 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1302 LKNVTVHVQGGEKVGIVGRTGAGKSSmtlcLFRILEAA----EGEIVIDG-LNVAHI------------------GL--- 1355
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKST----LMKILNGEvlldDGRIIYEQdLIVARLqqdpprnvegtvydfvaeGIeeq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1356 -------HDLRSQLTIIPQDPILFS-GTLRMNLDPFGRYSEED-IWRALELSHLNTfvssqpaglDFQCAEggdnLSVGQ 1426
Cdd:PRK11147 95 aeylkryHDISHLVETDPSEKNLNElAKLQEQLDHHNLWQLENrINEVLAQLGLDP---------DAALSS----LSGGW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1427 RQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTqFEDCTVLtIAH------RLNTimdynRVLVLDKGVVAEF 1500
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT-FQGSIIF-ISHdrsfirNMAT-----RIVDLDRGKLVSY 234
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
626-847 |
2.81e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 50.93 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 626 ITIHNGTFTWAQDLP---PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVK--------------- 687
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDditithktkdkyirp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 688 -----GSVAYVPQQAWIQNcTLQENVLFGqpmnPKRYQQALETCA-----LLADLdvlpGGDQTEIGEKGINLSGGQRQR 757
Cdd:PRK13646 83 vrkriGMVFQFPESQLFED-TVEREIIFG----PKNFKMNLDEVKnyahrLLMDL----GFSRDVMSQSPFQMSGGQMRK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 758 VSLARAVYSDANIFLLDDPLSAVDSHvAKHIFDQVIGPEGVLAGKTRVLVTHGISFLPQ-TDFIIVLAGGQVSEMGHYSA 836
Cdd:PRK13646 154 IAIVSILAMNPDIIVLDEPTAGLDPQ-SKRQVMRLLKSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKE 232
|
250
....*....|.
gi 1388591336 837 LLQHDGSFANF 847
Cdd:PRK13646 233 LFKDKKKLADW 243
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
643-827 |
3.00e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 49.24 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEmeklegvvsvkgsvayvpqqawiQNCTLQENVLfgqPMNPKRYQQA 722
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA-----------------------SGKARLISFL---PKFSRNKLIF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 723 LETCALLAD--LDVLPggdqteIGEKGINLSGGQRQRVSLARAVYSDA--NIFLLDDPLSAVDSHVAKHIFDQV--IGPE 796
Cdd:cd03238 65 IDQLQFLIDvgLGYLT------LGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIkgLIDL 138
|
170 180 190
....*....|....*....|....*....|.
gi 1388591336 797 GVlagkTRVLVTHGISFLPQTDFIIVLAGGQ 827
Cdd:cd03238 139 GN----TVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1011-1111 |
3.17e-06 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 50.94 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1011 YAALGILQGLLVMLSAFT-MVVGAIQAARLlHEALLHNKIRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLLNS 1089
Cdd:cd18577 53 FVYLGIGSFVLSYIQTACwTITGERQARRI-RKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQS 131
|
90 100 110
....*....|....*....|....*....|...
gi 1388591336 1090 FFTSISTI-----------MVIVASTPLFMVVV 1111
Cdd:cd18577 132 LSTFIAGFiiafiyswkltLVLLATLPLIAIVG 164
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
656-830 |
3.27e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 50.16 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 656 VAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-----------------SVAYVPQQ-AWIQNCTLQENV-----LFGQ 712
Cdd:PRK10584 39 IALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhqmdeearaklrakHVGFVFQSfMLIPTLNALENVelpalLRGE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 713 PMNPKRYQQA--LETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFD 790
Cdd:PRK10584 119 SSRQSRNGAKalLEQLGLGKRLDHLPA-----------QLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIAD 187
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1388591336 791 QVIGPEGVLAgKTRVLVTHGISFLPQTDFIIVLAGGQVSE 830
Cdd:PRK10584 188 LLFSLNREHG-TTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
643-832 |
3.28e-06 |
|
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: 51.73 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLG--EMEKLEGVVSVKgsVAYVPQQAWI-------QNCTLQENVL---- 709
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYH--VALCEKCGYVerpskvgEPCPVCGGTLepee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 710 --FGQPMNPKRY----QQAL---ETCALLADLDVLPGGDQT--EIGEKGI------------------------NLSGGQ 754
Cdd:TIGR03269 94 vdFWNLSDKLRRrirkRIAImlqRTFALYGDDTVLDNVLEAleEIGYEGKeavgravdliemvqlshrithiarDLSGGE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 755 RQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIgpEGVLAGKTRVLVThgiSFLPQ-----TDFIIVLAGGQVS 829
Cdd:TIGR03269 174 KQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALE--EAVKASGISMVLT---SHWPEviedlSDKAIWLENGEIK 248
|
...
gi 1388591336 830 EMG 832
Cdd:TIGR03269 249 EEG 251
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
641-788 |
3.33e-06 |
|
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: 49.57 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSAL---LGEMEKLEGVVSVKG------------SVAYVPQQAW-IQNCTL 704
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGipykefaekypgEIIYVSEEDVhFPTLTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 705 QENVLFgqpmnpkryqqALETCalladldvlpgGDQTEIGekginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHV 784
Cdd:cd03233 101 RETLDF-----------ALRCK-----------GNEFVRG-----ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
....
gi 1388591336 785 AKHI 788
Cdd:cd03233 154 ALEI 157
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
643-789 |
4.11e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGS--------------VAYVPQQA-WIQNCTLQEN 707
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfksskealengISMVHQELnLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 708 VLFGQ-PM------NPKRYQqalETCALLADLDVlpggdQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAV 780
Cdd:PRK10982 94 MWLGRyPTkgmfvdQDKMYR---DTKAIFDELDI-----DIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
....*....
gi 1388591336 781 DSHVAKHIF 789
Cdd:PRK10982 166 TEKEVNHLF 174
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
652-814 |
4.12e-06 |
|
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: 48.14 E-value: 4.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 652 KGALVAVVGPVGCGKSSLVSALLGEMEKLE-GVVSVKGSVAYVPQQAWIQNctlqenvlfgqpmnpkryqqaletcalla 730
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGgGVIYIDGEDILEEVLDQLLL----------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 731 dldvlpggdqTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFD----QVIGPEGVLAGKTRVL 806
Cdd:smart00382 52 ----------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelRLLLLLKSEKNLTVIL 121
|
....*...
gi 1388591336 807 VTHGISFL 814
Cdd:smart00382 122 TTNDEKDL 129
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1285-1495 |
4.20e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 50.47 E-value: 4.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVRYRPGLELVLK---NVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEI------------------ 1343
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1344 VIDGLNVAHI------GLHDLRSQLTIIPQ--DPILFSGTLRMNLdPFGRYS-----EEDIWRALELSHLntfvssqpAG 1410
Cdd:PRK13651 83 VLEKLVIQKTrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDI-IFGPVSmgvskEEAKKRAAKYIEL--------VG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1411 LDFQCAEGGD-NLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLE-TDDLIQGTIRTQFEDCTVLTIAHRLNTIMDY-N 1487
Cdd:PRK13651 154 LDESYLQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEILEIFDNLNKQGKTIILVTHDLDNVLEWtK 233
|
....*...
gi 1388591336 1488 RVLVLDKG 1495
Cdd:PRK13651 234 RTIFFKDG 241
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
993-1162 |
4.34e-06 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 50.17 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 993 NDAEEHGQQNKTSVRLGVYAALGILQGLLVMLSAFTMVVGAIQAARLLHEALLHNKIRSPQSFFDTTPSGRILNRFSKDI 1072
Cdd:cd18543 27 DGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1073 YVIDEVLAPTILMLLNSFFTSISTIMVIVASTPLFMVVVLPLAVLYGFVQRFyvatsrqLKRLESISRSP------IFSH 1146
Cdd:cd18543 107 SLVQRFLAFGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRF-------RRRYFPASRRAqdqagdLATV 179
|
170
....*....|....*.
gi 1388591336 1147 FSETVTGTSVIRAYGR 1162
Cdd:cd18543 180 VEESVTGIRVVKAFGR 195
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
634-781 |
4.43e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.46 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 634 TWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGS----------VAYVPQ-QAWIQNC 702
Cdd:PRK13543 18 AFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrsrfMAYLGHlPGLKADL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 703 TLQENVLFGQPMNPKRYQQaletcalladldvLPGGDQTEIGEKGI------NLSGGQRQRVSLARAVYSDANIFLLDDP 776
Cdd:PRK13543 98 STLENLHFLCGLHGRRAKQ-------------MPGSALAIVGLAGYedtlvrQLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
....*
gi 1388591336 777 LSAVD 781
Cdd:PRK13543 165 YANLD 169
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
641-792 |
4.56e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.21 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGS--------------VAYVPQQAWI-QNCTLQ 705
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQEPLLfPNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 706 ENVLFGQPMNPKRYQQALETCALLA---DLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDS 782
Cdd:PRK15439 105 ENILFGLPKRQASMQKMKQLLAALGcqlDLDSSAG-----------SLEVADRQIVEILRGLMRDSRILILDEPTASLTP 173
|
170
....*....|
gi 1388591336 783 HVAKHIFDQV 792
Cdd:PRK15439 174 AETERLFSRI 183
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
1045-1256 |
6.58e-06 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 49.77 E-value: 6.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1045 LHNKI-RSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLLNSFFT--SISTIMVIV-ASTPLFMVVVLPLAVLYGF 1120
Cdd:cd18545 79 LFSHLqKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTlvGIVIIMFSLnVRLALVTLAVLPLLVLVVF 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1121 V-QRFyvatSRQLKRLESISRSPIFSHFSETVTGTSVIRAYGR----IQDFKVLSDTKVDNNQKSSYPyiasNRWLGVHV 1195
Cdd:cd18545 159 LlRRR----ARKAWQRVRKKISNLNAYLHESISGIRVIQSFARedenEEIFDELNRENRKANMRAVRL----NALFWPLV 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388591336 1196 EF---VGNCVVLFAALFAVIGrNSLNPGLVglsVSYALQVTMAlnWM-IRMISD----LESNIIAVERV 1256
Cdd:cd18545 231 ELisaLGTALVYWYGGKLVLG-GAITVGVL---VAFIGYVGRF--WQpIRNLSNfynqLQSAMASAERI 293
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
646-781 |
7.52e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 49.12 E-value: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 646 LNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSV--------------KGSVAYVPQQAWI-QNCTLQENVLF 710
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedisllplharaRRGIGYLPQEASIfRRLSVYDNLMA 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1388591336 711 GQPM--NPKRYQQALETCALLADLDVLPGGDQTeigekGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD 781
Cdd:PRK10895 102 VLQIrdDLSAEQREDRANELMEEFHIEHLRDSM-----GQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
653-808 |
8.13e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 50.65 E-value: 8.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 653 GALVAVVGPVGCGKSSLVSALLGEMEK--LEGVVSVKGS---------VAYVPQQAWI-QNCTLQENVLFGQ----PMNP 716
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGnnFTGTILANNRkptkqilkrTGFVTQDDILyPHLTVRETLVFCSllrlPKSL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 717 KRYQQALETCALLADLDvLPGGDQTEIGEKGIN-LSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGp 795
Cdd:PLN03211 174 TKQEKILVAESVISELG-LTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGS- 251
|
170
....*....|...
gi 1388591336 796 egvLAGKTRVLVT 808
Cdd:PLN03211 252 ---LAQKGKTIVT 261
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
641-836 |
8.34e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.39 E-value: 8.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGS--VAYVPQQ------AWI------------- 699
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHevVTRSPQDglangiVYIsedrkrdglvlgm 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 700 ---QN---CTLQENVLFGQPMNPKRYQQALETCALLADLDVlPGGDQTeIGekgiNLSGGQRQRVSLARAVYSDANIFLL 773
Cdd:PRK10762 346 svkENmslTALRYFSRAGGSLKHADEQQAVSDFIRLFNIKT-PSMEQA-IG----LLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 774 DDPLSAVDSHVAKHIFdQVIG---PEGVlagkTRVLVThgiSFLPQ----TDFIIVLAGGQVSemGHYSA 836
Cdd:PRK10762 420 DEPTRGVDVGAKKEIY-QLINqfkAEGL----SIILVS---SEMPEvlgmSDRILVMHEGRIS--GEFTR 479
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
640-781 |
8.60e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.58 E-value: 8.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 640 PPTLHSLN---IQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSVAYVPQQAWIQNCTLQENVLFGQP--- 713
Cdd:PRK11308 25 ERLVKALDgvsFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNPygs 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 714 MNP-KRYQQAL-ETCALLADLDvlpggdQTEIGEKGINL------------------SGGQRQRVSLARAVYSDANIFLL 773
Cdd:PRK11308 105 LNPrKKVGQILeEPLLINTSLS------AAERREKALAMmakvglrpehydryphmfSGGQRQRIAIARALMLDPDVVVA 178
|
....*...
gi 1388591336 774 DDPLSAVD 781
Cdd:PRK11308 179 DEPVSALD 186
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
643-841 |
1.16e-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: 49.68 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGeMEKLEGVVSVKG-SVAYVPQQAW------IQnctlqenVLFGQP-- 713
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGqDLDGLSRRALrplrrrMQ-------VVFQDPfg 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 714 -MNP-------------------------KRYQQALETCALLAD-LDVLPggdqTEigekginLSGGQRQRVSLARAVYS 766
Cdd:COG4172 374 sLSPrmtvgqiiaeglrvhgpglsaaerrARVAEALEEVGLDPAaRHRYP----HE-------FSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 767 DANIFLLDDPLSAVDSHVAKHIFDqvigpegVLAGKTRvlvTHGISFLpqtdFI--------------IVLAGGQVSEMG 832
Cdd:COG4172 443 EPKLLVLDEPTSALDVSVQAQILD-------LLRDLQR---EHGLAYL----FIshdlavvralahrvMVMKDGKVVEQG 508
|
250
....*....|..
gi 1388591336 833 HYSALL---QHD 841
Cdd:COG4172 509 PTEQVFdapQHP 520
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
318-601 |
1.83e-05 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 48.18 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 318 LIQNLLGFVNPQLLSILIRFISDPTAPTWWGFLLAGLMFLSSTMQTLILHQYYHCIFVMALRLRTAIIGVIYRKALVITN 397
Cdd:cd18541 9 ILVDLLQLLIPRIIGRAIDALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 398 SVKRESTVGEMVNLMS--VDAQRFMdVSPFINLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNGAVSMKM-KT 474
Cdd:cd18541 89 SFYQKNRTGDLMARATndLNAVRMA-LGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIhKR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 475 YQVKQMKFKDsriklMS----EILNGIKVLKLYAWEPS----FLEQVKGIRQSELQLLRKGAYLQAISTFIwictPFLVT 546
Cdd:cd18541 168 FRKVQEAFSD-----LSdrvqESFSGIRVIKAFVQEEAeierFDKLNEEYVEKNLRLARVDALFFPLIGLL----IGLSF 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1388591336 547 LITLGV---YVYVDESNVLDaekaFVSLSL-FNILKIPLNMLPQLISGLTQASVSLKRI 601
Cdd:cd18541 239 LIVLWYggrLVIRGTITLGD----LVAFNSyLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1299-1453 |
2.04e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 47.25 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1299 ELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHiGLHDLRSQLTIIPQ----DPILfsg 1374
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHrsgiNPYL--- 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388591336 1375 TLRMNLdpfgRYSEEDIWRALELSHLNTFVSSQPAgLDFQCAEggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAID 1453
Cdd:PRK13540 90 TLRENC----LYDIHFSPGAVGITELCRLFSLEHL-IDYPCGL----LSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
749-833 |
2.33e-05 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 48.26 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 749 NLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDqvigpegVLA------GKTRVLVTHGISFLPQT-DFII 821
Cdd:PRK11153 140 QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILE-------LLKdinrelGLTIVLITHEMDVVKRIcDRVA 212
|
90
....*....|..
gi 1388591336 822 VLAGGQVSEMGH 833
Cdd:PRK11153 213 VIDAGRLVEQGT 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1275-1493 |
2.41e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 49.01 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1275 APEGWPTRGMVEFRNYSVRYrPGLELVLKNVTVHVqgGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIvidglnvahig 1354
Cdd:COG1245 332 PRREKEEETLVEYPDLTKSY-GGFSLEVEGGEIRE--GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV----------- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1355 lhdlRSQLTI------IPQDpilFSGTLRMNL-----DPFG-RYSEEDIWRALELSHLntfvssqpagLDFQCaeggDNL 1422
Cdd:COG1245 398 ----DEDLKIsykpqyISPD---YDGTVEEFLrsantDDFGsSYYKTEIIKPLGLEKL----------LDKNV----KDL 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388591336 1423 SVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFE--DCTVLTIAHRLnTIMDY--NRVLVLD 1493
Cdd:COG1245 457 SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAEnrGKTAMVVDHDI-YLIDYisDRLMVFE 530
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1049-1162 |
2.62e-05 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 47.86 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1049 IRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLLNSFFTSI-STIMVIVASTPL--FMVVVLPLAVLygfvqrFY 1125
Cdd:cd18575 80 LRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIgGLVMLFITSPKLtlLVLLVIPLVVL------PI 153
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1388591336 1126 VATSRQLKRLESISRSPIF---SHFSETVTGTSVIRAYGR 1162
Cdd:cd18575 154 ILFGRRVRRLSRASQDRLAdlsAFAEETLSAIKTVQAFTR 193
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
650-781 |
3.41e-05 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 47.80 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 650 IPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG-SVAYVPQQAW------IQnctlqenVLFGQPM---NP-KR 718
Cdd:COG4608 41 IRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGqDITGLSGRELrplrrrMQ-------MVFQDPYaslNPrMT 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388591336 719 YQQALEtcALLADLDVLPGGDQTEIGEK-----GIN----------LSGGQRQRVSLARAVYSDANIFLLDDPLSAVD 781
Cdd:COG4608 114 VGDIIA--EPLRIHGLASKAERRERVAEllelvGLRpehadrypheFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
646-840 |
3.71e-05 |
|
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: 47.74 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 646 LNIQIPKGALVAVVGPVGCGKSSLVSALLG---EMEKLEGVVSVKGS-----------------VAYVPQ---------- 695
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEdllklsekelrkirgreIQMIFQdpmtslnpvm 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 696 ----QawiqnctLQENVLFGQPMNPK-RYQQALEtcaLLADLdvlpggdqteigekGIN------------LSGGQRQRV 758
Cdd:COG0444 104 tvgdQ-------IAEPLRIHGGLSKAeARERAIE---LLERV--------------GLPdperrldrypheLSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 759 SLARAVYSDANIFLLDDPLSAVDSHVAKHIFDqvigpegVLA------GKTRVLVTHGISFLPQT-DFIIVLAGGQVSEM 831
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILN-------LLKdlqrelGLAILFITHDLGVVAEIaDRVAVMYAGRIVEE 232
|
....*....
gi 1388591336 832 GHYSALLQH 840
Cdd:COG0444 233 GPVEELFEN 241
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
649-776 |
3.82e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.41 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 649 QIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSV--KGSVAYV--------PQQAWIQNCT--LQENVLFGQPMNP 716
Cdd:PRK11147 341 QVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCgtKLEVAYFdqhraeldPEKTVMDNLAegKQEVMVNGRPRHV 420
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388591336 717 KRYQQaletcalladlDVL--PGGDQTEIGEkginLSGGQRQRVSLARAVYSDANIFLLDDP 776
Cdd:PRK11147 421 LGYLQ-----------DFLfhPKRAMTPVKA----LSGGERNRLLLARLFLKPSNLLILDEP 467
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
646-841 |
4.16e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.04 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 646 LNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGS-VAYVPQQAWIQnctLQENV-----LFGQPMNPKry 719
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKpVTAEQPEDYRK---LFSAVftdfhLFDQLLGPE-- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 720 QQALETCALLADLDVLPGGDQTEIGE---KGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKhIFDQVIGPE 796
Cdd:PRK10522 417 GKPANPALVEKWLERLKMAHKLELEDgriSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRR-EFYQVLLPL 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1388591336 797 GVLAGKTRVLVTHGISFLPQTDFIIVLAGGQVSEM-GHYSALLQHD 841
Cdd:PRK10522 496 LQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSELtGEERDAASRD 541
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
1012-1115 |
6.17e-05 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 46.66 E-value: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1012 AALGILQGLLVMLSAFTMVVGAIQAARLLHEALLHNKIRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLLNSFF 1091
Cdd:cd18551 43 VALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVL 122
|
90 100 110
....*....|....*....|....*....|....*
gi 1388591336 1092 TSISTIM-----------VIVASTPLFMVVVLPLA 1115
Cdd:cd18551 123 TVVGAVVlmflldwvltlVTLAVVPLAFLIILPLG 157
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
750-818 |
1.36e-04 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 45.60 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 750 LSGGQRQRVSLARAVYSDANIFLLDDPLSAVD-------------------------SH---VAKHIFDQVI----GpEG 797
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDmsvrsqiinlmlelqeklgisyiyvSQhlgIVKHISDKVLvmhqG-EV 228
|
90 100
....*....|....*....|.
gi 1388591336 798 VLAGKTRVLVTHgisflPQTD 818
Cdd:COG4167 229 VEYGKTAEVFAN-----PQHE 244
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1272-1453 |
1.58e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1272 SNRAPEGWPTRGMV--EFRNYSVrYRPGLE--LVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLF------RIleaaEG 1341
Cdd:NF040905 243 EDRYPERTPKIGEVvfEVKNWTV-YHPLHPerKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgrsygrNI----SG 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1342 EIVIDG-----LNVAHIGLHDL------RSQLTIIPQDPILFSGTLrMNLDPFGRYS----EEDIWRALEL-SHLNTFVS 1405
Cdd:NF040905 318 TVFKDGkevdvSTVSDAIDAGLayvtedRKGYGLNLIDDIKRNITL-ANLGKVSRRGvideNEEIKVAEEYrKKMNIKTP 396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1406 S--QPAGldfqcaeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAID 1453
Cdd:NF040905 397 SvfQKVG----------NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1312-1485 |
2.19e-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: 43.13 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1312 GEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIipqdpilfsgtlrmnldpfgryseedi 1391
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIV--------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1392 wralelshlntfvssqpagldfqcAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQF--- 1468
Cdd:smart00382 55 ------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLlll 110
|
170 180
....*....|....*....|.
gi 1388591336 1469 ----EDCTVLTIAHRLNTIMD 1485
Cdd:smart00382 111 lkseKNLTVILTTNDEKDLGP 131
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
640-781 |
2.28e-04 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 44.54 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 640 PPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGeMEKLEGVVSVKGSV-------------AYVPQQawiQNCTLQE 706
Cdd:PRK03695 9 STRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPleawsaaelarhrAYLSQQ---QTPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 707 NV-----LFGQPMNPKRYQQAL--ETCALLADLDVLPGGDQTeigekginLSGGQRQRVSLA-------RAVYSDANIFL 772
Cdd:PRK03695 85 PVfqyltLHQPDKTRTEAVASAlnEVAEALGLDDKLGRSVNQ--------LSGGEWQRVRLAavvlqvwPDINPAGQLLL 156
|
....*....
gi 1388591336 773 LDDPLSAVD 781
Cdd:PRK03695 157 LDEPMNSLD 165
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1009-1162 |
2.58e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 44.81 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1009 GVYAALGILQGLLVMLSAFTMVVGAIQAARLLHEALLHNKIRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLLN 1088
Cdd:cd18564 58 AALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLT 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1089 SFFTSIstIMVIVA---STPLFMVVVLPLAVLYGFVQRFY---VATSRQLKRLESIsrspIFSHFSETVTGTSVIRAYGR 1162
Cdd:cd18564 138 NLLTLV--GMLGVMfwlDWQLALIALAVAPLLLLAARRFSrriKEASREQRRREGA----LASVAQESLSAIRVVQAFGR 211
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1300-1497 |
3.16e-04 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 44.15 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1300 LVLKNVTV---------HVQGGEKVGIVGRTGAGKSSMTLCLFRILEaAEGEIVIDGLNVAHIGLHDL---RSQLTiiPQ 1367
Cdd:PRK03695 1 MQLNDVAVstrlgplsaEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELarhRAYLS--QQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1368 DPILFSgtlrMnldpfgryseeDIWRALELshlntfvsSQPAGLDFQCAEG-----------GD-------NLSVGQRQL 1429
Cdd:PRK03695 78 QTPPFA----M-----------PVFQYLTL--------HQPDKTRTEAVASalnevaealglDDklgrsvnQLSGGEWQR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1430 VCLARALLR-------KSRVLVLDEATAAIDLETDDLIQGTIRtqfEDC----TVLTIAHRLNTIMDY-NRVLVLDKGVV 1497
Cdd:PRK03695 135 VRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQQAALDRLLS---ELCqqgiAVVMSSHDLNHTLRHaDRVWLLKQGKL 211
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1317-1503 |
3.63e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 44.46 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1317 IVGRTGAGKSSMTLCLFRILEAAEGEIVI-DGLNVAHIGLHD---------------LRSQLTIIPQDP--ILFSGTLRM 1378
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQVgDIYIGDKKNNHElitnpyskkiknfkeLRRRVSMVFQFPeyQLFKDTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1379 NLdPFG----RYSEEDIwRALELSHLN------TFVSSQPAGLdfqcaeggdnlSVGQRQLVCLARALLRKSRVLVLDEA 1448
Cdd:PRK13631 137 DI-MFGpvalGVKKSEA-KKLAKFYLNkmglddSYLERSPFGL-----------SGGQKRRVAIAGILAIQPEILIFDEP 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1388591336 1449 TAAIDLETD-DLIQGTIRTQFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSP 1503
Cdd:PRK13631 204 TAGLDPKGEhEMMQLILDAKANNKTVFVITHTMEHVLEVaDEVIVMDKGKILKTGTP 260
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
643-789 |
3.65e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.16 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKG----------------SVAYvPQQAWIQNCTLQE 706
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldhklaaqlgiGIIY-QELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 707 NVLFGQPMNPK--------------RYQQALETCALLADLDvlpggdqteigEKGINLSGGQRQRVSLARAVYSDANIFL 772
Cdd:PRK09700 100 NLYIGRHLTKKvcgvniidwremrvRAAMMLLRVGLKVDLD-----------EKVANLSISHKQMLEIAKTLMLDAKVII 168
|
170
....*....|....*..
gi 1388591336 773 LDDPLSAVDSHVAKHIF 789
Cdd:PRK09700 169 MDEPTSSLTNKEVDYLF 185
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1285-1473 |
4.22e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.94 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1285 VEFRNYSVryrPGLELVlKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEI-VIDGLNVAHIGLH--DLRSQ 1361
Cdd:PRK11147 322 MENVNYQI---DGKQLV-KDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhCGTKLEVAYFDQHraELDPE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1362 LTII------PQDpILFSGTLRMnldpfgryseediwralELSHLNTFVSS-----QPAgldfqcaeggDNLSVGQRQLV 1430
Cdd:PRK11147 398 KTVMdnlaegKQE-VMVNGRPRH-----------------VLGYLQDFLFHpkramTPV----------KALSGGERNRL 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 1431 CLARALLRKSRVLVLDEATAAIDLETDDLI-------QGTI------RtQFEDCTV 1473
Cdd:PRK11147 450 LLARLFLKPSNLLILDEPTNDLDVETLELLeelldsyQGTVllvshdR-QFVDNTV 504
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
1014-1243 |
4.36e-04 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 43.93 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1014 LGILQGLLVMLSAFTMVVGAIQAARL-------LHEALLHnKIrspQSF----FDTTPSGRILNRFSKDIYVIDEVLAPT 1082
Cdd:cd18548 41 TGLLMLLLALLGLIAGILAGYFAAKAsqgfgrdLRKDLFE-KI---QSFsfaeIDKFGTSSLITRLTNDVTQVQNFVMML 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1083 ILMLLNSFFTSI-STIMVIVASTPL---FMVVVLPLAVLYGFVQRFYVATSRQL-KRLESISRSpifshFSETVTGTSVI 1157
Cdd:cd18548 117 LRMLVRAPIMLIgAIIMAFRINPKLaliLLVAIPILALVVFLIMKKAIPLFKKVqKKLDRLNRV-----VRENLTGIRVI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1158 RAYGR----IQDFKVLSDTKVDNNqkssypyIASNRWLGVH---VEFVGN----CVVLFAALFAVIGrnSLNPG-LVGLs 1225
Cdd:cd18548 192 RAFNRedyeEERFDKANDDLTDTS-------LKAGRLMALLnplMMLIMNlaivAILWFGGHLINAG--SLQVGdLVAF- 261
|
250
....*....|....*...
gi 1388591336 1226 VSYALQVTMALNWMIRMI 1243
Cdd:cd18548 262 INYLMQILMSLMMLSMVF 279
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
748-830 |
4.97e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 43.32 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 748 INLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDqvIGPEGVLAGKTRVLVTHGISFLPQTDFIIV----- 822
Cdd:PRK10908 136 IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILR--LFEEFNRVGVTVLMATHDIGLISRRSYRMLtlsdg 213
|
....*....
gi 1388591336 823 -LAGGQVSE 830
Cdd:PRK10908 214 hLHGGVGGE 222
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1009-1256 |
5.27e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 43.65 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1009 GVYAALGILQGLLVMLSAFTMVVGAIQA---ARL-------LHEALLHNKIRSPQSFFDTTPSGRILNRFSKDIYVIDEV 1078
Cdd:cd18563 37 GNTSLLLLLVLGLAGAYVLSALLGILRGrllARLgeritadLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1079 LAPTILMLLNSFFTSIST-IMVIVASTPLFMVVVLPLAVLYGFVQRFYVATSRQLKRLeSISRSPIFSHFSETVTGTSVI 1157
Cdd:cd18563 117 LSDGLPDFLTNILMIIGIgVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQ-WRRWSRLNSVLNDTLPGIRVV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1158 RAYGR----IQDFKVLSDTKVDNNQKssypyiASNRWLGVHvEFVGNCVVLFAALFAVIG-----RNSLNPGLVGLSVSY 1228
Cdd:cd18563 196 KAFGQekreIKRFDEANQELLDANIR------AEKLWATFF-PLLTFLTSLGTLIVWYFGgrqvlSGTMTLGTLVAFLSY 268
|
250 260
....*....|....*....|....*...
gi 1388591336 1229 ALQVTMALNWMIRMISDLESNIIAVERV 1256
Cdd:cd18563 269 LGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
1037-1119 |
7.41e-04 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 43.39 E-value: 7.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1037 ARL---LHEALLHNKIrspqSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLLNSFFTSISTIMVIVASTP---LFMVV 1110
Cdd:cd18780 75 ARLrkrLFSAIIAQEI----AFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWkltLVMLS 150
|
90
....*....|...
gi 1388591336 1111 VLPL----AVLYG 1119
Cdd:cd18780 151 VVPPlsigAVIYG 163
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
436-601 |
7.45e-04 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 43.19 E-value: 7.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 436 VILAIYFLWQILGPSALagvaVIVLLIPLNGAVSMKMKTyQVKQMkFKDSRIKL------MSEILNGIKVLKLYAWEPS- 508
Cdd:cd18542 127 FIGALIIMFSINWKLTL----ISLAIIPFIALFSYVFFK-KVRPA-FEEIREQEgelntvLQENLTGVRVVKAFAREDYe 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 509 ---FLEQVKGIRQSELQLLRKGAYLQAISTFIWICTPFLVTL----------ITLGVYVyvdesnvldaekAFVSLSlfN 575
Cdd:cd18542 201 iekFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWvggylvingeITLGELV------------AFISYL--W 266
|
170 180
....*....|....*....|....*.
gi 1388591336 576 ILKIPLNMLPQLISGLTQASVSLKRI 601
Cdd:cd18542 267 MLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
643-832 |
7.49e-04 |
|
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: 42.51 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGemekLEGVVSVKGSVAYVPQQawIQNCTLQENVLFGQPM---NPKRY 719
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG----HPKYEVTEGEILFKGED--ITDLPPEERARLGIFLafqYPPEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 720 qQALETCALLADLDVlpggdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD----SHVAKHIfDQVIGP 795
Cdd:cd03217 90 -PGVKNADFLRYVNE--------------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDidalRLVAEVI-NKLREE 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1388591336 796 egvlaGKTRVLVTH--GISFLPQTDFIIVLAGGQVSEMG 832
Cdd:cd03217 154 -----GKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
643-779 |
1.24e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.38 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLG-------------EMEKLE----------GVVSVKGSVAYVPQQAWI 699
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgtyegeiifEGEELQasnirdteraGIAIIHQELALVKELSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 700 QNCTLQENVLFGQPMN-PKRYQQALEtcaLLAD--LDVLPGgdqTEIGekgiNLSGGQRQRVSLARAVYSDANIFLLDDP 776
Cdd:PRK13549 101 ENIFLGNEITPGGIMDyDAMYLRAQK---LLAQlkLDINPA---TPVG----NLGLGQQQLVEIAKALNKQARLLILDEP 170
|
...
gi 1388591336 777 LSA 779
Cdd:PRK13549 171 TAS 173
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
751-788 |
1.78e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.77 E-value: 1.78e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1388591336 751 SGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHI 788
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQI 464
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
718-832 |
1.83e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.42 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 718 RYQQALETCALL------ADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQ 791
Cdd:PRK11022 127 RRQRAIDLLNQVgipdpaSRLDVYPH-----------QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIEL 195
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1388591336 792 VIGpegvLAGKTR---VLVTHGISFLPQT-DFIIVLAGGQVSEMG 832
Cdd:PRK11022 196 LLE----LQQKENmalVLITHDLALVAEAaHKIIVMYAGQVVETG 236
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1317-1502 |
1.96e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 42.17 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1317 IVGRTGAGKSSMTLCLFRILEAAEGEIVIDGlnvaHIgLHDLRSQLTIIP---------QDPILF-----SGTLRMNLDP 1382
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNG----RV-LFDAEKGICLPPekrrigyvfQDARLFphykvRGNLRYGMAK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1383 FGRYSEEDIWRALELSH-LNTFVSSqpagldfqcaeggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAID-------- 1453
Cdd:PRK11144 104 SMVAQFDKIVALLGIEPlLDRYPGS---------------LSGGEKQRVAIGRALLTAPELLLMDEPLASLDlprkrell 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1388591336 1454 --LETddLIQgTIRTqfedcTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDS 1502
Cdd:PRK11144 169 pyLER--LAR-EINI-----PILYVSHSLDEILRLaDRVVVLEQGKVKAFGP 212
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
709-781 |
1.97e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.80 E-value: 1.97e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388591336 709 LFGQPMN--PKRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD 781
Cdd:NF033858 366 LFHLPAAeiAARVAEMLERFDLADVADALPD-----------SLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1284-1504 |
1.97e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 42.14 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYRPGLElVLKNVTVHVQGGEKVGIVGRTGAGKSSmtlcLFRI---LEA-AEGEIVIDGLNVAHIGlhdlr 1359
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQ-VIKGIDLDVADGEFIVLVGPSGCGKST----LLRMvagLERiTSGEIWIGGRVVNELE----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1360 sqltiiPQD---PILFSG-------TLRMNLDpFG----RYSEEDI-------WRALELSHLntfvssqpagLDFQCAEg 1418
Cdd:PRK11650 73 ------PADrdiAMVFQNyalyphmSVRENMA-YGlkirGMPKAEIeervaeaARILELEPL----------LDRKPRE- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1419 gdnLSVGQRQLVCLARALLRKSRVLVLDEATAAID--------LETDDLiQGTIRT--------QFEdctVLTIAHRLnt 1482
Cdd:PRK11650 135 ---LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDaklrvqmrLEIQRL-HRRLKTtslyvthdQVE---AMTLADRV-- 205
|
250 260
....*....|....*....|..
gi 1388591336 1483 imdynrvLVLDKGVVAEFDSPV 1504
Cdd:PRK11650 206 -------VVMNGGVAEQIGTPV 220
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
650-789 |
2.04e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.59 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 650 IPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGS--------------VA-------YVPQQawiqncTLQENV 708
Cdd:PRK11288 27 CRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasttaalaagVAiiyqelhLVPEM------TVAENL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 709 LFGQPmnPKR---------YQQALETCALLAdLDVLPggdQTEIGEkginLSGGQRQRVSLARAVYSDANIFLLDDPLSA 779
Cdd:PRK11288 101 YLGQL--PHKggivnrrllNYEAREQLEHLG-VDIDP---DTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170
....*....|
gi 1388591336 780 VDSHVAKHIF 789
Cdd:PRK11288 171 LSAREIEQLF 180
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
1036-1132 |
3.41e-03 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 41.35 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1036 AARL---LHEALLhnkiRSPQSFFDTTPSGRILNRFSKDIYVIDEVLApTILM--LLNSFFTSISTIMVIVASTPLFMVV 1110
Cdd:cd18573 73 VARLrkrLFKSIL----RQDAAFFDKNKTGELVSRLSSDTSVVGKSLT-QNLSdgLRSLVSGVGGIGMMLYISPKLTLVM 147
|
90 100
....*....|....*....|....*....
gi 1388591336 1111 --VLP----LAVLYG-FVQRFyvatSRQL 1132
Cdd:cd18573 148 llVVPpiavGAVFYGrYVRKL----SKQV 172
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
648-684 |
3.52e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 3.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1388591336 648 IQIPKGaLVAVVGPVGCGKSSLVSAL---LGE-------MEKLEGVV 684
Cdd:TIGR02168 19 INFDKG-ITGIVGPNGCGKSNIVDAIrwvLGEqsakalrGGKMEDVI 64
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
1052-1161 |
3.70e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 41.34 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1052 PQSFFDTTPSGRILNRFSkDIYVIDEVLAPTILML-LNSFFTSISTIMVIVASTPLFMVVVLpLAVLYGFVQRFYVATSR 1130
Cdd:cd18555 89 PYSFFENRSSGDLLFRAN-SNVYIRQILSNQVISLiIDLLLLVIYLIYMLYYSPLLTLIVLL-LGLLIVLLLLLTRKKIK 166
|
90 100 110
....*....|....*....|....*....|.
gi 1388591336 1131 QLKRLESISRSPIFSHFSETVTGTSVIRAYG 1161
Cdd:cd18555 167 KLNQEEIVAQTKVQSYLTETLYGIETIKSLG 197
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
751-814 |
4.36e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.77 E-value: 4.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388591336 751 SGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVakhifdqVIGPEGVLAG--KTRVLVTHGISFL 814
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA-------VLWLETYLLKwpKTFIVVSHAREFL 404
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1284-1461 |
4.54e-03 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 40.84 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1284 MVEFRNYSVRYrPGlELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVA-----------H 1352
Cdd:PRK11248 1 MLQISHLYADY-GG-KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgaergvvfqN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1353 IGLHDLRSQltiipQDPILFSGTLRmnldpfGRYSEEDIWRALELSHLntfvssqpAGLdfqcaEGGDN-----LSVGQR 1427
Cdd:PRK11248 79 EGLLPWRNV-----QDNVAFGLQLA------GVEKMQRLEIAHQMLKK--------VGL-----EGAEKryiwqLSGGQR 134
|
170 180 190
....*....|....*....|....*....|....
gi 1388591336 1428 QLVCLARALLRKSRVLVLDEATAAIDLETDDLIQ 1461
Cdd:PRK11248 135 QRVGIARALAANPQLLLLDEPFGALDAFTREQMQ 168
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
310-601 |
4.73e-03 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 40.88 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 310 LLMSACFNLIQNLLGFVNPQLLSILIRFISDPTAPTWWGFLLAGLMFLSSTMQTLilhQYYHCIFV---MALRLRTAIIG 386
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSSGGLLALLVALFLLQAVLSAL---SSYLLGRTgerVVLDLRRRLWR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 387 VIYRkaLVITNSVKREStvGEMVNLMSVDAQRFMDV--SPFINLLwSAPLQVILAIYFL----WQILGpSALAGVAVIVL 460
Cdd:cd18551 78 RLLR--LPVSFFDRRRS--GDLVSRVTNDTTLLRELitSGLPQLV-TGVLTVVGAVVLMflldWVLTL-VTLAVVPLAFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 461 LIplnGAVSMKMKTYQVKQMKFKDSRIKLMSEILNGIKVLKLYAWEPSFLEQVKGIRQSELQLLRKGAYLQA-ISTFIWI 539
Cdd:cd18551 152 II---LPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEAlIGPLMGL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388591336 540 CTpFLVTLITLGVYVYVDESNVLDAEK--AFVsLSLFNILkIPLNMLPQLISGLTQASVSLKRI 601
Cdd:cd18551 229 AV-QLALLVVLGVGGARVASGALTVGTlvAFL-LYLFQLI-TPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
749-856 |
5.62e-03 |
|
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: 40.43 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 749 NLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDshVAKHIFDQVIGPEGVLAGKTRVLVTHGISFLPQ-TDFIIVLAGgq 827
Cdd:cd03236 139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLD--IKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYlSDYIHCLYG-- 214
|
90 100 110
....*....|....*....|....*....|..
gi 1388591336 828 vsEMGHYSALLQHDG---SFANFLRNYAPDED 856
Cdd:cd03236 215 --EPGAYGVVTLPKSvreGINEFLDGYLPTEN 244
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
643-780 |
6.50e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 40.96 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLG------------------------EMEKlEGVVSVKGSVAYVPQQAW 698
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwdgeiywsgsplkasnirDTER-AGIVIIHQELTLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 699 IQNCTL-QENVLFGQPMNpkrYQQALETC-ALLADLDVLPGGDQTEIGEKGinlsGGQRQRVSLARAVYSDANIFLLDDP 776
Cdd:TIGR02633 96 AENIFLgNEITLPGGRMA---YNAMYLRAkNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEP 168
|
....
gi 1388591336 777 LSAV 780
Cdd:TIGR02633 169 SSSL 172
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
648-684 |
7.31e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 39.37 E-value: 7.31e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1388591336 648 IQIPKGaLVAVVGPVGCGKSSLVSAL---LGE-------MEKLEGVV 684
Cdd:cd03278 18 IPFPPG-LTAIVGPNGSGKSNIIDAIrwvLGEqsakslrGEKMSDVI 63
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
1010-1256 |
9.69e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 39.83 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1010 VYAALGILQGLLVMLSAFTMVVGAIQAARLLHEALLHNKIRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAptilMLLNS 1089
Cdd:cd18572 41 LLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLS----TNLNV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1090 FFTSI-----STIMVIVASTPLFMV---VVLPLAVLYGFVQRFYVATSRQLKrlESISRSpifSHFSETVTGT-SVIRAY 1160
Cdd:cd18572 117 FLRNLvqlvgGLAFMFSLSWRLTLLafiTVPVIALITKVYGRYYRKLSKEIQ--DALAEA---NQVAEEALSNiRTVRSF 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388591336 1161 G----RIQDFKVLSDTKVDNNQKSSYPYiASNRWLgvhVEFVGNCVVlfAALFAVIGRNSLNPGL-VGLSVSYAL---QV 1232
Cdd:cd18572 192 AteerEARRYERALDKALKLSVRQALAY-AGYVAV---NTLLQNGTQ--VLVLFYGGHLVLSGRMsAGQLVTFMLyqqQL 265
|
250 260
....*....|....*....|....
gi 1388591336 1233 TMALNWMIRMISDLESNIIAVERV 1256
Cdd:cd18572 266 GEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| |
