|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-1285 |
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: 1385.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 20 DAQKCsPEKSASFFSKVTYSWFSRVITLGYKRPLEREDLFELNESDSSYTVCPTFEKQWRKE-----------------V 82
Cdd:TIGR00957 198 DPNPC-PESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKEckktrkqpvsavygkkdP 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 83 LRNQERQKVKASFYIEA-------HTKKPSLLYALWNTFKSVLIQVALFKVFADILSFTSPLIMKQMIIFCEHSSDFGWN 155
Cdd:TIGR00957 277 SKPKGSSQLDANEEVEAlivksphKPRKPSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPDWQ 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 156 GYGYAMALFVVVFLQTLILQRYQCFNMLTSAKVKTAVNGLIYKKALLLSNVSRQKFSTGEIINLMSADAQQLMDLTANLN 235
Cdd:TIGR00957 357 GYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYIN 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 236 LLWSAPFQILMAIYLLWQELGPAVLAGVAVLVFVIPINALAATKIKKLKKSQRKNKDKQIKLLKEILHGIKILKLYAWEP 315
Cdd:TIGR00957 437 MIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWEL 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 316 SYKNKIIKIRDQELEFQKSARYLTVFSMLTLTCIPFLVSLATLCVYFLLDEGNILTATKVFTSMSLFNILRIPLFELPTV 395
Cdd:TIGR00957 517 AFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENNILDAEKAFVSLALFNILRFPLNILPMV 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 396 ISTVVQTKISLGRLEDFLHTEELLPQNIETNYI---GDHAIEFTDATYSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSG 472
Cdd:TIGR00957 597 ISSIVQASVSLKRLRIFLSHEELEPDSIERRTIkpgEGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCG 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 473 KSSMLSAILGEMEKLTGVVQRKGSVAYVSQQAWIQNCILQVNILFGSIMKKEFYEQVLEACALLPDLEQLPKGDQTEIGE 552
Cdd:TIGR00957 677 KSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGE 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 553 RGVNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGKQLFEKVIGSLGLLKNKTRILVTHNLTLLPQMDLIVVMES 632
Cdd:TIGR00957 757 KGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSG 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 633 GRIAQMGTYQELLSKT-------RNLTNLHQVISEEEKAHAL-----KRASAVNSRTRPKDKILEQKPRP-------SLD 693
Cdd:TIGR00957 837 GKISEMGSYQELLQRDgafaeflRTYAPDEQQGHLEDSWTALvsgegKEAKLIENGMLVTDVVGKQLQRQlsasssdSGD 916
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 694 QGKQLS-----------------MKKEKIPVGGVKFSIILQYLQAFGWLWVWLTMVTYLGQNLVGIGQNLWLSAWAKEAk 756
Cdd:TIGR00957 917 QSRHHGssaelqkaeakeetwklMEADKAQTGQVELSVYWDYMKAIGLFITFLSIFLFVCNHVSALASNYWLSLWTDDP- 995
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 757 nMNDFTEwkQIRSNKLNIYGILGLIKGLFVCSGAYVITRGSLAASRTMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDI 836
Cdd:TIGR00957 996 -MVNGTQ--NNTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKEL 1072
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 837 FIIDMRLHYYLRLWVNCTLDVIGTILVIIGALPLFILGIIPSVFFYFSIQRYYVASSRQIRRLTGASRSPVISHFSETLS 916
Cdd:TIGR00957 1073 DTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLL 1152
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 917 GVSTIRAFGHQQRFIQQYKEVVNENLVCFYNNVISNRWLSVRLEFLGNLMVLFAALLAVLAGNSIDSATVGLSISYALNI 996
Cdd:TIGR00957 1153 GVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQV 1232
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 997 THSLNFWVKKACEIETNAVAVERVCEYENMDKEAPW-IMSRRPPLQWPNKGVVEFINYQARYRDELGLALQDITFQTHGE 1075
Cdd:TIGR00957 1233 TFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWqIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGG 1312
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1076 EKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKLNIIPQHPVLFSGTLQMNLDPLNKYSDSKLW 1155
Cdd:TIGR00957 1313 EKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVW 1392
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1156 EALELCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTIRKEFSDCT 1235
Cdd:TIGR00957 1393 WALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCT 1472
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|
gi 74136409 1236 ILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQNLIRQKGLFYEMTTDAGI 1285
Cdd:TIGR00957 1473 VLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAKDAGL 1522
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
9-1284 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 973.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 9 GGSYQRVRGGldaQKCSPEKSASFFSKVTYSWFSRVITLGYKRPLEREDLFELNESDSSYTVCPTFEKQWrkevlrNQER 88
Cdd:PLN03130 214 DYEYEELPGG---EQICPERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCW------DEEL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 89 QKvkasfyieahtKKPSLLYALWNTFKSVLIQVALFKVFADILSFTSPLIMKQMIIFCEhSSDFGWNGYGYAMALFVVVF 168
Cdd:PLN03130 285 KK-----------PKPWLLRALNNSLGGRFWLGGFFKIGNDLSQFVGPLLLNLLLESMQ-NGEPAWIGYIYAFSIFVGVV 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 169 LQTLILQRYQCFNMLTSAKVKTAVNGLIYKKALLLSNVSRQKFSTGEIINLMSADAQQLMDLTANLNLLWSAPFQILMAI 248
Cdd:PLN03130 353 LGVLCEAQYFQNVMRVGFRLRSTLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAM 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 249 YLLWQELGPAVLAGVAVLVFVIPINALAATKIKKLKKSQRKNKDKQIKLLKEILHGIKILKLYAWEPSYKNKIIKIRDQE 328
Cdd:PLN03130 433 VLLYQQLGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDE 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 329 LEFQKSARYLTVFSMLTLTCIPFLVSLATLCVYFLLdeGNILTATKVFTSMSLFNILRIPLFELPTVISTVVQTKISLGR 408
Cdd:PLN03130 513 LSWFRKAQLLSAFNSFILNSIPVLVTVVSFGVFTLL--GGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKR 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 409 LEDFLHTEE--LLPQ-NIETnyiGDHAIEFTDATYSWNKTG-MPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEM 484
Cdd:PLN03130 591 LEELLLAEErvLLPNpPLEP---GLPAISIKNGYFSWDSKAeRPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGEL 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 485 EKLTG--VVQRkGSVAYVSQQAWIQNCILQVNILFGSIMKKEFYEQVLEACALLPDLEQLPKGDQTEIGERGVNISGGQQ 562
Cdd:PLN03130 668 PPRSDasVVIR-GTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQK 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 563 HRVSLARAVYSGADIYLLDDPLSAVDVHVGKQLFEKVIGslGLLKNKTRILVTHNLTLLPQMDLIVVMESGRIAQMGTYQ 642
Cdd:PLN03130 747 QRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIK--DELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYE 824
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 643 ELLSK-------TRNLTNLHQVISEEEKAHALKRAS--AVNSRT--RPKDKILEQKPRpsldQGKQLSMKKEKIPVGGVK 711
Cdd:PLN03130 825 ELSNNgplfqklMENAGKMEEYVEENGEEEDDQTSSkpVANGNAnnLKKDSSSKKKSK----EGKSVLIKQEERETGVVS 900
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 712 FSIILQYLQAFGWLWVWLTMVT-YLGQNLVGIGQNLWLSAWAKEaknmndfTEWKQIRSNKLN-IYGILGLIKGLFVCSG 789
Cdd:PLN03130 901 WKVLERYKNALGGAWVVMILFLcYVLTEVFRVSSSTWLSEWTDQ-------GTPKTHGPLFYNlIYALLSFGQVLVTLLN 973
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 790 AYVITRGSLAASRTMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDMRLHYYLRLWVNCTLDVIGTiLVIIGALP 869
Cdd:PLN03130 974 SYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLST-FVLIGIVS 1052
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 870 LFIL-GIIPSVFFYFSIQRYYVASSRQIRRLTGASRSPVISHFSETLSGVSTIRAFGHQQRFIQQYKEVVNENLVCFYNN 948
Cdd:PLN03130 1053 TISLwAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVN 1132
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 949 VISNRWLSVRLEFLGNLMV-LFAALLAVLAGNSIDSA----TVGLSISYALNITHSLNFWVKKACEIETNAVAVERVCEY 1023
Cdd:PLN03130 1133 MSSNRWLAIRLETLGGLMIwLTASFAVMQNGRAENQAafasTMGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTY 1212
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1024 ENMDKEAPWIM-SRRPPLQWPNKGVVEFINYQARYRDELGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERA 1102
Cdd:PLN03130 1213 IDLPSEAPLVIeNNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELE 1292
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1103 GGKIIIDGIDISTIGLHDLRGKLNIIPQHPVLFSGTLQMNLDPLNKYSDSKLWEALELCHLKEFVQSLPEKLRHEISEGG 1182
Cdd:PLN03130 1293 RGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAG 1372
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1183 ENLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTIRKEFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVE 1262
Cdd:PLN03130 1373 ENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVE 1452
|
1290 1300
....*....|....*....|...
gi 74136409 1263 FEAPQNLIRQKG-LFYEMTTDAG 1284
Cdd:PLN03130 1453 FDTPENLLSNEGsAFSKMVQSTG 1475
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
11-1284 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 908.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 11 SYQRVRGGldAQKCsPEKSASFFSKVTYSWFSRVITLGYKRPLEREDLFELNESDSSYTVCPTFEKQWRKEVLRnqerqk 90
Cdd:PLN03232 216 EYDALRGG--ENIC-PERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEESRR------ 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 91 vkasfyieahtKKPSLLYALWNTFKSVLIQVALFKVFADILSFTSPLIMKQmIIFCEHSSDFGWNGYGYAMALFVVVFLQ 170
Cdd:PLN03232 287 -----------PKPWLLRALNNSLGGRFWLGGIFKIGHDLSQFVGPVILSH-LLQSMQEGDPAWVGYVYAFLIFFGVTFG 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 171 TLILQRYQCFNMLTSAKVKTAVNGLIYKKALLLSNVSRQKFSTGEIINLMSADAQQLMDLTANLNLLWSAPFQILMAIYL 250
Cdd:PLN03232 355 VLCESQYFQNVGRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVL 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 251 LWQELGPAVLAGVAVLVFVIPINALAATKIKKLKKSQRKNKDKQIKLLKEILHGIKILKLYAWEPSYKNKIIKIRDQELE 330
Cdd:PLN03232 435 LYQQLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELS 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 331 FQKSARYLTVFSMLTLTCIPFLVSLATLCVYFLLdeGNILTATKVFTSMSLFNILRIPLFELPTVISTVVQTKISLGRLE 410
Cdd:PLN03232 515 WFRKAQLLSAFNSFILNSIPVVVTLVSFGVFVLL--GGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIE 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 411 DFLHTEE-LLPQNIETNyIGDHAIEFTDATYSWN-KTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKL- 487
Cdd:PLN03232 593 ELLLSEErILAQNPPLQ-PGAPAISIKNGYFSWDsKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAe 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 488 TGVVQRKGSVAYVSQQAWIQNCILQVNILFGSIMKKEFYEQVLEACALLPDLEQLPKGDQTEIGERGVNISGGQQHRVSL 567
Cdd:PLN03232 672 TSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSM 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 568 ARAVYSGADIYLLDDPLSAVDVHVGKQLFEKVIGSLglLKNKTRILVTHNLTLLPQMDLIVVMESGRIAQMGTYQELLSK 647
Cdd:PLN03232 752 ARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDE--LKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKS 829
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 648 TRNLTNLHQVISEEEKAHALKRASAVNSRTRPKDKI-LEQKPRPSLDQGKQ---LSMKKEKIPVGGVKFSIILQYLQAFG 723
Cdd:PLN03232 830 GSLFKKLMENAGKMDATQEVNTNDENILKLGPTVTIdVSERNLGSTKQGKRgrsVLVKQEERETGIISWNVLMRYNKAVG 909
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 724 WLWV-WLTMVTYLGQNLVGIGQNLWLSAWAKEAKNMNDFTEWKQIrsnklnIYGILGLIKGLFVCSGAYVITRGSLAASR 802
Cdd:PLN03232 910 GLWVvMILLVCYLTTEVLRVSSSTWLSIWTDQSTPKSYSPGFYIV------VYALLGFGQVAVTFTNSFWLISSSLHAAK 983
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 803 TMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDMRLHYYLRLWVNCTLDVIGTILVIIGALPLFILGIIPSVFFY 882
Cdd:PLN03232 984 RLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILF 1063
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 883 FSIQRYYVASSRQIRRLTGASRSPVISHFSETLSGVSTIRAFGHQQRFIQQYKEVVNENLVCFYNNVISNRWLSVRLEFL 962
Cdd:PLN03232 1064 YAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETL 1143
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 963 GNLMV-LFAALLAVLAGNSIDSA----TVGLSISYALNITHSLNFWVKKACEIETNAVAVERVCEYENMDKEAPWIM-SR 1036
Cdd:PLN03232 1144 GGVMIwLTATFAVLRNGNAENQAgfasTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIeNN 1223
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1037 RPPLQWPNKGVVEFINYQARYRDELGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTI 1116
Cdd:PLN03232 1224 RPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKF 1303
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1117 GLHDLRGKLNIIPQHPVLFSGTLQMNLDPLNKYSDSKLWEALELCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLA 1196
Cdd:PLN03232 1304 GLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLA 1383
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1197 RALLRKTKILILDEATASIDFETDKLVQTTIRKEFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQNLI-RQKGL 1275
Cdd:PLN03232 1384 RALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLsRDTSA 1463
|
....*....
gi 74136409 1276 FYEMTTDAG 1284
Cdd:PLN03232 1464 FFRMVHSTG 1472
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
106-1279 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 683.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 106 LLYALWntfKSVLIQVaLFKVFADILSFTSPLIMKQMIIFC-EHSSDFGWnGYGYAMALFVVVFLQTLILQRYQCFNMLT 184
Cdd:PTZ00243 238 LFAALP---YYVWWQI-PFKLLSDVCTLTLPVLLKYFVKFLdADNATWGR-GLGLVLTLFLTQLIQSVCLHRFYYISIRC 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 185 SAKVKTAVNGLIYKKALLLSN--VSRQKFSTGEIINLMSADAQQLMDLTANLNLLWSAPFQILMAIYLLWQELGPAVLAG 262
Cdd:PTZ00243 313 GLQYRSALNALIFEKCFTISSksLAQPDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCALMA 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 263 VAVLVFVIPINALAATKIKKLKKSQRKNKDKQIKLLKEILHGIKILKLYAWEPSYKNKIIKIRDQELEFQKSARYLTVFS 342
Cdd:PTZ00243 393 VAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLARVAT 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 343 MLTLTCIPFLVSLATLCVYFLLdeGNILTATKVFTSMSLFNILRIPLFELPTVISTVVQTKISLGRLEDFLH-------- 414
Cdd:PTZ00243 473 SFVNNATPTLMIAVVFTVYYLL--GHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLEcdnatcst 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 415 ---TEELLPQNIE----------------TNYI----------------------------------------------- 428
Cdd:PTZ00243 551 vqdMEEYWREQREhstacqlaavlenvdvTAFVpvklprapkvktsllsralrmlcceqcrptkrhpspsvvvedtdygs 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 429 ---------------GDHAIEFTDATYSWNKTGMP---------VLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEM 484
Cdd:PTZ00243 631 pssasrhiveggtggGHEATPTSERSAKTPKMKTDdffelepkvLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQF 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 485 EKLTGVVQRKGSVAYVSQQAWIQNCILQVNILFGSIMKKEFYEQVLEACALLPDLEQLPKGDQTEIGERGVNISGGQQHR 564
Cdd:PTZ00243 711 EISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKAR 790
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 565 VSLARAVYSGADIYLLDDPLSAVDVHVGKQLFEKVIgsLGLLKNKTRILVTHNLTLLPQMDLIVVMESGRIAQMGTYQEL 644
Cdd:PTZ00243 791 VSLARAVYANRDVYLLDDPLSALDAHVGERVVEECF--LGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADF 868
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 645 LSktrnlTNLHQVISEEEKAHALKRASAVNSR-----------TRPKDKILEQKPRPSLDQGKQLS------MKKEKIPV 707
Cdd:PTZ00243 869 MR-----TSLYATLAAELKENKDSKEGDADAEvaevdaapggaVDHEPPVAKQEGNAEGGDGAALDaaagrlMTREEKAS 943
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 708 GGVKFSIILQYLQAFGWLWVWLTMV-TYLGQNLVGIGQNLWLSAWAKEAKNMNDFTEwkqirsnkLNIY---GILGLIKG 783
Cdd:PTZ00243 944 GSVPWSTYVAYLRFCGGLHAAGFVLaTFAVTELVTVSSGVWLSMWSTRSFKLSAATY--------LYVYlgiVLLGTFSV 1015
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 784 LFVCSGAYVITRgslAASRTMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDMRLHY-YLRLwVNCTLDVIGTIL 862
Cdd:PTZ00243 1016 PLRFFLSYEAMR---RGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMsYLYL-LQCLFSICSSIL 1091
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 863 VIIGALPLFILGIIPSVFFYFSIQRYYVASSRQIRRLTGASRSPVISHFSETLSGVSTIRAFGHQQRFIQQYKEVVNENL 942
Cdd:PTZ00243 1092 VTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVVY 1171
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 943 VCFYNNVISNRWLSVRLEFLGNLMVLFAA----LLAVLAGNSIDSATVGLSISYALNITHSLNFWVKKACEIETNAVAVE 1018
Cdd:PTZ00243 1172 SCSYLENVANRWLGVRVEFLSNIVVTVIAligvIGTMLRATSQEIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVE 1251
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1019 RVCEY-ENMDKEA-PWI------MSRR-----------------PPLQWPN---KGVVEFINYQARYRDELGLALQDITF 1070
Cdd:PTZ00243 1252 RLLYYtDEVPHEDmPELdeevdaLERRtgmaadvtgtvviepasPTSAAPHpvqAGSLVFEGVQMRYREGLPLVLRGVSF 1331
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1071 QTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKLNIIPQHPVLFSGTLQMNLDPLNKYS 1150
Cdd:PTZ00243 1332 RIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEAS 1411
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1151 DSKLWEALELCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRKTKILIL-DEATASIDFETDKLVQTTIRK 1229
Cdd:PTZ00243 1412 SAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMS 1491
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|.
gi 74136409 1230 EFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQNLI-RQKGLFYEM 1279
Cdd:PTZ00243 1492 AFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVmNRQSIFHSM 1542
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-1276 |
1.34e-157 |
|
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: 512.15 E-value: 1.34e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 25 SPEKSASFFSKVTYSWFSRVITLGYKRPLEREDLFELNESDSSYTVCPTFEKQWRKEVLRNQerqkvkasfyieahtKKP 104
Cdd:TIGR01271 4 SPVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASAK---------------KNP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 105 SLLYALWNTFKSVLIQVALFKVFADILSFTSPLIMKQMII-FCEHSSDFGWNGYGYAMALFVVVFLQTLILQRYQCFNML 183
Cdd:TIGR01271 69 KLLNALRRCFFWRFVFYGILLYFGEATKAVQPLLLGRIIAsYDPFNAPEREIAYYLALGLCLLFIVRTLLLHPAIFGLHH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 184 TSAKVKTAVNGLIYKKALLLSNVSRQKFSTGEIINLMSADAQQLMDLTANLNLLWSAPFQILMAIYLLWQELGPAVLAGV 263
Cdd:TIGR01271 149 LGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 264 AVLVFVIPINALAATKIKKLKKSQRKNKDKQIKLLKEILHGIKILKLYAWEPSYKNKIIKIRDQELEFQKSARYLTVFSM 343
Cdd:TIGR01271 229 GFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 344 LTLTCIPFLVSLATLCVYFLLdEGNILTatKVFTSMSLFNILRIPLF-ELPTVISTVVQTKISLGRLEDFLHTEE--LLP 420
Cdd:TIGR01271 309 SAFFFSGFFVVFLSVVPYALI-KGIILR--RIFTTISYCIVLRMTVTrQFPGAIQTWYDSLGAITKIQDFLCKEEykTLE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 421 QNIETNyigdhAIEFTDATYSW-----------------NKT---------------GMPVLKDLNIKIPEGALVAVVGQ 468
Cdd:TIGR01271 386 YNLTTT-----EVEMVNVTASWdegigelfekikqnnkaRKQpngddglffsnfslyVTPVLKNISFKLEKGQLLAVAGS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 469 VGSGKSSMLSAILGEMEKLTGVVQRKGSVAYVSQQAWIQNCILQVNILFGSIMKKEFYEQVLEACALLPDLEQLPKGDQT 548
Cdd:TIGR01271 461 TGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKT 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 549 EIGERGVNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGKQLFEKVIGSLglLKNKTRILVTHNLTLLPQMDLIV 628
Cdd:TIGR01271 541 VLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKL--MSNKTRILVTSKLEHLKKADKIL 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 629 VMESGRIAQMGTYQELLSKTRNLTNL---------------HQVISEEEKAHALKRASAVNSRTRPKDKILEQKPRPSLD 693
Cdd:TIGR01271 619 LLHEGVCYFYGTFSELQAKRPDFSSLllgleafdnfsaerrNSILTETLRRVSIDGDSTVFSGPETIKQSFKQPPPEFAE 698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 694 QGKQLSMKKEKIPVGgvKFSII---LQYLQAFGW---------------------------LWVWLTMVTYLGQN----- 738
Cdd:TIGR01271 699 KRKQSIILNPIASAR--KFSFVqmgPQKAQATTIedavrepserkfslvpedeqgeeslprGNQYHHGLQHQAQRrqsvl 776
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 739 -----------------------LVGIGQNLWLS----------------------------AWAKEAKNMNDFTEW--- 764
Cdd:TIGR01271 777 qlmthsnrgenrreqlqtsfrkkSSITQQNELASeldiysrrlskdsvyeiseeineedlkeCFADERENVFETTTWnty 856
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 765 -KQIRSNKLNIYGIL-----------GLIKGLFVCSG----------------------AYVITRGS------------- 797
Cdd:TIGR01271 857 lRYITTNRNLVFVLIfclviflaevaASLLGLWLITDnpsapnyvdqqhanasspdvqkPVIITPTSayyifyiyvgtad 936
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 798 -----------------LAASRTMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDMRLHYYLRLWVNCTLDVIGT 860
Cdd:TIGR01271 937 svlalgffrglplvhtlLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGA 1016
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 861 ILVIIGALPLFILGIIPSVFFYFSIQRYYVASSRQIRRLTGASRSPVISHFSETLSGVSTIRAFGHQQRFIQQYKEVVNE 940
Cdd:TIGR01271 1017 IFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNL 1096
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 941 NLVCFYNNVISNRWLSVRLEFLGNLMVLFAALLAVLAgNSIDSATVGLSISYALNITHSLNFWVKKACEIETNAVAVERV 1020
Cdd:TIGR01271 1097 HTANWFLYLSTLRWFQMRIDIIFVFFFIAVTFIAIGT-NQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRV 1175
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1021 CEYENMDKEAPWIMSRRPPLQ---------------WPNKGVVEFINYQARYRDELGLALQDITFQTHGEEKIGIVGRTG 1085
Cdd:TIGR01271 1176 FKFIDLPQEEPRPSGGGGKYQlstvlvienphaqkcWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTG 1255
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1086 AGKSTLSNCLFRIVERAGGKIIIDGIDIStIGLHDLRGKLNIIPQHPVLFSGTLQMNLDPLNKYSDSKLWEALELCHLKE 1165
Cdd:TIGR01271 1256 SGKSTLLSALLRLLSTEGEIQIDGVSWNS-VTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKS 1334
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1166 FVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTIRKEFSDCTILTIAHRLQS 1245
Cdd:TIGR01271 1335 VIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEA 1414
|
1450 1460 1470
....*....|....*....|....*....|.
gi 74136409 1246 IIDSDRVLVLDSGSIVEFEAPQNLIRQKGLF 1276
Cdd:TIGR01271 1415 LLECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
122-409 |
3.62e-138 |
|
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: 422.65 E-value: 3.62e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 122 ALFKVFADILSFTSPLIMKQMIIFCEHSSDFGWNGYGYAMALFVVVFLQTLILQRYQCFNMLTSAKVKTAVNGLIYKKAL 201
Cdd:cd18595 3 ALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 202 LLSNVSRQKFSTGEIINLMSADAQQLMDLTANLNLLWSAPFQILMAIYLLWQELGPAVLAGVAVLVFVIPINALAATKIK 281
Cdd:cd18595 83 RLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 282 KLKKSQRKNKDKQIKLLKEILHGIKILKLYAWEPSYKNKIIKIRDQELEFQKSARYLTVFSMLTLTCIPFLVSLATLCVY 361
Cdd:cd18595 163 KLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFATY 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 74136409 362 FLLDEGNILTATKVFTSMSLFNILRIPLFELPTVISTVVQTKISLGRL 409
Cdd:cd18595 243 VLSDPDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
727-1023 |
4.14e-128 |
|
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: 396.08 E-value: 4.14e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 727 VWLTMVTYLGQNLVGIGQNLWLSAWAKEakNMNDFTEWKQIRSNKLNIYGILGLIKGLFVCSGAYVITRGSLAASRTMYV 806
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDD--PALNGTQDTEQRDYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 807 QLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDMRLHYYLRLWVNCTLDVIGTILVIIGALPLFILGIIPSVFFYFSIQ 886
Cdd:cd18603 79 KLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 887 RYYVASSRQIRRLTGASRSPVISHFSETLSGVSTIRAFGHQQRFIQQYKEVVNENLVCFYNNVISNRWLSVRLEFLGNLM 966
Cdd:cd18603 159 RFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLI 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 74136409 967 VLFAALLAVLAGNSIDSATVGLSISYALNITHSLNFWVKKACEIETNAVAVERVCEY 1023
Cdd:cd18603 239 VLFAALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEY 295
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1046-1266 |
1.54e-117 |
|
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: 364.89 E-value: 1.54e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1046 GVVEFINYQARYRDELGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKL 1125
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1126 NIIPQHPVLFSGTLQMNLDPLNKYSDSKLWEALELCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRKTKI 1205
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74136409 1206 LILDEATASIDFETDKLVQTTIRKEFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAP 1266
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
433-634 |
1.45e-107 |
|
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: 337.52 E-value: 1.45e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNKTGM---PVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSVAYVSQQAWIQNC 509
Cdd:cd03250 1 ISVEDASFTWDSGEQetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 510 ILQVNILFGSIMKKEFYEQVLEACALLPDLEQLPKGDQTEIGERGVNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDV 589
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 74136409 590 HVGKQLFEKVIGSLgLLKNKTRILVTHNLTLLPQMDLIVVMESGR 634
Cdd:cd03250 161 HVGRHIFENCILGL-LLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
121-409 |
3.03e-100 |
|
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: 320.97 E-value: 3.03e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 121 VALFKVFADILSFTSPLIMKQMIIFCEHSSDFG-WNGYGYAMALFVVVFLQTLILQRYQCFNMLTSAKVKTAVNGLIYKK 199
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPlSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 200 ALLLSNVSRQKFSTGEIINLMSADAQQLMDLTANLNLLWSAPFQILMAIYLLWQELGPAVLAGVAVLVFVIPINALAATK 279
Cdd:cd18579 82 ALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 280 IKKLKKSQRKNKDKQIKLLKEILHGIKILKLYAWEPSYKNKIIKIRDQELEFQKSARYLTVFSMLTLTCIPFLVSLATLC 359
Cdd:cd18579 162 ISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 74136409 360 VYFLLdeGNILTATKVFTSMSLFNILRIPLFELPTVISTVVQTKISLGRL 409
Cdd:cd18579 242 TYVLL--GNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
774-1279 |
1.11e-91 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 307.86 E-value: 1.11e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 774 IYGILGLIKGLFVCSGAYVITRGSLAASRTMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDMRLHYYLRLWVNC 853
Cdd:COG1132 66 LLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRS 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 854 TLDVIGTILVIIGA---LPLFILGIIP-SVFFYFSIQRYYVASSRQIRRLTGAsrspVISHFSETLSGVSTIRAFGHQQR 929
Cdd:COG1132 146 VVTLIGALVVLFVIdwrLALIVLLVLPlLLLVLRLFGRRLRKLFRRVQEALAE----LNGRLQESLSGIRVVKAFGREER 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 930 FIQQYKEVVNENLVCFYNNVISNRWLSVRLEFLGNLMVLFAALL--AVLAGNSIDSATVGLSISYALNITHSL----NFW 1003
Cdd:COG1132 222 ELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVggLLVLSGSLTVGDLVAFILYLLRLFGPLrqlaNVL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1004 VkkacEIETNAVAVERVCEYENMDKEAPWIMSRRPPLqwPNKGVVEFINYQARYRDElGLALQDITFQTHGEEKIGIVGR 1083
Cdd:COG1132 302 N----QLQRALASAERIFELLDEPPEIPDPPGAVPLP--PVRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGP 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1084 TGAGKSTLSNCLFRIVE-------------RaggkiiidgidisTIGLHDLRGKLNIIPQHPVLFSGTLQMNL---DPln 1147
Cdd:COG1132 375 SGSGKSTLVNLLLRFYDptsgrilidgvdiR-------------DLTLESLRRQIGVVPQDTFLFSGTIRENIrygRP-- 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1148 KYSDSKLWEALELCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTI 1227
Cdd:COG1132 440 DATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEAL 519
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 74136409 1228 RKEFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQNLIRQKGLFYEM 1279
Cdd:COG1132 520 ERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARL 571
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1042-1266 |
2.86e-88 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 284.69 E-value: 2.86e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1042 WPNKGVVEFINYQARYRDELGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDL 1121
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1122 RGKLNIIPQHPVLFSGTLQMNLDPLNKYSDSKLWEALelchlkefvqslpeklrhEISEGGENLSMGQRQLVCLARALLR 1201
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74136409 1202 KTKILILDEATASIDFETDKLVQTTIRKEFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAP 1266
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
727-1023 |
3.07e-86 |
|
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: 282.47 E-value: 3.07e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 727 VWLTMVTYLGQNLVGIGQNLWLSAWAKEAKNMNDFTEWKQIrsnkLNIYGILGLIKGLFVCSGAYVITRGSLAASRTMYV 806
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYL----GVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 807 QLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDMRLHYYLRLWVNCTLDVIGTILVIIGALPLFILGIIPSVFFYFSIQ 886
Cdd:cd18580 77 KLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 887 RYYVASSRQIRRLTGASRSPVISHFSETLSGVSTIRAFGHQQRFIQQYKEVVNENLVCFYNNVISNRWLSVRLEFLGNLM 966
Cdd:cd18580 157 RYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 74136409 967 VLFAALLAVLAGNSIDSATVGLSISYALNITHSLNFWVKKACEIETNAVAVERVCEY 1023
Cdd:cd18580 237 ALVVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEY 293
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
123-409 |
3.01e-82 |
|
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: 271.25 E-value: 3.01e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 123 LFKVFADILSFTSPLIMKQMIIFCEHSSDFG-----WNGYGYAMALFVVVFLQTLILQRYQCFNMLTSAKVKTAVNGLIY 197
Cdd:cd18597 4 LLKLLADVLQVLSPLLLKYLINFVEDAYLGGpppsiGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTKAIY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 198 KKALLLSNVSRQKFSTGEIINLMSADAQQLMDLTANLNLLWSAPFQILMAIYLLWQELGPAVLAGVAVLVFVIPINALAA 277
Cdd:cd18597 84 RKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGFLM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 278 TKIKKLKKSQRKNKDKQIKLLKEILHGIKILKLYAWEPSYKNKIIKIRDQELEFQKSARYLTVFSMLTLTCIPFLVSLAT 357
Cdd:cd18597 164 KKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLASMLS 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 74136409 358 LCVYFLLdeGNILTATKVFTSMSLFNILRIPLFELPTVISTVVQTKISLGRL 409
Cdd:cd18597 244 FITYYAT--GHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
726-1023 |
3.03e-77 |
|
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: 257.40 E-value: 3.03e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 726 WVwLTMVTYLGQNLVGIGQNLWLSAWAKEAKNMNDFTEWKQIRSNKLNIYGILGLIKGLFVCSGAYVITRGSLAASRTMY 805
Cdd:cd18604 1 WA-LLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEVSVLYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 806 VQLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDMRLHYYLRLWVNCTLDVIGTILVIIGALPLFILGIIPSVFFYFSI 885
Cdd:cd18604 80 ERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 886 QRYYVASSRQIRRLTGASRSPVISHFSETLSGVSTIRAFGHQQRFIQQYKEVVNENLVCFYNNVISNRWLSVRLEFLGNL 965
Cdd:cd18604 160 GRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGAL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 966 MvLFAALLAVLAGNSIDSATVGLSISYALNITHSLNFWVKKACEIETNAVAVERVCEY 1023
Cdd:cd18604 240 F-SFATAALLVYGPGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEY 296
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
122-409 |
3.86e-76 |
|
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: 254.01 E-value: 3.86e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 122 ALFKVFADILSFTSPLIMKQMIIFCEHSSDFGWNGYGYAMALFVVVFLQTLILQRYQCFNMLTSAKVKTAVNGLIYKKAL 201
Cdd:cd18598 3 GLLKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYRKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 202 LLSNVSRQKFSTGEIINLMSADAQQLMDLTANLNLLWSAPFQILMAIYLLWQELGPAVLAGVAVLVFVIPINALAATKIK 281
Cdd:cd18598 83 RVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 282 KLKKSQRKNKDKQIKLLKEILHGIKILKLYAWEPSYKNKIIKIRDQELEFQKSARYLTVFSMLTLTCIPFLVSLATLCVY 361
Cdd:cd18598 163 ALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTPVLISILTFATY 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 74136409 362 FLLdeGNILTATKVFTSMSLFNILRIPLFELPTVISTVVQTKISLGRL 409
Cdd:cd18598 243 VLM--GNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
742-1023 |
1.14e-72 |
|
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: 244.31 E-value: 1.14e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 742 IGQNLWLSAWakeaknmndfTEWKQIRSNK--LNIYGILGLIKGLFVCSGAYVITRGSLAASRTMYVQLLNNVLHLPIQF 819
Cdd:cd18606 16 VFTNLWLSFW----------TEDFFGLSQGfyIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 820 FETNSTGQIISRFTKDIFIIDMRLHYYLRLWVNCTLDVIGTILVIIGALPLFILGIIPSVFFYFSIQRYYVASSRQIRRL 899
Cdd:cd18606 86 FDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRASSRELKRL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 900 TGASRSPVISHFSETLSGVSTIRAFGHQQRFIQQYKEVVNENLVCFYNNVISNRWLSVRLEFLGNLMVLFAALLAVLAGN 979
Cdd:cd18606 166 ESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLLVLIVALLCVTRRF 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 74136409 980 SIDSATVGLSISYALNITHSLNFWVKKACEIETNAVAVERVCEY 1023
Cdd:cd18606 246 SISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHY 289
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
122-409 |
4.38e-71 |
|
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: 240.47 E-value: 4.38e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 122 ALFKVFADILSFTSPLIMKQMIIFCEH-SSDFGWNGYGYAMALFVVVFLQTLILQRYQCFNMLTSAKVKTAVNGLIYKKA 200
Cdd:cd18596 3 ALLAVLSSVLSFAPPFFLNRLLRYLEDpGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 201 LLLSNVS-------------------RQKFSTGEIINLMSADAQQLMDLTANLNLLWSAPFQILMAIYLLWQELGPAVLA 261
Cdd:cd18596 83 LRRRDKSgssksseskkkdkeededeKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 262 GVAVLVFVIPINALAATKIKKLKKSQRKNKDKQIKLLKEILHGIKILKLYAWEPSYKNKIIKIRDQELEFQKSARYLTVF 341
Cdd:cd18596 163 GLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 342 SMLTLTCIPFLVSLATLCVYFLLdEGNILTATKVFTSMSLFNILRIPLFELPTVISTVVQTKISLGRL 409
Cdd:cd18596 243 LSLLWFLIPILVTVVTFATYTLV-MGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
746-1023 |
5.73e-71 |
|
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: 239.74 E-value: 5.73e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 746 LWLSAWAKeaKNMNDFTEWKQIRSNK-LNIYGILGLIKGLFVCSGAYVITRGSLAASRTMYVQLLNNVLHLPIQFFETNS 824
Cdd:cd18605 20 FWLSYWVS--HSNNSFFNFINDSFNFfLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKTP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 825 TGQIISRFTKDIFIIDMRLHYYLRLWVNCTLDVIGTILVIIGALPLFILGIIPSVFFYFSIQRYYVASSRQIRRLTGASR 904
Cdd:cd18605 98 VGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQRYYRATSRELKRLNSVNL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 905 SPVISHFSETLSGVSTIRAFGHQQRFIQQYKEVVNENLVCFYNNVISNRWLSVRLEFLGNLMVL---FAALLAVLAGNSI 981
Cdd:cd18605 178 SPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVLIVTfvaLTAVVQHFFGLSI 257
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 74136409 982 DSATVGLSISYALNITHSLNFWVKKACEIETNAVAVERVCEY 1023
Cdd:cd18605 258 DAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQY 299
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
729-1023 |
1.17e-70 |
|
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: 239.04 E-value: 1.17e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 729 LTMVTYLGQNLVGIGQNLWLSAW-------AKEAKNMNDFTEWKQIRSNKLNIYGILGL--IKGLFVCSGAYVITrgSLA 799
Cdd:cd18602 3 LVLALALLKQGLRVATDFWLADWteanhdvASVVFNITSSSLEDDEVSYYISVYAGLSLgaVILSLVTNLAGELA--GLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 800 ASRTMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDMRLHYYLRLWVNCTLDVIGTILVIIGALPLFILGIIPSV 879
Cdd:cd18602 81 AARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 880 FFYFSIQRYYVASSRQIRRLTGASRSPVISHFSETLSGVSTIRAFGHQQRFIQQYKEVVNENLVCFYNNVISNRWLSVRL 959
Cdd:cd18602 161 IVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74136409 960 EFLGNLMVLFAALLAVLAG--NSIDSATVGLSISYALNITHSLNFWVKKACEIETNAVAVERVCEY 1023
Cdd:cd18602 241 DYLGAVIVFLAALSSLTAAlaGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEY 306
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
107-647 |
2.60e-69 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 244.30 E-value: 2.60e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 107 LYALWNTFKSVLIQVALFKVFADILSFTSPLIMKQMIIFCEHSSDFGwNGYGYAMALFVVVFLQTLI--LQRYqcFNMLT 184
Cdd:COG1132 12 LLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLS-ALLLLLLLLLGLALLRALLsyLQRY--LLARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 185 SAKVKTAVNGLIYKKALLLSNVSRQKFSTGEIINLMSADAQQLMDLTAN-LNLLWSAPFQILMAIYLL----WQeLGPAV 259
Cdd:COG1132 89 AQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHgLPQLVRSVVTLIGALVVLfvidWR-LALIV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 260 LAGVAVLVFVIpinALAATKIKKLKKSQRKNKDKQIKLLKEILHGIKILKLYAWEPSYKNKIIKIRDQELEFQ-KSARYL 338
Cdd:COG1132 168 LLVLPLLLLVL---RLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANlRAARLS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 339 TVFSMLTLtcipFLVSLATLCVY----FLLDEGNIlTATKVFTSMSLFNILRIPLFELPTVISTVVQTKISLGRLEDFLH 414
Cdd:COG1132 245 ALFFPLME----LLGNLGLALVLlvggLLVLSGSL-TVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 415 TEELLPQNIETNYI--GDHAIEFTDATYSWNKtGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEME------K 486
Cdd:COG1132 320 EPPEIPDPPGAVPLppVRGEIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDptsgriL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 487 LTGVVQRK-------GSVAYVSQQAWI-QNCILQvNILFGsimKKEF-YEQVLEACA---LLPDLEQLPKGDQTEIGERG 554
Cdd:COG1132 399 IDGVDIRDltleslrRQIGVVPQDTFLfSGTIRE-NIRYG---RPDAtDEEVEEAAKaaqAHEFIEALPDGYDTVVGERG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 555 VNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGKQLFEKVigsLGLLKNKTRILVTHNLTLLPQMDLIVVMESGR 634
Cdd:COG1132 475 VNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEAL---ERLMKGRTTIVIAHRLSTIRNADRILVLDDGR 551
|
570
....*....|...
gi 74136409 635 IAQMGTYQELLSK 647
Cdd:COG1132 552 IVEQGTHEELLAR 564
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
776-1279 |
1.48e-68 |
|
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: 245.51 E-value: 1.48e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 776 GILGLIKGLFVCSGAYVITRGSLAASRTMYVQLLNNVLHLPIQFFETNSTGQIISRFtKDI-----FIIDMrlhyylrlw 850
Cdd:COG2274 203 LLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVesireFLTGS--------- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 851 vncTLDVIGTILVIIGALPL-----------FILGIIPSVFFYFSIQRYYVASSRQIRRLtGASRSpviSHFSETLSGVS 919
Cdd:COG2274 273 ---LLTALLDLLFVLIFLIVlffyspplalvVLLLIPLYVLLGLLFQPRLRRLSREESEA-SAKRQ---SLLVETLRGIE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 920 TIRAFGHQQRFIQQYKEVVNENLvcfyNNVISNRWLSVRLEFLGNLMVLFAALLAVLAG------NSIdsaTVGL---SI 990
Cdd:COG2274 346 TIKALGAESRFRRRWENLLAKYL----NARFKLRRLSNLLSTLSGLLQQLATVALLWLGaylvidGQL---TLGQliaFN 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 991 SYALNITHSLNFWVKKACEIETNAVAVERVCEYENMDKEAPwimSRRPPLQWPN-KGVVEFINYQARYRDELGLALQDIT 1069
Cdd:COG2274 419 ILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPERE---EGRSKLSLPRlKGDIELENVSFRYPGDSPPVLDNIS 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1070 FQTHGEEKIGIVGRTGAGKSTLSNCLFRI------------VERAggkiiidgidisTIGLHDLRGKLNIIPQHPVLFSG 1137
Cdd:COG2274 496 LTIKPGERVAIVGRSGSGKSTLLKLLLGLyeptsgrilidgIDLR------------QIDPASLRRQIGVVLQDVFLFSG 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1138 TLQMNL---DPlnKYSDSKLWEALELCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRKTKILILDEATAS 1214
Cdd:COG2274 564 TIRENItlgDP--DATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSA 641
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74136409 1215 IDFETDKLVQTTIRKEFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQNLIRQKGLFYEM 1279
Cdd:COG2274 642 LDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1046-1276 |
4.23e-67 |
|
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: 227.10 E-value: 4.23e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1046 GVVEFINYQARYRDELGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKL 1125
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1126 NIIPQHPVLFSGTLQMNLDPLNKYSDSKLWEALELCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRKTKI 1205
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74136409 1206 LILDEATASIDFETDKLVQTTIRKEFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQNLIRQK-GLF 1276
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVF 249
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
123-409 |
4.55e-66 |
|
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: 225.96 E-value: 4.55e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 123 LFKVFADILSFTSPLIMKQMIIFCEH------------------SSDFGWNGYGYAMALFVVVFLQTLILQRYQCFNMLT 184
Cdd:cd18591 4 ILKLLGDLLGFVGPLCISGIVDYVEEntysssnstdklsvsyvtVEEFFSNGYVLAVILFLALLLQATFSQASYHIVIRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 185 SAKVKTAVNGLIYKKALLLS--NVSRQKFSTGEIINLMSADAQQLMDLTANLNLLWSAPFQILMAIYLLWQELGPAVLAG 262
Cdd:cd18591 84 GIRLKTALQAMIYEKALRLSswNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 263 VAVLVFVIPINALAATKIKKLKKSQRKNKDKQIKLLKEILHGIKILKLYAWEPSYKNKIIKIRDQELEFQKSARYLTVFS 342
Cdd:cd18591 164 AALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWSLM 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74136409 343 MLTLTCIPFLVSLATLCVYFLLdEGNILTATKVFTSMSLFNILRIPLFELPTVISTVVQTKISLGRL 409
Cdd:cd18591 244 TFLTQASPILVTLVTFGLYPYL-EGEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
123-409 |
2.49e-64 |
|
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: 220.55 E-value: 2.49e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 123 LFKVFADILSFTSPLIMKQMIIFCEHSSDFGWNGYGYAMALFVVVFLQTLILQRYQCFNMLTSAKVKTAVNGLIYKKALL 202
Cdd:cd18559 4 LIKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 203 LSNVSRQKFSTGEIINLMSADAQQLMDLTANLNLLWSAPFQILMAIYLLWQELGPAVLAGVAVLVFVIPINALAATKIKK 282
Cdd:cd18559 84 SPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 283 LKKSQRKNKDKQIKLLKEILHGIKILKLYAWEPSYKNKIIKIRDQELEFQKSARYLTVFSMLTLTCIPFLVSLATLCVYF 362
Cdd:cd18559 164 LKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYV 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 74136409 363 LLDEGNILTATKVFTSMSLFNILRIPLFELPTVISTVVQTKISLGRL 409
Cdd:cd18559 244 SRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
74-656 |
2.33e-63 |
|
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: 230.11 E-value: 2.33e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 74 FEKQWRKEVLRnqerqkVKASFYIEAHTKKPSLLYALWNTF---KSVLIQVALFKVFADILSFTSPLIMKQMI--IFCEH 148
Cdd:COG2274 117 FAESWTGVALL------LEPTPEFDKRGEKPFGLRWFLRLLrryRRLLLQVLLASLLINLLALATPLFTQVVIdrVLPNQ 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 149 SSDFGWngyGYAMALFVVVFLQTLI--LQRYqcFNMLTSAKVKTAVNGLIYKKALLLSNVSRQKFSTGEIINLMSaDAQQ 226
Cdd:COG2274 191 DLSTLW---VLAIGLLLALLFEGLLrlLRSY--LLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVES 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 227 LMD-LTAN-LNLLWSAPFQILMAIYLLWqeLGP--AVLAGVAVLVFVIpINALAATKIKKLKKSQRKNKDKQIKLLKEIL 302
Cdd:COG2274 265 IREfLTGSlLTALLDLLFVLIFLIVLFF--YSPplALVVLLLIPLYVL-LGLLFQPRLRRLSREESEASAKRQSLLVETL 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 303 HGIKILKLYAWEPSYKNKIIKIRDQELEFQKSARYLTVFSMLTLTCIPFLVSLATLCV-YFLLDEGNI----LTAtkvft 377
Cdd:COG2274 342 RGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLgAYLVIDGQLtlgqLIA----- 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 378 smslFNILRI----PLFELPTVISTVVQTKISLGRLEDFLHTE---ELLPQNIETNYIGDHaIEFTDATYSWNKTGMPVL 450
Cdd:COG2274 417 ----FNILSGrflaPVAQLIGLLQRFQDAKIALERLDDILDLPperEEGRSKLSLPRLKGD-IELENVSFRYPGDSPPVL 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 451 KDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQ--------------RKgSVAYVSQQAWIQNCILQVNIL 516
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgidlrqidpaslRR-QIGVVLQDVFLFSGTIRENIT 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 517 FGsimKKEF-YEQVLEAC---ALLPDLEQLPKGDQTEIGERGVNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVG 592
Cdd:COG2274 571 LG---DPDAtDEEIIEAArlaGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETE 647
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74136409 593 KQLFEKVigsLGLLKNKTRILVTHNLTLLPQMDLIVVMESGRIAQMGTYQELLSKTRNLTNLHQ 656
Cdd:COG2274 648 AIILENL---RRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
433-633 |
2.86e-62 |
|
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: 211.81 E-value: 2.86e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNkTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVV-----------------QRKG 495
Cdd:cd03290 1 VQVTNGYFSWG-SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 496 SVAYVSQQAWIQNCILQVNILFGSIMKKEFYEQVLEACALLPDLEQLPKGDQTEIGERGVNISGGQQHRVSLARAVYSGA 575
Cdd:cd03290 80 SVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 576 DIYLLDDPLSAVDVHVGKQLFEKviGSLGLLKN--KTRILVTHNLTLLPQMDLIVVMESG 633
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQE--GILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
120-410 |
4.95e-58 |
|
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: 202.48 E-value: 4.95e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 120 QVALFKVFADILSFTSPLIMKQMI-IFCEHSSDFGWNGYGYAMALFVVVFLQTLILQRY----QCFNMltsaKVKTAVNG 194
Cdd:cd18594 1 LLGILLFLEESLKIVQPLLLGRLVaYFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYffglHRYGM----QLRIALSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 195 LIYKKALLLSNVSRQKFSTGEIINLMSADAQQLMDLTANLNLLWSAPFQILMAIYLLWQELGPAVLAGVAVLVFVIPINA 274
Cdd:cd18594 77 LIYKKTLKLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 275 LAATKIKKLKKSQRKNKDKQIKLLKEILHGIKILKLYAWEPSYKNKIIKIRDQELEFQKSARYLTVFSMLTLTCIPFLVS 354
Cdd:cd18594 157 YLGKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVS 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 74136409 355 LATLCVYFLLdeGNILTATKVFTSMSLFNILRIPL-FELPTVISTVVQTKISLGRLE 410
Cdd:cd18594 237 FATFVPYVLT--GNTLTARKVFTVISLLNALRMTItRFFPESIQTLSESRVSLKRIQ 291
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1039-1274 |
7.79e-57 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 207.30 E-value: 7.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1039 PLQWPNKGVVEFINYQARYRDElGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGL 1118
Cdd:COG4988 328 PLPAAGPPSIELEDVSFSYPGG-RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1119 HDLRGKLNIIPQHPVLFSGTLQMNL---DPlnKYSDSKLWEALELCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCL 1195
Cdd:COG4988 407 ASWRRQIAWVPQNPYLFAGTIRENLrlgRP--DASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74136409 1196 ARALLRKTKILILDEATASIDFETDKLVQTTIRKEFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQNLIRQKG 1274
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
723-1023 |
3.02e-56 |
|
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: 197.79 E-value: 3.02e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 723 GWLWVWLTMVTYLGQNLVGIGQNLWLSAWAKE------AKNMNDFTEWKQIRSN-----KLNIYGILGLIKGLFVCSGAY 791
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQgsgnttNNVDNSTVDSGNISDNpdlnfYQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 792 VITRGSLAASRTMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDMRLHYYLRLWVNCTLDVIGTILVIIGALPLF 871
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 872 ILGIIPSVFFYFSIQRYYVASSRQIRRLTGASRSPVISHFSETLSGVSTIRAFGHQQRFIQQYKEVVNENLVCFYNNVIS 951
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74136409 952 NRWLSVRLEFLGNLMVLFAALLAVLAGNSIDSATVGLSISYALNITHSLNFWVKKACEIETNAVAVERVCEY 1023
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEY 312
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1046-1274 |
1.09e-55 |
|
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: 193.21 E-value: 1.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1046 GVVEFINYQARYrDELGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKL 1125
Cdd:cd03254 1 GEIEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1126 NIIPQHPVLFSGTLQMNLDPLNKYSDSKLW-EALELCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRKTK 1204
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEViEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1205 ILILDEATASIDFETDKLVQTTIRKEFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQNLIRQKG 1274
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
180-647 |
3.33e-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: 202.69 E-value: 3.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 180 FNMLTSAKVKtavnglIYKKALLLSNVSRQKFSTGEIINLMSADAQQLMDLTanLNLLwsAPFQILMAIYL--------L 251
Cdd:COG4987 84 LRLLADLRVR------LYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLY--LRVL--LPLLVALLVILaavaflafF 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 252 WQELGPAVLAGVAVLVFVIPINALAATKikklKKSQRKNKDKQ---IKLLkEILHGIKILKLYAWEPSYKNKIIKIRDQE 328
Cdd:COG4987 154 SPALALVLALGLLLAGLLLPLLAARLGR----RAGRRLAAARAalrARLT-DLLQGAAELAAYGALDRALARLDAAEARL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 329 LEFQKSARYLTVFSMLTLTCIPFLVSLATLCV-YFLLDEGNI---LTATKVFTSMSLFNILrIPLfelPTVISTVVQTKI 404
Cdd:COG4987 229 AAAQRRLARLSALAQALLQLAAGLAVVAVLWLaAPLVAAGALsgpLLALLVLAALALFEAL-APL---PAAAQHLGRVRA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 405 SLGRLEDFLHTEELLPQNIETNYI-GDHAIEFTDATYSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGE 483
Cdd:COG4987 305 AARRLNELLDAPPAVTEPAEPAPApGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRF 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 484 MEKLTGVV-------------QRKGSVAYVSQQAWIQNCILQVNILFGSIMKKEfyEQVLEACA---LLPDLEQLPKGDQ 547
Cdd:COG4987 385 LDPQSGSItlggvdlrdldedDLRRRIAVVPQRPHLFDTTLRENLRLARPDATD--EELWAALErvgLGDWLAALPDGLD 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 548 TEIGERGVNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGKQLFEKVigsLGLLKNKTRILVTHNLTLLPQMDLI 627
Cdd:COG4987 463 TWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADL---LEALAGRTVLLITHRLAGLERMDRI 539
|
490 500
....*....|....*....|
gi 74136409 628 VVMESGRIAQMGTYQELLSK 647
Cdd:COG4987 540 LVLEDGRIVEQGTHEELLAQ 559
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
777-1276 |
7.07e-54 |
|
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: 198.79 E-value: 7.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 777 ILGLIKGLFVCSGAYVITRGSLAASRTMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDIfiiDMRLHY---YLRLWVNC 853
Cdd:TIGR02203 62 GLAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDS---EQVASAatdAFIVLVRE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 854 TLDVIGTILVII---GALPLFILGIIPSVFFyfsIQRYYVASSRQIRRLTGASRSPVISHFSETLSGVSTIRAFGHQQRF 930
Cdd:TIGR02203 139 TLTVIGLFIVLLyysWQLTLIVVVMLPVLSI---LMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 931 IQQYKEVVNENLVCFYNNVISNRWLSVRLEFLGNLMVLFAALLAVLAGNSiDSATVGLSISY---ALNITHSLNFWVKKA 1007
Cdd:TIGR02203 216 TRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQA-GSLTAGDFTAFitaMIALIRPLKSLTNVN 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1008 CEIETNAVAVERVCEYenMDKEAPWIMSRRPPLQwpNKGVVEFINYQARYRDELGLALQDITFQTHGEEKIGIVGRTGAG 1087
Cdd:TIGR02203 295 APMQRGLAAAESLFTL--LDSPPEKDTGTRAIER--ARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSG 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1088 KSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKLNIIPQHPVLFSGTLQMNL--DPLNKYSDSKLWEALELCHLKE 1165
Cdd:TIGR02203 371 KSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIayGRTEQADRAEIERALAAAYAQD 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1166 FVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTIRKEFSDCTILTIAHRLQS 1245
Cdd:TIGR02203 451 FVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLST 530
|
490 500 510
....*....|....*....|....*....|.
gi 74136409 1246 IIDSDRVLVLDSGSIVEFEAPQNLIRQKGLF 1276
Cdd:TIGR02203 531 IEKADRIVVMDDGRIVERGTHNELLARNGLY 561
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
446-646 |
9.25e-51 |
|
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: 181.21 E-value: 9.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 446 GMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSVAYVSQQAWIQNCILQVNILFGSIMKKEF 525
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 526 YEQVLEACALLPDLEQLPKGDQTEIGERGVNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGKQLFEKVIGSlgL 605
Cdd:cd03291 129 YKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCK--L 206
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 74136409 606 LKNKTRILVTHNLTLLPQMDLIVVMESGRIAQMGTYQELLS 646
Cdd:cd03291 207 MANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQS 247
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
147-409 |
1.13e-50 |
|
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: 181.26 E-value: 1.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 147 EHSSDFGWNGYGYAMALFVVVFLQTLILQRYqCFNML-TSAKVKTAVNGLIYKKALLLSNVSRQKFSTGEIINLMSADAQ 225
Cdd:cd18593 30 NGSSISLTEAYLYAGGVSLCSFLFIITHHPY-FFGMQrIGMRLRVACSSLIYRKALRLSQAALGKTTVGQIVNLLSNDVN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 226 QLMDLTANLNLLWSAPFQILMAIYLLWQELGPAVLAGVAVLVFVIPINALAATKIKKLKKSQRKNKDKQIKLLKEILHGI 305
Cdd:cd18593 109 RFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFGKLFSKLRRKTAARTDKRIRIMNEIINGI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 306 KILKLYAWEPSYKNKIIKIRDQELEFQKSARYLTVFSMLTLTCIPFLVSLATLCVYFLLdeGNILTATKVFTSMSLFNIL 385
Cdd:cd18593 189 RVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLTFLAYILL--GNILTAERVFVTMALYNAV 266
|
250 260
....*....|....*....|....*.
gi 74136409 386 RIP--LFeLPTVISTVVQTKISLGRL 409
Cdd:cd18593 267 RLTmtLF-FPFAIQFGSELSVSIRRI 291
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
806-1279 |
1.55e-50 |
|
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: 188.82 E-value: 1.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 806 VQLLNNVLHLPIQFFETNSTGQIISRFTKDIfiiDMRLHYYLRLWVNCTLDVIGTILVIIG------------ALPLFIL 873
Cdd:COG4987 92 VRLYRRLEPLAPAGLARLRSGDLLNRLVADV---DALDNLYLRVLLPLLVALLVILAAVAFlaffspalalvlALGLLLA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 874 GIIPSVFFYfsiqRYYVASSRQIRRLTGASRSpvisHFSETLSGVSTIRAFGHQQRFIQQYKEvvnenlvcfynnvISNR 953
Cdd:COG4987 169 GLLLPLLAA----RLGRRAGRRLAAARAALRA----RLTDLLQGAAELAAYGALDRALARLDA-------------AEAR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 954 WLSV--RLEFLGNLmvlfaallavlaGNSIDSATVGLS------ISYALNITHSLN-----------------------F 1002
Cdd:COG4987 228 LAAAqrRLARLSAL------------AQALLQLAAGLAvvavlwLAAPLVAAGALSgpllallvlaalalfealaplpaA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1003 WVkkacEIETNAVAVERVCEYENmdkEAPWIMSRRPPLQWPNKGVVEFINYQARYRDELGLALQDITFQTHGEEKIGIVG 1082
Cdd:COG4987 296 AQ----HLGRVRAAARRLNELLD---APPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVG 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1083 RTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKLNIIPQHPVLFSGTLQMNL---DPlnKYSDSKLWEALE 1159
Cdd:COG4987 369 PSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLrlaRP--DATDEELWAALE 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1160 LCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTIRKEFSDCTILTI 1239
Cdd:COG4987 447 RVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLI 526
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 74136409 1240 AHRLQSIIDSDRVLVLDSGSIVEFEAPQNLIRQKGLFYEM 1279
Cdd:COG4987 527 THRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
809-1279 |
6.57e-50 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 187.62 E-value: 6.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 809 LNNVLHLPIQFFETNSTGQIISRFTKDIFIIDmrlhyylRLWVNctldVIGTIL---VIIGAL--PLFILG--------- 874
Cdd:PRK10790 105 MDAALRQPLSAFDTQPVGQLISRVTNDTEVIR-------DLYVT----VVATVLrsaALIGAMlvAMFSLDwrmalvaim 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 875 IIPSVFFYFSI-QRYYVASSRQIRrltgASRSPVISHFSETLSGVSTIRAFGHQQRFIQQYKEVVNENLVCfynnvisnR 953
Cdd:PRK10790 174 IFPAVLVVMVIyQRYSTPIVRRVR----AYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMA--------R 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 954 WLSVRLE-FL--------------GNLMVLfaallavlaGNSiDSATVGLSISYA-LNITHSLNfwvKKACEIETN---- 1013
Cdd:PRK10790 242 MQTLRLDgFLlrpllslfsalilcGLLMLF---------GFS-ASGTIEVGVLYAfISYLGRLN---EPLIELTTQqsml 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1014 ---AVAVERVceYENMDKEAPWIMSRRPPLQwpnKGVVEFINYQARYRDElGLALQDITFQTHGEEKIGIVGRTGAGKST 1090
Cdd:PRK10790 309 qqaVVAGERV--FELMDGPRQQYGNDDRPLQ---SGRIDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKST 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1091 LSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKLNIIPQHPVLFSGTLQMNLDPLNKYSDSKLWEALELCHLKEFVQSL 1170
Cdd:PRK10790 383 LASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSL 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1171 PEKLRHEISEGGENLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTIRKEFSDCTILTIAHRLQSIIDSD 1250
Cdd:PRK10790 463 PDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEAD 542
|
490 500
....*....|....*....|....*....
gi 74136409 1251 RVLVLDSGSIVEFEAPQNLIRQKGLFYEM 1279
Cdd:PRK10790 543 TILVLHRGQAVEQGTHQQLLAAQGRYWQM 571
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1048-1279 |
3.09e-49 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 174.73 E-value: 3.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1048 VEFINYQARYRDELGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKLNI 1127
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1128 IPQHPVLFSGTLQMNLdplnKY-----SDSKLWEALELCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRK 1202
Cdd:cd03251 81 VSQDVFLFNDTVAENI----AYgrpgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74136409 1203 TKILILDEATASIDFETDKLVQTTIRKEFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQNLIRQKGLFYEM 1279
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
725-1023 |
7.83e-49 |
|
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: 176.74 E-value: 7.83e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 725 LWVWLTMvtylGQNLVGIGQNLWLSAWAKEAKNMNDFTEWKQI----------RSNKLNIYGILGLIKGLFVCSGAYVIT 794
Cdd:cd18601 7 LLVLLNI----AAQVLYVLSDWWLSYWANLEEKLNDTTDRVQGenstnvdiedLDRDFNLGIYAGLTAATFVFGFLRSLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 795 --RGSLAASRTMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDMRLHYYLRLWVNCTLDVIGTILVIIGALPLFI 872
Cdd:cd18601 83 ffHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPWVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 873 LGIIPSVFFYFSIQRYYVASSRQIRRLTGASRSPVISHFSETLSGVSTIRAFGHQQRFIQQYKEVVNENLVCFYNNVISN 952
Cdd:cd18601 163 IPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLATS 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74136409 953 RWLSVRLEFLGNLMVLFAALLAVLAGNSIDSATVGLSISYALNITHSLNFWVKKACEIETNAVAVERVCEY 1023
Cdd:cd18601 243 RWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEY 313
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
99-647 |
1.32e-47 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 179.95 E-value: 1.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 99 AHTKKPSLLYALWNTFKSVLIqVALFKVFADILSftsPLIMKQMiifceHSSDFGWngygYAMALFVVVFLQTLI--LQR 176
Cdd:COG4988 13 RGARRWLALAVLLGLLSGLLI-IAQAWLLASLLA---GLIIGGA-----PLSALLP----LLGLLLAVLLLRALLawLRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 177 YQCFNMltSAKVKTAVNGLIYKKALLLSNVSRQKFSTGEIINLMSADAQQLmdltanlnllwsapfQILMAIYL--LWQe 254
Cdd:COG4988 80 RAAFRA--AARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEAL---------------DGYFARYLpqLFL- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 255 lgpAVLAGVAVLVFVIPINALAAtkikkL-----------------KKSQRKNkDKQIKLLK-------EILHGIKILKL 310
Cdd:COG4988 142 ---AALVPLLILVAVFPLDWLSG-----LillvtapliplfmilvgKGAAKAS-RRQWRALArlsghflDRLRGLTTLKL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 311 YAWEPSYKNKIIKIRDqelEFQKSaryltvfSMLTLTcIPFLVS-----LATLC-----VYF---LLDegniltatkvfT 377
Cdd:COG4988 213 FGRAKAEAERIAEASE---DFRKR-------TMKVLR-VAFLSSavlefFASLSialvaVYIgfrLLG-----------G 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 378 SMSLFNILRI----PLFELPTvistvvqtkISLG--------------RLEDFLHTEE--LLPQNIETNYIGDHAIEFTD 437
Cdd:COG4988 271 SLTLFAALFVlllaPEFFLPL---------RDLGsfyharangiaaaeKIFALLDAPEpaAPAGTAPLPAAGPPSIELED 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 438 ATYSWNKtGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVV-------------QRKGSVAYVSQQA 504
Cdd:COG4988 342 VSFSYPG-GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingvdlsdldpaSWRRQIAWVPQNP 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 505 WIQNCILQVNILFGS-------ImkkefyEQVLEACALLPDLEQLPKGDQTEIGERGVNISGGQQHRVSLARAVYSGADI 577
Cdd:COG4988 421 YLFAGTIRENLRLGRpdasdeeL------EAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPL 494
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 578 YLLDDPLSAVDVHVGKQLFEKVigsLGLLKNKTRILVTHNLTLLPQMDLIVVMESGRIAQMGTYQELLSK 647
Cdd:COG4988 495 LLLDEPTAHLDAETEAEILQAL---RRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
122-409 |
2.77e-46 |
|
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: 168.12 E-value: 2.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 122 ALFKVFADILSFTSP-LIMKQMIIFCEHSSDFGWNGYGYAMALFVVVFLQTLILQRYQCFNMLTSAKVKTAVNGLIYKKA 200
Cdd:cd18592 3 ILLLLISLIFGFIGPtILIRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYKKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 201 LLLSNVSRQkfSTGEIINLMSADAQQLMDLTANLNLLWSAPFQILM-AIYLLWqELGPAVLAGVAVLVFVIPINALAATK 279
Cdd:cd18592 83 LRLRSLGDK--SVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILgIVYSTY-LLGPWALLGMLVFLLFYPLQAFIAKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 280 IKKLKKSQRKNKDKQIKLLKEILHGIKILKLYAWEPSYKNKIIKIRDQELEFQKSARYLTVFSMLTLTCIPFLVSLATLC 359
Cdd:cd18592 160 TGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 74136409 360 VYFLLdeGNILTATKVFTSMSLFNILRIPLFELPTVISTVVQTKISLGRL 409
Cdd:cd18592 240 AHVAL--GNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1046-1276 |
8.37e-46 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 166.57 E-value: 8.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1046 GVVEFINYQARYRDELGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVErAGGKIIIDGIDISTIGLHDLRGKL 1125
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1126 NIIPQHPVLFSGTLQMNLDPLNKYSDSKLWEALELCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRKTKI 1205
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74136409 1206 LILDEATASIDFETDKLVQTTIRKEFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQNLIRQKGLF 1276
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1048-1279 |
2.94e-45 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 163.56 E-value: 2.94e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1048 VEFINYQARYRDElGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKLNI 1127
Cdd:cd03253 1 IEFENVTFAYDPG-RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1128 IPQHPVLFSGTLQMNLdplnKY-----SDSKLWEALELCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRK 1202
Cdd:cd03253 80 VPQDTVLFNDTIGYNI----RYgrpdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74136409 1203 TKILILDEATASIDFETDKLVQTTIRKEFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQNLIRQKGLFYEM 1279
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1048-1258 |
1.51e-44 |
|
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: 159.09 E-value: 1.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1048 VEFINYQARYRDELGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKLNI 1127
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1128 IPQHPVLFSGTLQMNLdplnkysdsklwealelchlkefvqslpeklrheiseggenLSMGQRQLVCLARALLRKTKILI 1207
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 74136409 1208 LDEATASIDFETDKLVQTTIRKEFSDCTILTIAHRLQSIIDSDRVLVLDSG 1258
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1046-1261 |
2.24e-44 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 160.45 E-value: 2.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1046 GVVEFINYQARYRDELGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKL 1125
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1126 NIIPQHPVLFSGTLQMNL---DPLnkYSDSKLWEALELCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRK 1202
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNItlgAPL--ADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1203 TKILILDEATASIDFETDKLVQTTIRKEFSDCTILTIAHRlQSIID-SDRVLVLDSGSIV 1261
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHR-PSLLDlVDRIIVMDSGRIV 217
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
807-1279 |
1.99e-43 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 169.90 E-value: 1.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 807 QLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDMRLHYYLRLWV-NCTLDVIGTILVIIGALPLFILGII--PSVFFYF 883
Cdd:TIGR00958 239 DLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLrNLVMLLGLLGFMLWLSPRLTMVTLInlPLVFLAE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 884 SI-QRYYVASSRQIRRLTGASRSPVIshfsETLSGVSTIRAFGHQQRFIQQYKEVVNENLVCFYNNVISNRWLSVRLEFL 962
Cdd:TIGR00958 319 KVfGKRYQLLSEELQEAVAKANQVAE----EALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVL 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 963 GNLMVLFAALLAvlaGNSIDSATV--GLSIS---YALNITHSLNFWVKKACEIETNAVAVERVCEYenmdkeapwiMSRR 1037
Cdd:TIGR00958 395 GMLIQVLVLYYG---GQLVLTGKVssGNLVSfllYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEY----------LDRK 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1038 PPLQWPN-------KGVVEFINYQARY--RDELgLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIII 1108
Cdd:TIGR00958 462 PNIPLTGtlaplnlEGLIEFQDVSFSYpnRPDV-PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1109 DGIDISTIGLHDLRGKLNIIPQHPVLFSGTLQMNLD-PLNKYSDSKLWEALELCHLKEFVQSLPEKLRHEISEGGENLSM 1187
Cdd:TIGR00958 541 DGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSG 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1188 GQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTirKEFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQ 1267
Cdd:TIGR00958 621 GQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHK 698
|
490
....*....|..
gi 74136409 1268 NLIRQKGLFYEM 1279
Cdd:TIGR00958 699 QLMEDQGCYKHL 710
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1048-1281 |
3.84e-43 |
|
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: 157.32 E-value: 3.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1048 VEFINYQARY--RDELgLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKL 1125
Cdd:cd03249 1 IEFKNVSFRYpsRPDV-PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1126 NIIPQHPVLFSGTLQMNLdplnKY-----SDSKLWEALELCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLARALL 1200
Cdd:cd03249 80 GLVSQEPVLFDGTIAENI----RYgkpdaTDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1201 RKTKILILDEATASIDFETDKLVQTTIRKEFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQNLIRQKGLFYEMT 1280
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLV 235
|
.
gi 74136409 1281 T 1281
Cdd:cd03249 236 K 236
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1038-1279 |
1.34e-40 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 159.99 E-value: 1.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1038 PPLQwPNKGVVEFINYQARYRDELGLaLQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVE-------------RAgg 1104
Cdd:COG5265 349 PPLV-VGGGEVRFENVSFGYDPERPI-LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDvtsgrilidgqdiRD-- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1105 kiiidgidistIGLHDLRGKLNIIPQHPVLFSGTLQMNLdplnKY-----SDSKLWEALELCHLKEFVQSLPEKLRHEIS 1179
Cdd:COG5265 425 -----------VTQASLRAAIGIVPQDTVLFNDTIAYNI----AYgrpdaSEEEVEAAARAAQIHDFIESLPDGYDTRVG 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1180 EGGENLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTIRKEFSDCTILTIAHRLQSIIDSDRVLVLDSGS 1259
Cdd:COG5265 490 ERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGR 569
|
250 260
....*....|....*....|
gi 74136409 1260 IVEFEAPQNLIRQKGLFYEM 1279
Cdd:COG5265 570 IVERGTHAELLAQGGLYAQM 589
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
433-647 |
1.39e-40 |
|
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: 150.07 E-value: 1.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNkTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSML-----------SAILGEMEKLTGVVQ---RKgSVA 498
Cdd:cd03253 1 IEFENVTFAYD-PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILrllfrfydvssGSILIDGQDIREVTLdslRR-AIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 499 YVSQQAWIQNCILQVNILFGSIMKKEfyEQVLEAC--ALLPD-LEQLPKGDQTEIGERGVNISGGQQHRVSLARAVYSGA 575
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATD--EEVIEAAkaAQIHDkIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74136409 576 DIYLLDDPLSAVDVHVGKQLFEKVIgslGLLKNKTRILVTHNLTLLPQMDLIVVMESGRIAQMGTYQELLSK 647
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALR---DVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAK 225
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1048-1279 |
1.60e-40 |
|
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: 149.94 E-value: 1.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1048 VEFINYQARYRDELGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKLNI 1127
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1128 IPQHPVLFSGTLQMNLDPLNKYSD-SKLWEALELCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRKTKIL 1206
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSmERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74136409 1207 ILDEATASIDFETDKLVQTTIRKEFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQNLIRQKGLFYEM 1279
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
809-1281 |
2.59e-40 |
|
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: 160.29 E-value: 2.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 809 LNNVLHLPIQFFETNSTGQIISRFTKDIFIID----MRLHYYLRLWVnctLDVIGTILVIIGALpLFILGIIpSVFFYFS 884
Cdd:TIGR01193 236 IKHLFELPMSFFSTRRTGEIVSRFTDASSIIDalasTILSLFLDMWI---LVIVGLFLVRQNML-LFLLSLL-SIPVYAV 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 885 IQRYYVASSRQIRRLTGASRSPVISHFSETLSGVSTIRAFGHQQRFIQQ----YKEVVNENLVCFYNNVISNRwLSVRLE 960
Cdd:TIGR01193 311 IIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKidseFGDYLNKSFKYQKADQGQQA-IKAVTK 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 961 FLGNLMVLFAALLAVLAGNsidsATVGLSISYALNITHSLNFW---VKKACEIETNAVAVERVCEYENMDKEapWIMSR- 1036
Cdd:TIGR01193 390 LILNVVILWTGAYLVMRGK----LTLGQLITFNALLSYFLTPLeniINLQPKLQAARVANNRLNEVYLVDSE--FINKKk 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1037 RPPLQWPNKG-VVEFINYQARYRDElglALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDIST 1115
Cdd:TIGR01193 464 RTELNNLNGDiVINDVSYSYGYGSN---ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKD 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1116 IGLHDLRGKLNIIPQHPVLFSGTLQMNLDPLNK--YSDSKLWEALELCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLV 1193
Cdd:TIGR01193 541 IDRHTLRQFINYLPQEPYIFSGSILENLLLGAKenVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRI 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1194 CLARALLRKTKILILDEATASIDFETDKLVQTTIRKeFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQNLIRQK 1273
Cdd:TIGR01193 621 ALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRN 699
|
....*...
gi 74136409 1274 GLFYEMTT 1281
Cdd:TIGR01193 700 GFYASLIH 707
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
433-655 |
1.28e-39 |
|
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: 147.38 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKG-------------SVAY 499
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslrrQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 500 VSQQAWIQNCILQVNILFGSimKKEFYEQVLEAC--ALLPDL-EQLPKGDQTEIGERGVNISGGQQHRVSLARAVYSGAD 576
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGR--PGATREEVEEAAraANAHEFiMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 577 IYLLDDPLSAVDVHVgkqlfEKVI-GSLG-LLKNKTRILVTHNLTLLPQMDLIVVMESGRIAQMGTYQELLSKTRNLTNL 654
Cdd:cd03251 159 ILILDEATSALDTES-----ERLVqAALErLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
.
gi 74136409 655 H 655
Cdd:cd03251 234 H 234
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
777-1255 |
8.27e-38 |
|
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: 150.13 E-value: 8.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 777 ILGLIKGLFVCSGAYVITRGSLAASRTMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDMRLHYYLRLWVNCT-- 854
Cdd:TIGR02857 52 LVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAViv 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 855 ----LDVIGTILVIIGALPLFILGIIPsvFFYFSIQRYyvASSRQIRRLTGASRspVISHFSETLSGVSTIRAFGHQQRF 930
Cdd:TIGR02857 132 plaiLAAVFPQDWISGLILLLTAPLIP--IFMILIGWA--AQAAARKQWAALSR--LSGHFLDRLRGLPTLKLFGRAKAQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 931 IQQYKEVVNENlvcfynnviSNRWLSV-RLEFLGNLMVLFAAllavlagnSIDSATVGLSISYAL---NITHSLNFWV-- 1004
Cdd:TIGR02857 206 AAAIRRSSEEY---------RERTMRVlRIAFLSSAVLELFA--------TLSVALVAVYIGFRLlagDLDLATGLFVll 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1005 ----------------KKACEIETNAVAVERVCEyenmdkEAPWIMSRRPPLQWPNKGVVEFINYQARYRDElGLALQDI 1068
Cdd:TIGR02857 269 lapefylplrqlgaqyHARADGVAAAEALFAVLD------AAPRPLAGKAPVTAAPASSLEFSGVSVAYPGR-RPALRPV 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1069 TFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKLNIIPQHPVLFSGTLQMNLDPLNK 1148
Cdd:TIGR02857 342 SFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARP 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1149 Y-SDSKLWEALELCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTI 1227
Cdd:TIGR02857 422 DaSDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEAL 501
|
490 500
....*....|....*....|....*...
gi 74136409 1228 RKEFSDCTILTIAHRLQSIIDSDRVLVL 1255
Cdd:TIGR02857 502 RALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
433-647 |
2.29e-37 |
|
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: 140.44 E-value: 2.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNKtGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILG--------------EMEKLTGVVQRKgSVA 498
Cdd:cd03254 3 IEFENVNFSYDE-KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRfydpqkgqilidgiDIRDISRKSLRS-MIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 499 YVSQQAWIQNCILQVNILFGSIMKKEfyEQVLEACALL---PDLEQLPKGDQTEIGERGVNISGGQQHRVSLARAVYSGA 575
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATD--EEVIEAAKEAgahDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74136409 576 DIYLLDDPLSAVDVHVgkqlfEKVI--GSLGLLKNKTRILVTHNLTLLPQMDLIVVMESGRIAQMGTYQELLSK 647
Cdd:cd03254 159 KILILDEATSNIDTET-----EKLIqeALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1068-1279 |
5.59e-37 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 148.45 E-value: 5.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1068 ITFQTHGEEKIGIVGRTGAGKSTLSNCLF---------RI--VEraggkiiidgidISTIGLHDLRGKLNIIPQHPVLFS 1136
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLgflpyqgslKIngIE------------LRELDPESWRKHLSWVGQNPQLPH 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1137 GTLQMNLDPLNK-YSDSKLWEALELCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRKTKILILDEATASI 1215
Cdd:PRK11174 437 GTLRDNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74136409 1216 DFETDKLVQTTIRKEFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQNLIRQKGLFYEM 1279
Cdd:PRK11174 517 DAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
745-1023 |
1.73e-36 |
|
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: 140.04 E-value: 1.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 745 NLWLSAWAKEAKNMndfTEWK-QIRsnkLNIYGILGLIKGLFVCSGAYVITRGSLAASRTMYVQLLNNVLHLPIQFFETN 823
Cdd:cd18559 19 NLWLLLWFDDPVNG---PQEHgQVY---LSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 824 STGQIISRFTKDIFIIDMRLHYYLRLWVNCTLDVIGTILVIIGALPLFiLGIIPSVFFYFSIQRYYVASSRQIRRLTGAS 903
Cdd:cd18559 93 PSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMA-AVGIPLGLLYVPVNRVYAASSRQLKRLESVS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 904 RSPVISHFSETLSGVSTIRAFGHQQRFIQQYKEVVNENLVcFYNNVISNRWLSVRLEFLGNLMVLFAALLAVLAGNSIdS 983
Cdd:cd18559 172 KDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELA-YLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRHSL-A 249
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 74136409 984 ATVGLSISYALNITHSLNFWVKKACEIETNAVAVERVCEY 1023
Cdd:cd18559 250 GLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLER 289
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1045-1260 |
1.01e-35 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 135.68 E-value: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1045 KGVVEFINYQARYRDELG-LALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRG 1123
Cdd:cd03248 9 KGIVKFQNVTFAYPTRPDtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1124 KLNIIPQHPVLFSGTLQMNLD-PLNKYSDSKLWEALELCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRK 1202
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 1203 TKILILDEATASIDFETDKLVQTTIRKEFSDCTILTIAHRLQSIIDSDRVLVLDSGSI 1260
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
432-630 |
6.56e-35 |
|
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: 141.27 E-value: 6.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 432 AIEFTDATYSWNKTgMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQ-------------RKGSVA 498
Cdd:TIGR02857 321 SLEFSGVSVAYPGR-RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAvngvpladadadsWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 499 YVSQQAWIQNCILQVNILFG-SIMKKEFYEQVLEACALLPDLEQLPKGDQTEIGERGVNISGGQQHRVSLARAVYSGADI 577
Cdd:TIGR02857 400 WVPQHPFLFAGTIAENIRLArPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 74136409 578 YLLDDPLSAVDVHVGKQLFEKVigsLGLLKNKTRILVTHNLTLLPQMDLIVVM 630
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEAL---RALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
433-647 |
2.12e-34 |
|
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: 132.28 E-value: 2.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSW-NKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAIL-------------GEMEKLTGVVQRKGSVA 498
Cdd:cd03249 1 IEFKNVSFRYpSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLErfydptsgeilldGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 499 YVSQQAWIQNCILQVNILFGSIMKKEfyEQVLEAC--ALLPD-LEQLPKGDQTEIGERGVNISGGQQHRVSLARAVYSGA 575
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAkkANIHDfIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74136409 576 DIYLLDDPLSAVDVHVGKQLFEKVIgslGLLKNKTRILVTHNLTLLPQMDLIVVMESGRIAQMGTYQELLSK 647
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALD---RAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1045-1276 |
2.19e-34 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 140.54 E-value: 2.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1045 KGVVEFINYQARYRDELGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGK 1124
Cdd:PRK11176 339 KGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1125 LNIIPQHPVLFSGTLQMNLD--PLNKYSDSKLWEALELCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRK 1202
Cdd:PRK11176 419 VALVSQNVHLFNDTIANNIAyaRTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRD 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74136409 1203 TKILILDEATASIDFETDKLVQTTIRKEFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQNLIRQKGLF 1276
Cdd:PRK11176 499 SPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVY 572
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1045-1295 |
3.79e-34 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 139.71 E-value: 3.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1045 KGVVEFINYQARYrDELGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGK 1124
Cdd:PRK13657 332 KGAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1125 LNIIPQHPVLFSGTLQMNLDpLNK--YSDSKLWEALELCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRK 1202
Cdd:PRK13657 411 IAVVFQDAGLFNRSIEDNIR-VGRpdATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKD 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1203 TKILILDEATASIDFETDKLVQTTIRKEFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQNLIRQKGLFYEMTTD 1282
Cdd:PRK13657 490 PPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRA 569
|
250
....*....|...
gi 74136409 1283 AGITQESGTEKKL 1295
Cdd:PRK13657 570 QGMLQEDERRKQP 582
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
433-634 |
9.72e-34 |
|
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: 127.88 E-value: 9.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQ--------------RKgSVA 498
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILidgvdlrdldleslRK-NIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 499 YVSQQAWIQNcilqvnilfGSIMKkefyeqvleacallpdleqlpkgdqteigergvNI-SGGQQHRVSLARAVYSGADI 577
Cdd:cd03228 80 YVPQDPFLFS---------GTIRE---------------------------------NIlSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 74136409 578 YLLDDPLSAVDVHVGKQLFEKVigsLGLLKNKTRILVTHNLTLLPQMDLIVVMESGR 634
Cdd:cd03228 118 LILDEATSALDPETEALILEAL---RALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
431-635 |
1.76e-33 |
|
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: 128.86 E-value: 1.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 431 HAIEFTDATYSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILG--------------EMEKLTGVVQRKGs 496
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGlykptsgsvlldgtDIRQLDPADLRRN- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 497 VAYVSQQAWIQNCILQVNILFGSIMKKEfyEQVLEAcALLPDLEQL----PKGDQTEIGERGVNISGGQQHRVSLARAVY 572
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADD--ERILRA-AELAGVTDFvnkhPNGLDLQIGERGRGLSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74136409 573 SGADIYLLDDPLSAVDVHVGKQLFEKVigsLGLLKNKTRILVTHNLTLLPQMDLIVVMESGRI 635
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERL---RQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1046-1279 |
2.08e-33 |
|
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: 138.55 E-value: 2.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1046 GVVEFINYQARYRDELGLALQDITFQTHGEEKIGIVGRTGAGKSTLsnclFRIV---ER-AGGKIIIDGIDISTIGLHDL 1121
Cdd:TIGR03797 450 GAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTL----LRLLlgfETpESGSVFYDGQDLAGLDVQAV 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1122 RGKLNIIPQHPVLFSGTLQMNLDPLNKYSDSKLWEALELCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLR 1201
Cdd:TIGR03797 526 RRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVR 605
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 1202 KTKILILDEATASIDFETDKLVQTTIRKefSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQNLIRQKGLFYEM 1279
Cdd:TIGR03797 606 KPRILLFDEATSALDNRTQAIVSESLER--LKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQL 681
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
180-618 |
4.61e-33 |
|
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: 135.57 E-value: 4.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 180 FNMLTSAKVKTavngliYKKALLLSNVSRQKFSTGEIINLMSADAQQLMDLT------ANLNLLWSAPFqILMAIYLLWq 253
Cdd:TIGR02868 82 LRSLGALRVRV------YERLARQALAGRRRLRRGDLLGRLGADVDALQDLYvrvivpAGVALVVGAAA-VAAIAVLSV- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 254 ELGPAVLAGVAVLVFVIP-INALAATKIKKLKKSQRKNKDKQiklLKEILHGIKILKLYAWEPSYknkIIKIRDQELEFQ 332
Cdd:TIGR02868 154 PAALILAAGLLLAGFVAPlVSLRAARAAEQALARLRGELAAQ---LTDALDGAAELVASGALPAA---LAQVEEADRELT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 333 KSARYLTVFSMLTLTCIPFLVSLATLCVYFL-----LDEG--NILTATKVFTSMSLFNilriPLFELPTVISTVVQTKIS 405
Cdd:TIGR02868 228 RAERRAAAATALGAALTLLAAGLAVLGALWAggpavADGRlaPVTLAVLVLLPLAAFE----AFAALPAAAQQLTRVRAA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 406 LGRLEDFLHTEELLPQNI----ETNYIGDHAIEFTDATYSWnKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAIL 481
Cdd:TIGR02868 304 AERIVEVLDAAGPVAEGSapaaGAVGLGKPTLELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLA 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 482 GEMEKLTGVVQRKGS-------------VAYVSQQAWIQNCILQVNILFG--SIMKKEFYEqVLEACALLPDLEQLPKGD 546
Cdd:TIGR02868 383 GLLDPLQGEVTLDGVpvssldqdevrrrVSVCAQDAHLFDTTVRENLRLArpDATDEELWA-ALERVGLADWLRALPDGL 461
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74136409 547 QTEIGERGVNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGKQLFEKVigsLGLLKNKTRILVTHNL 618
Cdd:TIGR02868 462 DTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL---LAALSGRTVVLITHHL 530
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
430-646 |
6.34e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.51 E-value: 6.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 430 DHAIEFTDATYSWNKTgmPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVV--------QRKGSVAYVS 501
Cdd:COG1121 4 MPAIELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrlfgkpprRARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 502 QQAWIQ-------------NCILQVNILFGsiMKKEFYEQVLEACALLpDLEQLpKGDQteIGErgvnISGGQQHRVSLA 568
Cdd:COG1121 82 QRAEVDwdfpitvrdvvlmGRYGRRGLFRR--PSRADREAVDEALERV-GLEDL-ADRP--IGE----LSGGQQQRVLLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 569 RAVYSGADIYLLDDPLSAVDVHVGKQLFEkvigslgLLK-----NKTRILVTHNLTLLPQM-DLIVVMESGRIAQmGTYQ 642
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYE-------LLRelrreGKTILVVTHDLGAVREYfDRVLLLNRGLVAH-GPPE 223
|
....
gi 74136409 643 ELLS 646
Cdd:COG1121 224 EVLT 227
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
409-644 |
4.19e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 127.27 E-value: 4.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 409 LEDFLHTEELLPQNIETNYIGDHAIEF--TDAT-YSWNktGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEME 485
Cdd:PRK11174 324 LVTFLETPLAHPQQGEKELASNDPVTIeaEDLEiLSPD--GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 486 -----KLTGVVQRKGSVAYVSQQ-AWI-QNCIL-----QVNILFGSI-MKKEFYEQVLEACALLPDLEQLPKGDQTEIGE 552
Cdd:PRK11174 402 yqgslKINGIELRELDPESWRKHlSWVgQNPQLphgtlRDNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIGD 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 553 RGVNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGkqlfEKVIGSL-GLLKNKTRILVTHNLTLLPQMDLIVVME 631
Cdd:PRK11174 482 QAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSE----QLVMQALnAASRRQTTLMVTHQLEDLAQWDQIWVMQ 557
|
250
....*....|...
gi 74136409 632 SGRIAQMGTYQEL 644
Cdd:PRK11174 558 DGQIVQQGDYAEL 570
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
376-1276 |
4.41e-30 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 130.15 E-value: 4.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 376 FTSMSLFNILR---IPLFELPTVISTVVQTKISL---GRLEDFLHTEELLPQNIETNYIGD-HAIEFTDATYSWN-KTGM 447
Cdd:PTZ00265 319 FHGGSVISILLgvlISMFMLTIILPNITEYMKSLeatNSLYEIINRKPLVENNDDGKKLKDiKKIQFKNVRFHYDtRKDV 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 448 PVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAI----------------------------------------------- 480
Cdd:PTZ00265 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIerlydptegdiiindshnlkdinlkwwrskigvvsqdpllfsnsikn 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 481 --------LGEMEKLTGVVQRKGSVAYV---SQQAWIQNCILQVNILFGSI-------MKKEFY----EQVLEAC--ALL 536
Cdd:PTZ00265 479 nikyslysLKDLEALSNYYNEDGNDSQEnknKRNSCRAKCAGDLNDMSNTTdsnelieMRKNYQtikdSEVVDVSkkVLI 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 537 PD-LEQLPKGDQTEIGERGVNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDvHVGKQLFEKVIGSLGLLKNKTRILVT 615
Cdd:PTZ00265 559 HDfVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKGNENRITIIIA 637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 616 HNLTLLPQMDLIVVM---ESG-------------------------------------RIAQMGTY------QELLSKTR 649
Cdd:PTZ00265 638 HRLSTIRYANTIFVLsnrERGstvdvdiigedptkdnkennnknnkddnnnnnnnnnnKINNAGSYiieqgtHDALMKNK 717
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 650 N-----LTNLHQVISE-----------EEKAHALKR------ASAVNSRTRPKDK-ILEQKPRPSLDQGKQLSMKKEKIP 706
Cdd:PTZ00265 718 NgiyytMINNQKVSSKkssnndndkdsDMKSSAYKDsergydPDEMNGNSKHENEsASNKKSCKMSDENASENNAGGKLP 797
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 707 VGGVKF--------SIILQYLQAFGWLWVwlTMVTYLGQNLVGIGQNLWLSAWAKEAKNMNDFTEWkQIRSNKLNIYgIL 778
Cdd:PTZ00265 798 FLRNLFkrkpkapnNLRIVYREIFSYKKD--VTIIALSILVAGGLYPVFALLYAKYVSTLFDFANL-EANSNKYSLY-IL 873
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 779 GLIKGLFVCSGA--YVITRGSLAASRTMYVQLLNNVLHLPIQFFE--TNSTGQIISRFTKDIFIIDMRLhyylrlwvnct 854
Cdd:PTZ00265 874 VIAIAMFISETLknYYNNVIGEKVEKTMKRRLFENILYQEISFFDqdKHAPGLLSAHINRDVHLLKTGL----------- 942
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 855 ldvIGTILVIIGALPLFILGIIPSVFF-----------YFSIQRYYVASSRqirrltgASRSPVISHFSETLSGvsTIRA 923
Cdd:PTZ00265 943 ---VNNIVIFTHFIVLFLVSMVMSFYFcpivaavltgtYFIFMRVFAIRAR-------LTANKDVEKKEINQPG--TVFA 1010
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 924 FGHQQRFIQQYKEVVNEnlvCFYN-NVISNRWLSvrlEFLGNLMVLFAALLAVLAGNS--IDSATVGLSISYALNItHSL 1000
Cdd:PTZ00265 1011 YNSDDEIFKDPSFLIQE---AFYNmNTVIIYGLE---DYFCNLIEKAIDYSNKGQKRKtlVNSMLWGFSQSAQLFI-NSF 1083
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1001 NFWV------KKACEIE-----------TNAVAVERVC---EYEN----MDKEAPWIMSRR-------PPLQWPN----K 1045
Cdd:PTZ00265 1084 AYWFgsflirRGTILVDdfmkslftflfTGSYAGKLMSlkgDSENaklsFEKYYPLIIRKSnidvrdnGGIRIKNkndiK 1163
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1046 GVVEFINYQARYRDELGLAL-QDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRI-------------------------- 1098
Cdd:PTZ00265 1164 GKIEIMDVNFRYISRPNVPIyKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneqdyq 1243
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1099 -----------VERAGGKIIIDGIDISTI-----------------GLHDLRGKLNIIPQHPVLFSGTLQMNLdplnKY- 1149
Cdd:PTZ00265 1244 gdeeqnvgmknVNEFSLTKEGGSGEDSTVfknsgkilldgvdicdyNLKDLRNLFSIVSQEPMLFNMSIYENI----KFg 1319
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1150 -SDSKLWEALELCH---LKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQT 1225
Cdd:PTZ00265 1320 kEDATREDVKRACKfaaIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1399
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|....*....
gi 74136409 1226 TIR--KEFSDCTILTIAHRLQSIIDSDRVLVLD----SGSIVEFEAPQN--LIRQKGLF 1276
Cdd:PTZ00265 1400 TIVdiKDKADKTIITIAHRIASIKRSDKIVVFNnpdrTGSFVQAHGTHEelLSVQDGVY 1458
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
349-657 |
2.14e-29 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 125.13 E-value: 2.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 349 IPFLVSLATLCVYFLLDEGNI---LTA---TKVFTSMslFNILRiPLFELPTVIS------TVVQTKISLGRLEdflhTE 416
Cdd:PRK11176 255 IQLIASLALAFVLYAASFPSVmdtLTAgtiTVVFSSM--IALMR-PLKSLTNVNAqfqrgmAACQTLFAILDLE----QE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 417 ellpQNIETNYI----GDhaIEFTDATYSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAIL-------GEME 485
Cdd:PRK11176 328 ----KDEGKRVIerakGD--IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTrfydideGEIL 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 486 kLTGVVQR-------KGSVAYVSQQAWIQNCILQVNILFGSimkKEFY--EQVLEACAL---LPDLEQLPKGDQTEIGER 553
Cdd:PRK11176 402 -LDGHDLRdytlaslRNQVALVSQNVHLFNDTIANNIAYAR---TEQYsrEQIEEAARMayaMDFINKMDNGLDTVIGEN 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 554 GVNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVgkqlfEKVIGSL--GLLKNKTRILVTHNLTLLPQMDLIVVME 631
Cdd:PRK11176 478 GVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES-----ERAIQAAldELQKNRTSLVIAHRLSTIEKADEILVVE 552
|
330 340
....*....|....*....|....*.
gi 74136409 632 SGRIAQMGTYQELLSKTRNLTNLHQV 657
Cdd:PRK11176 553 DGEIVERGTHAELLAQNGVYAQLHKM 578
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
433-656 |
3.03e-29 |
|
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: 117.59 E-value: 3.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSVAYVSQQAWIQ---NC 509
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRrqvGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 510 ILQVNILFGSIMKKEF--------YEQVLEACALLPDLE---QLPKGDQTEIGERGVNISGGQQHRVSLARAVYSGADIY 578
Cdd:cd03252 81 VLQENVLFNRSIRDNIaladpgmsMERVIEAAKLAGAHDfisELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 579 LLDDPLSAVDVHVgkqlfEKVIGS--LGLLKNKTRILVTHNLTLLPQMDLIVVMESGRIAQMGTYQELLSKTRNLTNLHQ 656
Cdd:cd03252 161 IFDEATSALDYES-----EHAIMRnmHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
434-622 |
8.05e-29 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 115.32 E-value: 8.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 434 EFTDATYSWNktGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKG--------SVAYVSQQAW 505
Cdd:cd03235 1 EVEDLTVSYG--GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 506 IQNC----ILQV-------NILFGSIMKKEFYEQVLEACALLpDLEQLpkGDQTeIGErgvnISGGQQHRVSLARAVYSG 574
Cdd:cd03235 79 IDRDfpisVRDVvlmglygHKGLFRRLSKADKAKVDEALERV-GLSEL--ADRQ-IGE----LSGGQQQRVLLARALVQD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 74136409 575 ADIYLLDDPLSAVDVHVGKQLFEkVIGSLGlLKNKTRILVTHNLTLLP 622
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYE-LLRELR-REGMTILVVTHDLGLVL 196
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
727-966 |
2.82e-28 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 115.82 E-value: 2.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 727 VWLTMVTYLGQNLVGIGQNLWLSAWakeaknMNDFTEWKQIRSNKLNIY----GILGLIKGLFVCSGAYVITRGSLAASR 802
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRI------LDVLLPDGDPETQALNVYslalLLLGLAQFILSFLQSYLLNHTGERLSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 803 TMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDMRLHYYLRLWVNCTLDVIGTILVIIGALPLFILGIIPSVFFY 882
Cdd:pfam00664 75 RLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 883 FSIQRYYVASSRQIRRLTGASRSPVISHFSETLSGVSTIRAFGHQQRFIQQYKEVVNENLVCFYNNVISNRWLSVRLEFL 962
Cdd:pfam00664 155 ILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFI 234
|
....
gi 74136409 963 GNLM 966
Cdd:pfam00664 235 GYLS 238
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
432-658 |
2.46e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 118.77 E-value: 2.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 432 AIEFTDATYSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKG-------------SVA 498
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqpiadyseaalrqAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 499 YVSQQAWIQNCILQVNILFGSIMKKEfyEQVLEAcaL----LPDLEQLPKGDQTEIGERGVNISGGQQHRVSLARAVYSG 574
Cdd:PRK11160 418 VVSQRVHLFSATLRDNLLLAAPNASD--EALIEV--LqqvgLEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHD 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 575 ADIYLLDDPLSAVDVHVGKQLFEkvigslgLL----KNKTRILVTHNLTLLPQMDLIVVMESGRIAQMGTYQELLSKTRN 650
Cdd:PRK11160 494 APLLLLDEPTEGLDAETERQILE-------LLaehaQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGR 566
|
....*...
gi 74136409 651 LTNLHQVI 658
Cdd:PRK11160 567 YYQLKQRL 574
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1033-1279 |
6.28e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 117.62 E-value: 6.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1033 IMSRRPPLQWP-------NKGVVEFINYQARYRDELGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGK 1105
Cdd:PRK11160 317 ITEQKPEVTFPttstaaaDQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1106 IIIDGIDISTIGLHDLRGKLNIIPQHPVLFSGTLQMNL---DPlnKYSDSKLWEALELCHLKEFVQSlPEKLRHEISEGG 1182
Cdd:PRK11160 397 ILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGG 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1183 ENLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTIRKEFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVE 1262
Cdd:PRK11160 474 RQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIE 553
|
250
....*....|....*..
gi 74136409 1263 FEAPQNLIRQKGLFYEM 1279
Cdd:PRK11160 554 QGTHQELLAQQGRYYQL 570
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
118-389 |
8.12e-27 |
|
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: 111.58 E-value: 8.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 118 LIQVALFKVFADILSFTSPLIMKQMI-IFCEHSSDFGWNGYGYAMALFVVVFLQTLILQRYQCFNMLTSAKVKTAVNGLI 196
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILdVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 197 YKKALLLSNVSRQKFSTGEIINLMSADAQQLMDLTANLNLLWSAPFQILMAIYLLWQELGPAV-LAGVAVLVFVIPINAL 275
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLtLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 276 AATKIKKLKKSQRKNKDKQIKLLKEILHGIKILKLYAWEPSYKNKIIKIRDQELEFQ-KSARYLTVFSMLTLTCIPFLVS 354
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGiKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....*
gi 74136409 355 LATLCVYFLLDEGNiLTATKVFTSMSLFNILRIPL 389
Cdd:pfam00664 241 LALWFGAYLVISGE-LSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
433-640 |
1.27e-26 |
|
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: 109.12 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKG-SVAYVSQQAWIQN--C 509
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvDISKIGLHDLRSRisI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 510 ILQVNILF-GSIMK-----KEFYE----QVLEACALLPDLEQLPKGDQTEIGERGVNISGGQQHRVSLARAVYSGADIYL 579
Cdd:cd03244 83 IPQDPVLFsGTIRSnldpfGEYSDeelwQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74136409 580 LDDPLSAVDVHVGKQLfEKVIGSlgLLKNKTRILVTHNLTLLPQMDLIVVMESGRIAQMGT 640
Cdd:cd03244 163 LDEATASVDPETDALI-QKTIRE--AFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
439-648 |
3.78e-26 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 114.81 E-value: 3.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 439 TYSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQR-------------KGSVAYVSQQAW 505
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFhdipltklqldswRSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 506 IQNCILQVNILFGSI-MKKEFYEQVLEACALLPDLEQLPKGDQTEIGERGVNISGGQQHRVSLARAVYSGADIYLLDDPL 584
Cdd:PRK10789 400 LFSDTVANNIALGRPdATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74136409 585 SAVDVHVGKQLFEKvIGSLGllKNKTRILVTHNLTLLPQMDLIVVMESGRIAQMGTYQELLSKT 648
Cdd:PRK10789 480 SAVDGRTEHQILHN-LRQWG--EGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1064-1259 |
1.06e-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: 106.01 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLfriveraggkiiidgidistIG-LHDLRGKLNI------IPQHPVLFS 1136
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--------------------LGeLEKLSGSVSVpgsiayVSQEPWIQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1137 GTLQMNLDPLNKYSDSKLWEALELCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRKTKILILDEATASID 1216
Cdd:cd03250 80 GTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 74136409 1217 FET-DKLVQTTIRKEFSDC-TILTIAHRLQSIIDSDRVLVLDSGS 1259
Cdd:cd03250 160 AHVgRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
433-639 |
4.09e-25 |
|
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: 104.52 E-value: 4.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNKTgmPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEM-----------EKLTGVVQRKGSVAYVS 501
Cdd:cd03259 1 LELKGLSKTYGSV--RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLErpdsgeilidgRDVTGVPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 502 QQA----WiqnciLQV--NILFG----SIMKKEFYEQVLEACALLPDLEQLPKgdqtEIGErgvnISGGQQHRVSLARAV 571
Cdd:cd03259 79 QDYalfpH-----LTVaeNIAFGlklrGVPKAEIRARVRELLELVGLEGLLNR----YPHE----LSGGQQQRVALARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74136409 572 YSGADIYLLDDPLSAVDVHVGKQL---FEKVIGSLGLlknkTRILVTHNLT-LLPQMDLIVVMESGRIAQMG 639
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELreeLKELQRELGI----TTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
209-648 |
4.13e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 112.51 E-value: 4.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 209 QKFSTGEIINLMSADAQQLMD-LTANLN-LLWSAPFQILMAIYLLWqeLGPAVlagVAVLVFVIPINALAA----TKIKK 282
Cdd:TIGR00958 253 DENKTGELTSRLSSDTQTMSRsLSLNVNvLLRNLVMLLGLLGFMLW--LSPRL---TMVTLINLPLVFLAEkvfgKRYQL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 283 LKKSQRKNKDKQIKLLKEILHGIKILKLYAWEPS----YKNKIIKIRDqeLEFQKSARYLTVFSMLTLTCIPFLVSLATL 358
Cdd:TIGR00958 328 LSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGeasrFKEALEETLQ--LNKRKALAYAGYLWTTSVLGMLIQVLVLYY 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 359 CVYFLLD---EGNILTATKVFTsMSLFNILRiplfELPTVISTVVQTKISLGRLEDFLHTEELLPQNIETNYIGDHA-IE 434
Cdd:TIGR00958 406 GGQLVLTgkvSSGNLVSFLLYQ-EQLGEAVR----VLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNLEGlIE 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 435 FTDATYSW-NKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKG-------------SVAYV 500
Cdd:TIGR00958 481 FQDVSFSYpNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylhrQVALV 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 501 SQQAWIQNCILQVNILFG-SIMKKEFYEQVLEACALLPDLEQLPKGDQTEIGERGVNISGGQQHRVSLARAVYSGADIYL 579
Cdd:TIGR00958 561 GQEPVLFSGSVRENIAYGlTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLI 640
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74136409 580 LDDPLSAVDVHVgkqlfEKVIGSLGLLKNKTRILVTHNLTLLPQMDLIVVMESGRIAQMGTYQELLSKT 648
Cdd:TIGR00958 641 LDEATSALDAEC-----EQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1064-1279 |
5.64e-25 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 111.34 E-value: 5.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKLNIIPQHPVLFSGTLQMNL 1143
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1144 dPLNK--YSDSKLWEALELCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRKTKILILDEATASIDFETDK 1221
Cdd:PRK10789 410 -ALGRpdATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEH 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 1222 LVQTTIRKEFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQNLIRQKGLFYEM 1279
Cdd:PRK10789 489 QILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDM 546
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1048-1262 |
2.38e-24 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 101.24 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1048 VEFINYQARYRDELGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGlHDLRGKLNI 1127
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1128 IPQHPVLFSGTLQMNLdplnkysdsklwealelchlkefvqslpeklrheisegGENLSMGQRQLVCLARALLRKTKILI 1207
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 74136409 1208 LDEATASIDFETDKLVQTTIRKEFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVE 1262
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1065-1213 |
2.67e-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: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKLNIIPQHPVLFSG-TLQMNL 1143
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74136409 1144 -------DPLNKYSDSKLWEALElcHLkefvqSLPEKLRHEISEGGENLSMGQRQLVCLARALLRKTKILILDEATA 1213
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALE--KL-----GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1047-1263 |
5.66e-24 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 101.81 E-value: 5.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1047 VVEFINYQARYRDELGL--ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAG---GKIIIDGIDISTIGLHDL 1121
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSgsiIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1122 RGKLNIIPQHPvlFSgtlqmNLDPLNKYSDSkLWEALELcHLKEFVQSLPEKLRHEISEGGEN-----------LSMGQR 1190
Cdd:cd03257 81 RKEIQMVFQDP--MS-----SLNPRMTIGEQ-IAEPLRI-HGKLSKKEARKEAVLLLLVGVGLpeevlnrypheLSGGQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1191 QLVCLARALLRKTKILILDEATASIdfetDKLVQTTI-------RKEFsDCTILTIAHRLqSIID--SDRVLVLDSGSIV 1261
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSAL----DVSVQAQIldllkklQEEL-GLTLLFITHDL-GVVAkiADRVAVMYAGKIV 225
|
..
gi 74136409 1262 EF 1263
Cdd:cd03257 226 EE 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1064-1243 |
7.22e-24 |
|
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: 107.45 E-value: 7.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKLNIIPQHPVLFSGTLQMNL 1143
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1144 DPLNK-YSDSKLWEALELCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKL 1222
Cdd:TIGR02868 430 RLARPdATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADE 509
|
170 180
....*....|....*....|.
gi 74136409 1223 VQTTIRKEFSDCTILTIAHRL 1243
Cdd:TIGR02868 510 LLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
434-634 |
1.50e-23 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 98.47 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 434 EFTDATYSWNKTgmPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQrkgsvayvsqqawiqncilqv 513
Cdd:cd00267 1 EIENLSFRYGGR--TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL--------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 514 niLFGSIMKKEFYEQVLEACALLPDLeqlpkgdqteigergvniSGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGK 593
Cdd:cd00267 58 --IDGKDIAKLPLEELRRRIGYVPQL------------------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 74136409 594 QLFEkVIGSLgLLKNKTRILVTHNLTLL-PQMDLIVVMESGR 634
Cdd:cd00267 118 RLLE-LLREL-AEEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1064-1275 |
1.75e-23 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 106.14 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAG---GKIIIDGIDISTIGLHDLRGKLNIIPQHPvlFSgtlQ 1140
Cdd:COG1123 280 AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSgsiLFDGKDLTKLSRRSLRELRRRVQMVFQDP--YS---S 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1141 MN------------LDPLNKYSDSKLW----EALELCHL-KEFVQSLPeklrHEiseggenLSMGQRQLVCLARALLRKT 1203
Cdd:COG1123 355 LNprmtvgdiiaepLRLHGLLSRAERRervaELLERVGLpPDLADRYP----HE-------LSGGQRQRVAIARALALEP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1204 KILILDEATASIdfetDKLVQTTI-------RKEFsDCTILTIAHRLQSIID-SDRVLVLDSGSIVE-------FEAPQN 1268
Cdd:COG1123 424 KLLILDEPTSAL----DVSVQAQIlnllrdlQREL-GLTYLFISHDLAVVRYiADRVAVMYDGRIVEdgpteevFANPQH 498
|
....*..
gi 74136409 1269 LIRQKGL 1275
Cdd:COG1123 499 PYTRALL 505
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1048-1273 |
2.81e-23 |
|
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: 99.71 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1048 VEFINYQARYRDElGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCL---------------FRIVERaggkiiidgid 1112
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLngllkptsgevlvdgKDITKK----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1113 istiGLHDLRGKLNIIPQHPV--LFSGT---------LQMNLDPlnKYSDSKLWEALELCHLKEFvqslpekLRHEISEg 1181
Cdd:COG1122 69 ----NLRELRRKVGLVFQNPDdqLFAPTveedvafgpENLGLPR--EEIRERVEEALELVGLEHL-------ADRPPHE- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1182 genLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTIRK-EFSDCTILTIAHRLQSIID-SDRVLVLDSGS 1259
Cdd:COG1122 135 ---LSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGR 211
|
250
....*....|....
gi 74136409 1260 IVEFEAPQNLIRQK 1273
Cdd:COG1122 212 IVADGTPREVFSDY 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
433-635 |
3.13e-23 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 98.06 E-value: 3.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGsvAYVSQQAWIQ----- 507
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG--ADISQWDPNElgdhv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 508 NCILQVNILF-GSIMKkefyeqvleacallpdleqlpkgdqteigergvNI-SGGQQHRVSLARAVYSGADIYLLDDPLS 585
Cdd:cd03246 79 GYLPQDDELFsGSIAE---------------------------------NIlSGGQRQRLGLARALYGNPRILVLDEPNS 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 74136409 586 AVDVHvGKQLFEKVIGSLGlLKNKTRILVTHNLTLLPQMDLIVVMESGRI 635
Cdd:cd03246 126 HLDVE-GERALNQAIAALK-AAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
399-649 |
6.80e-23 |
|
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: 104.83 E-value: 6.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 399 VVQTKISLGRLEDFLHTEELLPQNIE----TnyigdHAIEFTDATYSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKS 474
Cdd:COG4618 298 FVSARQAYRRLNELLAAVPAEPERMPlprpK-----GRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKS 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 475 SMLSAILGEMEKLTGVV-------------QRKGSVAYVSQQawIQncilqvniLF-GSI------MKKEFYEQVLEACA 534
Cdd:COG4618 373 TLARLLVGVWPPTAGSVrldgadlsqwdreELGRHIGYLPQD--VE--------LFdGTIaeniarFGDADPEKVVAAAK 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 535 L--LPDL-EQLPKGDQTEIGERGVNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDvHVGKQlfeKVIGSLGLLK--NK 609
Cdd:COG4618 443 LagVHEMiLRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLD-DEGEA---ALAAAIRALKarGA 518
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 74136409 610 TRILVTHNLTLLPQMDLIVVMESGRIAQMGTYQELLSKTR 649
Cdd:COG4618 519 TVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLARLA 558
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
448-639 |
1.04e-22 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 96.74 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 448 PVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKG-SVAYVSQQAWIQNCilqvnilfgSIMkkefy 526
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGkDLASLSPKELARKI---------AYV----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 527 EQVLEACallpDLEQLpkgdqteiGERGVN-ISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGKQLFEkVIGSLGL 605
Cdd:cd03214 79 PQALELL----GLAHL--------ADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLE-LLRRLAR 145
|
170 180 190
....*....|....*....|....*....|....*
gi 74136409 606 LKNKTRILVTHNLTLLPQM-DLIVVMESGRIAQMG 639
Cdd:cd03214 146 ERGKTVVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1065-1263 |
1.54e-22 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 103.67 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVE------RaggkiiidgidistIGLHDLR-----------GKLni 1127
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPptagsvR--------------LDGADLSqwdreelgrhiGYL-- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1128 iPQHPVLFSGTLQMNLDPLNKYSDSKLWEALELCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRKTKILI 1207
Cdd:COG4618 412 -PQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVV 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 1208 LDEATASIDFETDKLVQTTIR--KEfSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEF 1263
Cdd:COG4618 491 LDEPNSNLDDEGEAALAAAIRalKA-RGATVVVITHRPSLLAAVDKLLVLRDGRVQAF 547
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1056-1258 |
2.41e-22 |
|
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: 96.77 E-value: 2.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1056 RYRDELGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKLNIIPQHP--- 1132
Cdd:cd03225 8 SYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPddq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1133 ---------VLFsGTLQMNLDPlnKYSDSKLWEALELCHLKEFvqslpekLRHEISEggenLSMGQRQLVCLARALLRKT 1203
Cdd:cd03225 88 ffgptveeeVAF-GLENLGLPE--EEIEERVEEALELVGLEGL-------RDRSPFT----LSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 1204 KILILDEATASIDFETDKLVQTTIrKEFSDC--TILTIAHRLQSIID-SDRVLVLDSG 1258
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELL-KKLKAEgkTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
432-673 |
2.81e-22 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 102.29 E-value: 2.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 432 AIEFTDATYSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILG---EMEKLTGVV-------------QRKG 495
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVlldgrdllelseaLRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 496 SVAYVSQQAWIQNCILQV--NILFG----SIMKKEFYEQVLEACALLpDLEQLPKGDQTEigergvnISGGQQHRVSLAR 569
Cdd:COG1123 84 RIGMVFQDPMTQLNPVTVgdQIAEAlenlGLSRAEARARVLELLEAV-GLERRLDRYPHQ-------LSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 570 AVYSGADIYLLDDPLSAVDVHVGKQLFEkVIGSLGLLKNKTRILVTHNLTLLPQM-DLIVVMESGRIAQMGTYQELLSKT 648
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILD-LLRELQRERGTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEILAAP 234
|
250 260
....*....|....*....|....*
gi 74136409 649 RNLTNLHQVISEEEKAHALKRASAV 673
Cdd:COG1123 235 QALAAVPRLGAARGRAAPAAAAAEP 259
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
432-651 |
3.97e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 99.38 E-value: 3.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 432 AIEFTDATYSWNKTgmPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGeMEKLTG--------VVQ----RKGSVAY 499
Cdd:COG3839 3 SLELENVSKSYGGV--EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG-LEDPTSgeiliggrDVTdlppKDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 500 VSQqawiqNCIL----QV--NILFGSIMKK----EFYEQVLEACALLpDLEQL----PKgdqteigergvNISGGQQHRV 565
Cdd:COG3839 80 VFQ-----SYALyphmTVyeNIAFPLKLRKvpkaEIDRRVREAAELL-GLEDLldrkPK-----------QLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 566 SLARAVYSGADIYLLDDPLSAVDVHVG-------KQLFEKvigsLGLlknkTRILVTHN----LTLlpqMDLIVVMESGR 634
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDAKLRvemraeiKRLHRR----LGT----TTIYVTHDqveaMTL---ADRIAVMNDGR 211
|
250
....*....|....*..
gi 74136409 635 IAQMGTYQELLSKTRNL 651
Cdd:COG3839 212 IQQVGTPEELYDRPANL 228
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
433-635 |
4.17e-22 |
|
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: 96.39 E-value: 4.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSW-NKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLsAILGEMEKLTG---VVQRK-----------GSV 497
Cdd:cd03248 12 VKFQNVTFAYpTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVV-ALLENFYQPQGgqvLLDGKpisqyehkylhSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 498 AYVSQQAWIQNCILQVNILFGsiMKKEFYEQVLEAC--ALLPD-LEQLPKGDQTEIGERGVNISGGQQHRVSLARAVYSG 574
Cdd:cd03248 91 SLVGQEPVLFARSLQDNIAYG--LQSCSFECVKEAAqkAHAHSfISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74136409 575 ADIYLLDDPLSAVDVHVGKQLFEKVIGSlglLKNKTRILVTHNLTLLPQMDLIVVMESGRI 635
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDW---PERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1056-1260 |
5.71e-22 |
|
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: 94.21 E-value: 5.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1056 RYRDELGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKLNIIPQHPVLF 1135
Cdd:cd03246 9 RYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDELF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1136 SGTLQMNLdplnkysdsklwealelchlkefvqslpeklrheiseggenLSMGQRQLVCLARALLRKTKILILDEATASI 1215
Cdd:cd03246 89 SGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 74136409 1216 DFETDKLVQTTIRK-EFSDCTILTIAHRLQSIIDSDRVLVLDSGSI 1260
Cdd:cd03246 128 DVEGERALNQAIAAlKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
778-1020 |
5.71e-22 |
|
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: 98.72 E-value: 5.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 778 LGLIKGLfvcsgayVITRGSLAASRTMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDMRLHYYLRLWVNCTLDV 857
Cdd:cd18600 86 MGFFRGL-------PLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 858 IGTILVIIGALPLFILGIIPSVFFYFSIQRYYVASSRQIRRLTGASRSPVISHFSETLSGVSTIRAFGHQQRFIQQYKEV 937
Cdd:cd18600 159 IGAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 938 VNENLVCFYNNVISNRWLSVRLEFLGNLMVLFAALLAVLAgNSIDSATVGLSISYALNITHSLNFWVKKACEIETNAVAV 1017
Cdd:cd18600 239 LNLHTANWFLYLSTLRWFQMRIEMIFVIFFTAVTFISIGT-TGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSV 317
|
...
gi 74136409 1018 ERV 1020
Cdd:cd18600 318 SRI 320
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
432-657 |
7.46e-22 |
|
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: 96.27 E-value: 7.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 432 AIEFTDATYSWNKTgmPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKG-------------SVA 498
Cdd:COG1120 1 MLEAENLSVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 499 YVSQQAwiqncilQVN--------ILFG--------SIMKKEFYEQVLEACALLpDLEQLpkgdqteiGERGVN-ISGGQ 561
Cdd:COG1120 79 YVPQEP-------PAPfgltvrelVALGryphlglfGRPSAEDREAVEEALERT-GLEHL--------ADRPVDeLSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 562 QHRVSLARAVYSGADIYLLDDPLSAVDVHVGKQLFEkVIGSLGLLKNKTRILVTHNLTLLPQM-DLIVVMESGRIAQMGT 640
Cdd:COG1120 143 RQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLE-LLRRLARERGRTVVMVLHDLNLAARYaDRLVLLKDGRIVAQGP 221
|
250
....*....|....*..
gi 74136409 641 YQELLSKtrnlTNLHQV 657
Cdd:COG1120 222 PEEVLTP----ELLEEV 234
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
448-645 |
1.15e-21 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 97.91 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 448 PVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGeMEK-------LTGVV--------QRKgsVAYVSQQ-AWIQNciL 511
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAG-LETpdsgrivLNGRDlftnlpprERR--VGFVFQHyALFPH--M 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 512 QV--NILFG----SIMKKEFYEQVLEacaLLpDLEQLPkgdqtEIGERGVN-ISGGQQHRVSLARAVYSGADIYLLDDPL 584
Cdd:COG1118 91 TVaeNIAFGlrvrPPSKAEIRARVEE---LL-ELVQLE-----GLADRYPSqLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74136409 585 SAVDVHVGKQLfEKVIGSlgLLK--NKTRILVTHNltllpQ---MDL---IVVMESGRIAQMGTYQELL 645
Cdd:COG1118 162 GALDAKVRKEL-RRWLRR--LHDelGGTTVFVTHD-----QeeaLELadrVVVMNQGRIEQVGTPDEVY 222
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
342-647 |
1.28e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 100.81 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 342 SMLTLTCIpFLVSLAtlcvyflLDEGNILTATKVFTSMSLFNILripLFELPTVISTVVQTKISLGRLEDFLHTEELLPQ 421
Cdd:PRK13657 250 STITMLAI-LVLGAA-------LVQKGQLRVGEVVAFVGFATLL---IGRLDQVVAFINQVFMAAPKLEEFFEVEDAVPD 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 422 NIE-------TNYIGDhaIEFTDATYSWNKTGmPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGV---- 490
Cdd:PRK13657 319 VRDppgaidlGRVKGA--VEFDDVSFSYDNSR-QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRilid 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 491 ------VQRKG---SVAYVSQQAWIQNCILQVNILFG--SIMKKEFYEqVLEACALLPDLEQLPKGDQTEIGERGVNISG 559
Cdd:PRK13657 396 gtdirtVTRASlrrNIAVVFQDAGLFNRSIEDNIRVGrpDATDEEMRA-AAERAQAHDFIERKPDGYDTVVGERGRQLSG 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 560 GQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGkqlfEKVIGSL-GLLKNKTRILVTHNLTLLPQMDLIVVMESGRIAQM 638
Cdd:PRK13657 475 GERQRLAIARALLKDPPILILDEATSALDVETE----AKVKAALdELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVES 550
|
....*....
gi 74136409 639 GTYQELLSK 647
Cdd:PRK13657 551 GSFDELVAR 559
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1035-1263 |
1.40e-21 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 100.50 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1035 SRRPPLQWPN-KGVVEFINYQARYRDELGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIidgidi 1113
Cdd:TIGR01842 303 SRDPAMPLPEpEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVR------ 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1114 stIGLHDLR-------GK-LNIIPQHPVLFSGTLQMNLDPLNKYSDS-KLWEALELCHLKEFVQSLPEKLRHEISEGGEN 1184
Cdd:TIGR01842 377 --LDGADLKqwdretfGKhIGYLPQDVELFPGTVAENIARFGENADPeKIIEAAKLAGVHELILRLPDGYDTVIGPGGAT 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1185 LSMGQRQLVCLARALLRKTKILILDEATASIDFETDK-LVQTTIRKEFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEF 1263
Cdd:TIGR01842 455 LSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQaLANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARF 534
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
433-639 |
1.81e-21 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 93.15 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGemekltgvvqrkgsvAYVSQQawiqncilq 512
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG---------------DLKPQQ--------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 513 vnilfGSIMKKEFYEQVLEAC--ALLPDLEQLPKGDQTEIGER-GVNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDV 589
Cdd:cd03247 57 -----GEITLDGVPVSDLEKAlsSLISVLNQRPYLFDTTLRNNlGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 74136409 590 HVGKQLFEKVigsLGLLKNKTRILVTHNLTLLPQMDLIVVMESGRIAQMG 639
Cdd:cd03247 132 ITERQLLSLI---FEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1064-1258 |
1.91e-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: 92.31 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAggkiiidgidistiglhdlrgklniipqhpvlfSGTLQMNL 1143
Cdd:cd00267 14 ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT---------------------------------SGEILIDG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1144 DPLNKYSDSKLwealelchlKEFVQSLPEklrheiseggenLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLV 1223
Cdd:cd00267 61 KDIAKLPLEEL---------RRRIGYVPQ------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERL 119
|
170 180 190
....*....|....*....|....*....|....*..
gi 74136409 1224 QTTIRKEFSD-CTILTIAHRLQSIID-SDRVLVLDSG 1258
Cdd:cd00267 120 LELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDG 156
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
433-635 |
2.35e-21 |
|
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: 94.09 E-value: 2.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNKTGM--PVLKDLNIKIPEGALVAVVGQVGSGKSSMLSaILGEMEKLT-GVVQ----------------- 492
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLN-ILGGLDRPTsGEVRvdgtdisklsekelaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 493 RKGSVAYVSQQawiQNCI--LQV--NILFGSIMKKEFYEQVLEACALLpdLEQLpkGDQTEIGERGVNISGGQQHRVSLA 568
Cdd:cd03255 80 RRRHIGFVFQS---FNLLpdLTAleNVELPLLLAGVPKKERRERAEEL--LERV--GLGDRLNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74136409 569 RAVYSGADIYLLDDPLSAVDVHVGKQLFEkVIGSLGLLKNKTRILVTHNLTLLPQMDLIVVMESGRI 635
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVME-LLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
432-656 |
3.02e-21 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 99.79 E-value: 3.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 432 AIEFTDATYSWnKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILG--------------EMEKLTGVVQRKGsV 497
Cdd:PRK10790 340 RIDIDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGyypltegeirldgrPLSSLSHSVLRQG-V 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 498 AYVSQQAWIQNCILQVNILFGSIMKKEFYEQVLEACALLPDLEQLPKGDQTEIGERGVNISGGQQHRVSLARAVYSGADI 577
Cdd:PRK10790 418 AMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQI 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 578 YLLDDPLSAVDVHVgKQLFEKvigSLGLLKNKTRILV-THNLTLLPQMDLIVVMESGRIAQMGTYQELLSKTRNLTNLHQ 656
Cdd:PRK10790 498 LILDEATANIDSGT-EQAIQQ---ALAAVREHTTLVViAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQ 573
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
434-634 |
3.23e-21 |
|
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: 93.30 E-value: 3.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 434 EFTDATYSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKG-SVAYVSQQAWIQNC--I 510
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkDLTKLSLKELRRKVglV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 511 LQ------VN------ILFG----SIMKKEFYE---QVLEACALLPDLEQLPKgdqteigergvNISGGQQHRVSLARAV 571
Cdd:cd03225 81 FQnpddqfFGptveeeVAFGlenlGLPEEEIEErveEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74136409 572 YSGADIYLLDDPLSAVDVHVGKQLFEKVIGslglLKN--KTRILVTHNL-TLLPQMDLIVVMESGR 634
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKK----LKAegKTIIIVTHDLdLLLELADRVIVLEDGK 211
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
433-645 |
4.06e-21 |
|
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: 93.90 E-value: 4.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNKtGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKG-------------SVAY 499
Cdd:cd03295 1 IEFENVTKRYGG-GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 500 VSQQAW------IQNCILQVNILFGsIMKKEFYEQVLEACALLpDLeqlpkgDQTEIGER-GVNISGGQQHRVSLARAVY 572
Cdd:cd03295 80 VIQQIGlfphmtVEENIALVPKLLK-WPKEKIRERADELLALV-GL------DPAEFADRyPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74136409 573 SGADIYLLDDPLSAVDVHVGKQLFEKVIgSLGLLKNKTRILVTHNL-TLLPQMDLIVVMESGRIAQMGTYQELL 645
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFK-RLQQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1047-1269 |
5.98e-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: 98.44 E-value: 5.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1047 VVEFINYQARYRDELGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVE---RAGGKIIIDGIDISTIGLHDLRG 1123
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1124 KLNIIPQHP--VLFSGTL--QMNLDPLNKYSDS-----KLWEALELCHLKEFVQSLPeklrHEiseggenLSMGQRQLVC 1194
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVgdQIAEALENLGLSRaearaRVLELLEAVGLERRLDRYP----HQ-------LSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1195 LARALLRKTKILILDEATASIDFETDKLVQTTIRK--EFSDCTILTIAHRLQSIID-SDRVLVLDSGSIVE-------FE 1264
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEdgppeeiLA 232
|
....*
gi 74136409 1265 APQNL 1269
Cdd:COG1123 233 APQAL 237
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
433-637 |
7.72e-21 |
|
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: 92.53 E-value: 7.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSW--NKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKG--------SVAYVSQ 502
Cdd:cd03293 1 LEVRNVSKTYggGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepvtgpgpDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 503 QA----WiqnciLQV--NILFG----SIMKKEFYEQVLEACAL--LPDLEQL-PKgdqteigergvNISGGQQHRVSLAR 569
Cdd:cd03293 81 QDallpW-----LTVldNVALGlelqGVPKAEARERAEELLELvgLSGFENAyPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74136409 570 AVYSGADIYLLDDPLSAVDVHVGKQLFEKVigsLGLLK--NKTRILVTHNLT---LLPqmDLIVVMES--GRIAQ 637
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEEL---LDIWRetGKTVLLVTHDIDeavFLA--DRVVVLSArpGRIVA 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1064-1267 |
1.40e-20 |
|
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: 92.26 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTL---SNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKLNIIPQHPVLFSG-TL 1139
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLircINGLERPTSGSVLVDGTDLTLLSGKELRKARRRIGMIFQHFNLLSSrTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1140 QMNLD-PL------NKYSDSKLWEALELCHLKEFVQSLPEklrheiseggeNLSMGQRQLVCLARALLRKTKILILDEAT 1212
Cdd:cd03258 100 FENVAlPLeiagvpKAEIEERVLELLELVGLEDKADAYPA-----------QLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74136409 1213 ASIDFETDKLVQT---TIRKEFsDCTILTIAHRLQSIID-SDRVLVLDSGSIVE-------FEAPQ 1267
Cdd:cd03258 169 SALDPETTQSILAllrDINREL-GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEegtveevFANPQ 233
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
430-636 |
2.62e-20 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 92.07 E-value: 2.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 430 DHAIEFTDA--TYSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGeMEKLT-GVVQRKG--------SVA 498
Cdd:COG1116 5 APALELRGVskRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAG-LEKPTsGEVLVDGkpvtgpgpDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 499 YVSQQA----WiqnciLQV--NILFG----SIMKKEFYEQVLEACAL--LPDLEQ-LPKgdqteigergvNISGGQQHRV 565
Cdd:COG1116 84 VVFQEPallpW-----LTVldNVALGlelrGVPKAERRERARELLELvgLAGFEDaYPH-----------QLSGGMRQRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 566 SLARAVYSGADIYLLDDPLSAVDVHVGKQLFEKVigsLGLLK--NKTRILVTHNLT---LLPqmDLIVVMES--GRIA 636
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDALTRERLQDEL---LRLWQetGKTVLFVTHDVDeavFLA--DRVVVLSArpGRIV 220
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
438-650 |
3.67e-20 |
|
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: 91.40 E-value: 3.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 438 ATYSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILG-----------EMEKLTGVVQRK--GSVAYVSQQA 504
Cdd:COG1124 9 VSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGlerpwsgevtfDGRPVTRRRRKAfrRRVQMVFQDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 505 W--------IQNCILQVNILFGSIMKKEFYEQVLEACALLPDL-----EQLpkgdqteigergvniSGGQQHRVSLARAV 571
Cdd:COG1124 89 YaslhprhtVDRILAEPLRIHGLPDREERIAELLEQVGLPPSFldrypHQL---------------SGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 572 YSGADIYLLDDPLSAVDVHVGKQ---LFEKVIGSLGLlknkTRILVTHNLTLLPQM-DLIVVMESGRIAQMGTYQELLSK 647
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEilnLLKDLREERGL----TYLFVSHDLAVVAHLcDRVAVMQNGRIVEELTVADLLAG 229
|
...
gi 74136409 648 TRN 650
Cdd:COG1124 230 PKH 232
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
448-650 |
5.42e-20 |
|
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: 90.48 E-value: 5.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 448 PVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILG-----------EMEKLTGVVQRKGSVAYVSQQ-AWIQNCILQVNI 515
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGlerpdsgtilfGGEDATDVPVQERNVGFVFQHyALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 516 LFGSIMKK--------EFYEQVLEacalLPDLEQLPKgdqteIGERGVN-ISGGQQHRVSLARAVYSGADIYLLDDPLSA 586
Cdd:cd03296 96 AFGLRVKPrserppeaEIRAKVHE----LLKLVQLDW-----LADRYPAqLSGGQRQRVALARALAVEPKVLLLDEPFGA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 587 VDVHVGKQL---FEKVIGSLGLlknkTRILVTHNLT-LLPQMDLIVVMESGRIAQMGTYQELLSKTRN 650
Cdd:cd03296 167 LDAKVRKELrrwLRRLHDELHV----TTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYDHPAS 230
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
449-650 |
5.43e-20 |
|
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: 90.47 E-value: 5.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 449 VLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILG-----------EMEKLTGVVQRKGSVAYVSQQ-AWIQNCILQVNIL 516
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGfikpdsgkillNGKDITNLPPEKRDISYVPQNyALFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 517 FG----SIMKKEFYEQVLEACALLPDLEQLPKGDQTeigergvnISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVhvg 592
Cdd:cd03299 94 YGlkkrKVDKKEIERKVLEIAEMLGIDHLLNRKPET--------LSGGEQQRVAIARALVVNPKILLLDEPFSALDV--- 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74136409 593 kQLFEKVIGSLGLLKNK---TRILVTHNLTLLPQM-DLIVVMESGRIAQMGTYQELLSKTRN 650
Cdd:cd03299 163 -RTKEKLREELKKIRKEfgvTVLHVTHDFEEAWALaDKVAIMLNGKLIQVGKPEEVFKKPKN 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1048-1282 |
5.71e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 91.62 E-value: 5.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1048 VEFINYqaRYRDELGLALQDITFQTHGEEKIGIVGRTGAGKSTLS---NCLFRiVERAGGKIIIDGIDISTIglHDLRGK 1124
Cdd:PRK13635 8 VEHISF--RYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAkllNGLLL-PEAGTITVGGMVLSEETV--WDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1125 LNIIPQHP-VLFSGT---------LQMNLDPLNKYSDsKLWEALELCHLKEFVQSLPEKLrheiseggenlSMGQRQLVC 1194
Cdd:PRK13635 83 VGMVFQNPdNQFVGAtvqddvafgLENIGVPREEMVE-RVDQALRQVGMEDFLNREPHRL-----------SGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1195 LARALLRKTKILILDEATASIDFETDKLVQTTIR--KEFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQNLIRQ 1272
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
250
....*....|
gi 74136409 1273 KGLFYEMTTD 1282
Cdd:PRK13635 231 GHMLQEIGLD 240
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
448-647 |
9.99e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 94.89 E-value: 9.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 448 PVLKDLNIKIPEGALVAVVGQVGSGKSSmLS------------AILGEMEKLTGVVQR--KGSVAYVSQQAWIQNCILQV 513
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKST-LArllfrfydvtsgRILIDGQDIRDVTQAslRAAIGIVPQDTVLFNDTIAY 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 514 NILFGSI-MKKEFYEQVLEACALLPDLEQLPKGDQTEIGERGVNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVg 592
Cdd:COG5265 451 NIAYGRPdASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT- 529
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 74136409 593 kqlfEKVI-GSLGLL-KNKTRILVTHNLTLLPQMDLIVVMESGRIAQMGTYQELLSK 647
Cdd:COG5265 530 ----ERAIqAALREVaRGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQ 582
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
433-648 |
1.07e-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: 89.48 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNktGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSVAYVSQQAWIQNCILQ 512
Cdd:cd03261 1 IELRGLTKSFG--GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 513 VNILFGSimkkefyeqvleaCALLPDL-------------EQLPKGDQTEI--------GERGV------NISGGQQHRV 565
Cdd:cd03261 79 MGMLFQS-------------GALFDSLtvfenvafplrehTRLSEEEIREIvlekleavGLRGAedlypaELSGGMKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 566 SLARAVYSGADIYLLDDPLSAVDvHVGKQLFEKVIGSLGLLKNKTRILVTHNL-TLLPQMDLIVVMESGRIAQMGTYQEL 644
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLD-PIASGVIDDLIRSLKKELGLTSIMVTHDLdTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
....
gi 74136409 645 LSKT 648
Cdd:cd03261 225 RASD 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
432-644 |
1.50e-19 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 91.70 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 432 AIEFTDATYSWNKTgmPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILG-EM----------EKLTGVV--QRKgsVA 498
Cdd:COG3842 5 ALELENVSKRYGDV--TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGfETpdsgrilldgRDVTGLPpeKRN--VG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 499 YVSQ-----------QawiqncilqvNILFGSIMKK----EFYEQVLEACALLpDLEQLpkgdqteiGERGVN-ISGGQQ 562
Cdd:COG3842 81 MVFQdyalfphltvaE----------NVAFGLRMRGvpkaEIRARVAELLELV-GLEGL--------ADRYPHqLSGGQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 563 HRVSLARAVYSGADIYLLDDPLSAVDVHVGKQL-FE--KVIGSLGLlknkTRILVTHN----LTLlpqMDLIVVMESGRI 635
Cdd:COG3842 142 QRVALARALAPEPRVLLLDEPLSALDAKLREEMrEElrRLQRELGI----TFIYVTHDqeeaLAL---ADRIAVMNDGRI 214
|
....*....
gi 74136409 636 AQMGTYQEL 644
Cdd:COG3842 215 EQVGTPEEI 223
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1064-1271 |
1.55e-19 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 89.48 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKLNIIPQHPvlfSGTL--QM 1141
Cdd:COG1124 20 VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDP---YASLhpRH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1142 NLD-----PLN----KYSDSKLWEALELCHLKEfvqSLPEKLRHEiseggenLSMGQRQLVCLARALLRKTKILILDEAT 1212
Cdd:COG1124 97 TVDrilaePLRihglPDREERIAELLEQVGLPP---SFLDRYPHQ-------LSGGQRQRVAIARALILEPELLLLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 1213 ASIDFetdkLVQ-------TTIRKEFsDCTILTIAHRLQsIID--SDRVLVLDSGSIVEFEAPQNLIR 1271
Cdd:COG1124 167 SALDV----SVQaeilnllKDLREER-GLTYLFVSHDLA-VVAhlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
433-639 |
1.93e-19 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 88.08 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNKTgmPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGeMEKLTG------------VVQRKGSVAYV 500
Cdd:cd03301 1 VELENVTKRFGNV--TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAG-LEEPTSgriyiggrdvtdLPPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 501 SQQ-AWIQNCILQVNILFGSIMKK----EFYEQVLEACALLpDLEQL----PKgdqteigergvNISGGQQHRVSLARAV 571
Cdd:cd03301 78 FQNyALYPHMTVYDNIAFGLKLRKvpkdEIDERVREVAELL-QIEHLldrkPK-----------QLSGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74136409 572 YSGADIYLLDDPLSAVDVHVGKQLFEKvIGSLGLLKNKTRILVTHNLTLLPQM-DLIVVMESGRIAQMG 639
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKLRVQMRAE-LKRLQQRLGTTTIYVTHDQVEAMTMaDRIAVMNDGQIQQIG 213
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1062-1267 |
3.29e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 93.33 E-value: 3.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1062 GLALQDITFQT-HGE-------------EKIGIVGRTGAGKSTLsnclFRiveraggkiiidgidiS----------TIG 1117
Cdd:COG4178 362 ALALEDLTLRTpDGRplledlslslkpgERLLITGPSGSGKSTL----LR----------------AiaglwpygsgRIA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1118 LHDLRGKLnIIPQHPVLFSGTLQMNL---DPLNKYSDSKLWEALELCHLKEFVQSLpeklrHEISEGGENLSMGQRQLVC 1194
Cdd:COG4178 422 RPAGARVL-FLPQRPYLPLGTLREALlypATAEAFSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLA 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74136409 1195 LARALLRKTKILILDEATASIDFETDKLVQTTIRKEFSDCTILTIAHRlQSIID-SDRVLVLDSGSIVEFEAPQ 1267
Cdd:COG4178 496 FARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR-STLAAfHDRVLELTGDGSWQLLPAE 568
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
439-635 |
3.63e-19 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 87.95 E-value: 3.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 439 TYSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILG-----------EMEKLTGVVQ-----RKGSVAYVSQ 502
Cdd:cd03257 10 SFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGllkptsgsiifDGKDLLKLSRrlrkiRRKEIQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 503 QAW--------IQNCILQVNILFGSIMKKEFYEQV--LEACALLPD---LEQLPkgDQteigergvnISGGQQHRVSLAR 569
Cdd:cd03257 90 DPMsslnprmtIGEQIAEPLRIHGKLSKKEARKEAvlLLLVGVGLPeevLNRYP--HE---------LSGGQRQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74136409 570 AVYSGADIYLLDDPLSAVDVHVGKQLfekvigsLGLLK------NKTRILVTHNLTLLPQM-DLIVVMESGRI 635
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQI-------LDLLKklqeelGLTLLFITHDLGVVAKIaDRVAVMYAGKI 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
450-585 |
9.28e-19 |
|
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: 84.24 E-value: 9.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 450 LKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKG-------------SVAYVSQQAWIQNcILQV--N 514
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslrkEIGYVFQDPQLFP-RLTVreN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74136409 515 ILFG----SIMKKEFYEQVLEACALLPDLEQLPkgdqTEIGERGVNISGGQQHRVSLARAVYSGADIYLLDDPLS 585
Cdd:pfam00005 80 LRLGlllkGLSKREKDARAEEALEKLGLGDLAD----RPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1047-1271 |
2.47e-18 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 85.91 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1047 VVEFINYQARYRDELglALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAggkiiidgidiS---TIGLHDLRG 1123
Cdd:COG1121 6 AIELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPT-----------SgtvRLFGKPPRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1124 KLNII---PQH-------PVLFSGTLQMNLDP-------LNKYSDSKLWEALELCHLKEFvqslpekLRHEISEggenLS 1186
Cdd:COG1121 73 ARRRIgyvPQRaevdwdfPITVRDVVLMGRYGrrglfrrPSRADREAVDEALERVGLEDL-------ADRPIGE----LS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1187 MGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTI---RKEfsDCTILTIAHRLQSIID-SDRVLVLD-----S 1257
Cdd:COG1121 142 GGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLrelRRE--GKTILVVTHDLGAVREyFDRVLLLNrglvaH 219
|
250
....*....|....
gi 74136409 1258 GSIVEFEAPQNLIR 1271
Cdd:COG1121 220 GPPEEVLTPENLSR 233
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
432-635 |
3.97e-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: 3.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 432 AIEFTDATYSWN--KTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSaILGEMEKLT-GVVQ---------------- 492
Cdd:COG1136 4 LLELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILGGLDRPTsGEVLidgqdisslserelar 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 493 -RKGSVAYVSQQ--------AWiQNCILQvnILFGSIMKKEFYEQVLEAcallpdLEQLpkgdqtEIGERGVN----ISG 559
Cdd:COG1136 83 lRRRHIGFVFQFfnllpeltAL-ENVALP--LLLAGVSRKERRERAREL------LERV------GLGDRLDHrpsqLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 560 GQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGKQLFEkvigslgLLK------NKTRILVTHNLTLLPQMDLIVVMESG 633
Cdd:COG1136 148 GQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLE-------LLRelnrelGTTIVMVTHDPELAARADRVIRLRDG 220
|
..
gi 74136409 634 RI 635
Cdd:COG1136 221 RI 222
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1065-1261 |
5.51e-18 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 82.87 E-value: 5.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKLNIIPQhpvlfsgtlqmnld 1144
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ-------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1145 plnkysdsklweALELCHLKEFVQSlpeklrhEISEggenLSMGQRQLVCLARALLRKTKILILDEATASIDF----ETD 1220
Cdd:cd03214 81 ------------ALELLGLAHLADR-------PFNE----LSGGERQRVLLARALAQEPPILLLDEPTSHLDIahqiELL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 74136409 1221 KLVQTTIRKEfsDCTILTIAHRL-QSIIDSDRVLVLDSGSIV 1261
Cdd:cd03214 138 ELLRRLARER--GKTVVMVLHDLnLAARYADRVILLKDGRIV 177
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
864-1293 |
6.09e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 90.42 E-value: 6.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 864 IIGALPLFILgiIPsvffyfsIQRYYVassRQIRRLT--GASRS-PVISHFSETLSGVSTIRAFGHQQRFIQQYKEVVNE 940
Cdd:PLN03232 444 LFGSLILFLL--IP-------LQTLIV---RKMRKLTkeGLQWTdKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNE 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 941 NLVCFYNNVISNRWLSVRLEFLGNLMVLFAALLAVLAGNSIDSATVGLSISYALNITHSLNFWVKKACEIETNAVAVERV 1020
Cdd:PLN03232 512 ELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRI 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1021 ceyENMDKEAPWIMSRRPPLQwPNKGVVEFINYQARYRDEL-GLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIV 1099
Cdd:PLN03232 592 ---EELLLSEERILAQNPPLQ-PGAPAISIKNGYFSWDSKTsKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGEL 667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1100 ERAGGKIIidgidistiglhDLRGKLNIIPQHPVLFSGTLQMNLDPLNKYSDSKLWEALELCHLKEFVQSLPEKLRHEIS 1179
Cdd:PLN03232 668 SHAETSSV------------VIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIG 735
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1180 EGGENLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLV-QTTIRKEFSDCTILTIAHRLQSIIDSDRVLVLDSG 1258
Cdd:PLN03232 736 ERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEG 815
|
410 420 430
....*....|....*....|....*....|....*
gi 74136409 1259 SIVEFEAPQNLIRQKGLFYEMTTDAGITQESGTEK 1293
Cdd:PLN03232 816 MIKEEGTFAELSKSGSLFKKLMENAGKMDATQEVN 850
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
449-644 |
6.64e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 87.08 E-value: 6.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 449 VLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGeMEKLT-GVVQRKGSvaYVSQQAwIQN---CI------------LQ 512
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAG-LEKPTeGQIFIDGE--DVTHRS-IQQrdiCMvfqsyalfphmsLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 513 VNILFGSIM----KKEFYEQVLEACALLpDLEQLpkgdqteiGERGVN-ISGGQQHRVSLARAVYSGADIYLLDDPLSAV 587
Cdd:PRK11432 97 ENVGYGLKMlgvpKEERKQRVKEALELV-DLAGF--------EDRYVDqISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 588 DVHVGKQLFEKvIGSLGLLKNKTRILVTHNLT-LLPQMDLIVVMESGRIAQMGTYQEL 644
Cdd:PRK11432 168 DANLRRSMREK-IRELQQQFNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1064-1274 |
6.91e-18 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 84.52 E-value: 6.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRiVERAGGKIIIDGIDISTIGLHDLRGKLNIIPQHPVLFSG-TLQMN 1142
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAG-LLKPDSGSILIDGEDVRKEPREARRQIGVLPDERGLYDRlTVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1143 LD---PLNKYSDSKLWEALElchlkEFVQSLpeKLRHEISEGGENLSMGQRQLVCLARALLRKTKILILDEATASIDFET 1219
Cdd:COG4555 95 IRyfaELYGLFDEELKKRIE-----ELIELL--GLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 1220 DKLVQTTIR--KEfSDCTILTIAHRLQSIID-SDRVLVLDSGSIVEFEAPQNLIRQKG 1274
Cdd:COG4555 168 RRLLREILRalKK-EGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
448-635 |
8.55e-18 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 82.45 E-value: 8.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 448 PVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVqrkgsvayvsqqawiqncilqvnILFGSIMKKEFyE 527
Cdd:cd03230 14 TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEI-----------------------KVLGKDIKKEP-E 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 528 QVLEACALLPDLEQLPkgdQTEIGERGVNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVhVGKQLFEKVIGSLGlLK 607
Cdd:cd03230 70 EVKRRIGYLPEEPSLY---ENLTVRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP-ESRREFWELLRELK-KE 144
|
170 180
....*....|....*....|....*....
gi 74136409 608 NKTRILVTHNLTLLPQM-DLIVVMESGRI 635
Cdd:cd03230 145 GKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
433-651 |
8.58e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 86.92 E-value: 8.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNKTgmPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGeMEKLT-GVVQRKG-SVAYVSQQAWIQNCI 510
Cdd:PRK09452 15 VELRGISKSFDGK--EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAG-FETPDsGRIMLDGqDITHVPAENRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 511 LQV-----------NILFGSIMKK----EFYEQVLEACALLpDLEQLpkgdqteiGERGV-NISGGQQHRVSLARAVYSG 574
Cdd:PRK09452 92 FQSyalfphmtvfeNVAFGLRMQKtpaaEITPRVMEALRMV-QLEEF--------AQRKPhQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 575 ADIYLLDDPLSAVDVHVGKQL---FEKVIGSLGLlknkTRILVTHN----LTLlpqMDLIVVMESGRIAQMGTYQELLSK 647
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMqneLKALQRKLGI----TFVFVTHDqeeaLTM---SDRIVVMRDGRIEQDGTPREIYEE 235
|
....
gi 74136409 648 TRNL 651
Cdd:PRK09452 236 PKNL 239
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1056-1256 |
9.87e-18 |
|
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: 83.35 E-value: 9.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1056 RYRDELglALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLfriveraggkiiidgidistIGLHDL-RGKLNI------- 1127
Cdd:cd03235 8 SYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAI--------------------LGLLKPtSGSIRVfgkplek 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1128 -------IPQH-------PVLFSGTLQMNLDP-------LNKYSDSKLWEALELCHLKEFVQslpeklrHEISEggenLS 1186
Cdd:cd03235 66 erkrigyVPQRrsidrdfPISVRDVVLMGLYGhkglfrrLSKADKAKVDEALERVGLSELAD-------RQIGE----LS 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74136409 1187 MGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTIRK-EFSDCTILTIAHRLQSIIDS-DRVLVLD 1256
Cdd:cd03235 135 GGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYfDRVLLLN 206
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
450-639 |
1.07e-17 |
|
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: 83.11 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 450 LKDLNIKIP---EGALVAVVGQVGSGKSSMLSAILGeMEKLT-------GVV-------------QRKgsVAYVSQQ-AW 505
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAG-LEKPDggtivlnGTVlfdsrkkinlppqQRK--IGLVFQQyAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 506 IQNCILQVNILFG-----SIMKKEFYEQVLEACALlpdleqlpkgdqTEIGERGV-NISGGQQHRVSLARAVYSGADIYL 579
Cdd:cd03297 87 FPHLNVRENLAFGlkrkrNREDRISVDELLDLLGL------------DHLLNRYPaQLSGGEKQRVALARALAAQPELLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74136409 580 LDDPLSAVDVHVGKQLfEKVIGSLGLLKNKTRILVTHNLTLLPQM-DLIVVMESGRIAQMG 639
Cdd:cd03297 155 LDEPFSALDRALRLQL-LPELKQIKKNLNIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
774-965 |
1.32e-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: 84.91 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 774 IYGILGLIKGLFVCSGAYVITRGSLAASRTMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDmrlhyylRLWVNC 853
Cdd:cd07346 44 LLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQ-------NLVSSG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 854 TLDVIGTILVIIGAL--------PLFILGIIPSVFFYFSIQRYyvasSRQIRRLTGASR---SPVISHFSETLSGVSTIR 922
Cdd:cd07346 117 LLQLLSDVLTLIGALvilfylnwKLTLVALLLLPLYVLILRYF----RRRIRKASREVReslAELSAFLQESLSGIRVVK 192
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 74136409 923 AFGHQQRFIQQYKEVVNENLVCFYNNVISNRWLSVRLEFLGNL 965
Cdd:cd07346 193 AFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTAL 235
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1065-1259 |
1.53e-17 |
|
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: 82.76 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDL----RGKLNIIPQHPVLFSGTLQ 1140
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1141 MNL---DPLNKYSDSKLWEAlelCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRKTKILILDEATASIDF 1217
Cdd:cd03290 97 ENItfgSPFNKQRYKAVTDA---CSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 74136409 1218 E-TDKLVQTTIRKEFSD--CTILTIAHRLQSIIDSDRVLVLDSGS 1259
Cdd:cd03290 174 HlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
449-644 |
1.95e-17 |
|
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: 83.00 E-value: 1.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 449 VLKDLNIKIPEGALVAVVGQVGSGKSSMLSAI-----LGEMEKLTGVVQRKGSVAYvsqqAWIQNCIL---QVNILF--- 517
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIY----DLDVDVLElrrRVGMVFqkp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 518 ----GSIM--------------KKEFYEQVLEAC--ALLPDleqlpkgdqtEIGER--GVNISGGQQHRVSLARAVYSGA 575
Cdd:cd03260 91 npfpGSIYdnvayglrlhgiklKEELDERVEEALrkAALWD----------EVKDRlhALGLSGGQQQRLCLARALANEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74136409 576 DIYLLDDPLSAVDVhVGKQLFEKVIGSLGllKNKTRILVTHNltlLPQM----DLIVVMESGRIAQMGTYQEL 644
Cdd:cd03260 161 EVLLLDEPTSALDP-ISTAKIEELIAELK--KEYTIVIVTHN---MQQAarvaDRTAFLLNGRLVEFGPTEQI 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
430-654 |
3.12e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 83.26 E-value: 3.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 430 DHAIEFTDATYSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGeMEKLTgvvqrKGSVAYVSQQAWIQN- 508
Cdd:PRK13648 5 NSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIG-IEKVK-----SGEIFYNNQAITDDNf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 509 --------------------CILQVNILFG----SIMKKEFYEQVLEAcalLPDLEQLPKGDQTEigergVNISGGQQHR 564
Cdd:PRK13648 79 eklrkhigivfqnpdnqfvgSIVKYDVAFGlenhAVPYDEMHRRVSEA---LKQVDMLERADYEP-----NALSGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 565 VSLARAVYSGADIYLLDDPLSAVDVHVGKQLFEkVIGSLGLLKNKTRILVTHNLTLLPQMDLIVVMESGRIAQMGTYQEL 644
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNLLD-LVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
250
....*....|
gi 74136409 645 LSKTRNLTNL 654
Cdd:PRK13648 230 FDHAEELTRI 239
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
433-646 |
3.64e-17 |
|
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: 86.50 E-value: 3.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWN---KTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILG--------------EMEKLTGVVQRK- 494
Cdd:COG1123 261 LEVRNLSKRYPvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGllrptsgsilfdgkDLTKLSRRSLREl 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 495 -GSVAYVSQQAW--------IQNCILQVNILFGSIMKKEFYEQV---LEACALLPD-LEQLPkgdqteiGErgvnISGGQ 561
Cdd:COG1123 341 rRRVQMVFQDPYsslnprmtVGDIIAEPLRLHGLLSRAERRERVaelLERVGLPPDlADRYP-------HE----LSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 562 QHRVSLARAVYSGADIYLLDDPLSAVDVHVGKQLfekvigsLGLLK------NKTRILVTHNLTLLPQM-DLIVVMESGR 634
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQI-------LNLLRdlqrelGLTYLFISHDLAVVRYIaDRVAVMYDGR 482
|
250
....*....|..
gi 74136409 635 IAQMGTYQELLS 646
Cdd:COG1123 483 IVEDGPTEEVFA 494
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
446-644 |
4.08e-17 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 81.90 E-value: 4.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 446 GMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILG-----------EMEKLTGVVQRKGSVAYVSQQ-AWIQNCILQV 513
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGfetptsgeillDGKDITNLPPHKRPVNTVFQNyALFPHLTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 514 NILFGSIMKK----EFYEQVLEACALLpDLEQLPKGDQTEIgergvniSGGQQHRVSLARAVYSGADIYLLDDPLSAVDV 589
Cdd:cd03300 92 NIAFGLRLKKlpkaEIKERVAEALDLV-QLEGYANRKPSQL-------SGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74136409 590 HVGKQL---FEKVIGSLGLlknkTRILVTHN----LTLlpqMDLIVVMESGRIAQMGTYQEL 644
Cdd:cd03300 164 KLRKDMqleLKRLQKELGI----TFVFVTHDqeeaLTM---SDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1064-1263 |
7.44e-17 |
|
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: 81.07 E-value: 7.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVEraggkIIIDGIDISTIGLHD------------LRGKLNIIPQH 1131
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLND-----LIPGAPDEGEVLLDGkdiydldvdvleLRRRVGMVFQK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1132 PVLFSGTLQMNLD---PLNKYSDSKLW-----EALELCHLKEFVqslpeKLRheisEGGENLSMGQRQLVCLARALLRKT 1203
Cdd:cd03260 90 PNPFPGSIYDNVAyglRLHGIKLKEELderveEALRKAALWDEV-----KDR----LHALGLSGGQQQRLCLARALANEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74136409 1204 KILILDEATASIDFETDKLVQTTIRKEFSDCTILTIAHRLQSIID-SDRVLVLDSGSIVEF 1263
Cdd:cd03260 161 EVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEF 221
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
433-644 |
1.33e-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: 80.69 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNkTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVV----------------QRKGS 496
Cdd:cd03256 1 IEVENLSKTYP-NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVlidgtdinklkgkalrQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 497 VAYVSQQawiQNCILQV----NILFGSIMKKEFY---------EQVLEACALLPDLEQLPKGDQteigeRGVNISGGQQH 563
Cdd:cd03256 80 IGMIFQQ---FNLIERLsvleNVLSGRLGRRSTWrslfglfpkEEKQRALAALERVGLLDKAYQ-----RADQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 564 RVSLARAVYSGADIYLLDDPLSAVDVHVGKQLfekvigsLGLLKnktRILVTHNLTL---LPQMDL-------IVVMESG 633
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQV-------MDLLK---RINREEGITVivsLHQVDLareyadrIVGLKDG 221
|
250
....*....|.
gi 74136409 634 RIAQMGTYQEL 644
Cdd:cd03256 222 RIVFDGPPAEL 232
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
433-648 |
1.63e-16 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 80.49 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNKTgmPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVV------------QRKGSVAYV 500
Cdd:COG1131 1 IEVRGLTKRYGDK--TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrvlgedvardpaEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 501 SQQAWIQN--CILQVNILFGSIMK------KEFYEQVLEACALLPDLEQLPKgdqteigergvNISGGQQHRVSLARAVY 572
Cdd:COG1131 79 PQEPALYPdlTVRENLRFFARLYGlprkeaRERIDELLELFGLTDAADRKVG-----------TLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74136409 573 SGADIYLLDDPLSAVDVhVGKQLFEKVIGSLGlLKNKTRILVTHNLTLLPQM-DLIVVMESGRIAQMGTYQELLSKT 648
Cdd:COG1131 148 HDPELLILDEPTSGLDP-EARRELWELLRELA-AEGKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKARL 222
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
433-646 |
1.77e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 80.52 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNKTgmPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAIlGEMEKLTG---------VVQRKGSVAYVSQQ 503
Cdd:PRK09493 2 IEFKNVSKHFGPT--QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCI-NKLEEITSgdlivdglkVNDPKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 504 AWI---------QNCILQvNILFGSI----MKKEFYEQVleACALLpdleqlpkgDQTEIGERG----VNISGGQQHRVS 566
Cdd:PRK09493 79 AGMvfqqfylfpHLTALE-NVMFGPLrvrgASKEEAEKQ--ARELL---------AKVGLAERAhhypSELSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 567 LARAVYSGADIYLLDDPLSAVDVHVGKQLFeKVIGSL---GLlknkTRILVTHNLTLLPQM-DLIVVMESGRIAQMGTYQ 642
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPELRHEVL-KVMQDLaeeGM----TMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQ 221
|
....
gi 74136409 643 ELLS 646
Cdd:PRK09493 222 VLIK 225
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1064-1261 |
1.99e-16 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 77.85 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFriveraggkiiidgidistiGLHdlrgklniipqHPVlfSGTLQMNL 1143
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILS--------------------GLY-----------KPD--SGEILVDG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1144 DPLNKYSDSKLWEA-LELCHlkefvQslpeklrheiseggenLSMGQRQLVCLARALLRKTKILILDEATASI-DFETDK 1221
Cdd:cd03216 62 KEVSFASPRDARRAgIAMVY-----Q----------------LSVGERQMVEIARALARNARLLILDEPTAALtPAEVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 74136409 1222 LVQT--TIRKEfsDCTILTIAHRLQSIID-SDRVLVLDSGSIV 1261
Cdd:cd03216 121 LFKVirRLRAQ--GVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
433-634 |
4.91e-16 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 77.23 E-value: 4.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNKTgmPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGeMEKLTG--------VVQRKGSVAYVSQQA 504
Cdd:cd03229 1 LELKNVSKRYGQK--TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAG-LEEPDSgsilidgeDLTDLEDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 505 WiqNCILQVNILFgsimkkeFYEQVLEACALLpdleqlpkgdqteigergvnISGGQQHRVSLARAVYSGADIYLLDDPL 584
Cdd:cd03229 78 I--GMVFQDFALF-------PHLTVLENIALG--------------------LSGGQQQRVALARALAMDPDVLLLDEPT 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 74136409 585 SAVDVhVGKQLFEKVIGSLGLLKNKTRILVTHNLTLLPQM-DLIVVMESGR 634
Cdd:cd03229 129 SALDP-ITRREVRALLKSLQAQLGITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
432-639 |
6.38e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.54 E-value: 6.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 432 AIEFTDATYSWnKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQ----------RKGSVAYVS 501
Cdd:PRK15056 6 GIVVNDVTVTW-RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISilgqptrqalQKNLVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 502 QQA---WIQNCILQVNILFGS--------IMKKEFYEQVLEACALLPDLEQLPKgdqtEIGErgvnISGGQQHRVSLARA 570
Cdd:PRK15056 85 QSEevdWSFPVLVEDVVMMGRyghmgwlrRAKKRDRQIVTAALARVDMVEFRHR----QIGE----LSGGQKKRVFLARA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74136409 571 VYSGADIYLLDDPLSAVDVhvgkQLFEKVIGSLGLLKN--KTRILVTHNLTLLPQMDLIVVMESGRIAQMG 639
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDV----KTEARIISLLRELRDegKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1060-1261 |
1.53e-15 |
|
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: 76.91 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1060 ELGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAggkiiidgidISTIGLH-------DLRGKLNIIPQHP 1132
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKES----------SGSILLNgkpikakERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1133 --VLFSGTLQMNLDPLNKYSDSKLWEA---LELCHLKEFvqslpeKLRHEISeggenLSMGQRQLVCLARALLRKTKILI 1207
Cdd:cd03226 81 dyQLFTDSVREELLLGLKELDAGNEQAetvLKDLDLYAL------KERHPLS-----LSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 74136409 1208 LDEATASIDFETDKLVQTTIRKEFS-DCTILTIAHRLQSIID-SDRVLVLDSGSIV 1261
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1056-1272 |
1.77e-15 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 77.41 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1056 RYRDelGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCL---------------FRIVERAggkiiidgidistiglHD 1120
Cdd:COG1131 9 RYGD--KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLlgllrptsgevrvlgEDVARDP----------------AE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1121 LRGKLNIIPQHPVLFSG-TLQMNLD------PLNK-YSDSKLWEALELCHLKEFVQSLPEKlrheiseggenLSMGQRQL 1192
Cdd:COG1131 71 VRRRIGYVPQEPALYPDlTVRENLRffarlyGLPRkEARERIDELLELFGLTDAADRKVGT-----------LSGGMKQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1193 VCLARALLRKTKILILDEATASIDFETDKLVQTTIRKEFSD-CTILTIAHRLQSIID-SDRVLVLDSGSIVEFEAPQNLI 1270
Cdd:COG1131 140 LGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELK 219
|
..
gi 74136409 1271 RQ 1272
Cdd:COG1131 220 AR 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1065-1270 |
2.59e-15 |
|
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: 77.39 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKLNIIPQHPVL-FSGTL---- 1139
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPPApFGLTVrelv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1140 -------QMNLDPLNKYSDSKLWEALELCHLkefvqslpEKLRH-EISEggenLSMGQRQLVCLARALLRKTKILILDEA 1211
Cdd:COG1120 97 algryphLGLFGRPSAEDREAVEEALERTGL--------EHLADrPVDE----LSGGERQRVLIARALAQEPPLLLLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74136409 1212 TASIDF----ETDKLVQTTIRKEfsDCTILTIAHRL-QSIIDSDRVLVLDSGSIVEFEAPQNLI 1270
Cdd:COG1120 165 TSHLDLahqlEVLELLRRLARER--GRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1048-1260 |
3.49e-15 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 74.74 E-value: 3.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1048 VEFINYQARYRDelGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVeRAGGKIIIDGIDISTIGLHDLRGKLNI 1127
Cdd:cd03230 1 IEVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLL-KPDSGEIKVLGKDIKKEPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1128 IPQHPVLfsgtlqmnldplnkYSDSKLWEALELchlkefvqslpeklrheiseggenlSMGQRQLVCLARALLRKTKILI 1207
Cdd:cd03230 78 LPEEPSL--------------YENLTVRENLKL-------------------------SGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 74136409 1208 LDEATASIDFETDKLVQTTIRKE-FSDCTILTIAHRLQSIID-SDRVLVLDSGSI 1260
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELkKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
432-645 |
3.56e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 77.34 E-value: 3.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 432 AIEFTDATYSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSS---MLSAIL----GEMeKLTGVVQRKGSVAYVSQQA 504
Cdd:PRK13632 7 MIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTiskILTGLLkpqsGEI-KIDGITISKENLKEIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 505 WI--QNCILQV-------NILFG----SIMKKEFYEQVLEACALLPDLEQLPKGDQteigergvNISGGQQHRVSLARAV 571
Cdd:PRK13632 86 GIifQNPDNQFigatvedDIAFGlenkKVPPKKMKDIIDDLAKKVGMEDYLDKEPQ--------NLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74136409 572 YSGADIYLLDDPLSAVDVHvGKQLFEKVIGSLGLLKNKTRILVTHNLTLLPQMDLIVVMESGRIAQMGTYQELL 645
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPK-GKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
432-644 |
3.90e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 78.59 E-value: 3.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 432 AIEFTDATYSWNKTgmPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGS-----------VAYV 500
Cdd:PRK10851 2 SIEIANIKKSFGRT--QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 501 SQQ-AWIQNCILQVNILFGSIM--------KKEFYEQVLEacalLPDLEQLPkgdqtEIGER-GVNISGGQQHRVSLARA 570
Cdd:PRK10851 80 FQHyALFRHMTVFDNIAFGLTVlprrerpnAAAIKAKVTQ----LLEMVQLA-----HLADRyPAQLSGGQKQRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 571 VYSGADIYLLDDPLSAVDVHVGK-------QLFEKvigslglLKNkTRILVTHNLT-LLPQMDLIVVMESGRIAQMGTYQ 642
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKelrrwlrQLHEE-------LKF-TSVFVTHDQEeAMEVADRVVVMSQGNIEQAGTPD 222
|
..
gi 74136409 643 EL 644
Cdd:PRK10851 223 QV 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
451-644 |
4.33e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 78.53 E-value: 4.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 451 KDLNIKIPEGALVAVVGQVGSGKSSMLSAILGeMEKLTG------------VVQRKGSVAYVSQQ-AWIQNCILQVNILF 517
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAG-LEDITSgdlfigekrmndVPPAERGVGMVFQSyALYPHLSVAENMSF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 518 G----SIMKKEFY---EQVLEACALLPDLEQLPKGdqteigergvnISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVH 590
Cdd:PRK11000 99 GlklaGAKKEEINqrvNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 74136409 591 VGKQL-FEkvIGSLGLLKNKTRILVTHN----LTLlpqMDLIVVMESGRIAQMGTYQEL 644
Cdd:PRK11000 168 LRVQMrIE--ISRLHKRLGRTMIYVTHDqveaMTL---ADKIVVLDAGRVAQVGKPLEL 221
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1044-1273 |
5.08e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 76.95 E-value: 5.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1044 NKGVVEFINYQARYRDELGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRG 1123
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1124 KLNIIPQHP------------VLFSgtLQMNLDPLNKYSDsKLWEALELCHLKEFVQSLPeklrheiseggENLSMGQRQ 1191
Cdd:PRK13632 84 KIGIIFQNPdnqfigatveddIAFG--LENKKVPPKKMKD-IIDDLAKKVGMEDYLDKEP-----------QNLSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1192 LVCLARALLRKTKILILDEATASIDFETDKLVQTTIR--KEFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQNL 1269
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
|
....
gi 74136409 1270 IRQK 1273
Cdd:PRK13632 230 LNNK 233
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
433-655 |
5.22e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 77.13 E-value: 5.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNKtGMP----VLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVV----------------- 491
Cdd:PRK13646 3 IRFDNVSYTYQK-GTPyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVtvdditithktkdkyir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 492 ---QRKGSVAYVSQQAWIQNCIlQVNILFGSIMKKEFYEQVLE-ACALLPDLeqlpkGDQTEIGERG-VNISGGQQHRVS 566
Cdd:PRK13646 82 pvrKRIGMVFQFPESQLFEDTV-EREIIFGPKNFKMNLDEVKNyAHRLLMDL-----GFSRDVMSQSpFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 567 LARAVYSGADIYLLDDPLSAVDVHVGKQLFeKVIGSLGLLKNKTRILVTHNLTLLPQ-MDLIVVMESGRIAQMGTYQELL 645
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVM-RLLKSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELF 234
|
250
....*....|
gi 74136409 646 SKTRNLTNLH 655
Cdd:PRK13646 235 KDKKKLADWH 244
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
433-683 |
5.49e-15 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 76.82 E-value: 5.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILgEMEKLTGVVQRKG-SVAYVSQQAWIQ--NC 509
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvSWNSVPLQKWRKafGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 510 ILQVNILFGSIMKKEF--YEQ--------VLEACALLPDLEQLPKGDQTEIGERGVNISGGQQHRVSLARAVYSGADIYL 579
Cdd:cd03289 82 IPQKVFIFSGTFRKNLdpYGKwsdeeiwkVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 580 LDDPLSAVDvHVGKQLFEKVIGSlgLLKNKTRILVTHNLTLLPQMDLIVVMESGRIAQMGTYQELLSKTrnlTNLHQVIS 659
Cdd:cd03289 162 LDEPSAHLD-PITYQVIRKTLKQ--AFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEK---SHFKQAIS 235
|
250 260
....*....|....*....|....
gi 74136409 660 EEEKAHALKRASAVNSRTRPKDKI 683
Cdd:cd03289 236 PSDRLKLFPRRNSSKSKRKPRPQI 259
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
433-654 |
5.68e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 76.98 E-value: 5.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNKtGMP----VLKDLNIKIPEGALVAVVGQVGSGKSSMLsailgemEKLTGVVQ-RKGSVAyvsqqawIQ 507
Cdd:PRK13634 3 ITFQKVEHRYQY-KTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLL-------QHLNGLLQpTSGTVT-------IG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 508 NCILQ--------------VNILFGSIMKKEFYEQVLEACALLP--------DLEQLPK------GDQTEIGERG-VNIS 558
Cdd:PRK13634 68 ERVITagkknkklkplrkkVGIVFQFPEHQLFEETVEKDICFGPmnfgvseeDAKQKARemielvGLPEELLARSpFELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 559 GGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGKQLFEkVIGSLGLLKNKTRILVTHNLTLLPQ-MDLIVVMESGRIAQ 637
Cdd:PRK13634 148 GGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMME-MFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFL 226
|
250
....*....|....*..
gi 74136409 638 MGTYQELLSKTRNLTNL 654
Cdd:PRK13634 227 QGTPREIFADPDELEAI 243
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
449-635 |
8.21e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 79.38 E-value: 8.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 449 VLKDLNIKIPEGALVAVVGQVGSGKSSMLSaILGEMEKLTG----------------------------VVQRKGSVAYV 500
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDKPTSgtyrvagqdvatldadalaqlrrehfgfIFQRYHLLSHL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 501 SQQawiQNciLQVNILFGSIMKKEFYEQvleACALLPDLeqlpkGDQTEIGERGVNISGGQQHRVSLARAVYSGADIYLL 580
Cdd:PRK10535 102 TAA---QN--VEVPAVYAGLERKQRLLR---AQELLQRL-----GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 74136409 581 DDPLSAVDVHVGkqlfEKVIGSLGLLKNK--TRILVTHNLTLLPQMDLIVVMESGRI 635
Cdd:PRK10535 169 DEPTGALDSHSG----EEVMAILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
118-409 |
8.32e-15 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 76.44 E-value: 8.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 118 LIQVALFKVFADILSFTSPLIMKQMIIFCEHSSDFGWNGYgYAMALFVVVFLQTLI--LQRYqcFNMLTSAKVKTAVNGL 195
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLW-IALLLLLLALLRALLsyLRRY--LAARLGQRVVFDLRRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 196 IYKKALLLSNVSRQKFSTGEIINLMSADAQQLMDL-TANLNLLWSAPFQILMA-IYLLWqeLGPAV-LAGVAVLVFVIPI 272
Cdd:cd07346 78 LFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLvSSGLLQLLSDVLTLIGAlVILFY--LNWKLtLVALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 273 NALAATKIKKLKKSQRKNKDKQIKLLKEILHGIKILKLYAWEpsyKNKIIKIRDQELEFQKSARYLTVFSMLTLTCIPFL 352
Cdd:cd07346 156 LRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAE---EREIERFREANRDLRDANLRAARLSALFSPLIGLL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74136409 353 VSLATLCV-----YFLLDegNILTATKVFTSMSLFNILRIPLFELPTVISTVVQTKISLGRL 409
Cdd:cd07346 233 TALGTALVllyggYLVLQ--GSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1064-1260 |
8.46e-15 |
|
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: 74.83 E-value: 8.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSN---CLFRIVERAGGKIIIDGIDISTIGLHDLRGK-LNIIPQH-------- 1131
Cdd:cd03255 19 ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNilgGLDRPTSGEVRVDGTDISKLSEKELAAFRRRhIGFVFQSfnllpdlt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1132 -------PVLFSGtlqmnldplNKYSDSKLW--EALELCHLKEfvqslpeKLRHEISEggenLSMGQRQLVCLARALLRK 1202
Cdd:cd03255 99 alenvelPLLLAG---------VPKKERRERaeELLERVGLGD-------RLNHYPSE----LSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1203 TKILILDEATASIDFETDKLVQTTIRK--EFSDCTILTIAHRLQSIIDSDRVLVLDSGSI 1260
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1064-1258 |
8.58e-15 |
|
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: 73.76 E-value: 8.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLH--DLRGKLNIIPQHPVLFSgtlqm 1141
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRIGMVFQDFALFP----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1142 nldplnkysdsklwealelcHLKefvqslpekLRHEISEGgenLSMGQRQLVCLARALLRKTKILILDEATASIDFETDK 1221
Cdd:cd03229 90 --------------------HLT---------VLENIALG---LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 74136409 1222 LVQTTIR--KEFSDCTILTIAHRLQSIID-SDRVLVLDSG 1258
Cdd:cd03229 138 EVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
433-647 |
8.79e-15 |
|
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: 75.31 E-value: 8.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDAT--YSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGeMEKLT-----------------GVVQR 493
Cdd:cd03258 2 IELKNVSkvFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING-LERPTsgsvlvdgtdltllsgkELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 494 KGSVAYVSQQawiqncilqVNIL-----FGSIM---------KKEFYEQVLEACALLpDLEQlpKGDQteigeRGVNISG 559
Cdd:cd03258 81 RRRIGMIFQH---------FNLLssrtvFENVAlpleiagvpKAEIEERVLELLELV-GLED--KADA-----YPAQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 560 GQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGKQ---LFEKVIGSLGLlknkTRILVTHnltllpQMDLI-------VV 629
Cdd:cd03258 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTQSilaLLRDINRELGL----TIVLITH------EMEVVkricdrvAV 213
|
250
....*....|....*...
gi 74136409 630 MESGRIAQMGTYQELLSK 647
Cdd:cd03258 214 MEKGEVVEEGTVEEVFAN 231
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1064-1266 |
9.71e-15 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 75.30 E-value: 9.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRG----------KLNIIPQHPV 1133
Cdd:cd03256 16 ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrqigmifqQFNLIERLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1134 L---FSGTL-QMNLDP--LNKYSDSKLWEALELchLKEFvqSLPEKLRHEISEggenLSMGQRQLVCLARALLRKTKILI 1207
Cdd:cd03256 96 LenvLSGRLgRRSTWRslFGLFPKEEKQRALAA--LERV--GLLDKAYQRADQ----LSGGQQQRVAIARALMQQPKLIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74136409 1208 LDEATASIDFETDKLVQ---TTIRKEFSDCTILTIaHRLQSIID-SDRVLVLDSGSIVeFEAP 1266
Cdd:cd03256 168 ADEPVASLDPASSRQVMdllKRINREEGITVIVSL-HQVDLAREyADRIVGLKDGRIV-FDGP 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
446-646 |
1.12e-14 |
|
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: 74.78 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 446 GMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQ---------------RKGsVAYVSQqawiQNCI 510
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRfdgrditglppheraRAG-IGYVPE----GRRI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 511 ---LQV--NILFGS--IMKKEFYEQVLEACALLPDLEQLPKgdqteigERGVNISGGQQHRVSLARAVYSGADIYLLDDP 583
Cdd:cd03224 87 fpeLTVeeNLLLGAyaRRRAKRKARLERVYELFPRLKERRK-------QLAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74136409 584 ---LSAVDVhvgKQLFEKV--IGSLGLlknkTRILVTHNLTLLPQM-DLIVVMESGRIAQMGTYQELLS 646
Cdd:cd03224 160 segLAPKIV---EEIFEAIreLRDEGV----TILLVEQNARFALEIaDRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
443-645 |
1.63e-14 |
|
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: 75.37 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 443 NKTGMPV-LKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQ-----------------RKGSVAYVSQQA 504
Cdd:cd03294 32 KKTGQTVgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLidgqdiaamsrkelrelRRKKISMVFQSF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 505 WI--QNCILQvNILFG----SIMKKEFYE---QVLEACALLPDLEQLPKgdqteigergvNISGGQQHRVSLARAVYSGA 575
Cdd:cd03294 112 ALlpHRTVLE-NVAFGlevqGVPRAEREEraaEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDP 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74136409 576 DIYLLDDPLSAVDVHVGKQLFEKVigsLGLLKN--KTRILVTHNLT-LLPQMDLIVVMESGRIAQMGTYQELL 645
Cdd:cd03294 180 DILLMDEAFSALDPLIRREMQDEL---LRLQAElqKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
437-683 |
1.66e-14 |
|
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: 79.18 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 437 DATYSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILgEMEKLTGVVQRKG-SVAYVSQQAWIQ--NCILQV 513
Cdd:TIGR01271 1222 GLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGvSWNSVTLQTWRKafGVIPQK 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 514 NILFGSIMKKEF--YEQ--------VLEACALLPDLEQLPKGDQTEIGERGVNISGGQQHRVSLARAVYSGADIYLLDDP 583
Cdd:TIGR01271 1301 VFIFSGTFRKNLdpYEQwsdeeiwkVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEP 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 584 LSAVDvHVGKQLFEKVIGSlgLLKNKTRILVTHNLTLLPQMDLIVVMESGRIAQMGTYQELLSKTrnlTNLHQVISEEEK 663
Cdd:TIGR01271 1381 SAHLD-PVTLQIIRKTLKQ--SFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNET---SLFKQAMSAADR 1454
|
250 260
....*....|....*....|
gi 74136409 664 AHALKRASAVNSRTRPKDKI 683
Cdd:TIGR01271 1455 LKLFPLHRRNSSKRKPQPKI 1474
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1044-1275 |
1.81e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 75.17 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1044 NKGVVEFINYQARYRDELGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRG 1123
Cdd:PRK13648 4 KNSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1124 KLNIIPQHP------------VLFSgtLQMNLDPLNKYSdSKLWEALELCHLKEFVQSLPeklrheiseggENLSMGQRQ 1191
Cdd:PRK13648 84 HIGIVFQNPdnqfvgsivkydVAFG--LENHAVPYDEMH-RRVSEALKQVDMLERADYEP-----------NALSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1192 LVCLARALLRKTKILILDEATASIDFETDKLVQTTIR--KEFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQNL 1269
Cdd:PRK13648 150 RVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
....*..
gi 74136409 1270 IR-QKGL 1275
Cdd:PRK13648 230 FDhAEEL 236
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
446-588 |
2.02e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 73.04 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 446 GMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKG--SVAYVSQQawiqncilqvnilfgSIMKK 523
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQR---------------SEVPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 524 EFYEQVLEACAL-----LPDLEQLPKGDQTEIGE------------RGVN-ISGGQQHRVSLARAVYSGADIYLLDDPLS 585
Cdd:NF040873 69 SLPLTVRDLVAMgrwarRGLWRRLTRDDRAAVDDalervgladlagRQLGeLSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
...
gi 74136409 586 AVD 588
Cdd:NF040873 149 GLD 151
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
430-654 |
3.76e-14 |
|
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: 73.58 E-value: 3.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 430 DHAIEFTDATYSWNKTgmPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVV-----QRKGSV------- 497
Cdd:COG1119 1 DPLLELRNVTVRRGGK--TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrlfgERRGGEdvwelrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 498 --AYVSQ--QAWIQNCI--LQVNI--LFGSImkkEFY-----EQVLEACALLPDLEQLPKGDQTeIGErgvnISGGQQHR 564
Cdd:COG1119 79 riGLVSPalQLRFPRDEtvLDVVLsgFFDSI---GLYreptdEQRERARELLELLGLAHLADRP-FGT----LSQGEQRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 565 VSLARAVYSGADIYLLDDPLSAVDVHvGKQLFEKVIGSLGLLKNKTRILVTHNLT-LLPQMDLIVVMESGRIAQMGTYQE 643
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLG-ARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGITHVLLLKDGRVVAAGPKEE 229
|
250
....*....|.
gi 74136409 644 LLSkTRNLTNL 654
Cdd:COG1119 230 VLT-SENLSEA 239
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
448-600 |
4.52e-14 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 72.51 E-value: 4.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 448 PVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKG------------SVAYVSQQ-AWIQNCILQVN 514
Cdd:COG4133 16 LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLAYLGHAdGLKPELTVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 515 ILFGSIMKKEFY--EQVLEACAL--LPDLEQLPKGdqteigergvNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVH 590
Cdd:COG4133 96 LRFWAALYGLRAdrEAIDEALEAvgLAGLADLPVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA 165
|
170
....*....|
gi 74136409 591 vGKQLFEKVI 600
Cdd:COG4133 166 -GVALLAELI 174
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
777-942 |
5.64e-14 |
|
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: 74.00 E-value: 5.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 777 ILGLIKGLFVCSGAYVITRGSLAASRTMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIdmrlhyylRLWVNCTLD 856
Cdd:cd18552 47 GLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQV--------QNALTSALT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 857 VIG----TILVIIGA-------LPLFILGIIPSVFFYFS-IQRYYVASSRQIRRLTGAsrspVISHFSETLSGVSTIRAF 924
Cdd:cd18552 119 VLVrdplTVIGLLGVlfyldwkLTLIALVVLPLAALPIRrIGKRLRKISRRSQESMGD----LTSVLQETLSGIRVVKAF 194
|
170
....*....|....*...
gi 74136409 925 GHQQRFIQQYKEVVNENL 942
Cdd:cd18552 195 GAEDYEIKRFRKANERLR 212
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
774-965 |
8.68e-14 |
|
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: 73.58 E-value: 8.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 774 IYGILGLIKGLFVCSGAYVITRGSLAASRTMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDMrlhyylrLWVNC 853
Cdd:cd18544 46 LYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNE-------LFTSG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 854 TLDVIGTILVIIGA----------LPLFILGIIPsVFFYFSI--QRYYVASSRQIRRLTGAsrspVISHFSETLSGVSTI 921
Cdd:cd18544 119 LVTLIGDLLLLIGIliamfllnwrLALISLLVLP-LLLLATYlfRKKSRKAYREVREKLSR----LNAFLQESISGMSVI 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 74136409 922 RAFGHQQRFIQQYKEVVNENLVCFYNNVISNRWLSVRLEFLGNL 965
Cdd:cd18544 194 QLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSL 237
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1064-1262 |
1.24e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.05 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFriveraggkiiidgidistiGLHD-------LRGK------------ 1124
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILS--------------------GVYQpdsgeilLDGEpvrfrsprdaqa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1125 ---------LNIIPQHPV---LFSGTLQMNLDPLNkysdsklW-----EALELchLKEFvqSLPEKLRHEISEggenLSM 1187
Cdd:COG1129 79 agiaiihqeLNLVPNLSVaenIFLGREPRRGGLID-------WramrrRAREL--LARL--GLDIDPDTPVGD----LSV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74136409 1188 GQRQLVCLARALLRKTKILILDEATASIDF-ETDKLVQtTIR--KEfSDCTILTIAHRLQSIID-SDRVLVLDSGSIVE 1262
Cdd:COG1129 144 AQQQLVEIARALSRDARVLILDEPTASLTErEVERLFR-IIRrlKA-QGVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
429-645 |
1.30e-13 |
|
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: 71.93 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 429 GDHAIEFTDATYSWNktGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKG-SVAYVSQQAWIQ 507
Cdd:COG1127 2 SEPMIEVRNLTKSFG--DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqDITGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 508 nciLQVNI--------LFGS------IM----------KKEFYEQVLEACAL--LPDLEQL-PkgdqteiGErgvnISGG 560
Cdd:COG1127 80 ---LRRRIgmlfqggaLFDSltvfenVAfplrehtdlsEAEIRELVLEKLELvgLPGAADKmP-------SE----LSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 561 QQHRVSLARAVYSGADIYLLD------DPLSAVDVHvgkQLFEKVIGSLGLlknkTRILVTHNLTLLPQM-DLIVVMESG 633
Cdd:COG1127 146 MRKRVALARALALDPEILLYDeptaglDPITSAVID---ELIRELRDELGL----TSVVVTHDLDSAFAIaDRVAVLADG 218
|
250
....*....|..
gi 74136409 634 RIAQMGTYQELL 645
Cdd:COG1127 219 KIIAEGTPEELL 230
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
430-654 |
2.03e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 72.14 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 430 DHAIEFTDATYSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSS---MLSAILGEMEKLTGVVQRKGsVAYVSQQAWi 506
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDG-ITLTAKTVW- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 507 qNCILQVNILFGSIMKKEFYEQVLEACALLPDLEQLPKGDQTEIGERGV--------------NISGGQQHRVSLARAVY 572
Cdd:PRK13640 81 -DIREKVGIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLadvgmldyidsepaNLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 573 SGADIYLLDDPLSAVDVHvGKQLFEKVIGSLGLLKNKTRILVTHNLTLLPQMDLIVVMESGRIAQMGTYQELLSKTRNLT 652
Cdd:PRK13640 160 VEPKIIILDESTSMLDPA-GKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVEMLK 238
|
..
gi 74136409 653 NL 654
Cdd:PRK13640 239 EI 240
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
448-644 |
2.21e-13 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 70.61 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 448 PVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKG-SVayVSQQAWIQNCI---LQVNILFgsimkK 523
Cdd:cd03263 16 PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGySI--RTDRKAARQSLgycPQFDALF-----D 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 524 EFY-EQVLEACALLPDLEQLPKGDQTEIGERGVNI-----------SGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHV 591
Cdd:cd03263 89 ELTvREHLRFYARLKGLPKSEIKEEVELLLRVLGLtdkankrartlSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 592 GKQLFEKVigsLGLLKNKTRILVTHNltllpqMDL-------IVVMESGRIAQMGTYQEL 644
Cdd:cd03263 169 RRAIWDLI---LEVRKGRSIILTTHS------MDEaealcdrIAIMSDGKLRCIGSPQEL 219
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
433-621 |
2.21e-13 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 68.63 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNktGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQR--KGSVAYVSQQawiqnci 510
Cdd:cd03221 1 IELENLSKTYG--GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWgsTVKIGYFEQL------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 511 lqvnilfgsimkkefyeqvleacallpdleqlpkgdqteigergvniSGGQQHRVSLARAVYSGADIYLLDDPLSAVDVH 590
Cdd:cd03221 72 -----------------------------------------------SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
|
170 180 190
....*....|....*....|....*....|.
gi 74136409 591 vGKQLFEKVIGSLgllkNKTRILVTHNLTLL 621
Cdd:cd03221 105 -SIEALEEALKEY----PGTVILVSHDRYFL 130
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
432-646 |
2.57e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 71.32 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 432 AIEFTDATYSWNktGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAI--LGEMEKLT---GVVQRKGSVAYVSQQAWI 506
Cdd:PRK11264 3 AIEVKNLVKKFH--GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlLEQPEAGTirvGDITIDTARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 507 QNCILQVNILFGS------------------IMKKEFYEqvlEACALLPDLeqLPK----GDQTEIGERgvnISGGQQHR 564
Cdd:PRK11264 81 RQLRQHVGFVFQNfnlfphrtvleniiegpvIVKGEPKE---EATARAREL--LAKvglaGKETSYPRR---LSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 565 VSLARAVYSGADIYLLDDPLSAVDvhvgKQLFEKVIGSLGLL--KNKTRILVTHNLTLLPQM-DLIVVMESGRIAQMGTY 641
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALD----PELVGEVLNTIRQLaqEKRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPA 228
|
....*
gi 74136409 642 QELLS 646
Cdd:PRK11264 229 KALFA 233
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
258-646 |
2.91e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.07 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 258 AVLAGVAVL---VFVIPINALAATKIKKLKKSQR------KNKDKQIK----LLKEILHGIKILKLYAWEPSYKNKIIKI 324
Cdd:PTZ00265 972 AVLTGTYFIfmrVFAIRARLTANKDVEKKEINQPgtvfayNSDDEIFKdpsfLIQEAFYNMNTVIIYGLEDYFCNLIEKA 1051
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 325 RDQELEFQKsaRYLTVFSML---TLTCIPFLVSLATLCVYFLLDEGNILTATKVftsMSLFNILRIPLF--ELPTVISTV 399
Cdd:PTZ00265 1052 IDYSNKGQK--RKTLVNSMLwgfSQSAQLFINSFAYWFGSFLIRRGTILVDDFM---KSLFTFLFTGSYagKLMSLKGDS 1126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 400 VQTKISLGRLEDFLHTEELLPQ------NIETNYIGDHAIEFTDATYSW-NKTGMPVLKDLNIKIPEGALVAVVGQVGSG 472
Cdd:PTZ00265 1127 ENAKLSFEKYYPLIIRKSNIDVrdnggiRIKNKNDIKGKIEIMDVNFRYiSRPNVPIYKDLTFSCDSKKTTAIVGETGSG 1206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 473 KSSMLSAIL------------------GEMEKL------------------------------TGVVQRKGSV------- 497
Cdd:PTZ00265 1207 KSTVMSLLMrfydlkndhhivfknehtNDMTNEqdyqgdeeqnvgmknvnefsltkeggsgedSTVFKNSGKIlldgvdi 1286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 498 ------------AYVSQQAWIQNCILQVNILFGSimKKEFYEQVLEAC---ALLPDLEQLPKGDQTEIGERGVNISGGQQ 562
Cdd:PTZ00265 1287 cdynlkdlrnlfSIVSQEPMLFNMSIYENIKFGK--EDATREDVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQK 1364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 563 HRVSLARAVYSGADIYLLDDPLSAVDVHvGKQLFEKVIGSLGLLKNKTRILVTHNLTLLPQMDLIVVM----ESGRIAQM 638
Cdd:PTZ00265 1365 QRIAIARALLREPKILLLDEATSSLDSN-SEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQA 1443
|
....*....
gi 74136409 639 -GTYQELLS 646
Cdd:PTZ00265 1444 hGTHEELLS 1452
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1045-1269 |
3.59e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 71.30 E-value: 3.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1045 KGVVEFINYQARY-RDELGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRG 1123
Cdd:PRK13650 2 SNIIEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1124 KLNIIPQHP------------VLFSgtLQMNLDPLnKYSDSKLWEALELCHLKEFVQSLPEKLrheiseggenlSMGQRQ 1191
Cdd:PRK13650 82 KIGMVFQNPdnqfvgatveddVAFG--LENKGIPH-EEMKERVNEALELVGMQDFKEREPARL-----------SGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1192 LVCLARALLRKTKILILDEATASIDFETD-KLVQT--TIRKEFsDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQN 1268
Cdd:PRK13650 148 RVAIAGAVAMRPKIIILDEATSMLDPEGRlELIKTikGIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRE 226
|
.
gi 74136409 1269 L 1269
Cdd:PRK13650 227 L 227
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
433-640 |
4.17e-13 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 69.75 E-value: 4.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKG-------------SVAY 499
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 500 VSQQAWIQNCILQVNI-LFGSIMKKEFYEqvleacALlpdleqlpkgdqtEIGERGVNISGGQQHRVSLARAVYSGADIY 578
Cdd:cd03369 87 IPQDPTLFSGTIRSNLdPFDEYSDEEIYG------AL-------------RVSEGGLNLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74136409 579 LLDDPLSAVDVHVgKQLFEKVIGSlgLLKNKTRILVTHNLTLLPQMDLIVVMESGRIAQMGT 640
Cdd:cd03369 148 VLDEATASIDYAT-DALIQKTIRE--EFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
426-655 |
5.28e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 71.19 E-value: 5.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 426 NYIGDHAIEFTDATYSwNKTGMP--VLKDLNIKIPEGALVAVVGQVGSGKSSMLS------------------AILGEME 485
Cdd:PRK13645 2 DFSKDIILDNVSYTYA-KKTPFEfkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQltngliisetgqtivgdyAIPANLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 486 KLTGVVQRKGSVAYVSQQAWIQ--NCILQVNILFGSIM----KKEFYEQVLEacalLPDLEQLPKgdqtEIGERG-VNIS 558
Cdd:PRK13645 81 KIKEVKRLRKEIGLVFQFPEYQlfQETIEKDIAFGPVNlgenKQEAYKKVPE----LLKLVQLPE----DYVKRSpFELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 559 GGQQHRVSLARAVYSGADIYLLDDPLSAVDVHvGKQLFEKVIGSLGLLKNKTRILVTHNL-TLLPQMDLIVVMESGRIAQ 637
Cdd:PRK13645 153 GGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK-GEEDFINLFERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVIS 231
|
250
....*....|....*...
gi 74136409 638 MGTYQELLSKTRNLTNLH 655
Cdd:PRK13645 232 IGSPFEIFSNQELLTKIE 249
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1064-1267 |
6.99e-13 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 71.24 E-value: 6.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGkiiidgidisTIG----------------LHDLRGK-LN 1126
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGI----------TSGeilfdgedllklsekeLRKIRGReIQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1127 IIPQHPvlfsgtlqMN-LDPL--------------NKYSDSKLW----EALELCHL---KEFVQSLPeklrHEiseggen 1184
Cdd:COG0444 90 MIFQDP--------MTsLNPVmtvgdqiaeplrihGGLSKAEAReraiELLERVGLpdpERRLDRYP----HE------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1185 LSMGQRQLVCLARALLRKTKILILDEATASIdfetDKLVQTTI-------RKEFsDCTILTIAHRLqSIID--SDRVLVL 1255
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTAL----DVTIQAQIlnllkdlQREL-GLAILFITHDL-GVVAeiADRVAVM 224
|
250
....*....|....*....
gi 74136409 1256 DSGSIVE-------FEAPQ 1267
Cdd:COG0444 225 YAGRIVEegpveelFENPR 243
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1034-1262 |
7.71e-13 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 70.12 E-value: 7.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1034 MSRRPPLqwpnkgvVEFINYQARYRDELG--LALQDITFQTHGEEKIGIVGRTGAGKSTLsnclFRIV---ERAggkiii 1108
Cdd:COG1116 1 MSAAAPA-------LELRGVSKRFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKSTL----LRLIaglEKP------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1109 dgidisTIG--------LHDLRGKLNIIPQHPVLF----------SGTLQMNLDPlnKYSDSKLWEALELCHLKEFVQSL 1170
Cdd:COG1116 64 ------TSGevlvdgkpVTGPGPDRGVVFQEPALLpwltvldnvaLGLELRGVPK--AERRERARELLELVGLAGFEDAY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1171 PeklrHEiseggenLSMGQRQLVCLARALLRKTKILILDEATASIDFET-----DKLVQttIRKEfSDCTILTIAH---- 1241
Cdd:COG1116 136 P----HQ-------LSGGMRQRVAIARALANDPEVLLMDEPFGALDALTrerlqDELLR--LWQE-TGKTVLFVTHdvde 201
|
250 260
....*....|....*....|....*
gi 74136409 1242 --RLqsiidSDRVLVLDS--GSIVE 1262
Cdd:COG1116 202 avFL-----ADRVVVLSArpGRIVE 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
433-635 |
8.90e-13 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 68.93 E-value: 8.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSwNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEmEKLT-GVVQ---------RKGSVAYVSQ 502
Cdd:COG2884 2 IRFENVSKR-YPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGE-ERPTsGQVLvngqdlsrlKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 503 QawI----QNCIL----QV--NILFgsIM------KKEFYEQVLEACAL--LPDLE-QLPkgdqteigergVNISGGQQH 563
Cdd:COG2884 80 R--IgvvfQDFRLlpdrTVyeNVAL--PLrvtgksRKEIRRRVREVLDLvgLSDKAkALP-----------HELSGGEQQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74136409 564 RVSLARAVYSGADIYLLD------DPLSAVDVHvgkQLFEKvIGSLGllknKTRILVTHNLTLLPQMDL-IVVMESGRI 635
Cdd:COG2884 145 RVAIARALVNRPELLLADeptgnlDPETSWEIM---ELLEE-INRRG----TTVLIATHDLELVDRMPKrVLELEDGRL 215
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1065-1259 |
9.23e-13 |
|
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: 70.27 E-value: 9.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGgkiiidgidistiGLHDLRGKLNIIPQHPVLFSGTLQMNLD 1144
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSE-------------GKIKHSGRISFSSQFSWIMPGTIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1145 PLNKYSDSKLWEALELCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLV- 1223
Cdd:cd03291 120 FGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIf 199
|
170 180 190
....*....|....*....|....*....|....*.
gi 74136409 1224 QTTIRKEFSDCTILTIAHRLQSIIDSDRVLVLDSGS 1259
Cdd:cd03291 200 ESCVCKLMANKTRILVTSKMEHLKKADKILILHEGS 235
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1064-1261 |
9.46e-13 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 69.39 E-value: 9.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCL--------------------FRIVERAGgkiiidgidistiglhdlRG 1123
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLIsgflrptsgsvlfdgeditgLPPHEIAR------------------LG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1124 ------KLNIIPQHPVL-------FSGTLQMNLDPLNKYSDSKLWE----ALELCHLkefvqslpEKLRHEISeggENLS 1186
Cdd:cd03219 77 igrtfqIPRLFPELTVLenvmvaaQARTGSGLLLARARREEREAREraeeLLERVGL--------ADLADRPA---GELS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74136409 1187 MGQRQLVCLARALLRKTKILILDEATASIDF-ETDKLVQ--TTIRKEfsDCTILTIAHRLQSIID-SDRVLVLDSGSIV 1261
Cdd:cd03219 146 YGQQRRLEIARALATDPKLLLLDEPAAGLNPeETEELAEliRELRER--GITVLLVEHDMDVVMSlADRVTVLDQGRVI 222
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1063-1272 |
9.73e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 69.01 E-value: 9.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1063 LALQDITFQTHGE-----------EKIGIVGRTGAGKSTLSNCL--FriveraggkiiidgidistigLHDLRGKLNI-- 1127
Cdd:COG3840 2 LRLDDLTYRYGDFplrfdltiaagERVAILGPSGAGKSTLLNLIagF---------------------LPPDSGRILWng 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1128 -------IPQHPV--------LFSG-TLQMN----LDPLNKYSD---SKLWEALELCHLKEFVQSLPEKLrheiseggen 1184
Cdd:COG3840 61 qdltalpPAERPVsmlfqennLFPHlTVAQNiglgLRPGLKLTAeqrAQVEQALERVGLAGLLDRLPGQL---------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1185 lSMGQRQLVCLARALLRKTKILILDEATASID----FETDKLVQtTIRKEFsDCTILTIAHRLQSIID-SDRVLVLDSGS 1259
Cdd:COG3840 131 -SGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVD-ELCRER-GLTVLMVTHDPEDAARiADRVLLVADGR 207
|
250
....*....|...
gi 74136409 1260 IVEFEAPQNLIRQ 1272
Cdd:COG3840 208 IAADGPTAALLDG 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1063-1261 |
9.91e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.37 E-value: 9.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1063 LALQDITFQTH-GEekI-GIVGRTGAGKSTLSNCLFriveraggkiiidgidistiGLHD-------LRGK--------- 1124
Cdd:COG3845 19 VANDDVSLTVRpGE--IhALLGENGAGKSTLMKILY--------------------GLYQpdsgeilIDGKpvrirsprd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1125 ---LNI--IPQHPVLFsgtlqmnlDPLNkysdskLWE--ALELCHLKEFVQSLpEKLRHEISEGGE-------------N 1184
Cdd:COG3845 77 aiaLGIgmVHQHFMLV--------PNLT------VAEniVLGLEPTKGGRLDR-KAARARIRELSErygldvdpdakveD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1185 LSMGQRQLVCLARALLRKTKILILDEATASI-DFETDKLVQT--TIRKEfsDCTILTIAHRLQSIID-SDRVLVLDSGSI 1260
Cdd:COG3845 142 LSVGEQQRVEILKALYRGARILILDEPTAVLtPQEADELFEIlrRLAAE--GKSIIFITHKLREVMAiADRVTVLRRGKV 219
|
.
gi 74136409 1261 V 1261
Cdd:COG3845 220 V 220
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1063-1272 |
1.10e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 70.12 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1063 LALQDITFQTHGEEKIGIVGRTGAGKSTLS---NCLFriVERAGGKIIIDGIDISTIGLHDLRGKLNIIPQHP------- 1132
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAkhmNALL--IPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNPdnqivat 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1133 -----VLFsGTLQMNLDPlnKYSDSKLWEALELCHLKEFVQSLPEKlrheiseggenLSMGQRQLVCLARALLRKTKILI 1207
Cdd:PRK13633 102 iveedVAF-GPENLGIPP--EEIRERVDESLKKVGMYEYRRHAPHL-----------LSGGQKQRVAIAGILAMRPECII 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74136409 1208 LDEATASIDFETDKLVQTTIRK--EFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQNLIRQ 1272
Cdd:PRK13633 168 FDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
449-639 |
1.14e-12 |
|
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: 68.71 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 449 VLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSVAYV-SQQAWIQNcILQV--NILF-GSIM--K 522
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLlGLGGGFNP-ELTGreNIYLnGRLLglS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 523 KEFYEQVLEACAllpdleqlpkgDQTEIGERG----VNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHvgkqlF-E 597
Cdd:cd03220 116 RKEIDEKIDEII-----------EFSELGDFIdlpvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA-----FqE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 74136409 598 KVIGSLGLLKNKTR--ILVTHNLTLLPQM-DLIVVMESGRIAQMG 639
Cdd:cd03220 180 KCQRRLRELLKQGKtvILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
452-646 |
1.39e-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: 70.90 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 452 DLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQ-----------------RKGSVAYVSQQAwiqncIL--- 511
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevlqdsargiflppHRRRIGYVFQEA-----RLfph 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 512 ---QVNILFGsiMKKEF-------YEQVLEACALLPDLEQLPkgdqteigergVNISGGQQHRVSLARAVYSGADIYLLD 581
Cdd:COG4148 92 lsvRGNLLYG--RKRAPraerrisFDEVVELLGIGHLLDRRP-----------ATLSGGERQRVAIGRALLSSPRLLLMD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74136409 582 DPLSAVDVHVgKQ----LFEKVIGSLGLlknktRIL-VTHNLTLLPQM-DLIVVMESGRIAQMGTYQELLS 646
Cdd:COG4148 159 EPLAALDLAR-KAeilpYLERLRDELDI-----PILyVSHSLDEVARLaDHVVLLEQGRVVASGPLAEVLS 223
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
774-966 |
1.43e-12 |
|
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: 69.74 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 774 IYGILGLIKGLFVCSGA------YVITRGSLAASRTMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDMRLHyyl 847
Cdd:cd18547 44 LLRILLLLLGLYLLSALfsylqnRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALS--- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 848 rlwvNCTLDVIGTILVIIGA----------LPLFILGIIPSVFFYFSI-----QRYYVASSRQIRRLTGasrspvisHFS 912
Cdd:cd18547 121 ----QSLTQLISSILTIVGTlimmlyisplLTLIVLVTVPLSLLVTKFiakrsQKYFRKQQKALGELNG--------YIE 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 74136409 913 ETLSGVSTIRAFGHQQRFIQQYKEvVNENLvcfYNNvisnrwlSVRLEFLGNLM 966
Cdd:cd18547 189 EMISGQKVVKAFNREEEAIEEFDE-INEEL---YKA-------SFKAQFYSGLL 231
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1056-1262 |
1.44e-12 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 68.27 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1056 RYRDELG--LALQDITFQTHGEEKIGIVGRTGAGKSTLsnclFRIV---ERAggkiiidgidisTIG--------LHDLR 1122
Cdd:cd03293 9 TYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTL----LRIIaglERP------------TSGevlvdgepVTGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1123 GKLNIIPQHPVLFS-GTLQMN--LDPLNKYSDSKLW-----EALELCHLKEFVQSLPeklrHEiseggenLSMGQRQLVC 1194
Cdd:cd03293 73 PDRGYVFQQDALLPwLTVLDNvaLGLELQGVPKAEAreraeELLELVGLSGFENAYP----HQ-------LSGGMRQRVA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74136409 1195 LARALLRKTKILILDEATASIDFETDKLVQTTIRK--EFSDCTILTIAHRL-QSIIDSDRVLVLDS--GSIVE 1262
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIdEAVFLADRVVVLSArpGRIVA 214
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1064-1263 |
1.95e-12 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 67.93 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHdlRGKLNIIPQHPVLFSG-TLQMN 1142
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPHlTVAEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1143 LD-PLNKYSDSK------LWEALELCHLKEFVQSLPEKLrheiseggenlSMGQRQLVCLARALLRKTKILILDEATASI 1215
Cdd:cd03259 93 IAfGLKLRGVPKaeirarVRELLELVGLEGLLNRYPHEL-----------SGGQQQRVALARALAREPSLLLLDEPLSAL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 74136409 1216 DFETDKLVQTTIRK--EFSDCTILTIAHRLQSIID-SDRVLVLDSGSIVEF 1263
Cdd:cd03259 162 DAKLREELREELKElqRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQV 212
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1080-1242 |
2.30e-12 |
|
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: 66.41 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1080 IVGRTGAGKSTLsnclFRIVERaggkiiIDGIDISTIGLHDLRGKLnIIPQHPVLFSGTLQMNLdplnkysdSKLWeale 1159
Cdd:cd03223 32 ITGPSGTGKSSL----FRALAG------LWPWGSGRIGMPEGEDLL-FLPQRPYLPLGTLREQL--------IYPW---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1160 lchlkefvqslpeklrheisegGENLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTIRKEFsdCTILTI 1239
Cdd:cd03223 89 ----------------------DDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG--ITVISV 144
|
...
gi 74136409 1240 AHR 1242
Cdd:cd03223 145 GHR 147
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
433-639 |
2.53e-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: 67.19 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYS----WNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILG--EMEKLTGVV----------QRKGS 496
Cdd:cd03213 4 LSFRNLTVTvkssPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVlingrpldkrSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 497 VAYVSQQawiqncilqvNILFGSIMKKEFyeqvLEACALLpdleqlpkgdqteigeRGvnISGGQQHRVSLARAVYSGAD 576
Cdd:cd03213 84 IGYVPQD----------DILHPTLTVRET----LMFAAKL----------------RG--LSGGERKRVSIALELVSNPS 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 577 IYLLDDPLSAVDVHVGKQLfekvigsLGLLK-----NKTRILVTHNLT--LLPQMDLIVVMESGRIAQMG 639
Cdd:cd03213 132 LLFLDEPTSGLDSSSALQV-------MSLLRrladtGRTIICSIHQPSseIFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1064-1277 |
2.87e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 68.86 E-value: 2.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLS---NCLFRivERAGGKIIIDGIDISTIGLHDLRGKLNIIPQHPV------- 1133
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLAlhlNGLLR--PQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNPEtqfvgrt 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1134 ----LFSGTLQMNLDP--LNKYSDSKLWEaLELchlkefvqslpEKLRHeisEGGENLSMGQRQLVCLARALLRKTKILI 1207
Cdd:PRK13644 95 veedLAFGPENLCLPPieIRKRVDRALAE-IGL-----------EKYRH---RSPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74136409 1208 LDEATASIDFETDKLVQTTIRKEFSDC-TILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQNLIRQKGLFY 1277
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQT 230
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1047-1265 |
3.15e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 67.38 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1047 VVEFINYQARYRDElGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIvERAggkiiidgidisTIG--------- 1117
Cdd:COG2884 1 MIRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGE-ERP------------TSGqvlvngqdl 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1118 -------LHDLRGKLNIIPQ-HPVLFSGTLQMNLD-PL------NKYSDSKLWEALELCHLKEFVQSLPeklrHEISeGG 1182
Cdd:COG2884 67 srlkrreIPYLRRRIGVVFQdFRLLPDRTVYENVAlPLrvtgksRKEIRRRVREVLDLVGLSDKAKALP----HELS-GG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1183 EnlsmgqRQLVCLARALLRKTKILILDEATASIDFET-DKLVQttIRKEFSD--CTILtIA-HRLqSIIDS--DRVLVLD 1256
Cdd:COG2884 142 E------QQRVAIARALVNRPELLLADEPTGNLDPETsWEIME--LLEEINRrgTTVL-IAtHDL-ELVDRmpKRVLELE 211
|
....*....
gi 74136409 1257 SGSIVEFEA 1265
Cdd:COG2884 212 DGRLVRDEA 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
438-637 |
3.50e-12 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 67.96 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 438 ATYSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSV--------AYVSQQ----AW 505
Cdd:COG4525 11 VRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVVFQKdallPW 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 506 iqnciLQV--NILFG----SIMKKEFYEQVLEACALLpDLEQLpkgdqteiGERGV-NISGGQQHRVSLARAVYSGADIY 578
Cdd:COG4525 91 -----LNVldNVAFGlrlrGVPKAERRARAEELLALV-GLADF--------ARRRIwQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 579 LLDDPLSAVDVHVGKQLFEKvigslgLLK-----NKTRILVTHNL--TLLPQMDLIvVMES--GRIAQ 637
Cdd:COG4525 157 LMDEPFGALDALTREQMQEL------LLDvwqrtGKGVFLITHSVeeALFLATRLV-VMSPgpGRIVE 217
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
442-639 |
3.52e-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: 67.30 E-value: 3.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 442 WNKTGMpVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEK---LTGVV----------QRKGSVAYVSQQ-AWIQ 507
Cdd:cd03234 16 WNKYAR-ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQIlfngqprkpdQFQKCVAYVRQDdILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 508 NCILQVNILFGSIM-----KKEFYEQVLEACALLPDLEQLPKGdqteiGERGVNISGGQQHRVSLARAVYSGADIYLLDD 582
Cdd:cd03234 95 GLTVRETLTYTAILrlprkSSDAIRKKRVEDVLLRDLALTRIG-----GNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74136409 583 PLSAVDVHVGKQLFEkvigslgLLK-----NKTRILVTHNLT--LLPQMDLIVVMESGRIAQMG 639
Cdd:cd03234 170 PTSGLDSFTALNLVS-------TLSqlarrNRIVILTIHQPRsdLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
432-650 |
3.83e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 68.14 E-value: 3.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 432 AIEFTDATYSWNKtgMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAiLGEMEKLTGVVQRKGSVAYVSQQAW-----I 506
Cdd:PRK14258 7 AIKVNNLSFYYDT--QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQNIYerrvnL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 507 QNCILQVNILFG--SIMKKEFYEQVLEACALL---PDLE-------QLPKGD-----QTEIGERGVNISGGQQHRVSLAR 569
Cdd:PRK14258 84 NRLRRQVSMVHPkpNLFPMSVYDNVAYGVKIVgwrPKLEiddivesALKDADlwdeiKHKIHKSALDLSGGQQQRLCIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 570 AVYSGADIYLLDDPLSAVDvHVGKQLFEKVIGSLGLLKNKTRILVTHNLTLLPQM-DLIVVMES--GRIAQM---GTYQE 643
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLD-PIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLsDFTAFFKGneNRIGQLvefGLTKK 242
|
250
....*....|..
gi 74136409 644 LL-----SKTRN 650
Cdd:PRK14258 243 IFnsphdSRTRE 254
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
433-639 |
5.88e-12 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 66.36 E-value: 5.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNKTGMpvlkDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKG-SVAYVSQQAWIQNCIL 511
Cdd:cd03298 1 VRLDKIRFSYGEQPM----HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvDVTAAPPADRPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 512 QVNILFGSIMkkefYEQVLeACALLPDLeQLPKGDQTEI----GERGVN---------ISGGQQHRVSLARAVYSGADIY 578
Cdd:cd03298 77 QENNLFAHLT----VEQNV-GLGLSPGL-KLTAEDRQAIevalARVGLAglekrlpgeLSGGERQRVALARVLVRDKPVL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74136409 579 LLDDPLSAVDVHVGKQLFEKVIGSLGLLKNkTRILVTHNLTLLPQM-DLIVVMESGRIAQMG 639
Cdd:cd03298 151 LLDEPFAALDPALRAEMLDLVLDLHAETKM-TVLMVTHQPEDAKRLaQRVVFLDNGRIAAQG 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
443-650 |
6.02e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 69.29 E-value: 6.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 443 NKTGMPV-LKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQ-----------------RKGSVAYVSQQ- 503
Cdd:PRK10070 36 EKTGLSLgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLidgvdiakisdaelrevRRKKIAMVFQSf 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 504 AWIQNCILQVNILFG----SIMKKEFYEQVLEACALLpDLEQLPKGDQTEIgergvniSGGQQHRVSLARAVYSGADIYL 579
Cdd:PRK10070 116 ALMPHMTVLDNTAFGmelaGINAEERREKALDALRQV-GLENYAHSYPDEL-------SGGMRQRVGLARALAINPDILL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74136409 580 LDDPLSAVDVHVGKQLFEKVIgSLGLLKNKTRILVTHNLTLLPQM-DLIVVMESGRIAQMGTYQELLSKTRN 650
Cdd:PRK10070 188 MDEAFSALDPLIRTEMQDELV-KLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNNPAN 258
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1064-1267 |
6.80e-12 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 68.22 E-value: 6.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVEraggkiiidgidiSTIG----------------LHDLRGKLNI 1127
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEE-------------PTSGeilfdgqditglsgreLRPLRRRMQM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1128 IPQHPvlfsgtlQMNLDPLNKYSDSkLWEALELcH-------LKEFVQSLPEK--LR--------HEiseggenLSMGQR 1190
Cdd:COG4608 100 VFQDP-------YASLNPRMTVGDI-IAEPLRI-HglaskaeRRERVAELLELvgLRpehadrypHE-------FSGGQR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1191 QLVCLARALLRKTKILILDEATASIdfetDKLVQTTI-------RKEFsDCTILTIAHRLqSIID--SDRVLVLDSGSIV 1261
Cdd:COG4608 164 QRIGIARALALNPKLIVCDEPVSAL----DVSIQAQVlnlledlQDEL-GLTYLFISHDL-SVVRhiSDRVAVMYLGKIV 237
|
250
....*....|...
gi 74136409 1262 E-------FEAPQ 1267
Cdd:COG4608 238 EiaprdelYARPL 250
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
449-650 |
7.02e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 67.38 E-value: 7.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 449 VLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSVAYVSQQAWIQNCIL---QVNILFGS------ 519
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAIKlrkEVGMVFQQpnpfph 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 520 ---------------IMKKEFYEQVLEACallpdLEQLpkGDQTEIGER----GVNISGGQQHRVSLARAVYSGADIYLL 580
Cdd:PRK14246 105 lsiydniayplkshgIKEKREIKKIVEEC-----LRKV--GLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74136409 581 DDPLSAVDVhVGKQLFEKVIGSLGllKNKTRILVTHNLTLLPQM-DLIVVMESGRIAQMGTYQELLSKTRN 650
Cdd:PRK14246 178 DEPTSMIDI-VNSQAIEKLITELK--NEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGSSNEIFTSPKN 245
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1043-1295 |
8.17e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 67.52 E-value: 8.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1043 PNKGVVEFINYQARYRDELGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIG---LH 1119
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTaktVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1120 DLRGKLNIIPQHP------------VLFSgtLQMNLDPLNKYSdSKLWEALELCHLKEFVQSLPEklrheiseggeNLSM 1187
Cdd:PRK13640 81 DIREKVGIVFQNPdnqfvgatvgddVAFG--LENRAVPRPEMI-KIVRDVLADVGMLDYIDSEPA-----------NLSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1188 GQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTIRK--EFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEA 1265
Cdd:PRK13640 147 GQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKlkKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 74136409 1266 PQN------LIRQKGL----FYEM-----TTDAGITQESGTEKKL 1295
Cdd:PRK13640 227 PVEifskveMLKEIGLdipfVYKLknklkEKGISVPQEINTEEKL 271
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
433-646 |
8.32e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 67.32 E-value: 8.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWnKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSVAyvSQQAWIQNCILQ 512
Cdd:PRK13644 2 IRLENVSYSY-PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDT--GDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 513 VNILFGSIMKKEFYEQVLEACALLPDLEQLPKGDQTEIGERGV--------------NISGGQQHRVSLARAVYSGADIY 578
Cdd:PRK13644 79 VGIVFQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALaeiglekyrhrspkTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 579 LLDDPLSAVDVHVGKQLFEKvIGSLGlLKNKTRILVTHNLTLLPQMDLIVVMESGRIAQMGTYQELLS 646
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLER-IKKLH-EKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1065-1271 |
9.22e-12 |
|
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: 66.37 E-value: 9.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAG---GKIIIDGIDISTIGLHDLRGKLNIIPQHPVLFSG-TLQ 1140
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSgevLIDGEDISGLSEAELYRLRRRMGMLFQSGALFDSlTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1141 MNLD-PLNKYSDSKLW-------EALELCHLKEFVQSLPeklrHEISeGGenlsMGQRqlVCLARALLRKTKILILDEAT 1212
Cdd:cd03261 96 ENVAfPLREHTRLSEEeireivlEKLEAVGLRGAEDLYP----AELS-GG----MKKR--VALARALALDPELLLYDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74136409 1213 ASID----FETDKLVQtTIRKEFsDCTILTIAHRLQSIID-SDRVLVLDSGSIVEFEAPQNLIR 1271
Cdd:cd03261 165 AGLDpiasGVIDDLIR-SLKKEL-GLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1048-1271 |
1.10e-11 |
|
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: 66.17 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1048 VEFINYQARYRDElGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKLNI 1127
Cdd:cd03295 1 IEFENVTKRYGGG-KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1128 IPQHPVLFSG-TLQMN--LDP-LNKYS----DSKLWEALELCHL--KEFVQSLPeklrHEiseggenLSMGQRQLVCLAR 1197
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPkLLKWPkekiRERADELLALVGLdpAEFADRYP----HE-------LSGGQQQRVGVAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1198 ALLRKTKILILDEATASIdfetDKLVQTTIRKEFSDC------TILTIAHRLQSIID-SDRVLVLDSGSIVEFEAPQNLI 1270
Cdd:cd03295 149 ALAADPPLLLMDEPFGAL----DPITRDQLQEEFKRLqqelgkTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEIL 224
|
.
gi 74136409 1271 R 1271
Cdd:cd03295 225 R 225
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
449-635 |
1.20e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 66.62 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 449 VLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGeMEKLTGVVQRKGSVAYVS---------QQA----W---IQNCILQ 512
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG-LETPSAGELLAGTAPLAEaredtrlmfQDArllpWkkvIDNVGLG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 513 vniLFGSImkKEFYEQVLEACALLPDLEQLPKGdqteigergvnISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVG 592
Cdd:PRK11247 106 ---LKGQW--RDAALQALAAVGLADRANEWPAA-----------LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 74136409 593 KQLfEKVIGSLGLLKNKTRILVTHNLTLLPQM-DLIVVMESGRI 635
Cdd:PRK11247 170 IEM-QDLIESLWQQHGFTVLLVTHDVSEAVAMaDRVLLIEEGKI 212
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
428-646 |
1.23e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 68.33 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 428 IGDHAIEFTDATyswnktgmpVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKG------SVAYVS 501
Cdd:PRK09536 6 VSDLSVEFGDTT---------VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 502 QQawIQNCILQVNILFgsimkkEF-YEQVLEAcALLPDLEQLpkGDQTEIGERGV------------------NISGGQQ 562
Cdd:PRK09536 77 RR--VASVPQDTSLSF------EFdVRQVVEM-GRTPHRSRF--DTWTETDRAAVeramertgvaqfadrpvtSLSGGER 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 563 HRVSLARAVYSGADIYLLDDPLSAVDVHVGKQLFEkVIGSLgLLKNKTRILVTHNLTLLPQM-DLIVVMESGRIAQMGTY 641
Cdd:PRK09536 146 QRVLLARALAQATPVLLLDEPTASLDINHQVRTLE-LVRRL-VDDGKTAVAAIHDLDLAARYcDELVLLADGRVRAAGPP 223
|
....*
gi 74136409 642 QELLS 646
Cdd:PRK09536 224 ADVLT 228
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
807-942 |
1.51e-11 |
|
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: 66.74 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 807 QLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDMrlhyylrlwvnctldVIGT--------ILVIIGA----------L 868
Cdd:cd18575 74 AVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQT---------------VVGSslsialrnLLLLIGGlvmlfitspkL 138
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74136409 869 PLFILGIIPSVFFYFsiqryyVASSRQIRRLTGASRSPV--ISHF-SETLSGVSTIRAFGHQQRFIQQYKEVVNENL 942
Cdd:cd18575 139 TLLVLLVIPLVVLPI------ILFGRRVRRLSRASQDRLadLSAFaEETLSAIKTVQAFTREDAERQRFATAVEAAF 209
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
449-649 |
1.53e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.87 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 449 VLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSVAyvsqqawiqnCILQV------------NIL 516
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVS----------ALLELgagfhpeltgreNIY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 517 F-GSI--MKKEFYEQVLEACAllpdleqlpkgDQTEIGE------RgvNISGGQQHRVSLARAVYSGADIYLLDDPLSAV 587
Cdd:COG1134 111 LnGRLlgLSRKEIDEKFDEIV-----------EFAELGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVG 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74136409 588 DVHvgkqlF-EKVIGSLGLLKNKTR--ILVTHNLTLLPQM-DLIVVMESGRIAQMGT-------YQELLSKTR 649
Cdd:COG1134 178 DAA-----FqKKCLARIRELRESGRtvIFVSHSMGAVRRLcDRAIWLEKGRLVMDGDpeeviaaYEALLAGRE 245
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1064-1262 |
1.65e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 67.13 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTL---SNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKLNIIPQHPVLFSG--- 1137
Cdd:PRK11153 20 ALNNVSLHIPAGEIFGVIGASGAGKSTLircINLLERPTSGRVLVDGQDLTALSEKELRKARRQIGMIFQHFNLLSSrtv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1138 ----TLQMNLDPLNKYS-DSKLWEALELCHLKEFVQSLPeklrheiseggENLSMGQRQLVCLARALLRKTKILILDEAT 1212
Cdd:PRK11153 100 fdnvALPLELAGTPKAEiKARVTELLELVGLSDKADRYP-----------AQLSGGQKQRVAIARALASNPKVLLCDEAT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 74136409 1213 ASIDFETDKLVQTTIRK---EFSdCTILTIAHRLQSI--IdSDRVLVLDSGSIVE 1262
Cdd:PRK11153 169 SALDPATTRSILELLKDinrELG-LTIVLITHEMDVVkrI-CDRVAVIDAGRLVE 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1048-1260 |
2.34e-11 |
|
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: 64.74 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1048 VEFINYQARYRDELgLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDIStiGLHD-----LR 1122
Cdd:cd03292 1 IEFINVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS--DLRGraipyLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1123 GKLNIIPQHPVLfsgtlqmnLDPLNKYSDSKLweALELCHL--KEFVQSLPEKLR-----HEISEGGENLSMGQRQLVCL 1195
Cdd:cd03292 78 RKIGVVFQDFRL--------LPDRNVYENVAF--ALEVTGVppREIRKRVPAALElvglsHKHRALPAELSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74136409 1196 ARALLRKTKILILDEATASIDFETDKLVQTTIRKEFSDCTILTIAHRLQSIID--SDRVLVLDSGSI 1260
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDttRHRVIALERGKL 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
448-583 |
2.49e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.78 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 448 PVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKG--SVAYVSQQAW------IQNCILQVNILFGS 519
Cdd:COG0488 12 PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPldddltVLDTVLDGDAELRA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 520 IMKK--EFYEQVLEACALLPDLEQLpkgdQTEIGERGV--------------------------NISGGQQHRVSLARAV 571
Cdd:COG0488 92 LEAEleELEAKLAEPDEDLERLAEL----QEEFEALGGweaearaeeilsglgfpeedldrpvsELSGGWRRRVALARAL 167
|
170
....*....|..
gi 74136409 572 YSGADIYLLDDP 583
Cdd:COG0488 168 LSEPDLLLLDEP 179
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
446-646 |
2.55e-11 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 65.00 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 446 GMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQ---------------RKGsVAYVSQqawIQNCI 510
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfdgeditglpphriaRLG-IGYVPE---GRRIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 511 --LQV--NILFGSIMKKEF--YEQVLE-ACALLPDLEQLpkgdqteIGERGVNISGGQQHRVSLARAVYSGADIYLLDDP 583
Cdd:COG0410 91 psLTVeeNLLLGAYARRDRaeVRADLErVYELFPRLKER-------RRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74136409 584 ---LSAVDVhvgKQLFEKV--IGSLGLlknkTRILVTHNLTLLPQM-DLIVVMESGRIAQMGTYQELLS 646
Cdd:COG0410 164 slgLAPLIV---EEIFEIIrrLNREGV----TILLVEQNARFALEIaDRAYVLERGRIVLEGTAAELLA 225
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
431-655 |
3.48e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 65.59 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 431 HAIEFTDATYSWnKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGS-------------V 497
Cdd:PRK13652 2 HLIETRDLCYSY-SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 498 AYVSQQA--WIQNCILQVNILFGSI---MKKEFYEQVLEACALLPDLEQLpkgdQTEIGErgvNISGGQQHRVSLARAVY 572
Cdd:PRK13652 81 GLVFQNPddQIFSPTVEQDIAFGPInlgLDEETVAHRVSSALHMLGLEEL----RDRVPH---HLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 573 SGADIYLLDDPLSAVDVHVGKQLFeKVIGSLGLLKNKTRILVTHNLTLLPQM-DLIVVMESGRIAQMGTYQELLSKTRNL 651
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELI-DFLNDLPETYGMTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEIFLQPDLL 232
|
....
gi 74136409 652 TNLH 655
Cdd:PRK13652 233 ARVH 236
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
433-646 |
3.56e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 65.42 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKG------SVAYVSQQAWI 506
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseeTVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 507 --QN-------CILQVNILFG----SIMKKEFYEQVLEAcallpdLEQLpkGDQTEIGERGVNISGGQQHRVSLARAVYS 573
Cdd:PRK13635 86 vfQNpdnqfvgATVQDDVAFGleniGVPREEMVERVDQA------LRQV--GMEDFLNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74136409 574 GADIYLLDDPLSAVDvHVGKQlfeKVIGSLGLLKNKTRILV---THNLTLLPQMDLIVVMESGRIAQMGTYQELLS 646
Cdd:PRK13635 158 QPDIIILDEATSMLD-PRGRR---EVLETVRQLKEQKGITVlsiTHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
430-646 |
4.30e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 65.14 E-value: 4.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 430 DHAIEFTDATYSWnKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSVAYVSQQAWIQNc 509
Cdd:PRK13647 2 DNIIEVEDLHFRY-KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 510 ilQVNILFGSIMKKEFYEQVLEACALLPDLEQLpkgDQTEIGER------GVN-----------ISGGQQHRVSLARAVY 572
Cdd:PRK13647 80 --KVGLVFQDPDDQVFSSTVWDDVAFGPVNMGL---DKDEVERRveealkAVRmwdfrdkppyhLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 573 SGADIYLLDDPLSAVDVHVGKQLFEkvigSLGLLKN--KTRILVTHNLTLLPQ-MDLIVVMESGR-IAQMGtyQELLS 646
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLME----ILDRLHNqgKTVIVATHDVDLAAEwADQVIVLKEGRvLAEGD--KSLLT 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1065-1228 |
4.44e-11 |
|
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: 63.65 E-value: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQTHGEEKIGIVGRTGAGKSTLsnclFRIV---ERAGGKIIIDGIDISTIGLHDLRGKLNIIPQHPVLFSG-TLQ 1140
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTL----LRILaglLPPSAGEVLWNGEPIRDAREDYRRRLAYLGHADGLKPElTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1141 MNLDPLNKY-----SDSKLWEALELCHLKEFvqsLPEKLRHeiseggenLSMGQRQLVCLARALLRKTKILILDEATASI 1215
Cdd:COG4133 94 ENLRFWAALyglraDREAIDEALEAVGLAGL---ADLPVRQ--------LSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170
....*....|...
gi 74136409 1216 DFETDKLVQTTIR 1228
Cdd:COG4133 163 DAAGVALLAELIA 175
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
433-651 |
5.94e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 65.07 E-value: 5.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNKtGMP----VLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEME------------------KLTGV 490
Cdd:PRK13637 3 IKIENLTHIYME-GTPfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKptsgkiiidgvditdkkvKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 491 VQRKGSVAYVSQQAWIQNCILQvNILFG----SIMKKEFYEQVLEACALLpdleqlpKGDQTEIGERG-VNISGGQQHRV 565
Cdd:PRK13637 82 RKKVGLVFQYPEYQLFEETIEK-DIAFGpinlGLSEEEIENRVKRAMNIV-------GLDYEDYKDKSpFELSGGQKRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 566 SLARAVYSGADIYLLDDPLSAVDVHVGKQLFEKvIGSLGLLKNKTRILVTHNLTLLPQM-DLIVVMESGRIAQMGTYQEL 644
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRDEILNK-IKELHKEYNMTIILVSHSMEDVAKLaDRIIVMNKGKCELQGTPREV 232
|
....*..
gi 74136409 645 LSKTRNL 651
Cdd:PRK13637 233 FKEVETL 239
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1064-1269 |
5.99e-11 |
|
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: 63.61 E-value: 5.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGgkiiidgidiSTIGL--HDLRGK---------LNIIPQHP 1132
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRS----------GSIRFdgRDITGLppheraragIGYVPEGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1133 VLFSG-----TLQMNLDPLNKYSDSKLWE-ALELchlkeFVQsLPEKLRHEisegGENLSMGQRQLVCLARALLRKTKIL 1206
Cdd:cd03224 85 RIFPEltveeNLLLGAYARRRAKRKARLErVYEL-----FPR-LKERRKQL----AGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1207 ILDEATASIdfeTDKLVQT------TIRKEfsDCTILTIAHRLQSIID-SDRVLVLDSGSIVEFEAPQNL 1269
Cdd:cd03224 155 LLDEPSEGL---APKIVEEifeairELRDE--GVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAEL 219
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
433-644 |
6.26e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 64.75 E-value: 6.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNKT---GMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVqRKGS--VAYVSQQAWIQ 507
Cdd:PRK13643 2 IKFEKVNYTYQPNspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV-TVGDivVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 508 NCILQVNILFGSIMKKEFYEQVLEACALLPDLEQLPKGDQTEIGERGVN---------------ISGGQQHRVSLARAVY 572
Cdd:PRK13643 81 PVRKKVGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEmvgladefwekspfeLSGGQMRRVAIAGILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 573 SGADIYLLDDPLSAVDVHVG---KQLFEKVIGSlgllkNKTRILVTHNL-TLLPQMDLIVVMESGRIAQMGT----YQEL 644
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARiemMQLFESIHQS-----GQTVVLVTHLMdDVADYADYVYLLEKGHIISCGTpsdvFQEV 235
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1185-1261 |
8.64e-11 |
|
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: 63.95 E-value: 8.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1185 LSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTIRK--EFSDCTILTIAHRLQSIIDS-DRVLVLDSGSIV 1261
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVV 222
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
449-637 |
9.04e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 63.30 E-value: 9.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 449 VLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKG-SVAYVSQ--QAWIQN----CILQVN------- 514
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqPMSKLSSaaKAELRNqklgFIYQFHhllpdft 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 515 --------ILFGSIMKKEFYEQVLEACALLpDLEQLPKGDQTEIgergvniSGGQQHRVSLARAVYSGADIYLLDDPLSA 586
Cdd:PRK11629 104 alenvampLLIGKKKPAEINSRALEMLAAV-GLEHRANHRPSEL-------SGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 74136409 587 VDVHVGKQLFEkVIGSLGLLKNKTRILVTHNLTLLPQMDLIVVMESGRIAQ 637
Cdd:PRK11629 176 LDARNADSIFQ-LLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTA 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
433-646 |
9.20e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 64.33 E-value: 9.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNKtGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSVAYVSQQAWIqNCILQ 512
Cdd:PRK13639 2 LETRDLKYSYPD-GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLL-EVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 513 VNILFGSIMKKEFYEQVLEACALLP--------DLEQLPKGDQTEIGERGV------NISGGQQHRVSLARAVYSGADIY 578
Cdd:PRK13639 80 VGIVFQNPDDQLFAPTVEEDVAFGPlnlglskeEVEKRVKEALKAVGMEGFenkpphHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74136409 579 LLDDPLSAVDVHVGKQLfekvigsLGLLK--NK---TRILVTHNLTLLP-QMDLIVVMESGRIAQMGTYQELLS 646
Cdd:PRK13639 160 VLDEPTSGLDPMGASQI-------MKLLYdlNKegiTIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1064-1273 |
1.00e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 64.71 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTH-GEekI-GIVGRTGAGKSTLSNCLFRIvERAggkiiidgidisTIG----------------LHDLRGKL 1125
Cdd:COG1135 20 ALDDVSLTIEkGE--IfGIIGYSGAGKSTLIRCINLL-ERP------------TSGsvlvdgvdltalsereLRAARRKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1126 NIIPQHPVLFSG-TLQMNLD-PLnkysdsKLW------------EALELCHLKEFVQSLPeklrheiseggENLSMGQRQ 1191
Cdd:COG1135 85 GMIFQHFNLLSSrTVAENVAlPL------EIAgvpkaeirkrvaELLELVGLSDKADAYP-----------SQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1192 LVCLARALLRKTKILILDEATASIDFET-----DKLVQttIRKEFsDCTILTIAHRL---QSIidSDRVLVLDSGSIVE- 1262
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPETtrsilDLLKD--INREL-GLTIVLITHEMdvvRRI--CDRVAVLENGRIVEq 222
|
250
....*....|....*..
gi 74136409 1263 ------FEAPQNLIRQK 1273
Cdd:COG1135 223 gpvldvFANPQSELTRR 239
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
446-640 |
1.03e-10 |
|
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: 66.58 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 446 GMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSVAYVSQQAWIQNCIL--QVNILFGSIMKK 523
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMcpQHNILFHHLTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 524 E---FYEQV---------LEACALLPDleqlpKGDQTEIGERGVNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHV 591
Cdd:TIGR01257 1022 EhilFYAQLkgrsweeaqLEMEAMLED-----TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 74136409 592 GKQLFEKVigsLGLLKNKTRILVTHNLTLLPQM-DLIVVMESGRIAQMGT 640
Cdd:TIGR01257 1097 RRSIWDLL---LKYRSGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGT 1143
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
448-647 |
1.32e-10 |
|
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: 63.39 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 448 PVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKG-SVAYVSQQAWIQ--NCILQVNILF-GSI--- 520
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGiDISKLPLHTLRSrlSIILQDPILFsGSIrfn 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 521 -------MKKEFYEqVLEACALLPDLEQLPKGDQTEIGERGVNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVgK 593
Cdd:cd03288 115 ldpeckcTDDRLWE-ALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT-E 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 74136409 594 QLFEKVIgsLGLLKNKTRILVTHNLTLLPQMDLIVVMESGRIAQMGTYQELLSK 647
Cdd:cd03288 193 NILQKVV--MTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQ 244
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
446-618 |
1.40e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 63.18 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 446 GMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSV--------AYVSQQ----AWiQNciLQV 513
Cdd:PRK11248 13 GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPvegpgaerGVVFQNegllPW-RN--VQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 514 NILFG---SIMKKEFYEQVLeacallpdLEQLPKGDQTEIGERGV-NISGGQQHRVSLARAVYSGADIYLLDDPLSAVDV 589
Cdd:PRK11248 90 NVAFGlqlAGVEKMQRLEIA--------HQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
170 180 190
....*....|....*....|....*....|....
gi 74136409 590 HVGKQLFEKvigslgLLK-----NKTRILVTHNL 618
Cdd:PRK11248 162 FTREQMQTL------LLKlwqetGKQVLLITHDI 189
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
449-640 |
1.40e-10 |
|
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: 62.84 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 449 VLKDLNIKIPEGALVAVVGQVGSGKSSMLSaILGEMEKLT-GVVQ-----------------RKGSVAYVSQQ------- 503
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLG-LLAGLDRPTsGTVRlagqdlfaldedararlRARHVGFVFQSfqllptl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 504 -AwIQNCILQVNiLFGSIMKKEFYEQVLEACALLPDLEQLPKGdqteigergvnISGGQQHRVSLARAVYSGADIYLLDD 582
Cdd:COG4181 106 tA-LENVMLPLE-LAGRRDARARARALLERVGLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAILFADE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74136409 583 PLSAVDVHVGkqlfEKVIgslGLL--KNKTR----ILVTHNLTLLPQMDLIVVMESGRIAQMGT 640
Cdd:COG4181 173 PTGNLDAATG----EQII---DLLfeLNRERgttlVLVTHDPALAARCDRVLRLRAGRLVEDTA 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
433-588 |
1.44e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 63.49 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNKTGMPVlkDLNIKipEGALVAVVGQVGSGKSSMLSAILG----------EMEKLTGVVQRKGSVA---- 498
Cdd:PRK09984 7 VEKLAKTFNQHQALHAV--DLNIH--HGEMVALLGPSGSGKSTLLRHLSGlitgdksagsHIELLGRTVQREGRLArdir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 499 -------YVSQQAWIQN--CILQvNILFGSIMKKEFYEQVLEAcaLLPDLEQLPKGDQTEIG------ERGVNISGGQQH 563
Cdd:PRK09984 83 ksrantgYIFQQFNLVNrlSVLE-NVLIGALGSTPFWRTCFSW--FTREQKQRALQALTRVGmvhfahQRVSTLSGGQQQ 159
|
170 180
....*....|....*....|....*
gi 74136409 564 RVSLARAVYSGADIYLLDDPLSAVD 588
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLD 184
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1056-1269 |
1.50e-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: 62.52 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1056 RYRDELGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVEraggkiiidgidiSTIG------------LHDLRG 1123
Cdd:cd03263 9 TYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELR-------------PTSGtayingysirtdRKAARQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1124 KLNIIPQHPVLFSgtlqmNLDPlnkysdsklWEALELCHLkefVQSLPEKLRHEISEGGE--------------NLSMGQ 1189
Cdd:cd03263 76 SLGYCPQFDALFD-----ELTV---------REHLRFYAR---LKGLPKSEIKEEVELLLrvlgltdkankrarTLSGGM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1190 RQLVCLARALLRKTKILILDEATASIDFETDKLVQTTIRKEFSDCTILTIAHRLQSI-IDSDRVLVLDSGSIVEFEAPQN 1268
Cdd:cd03263 139 KRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIAIMSDGKLRCIGSPQE 218
|
.
gi 74136409 1269 L 1269
Cdd:cd03263 219 L 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
449-635 |
1.55e-10 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 62.16 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 449 VLKDLNIKIPEGALVAVVGQVGSGKSSMLSAI-------LGEM----EKLTG----VVQRKGSVAYVSQQ--AWIQNCIL 511
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCInlleepdSGTIiidgLKLTDdkknINELRQKVGMVFQQfnLFPHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 512 QvNILFGSI----MKKEfyEQVLEACALLPDLEQLPKGDQteigeRGVNISGGQQHRVSLARAVYSGADIYLLDDPLSAV 587
Cdd:cd03262 95 E-NITLAPIkvkgMSKA--EAEERALELLEKVGLADKADA-----YPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSAL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74136409 588 D-------VHVGKQLFEkvigslgllKNKTRILVTHnltllpQM-------DLIVVMESGRI 635
Cdd:cd03262 167 DpelvgevLDVMKDLAE---------EGMTMVVVTH------EMgfarevaDRVIFMDDGRI 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
446-650 |
1.55e-10 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 62.70 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 446 GMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGeMEKLT-GVV----------------QRKgSVAYVSQQ----- 503
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINL-LEEPDsGTItvdgedltdskkdinkLRR-KVGMVFQQfnlfp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 504 ---AwIQNCIL-QVNILfgsIMKKEfyEQVLEACALLpdleqlpkgDQTEIGERG----VNISGGQQHRVSLARAVYSGA 575
Cdd:COG1126 91 hltV-LENVTLaPIKVK---KMSKA--EAEERAMELL---------ERVGLADKAdaypAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 576 DIYLLDDPLSAVD------VhvgkqlfEKVIGSL---GLlknkTRILVTHnltllpQM-------DLIVVMESGRIAQMG 639
Cdd:COG1126 156 KVMLFDEPTSALDpelvgeV-------LDVMRDLakeGM----TMVVVTH------EMgfarevaDRVVFMDGGRIVEEG 218
|
250
....*....|.
gi 74136409 640 TYQELLSKTRN 650
Cdd:COG1126 219 PPEEFFENPQH 229
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
432-657 |
1.77e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 62.87 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 432 AIEFTDATYSWNKTgmPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKG-------------SVA 498
Cdd:PRK13548 2 MLEARNLSVRLGGR--TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 499 YVSQQAwiqncilqvNILF--------------GSIMKKEFYEQVLEACALLpDLEQLPKGDQTEIgergvniSGGQQHR 564
Cdd:PRK13548 80 VLPQHS---------SLSFpftveevvamgrapHGLSRAEDDALVAAALAQV-DLAHLAGRDYPQL-------SGGEQQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 565 VSLARA------VYSGADIYLLDDPLSAVDV-HvgkQLfekviGSLGLLKNKTR------ILVTHNLTLLPQM-DLIVVM 630
Cdd:PRK13548 143 VQLARVlaqlwePDGPPRWLLLDEPTSALDLaH---QH-----HVLRLARQLAHerglavIVVLHDLNLAARYaDRIVLL 214
|
250 260
....*....|....*....|....*..
gi 74136409 631 ESGRIAQMGTYQELLSKtrnlTNLHQV 657
Cdd:PRK13548 215 HQGRLVADGTPAEVLTP----ETLRRV 237
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
430-647 |
1.79e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 63.33 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 430 DHAIEFTDATYSWNKtGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSVAYVSQQAwIQNC 509
Cdd:PRK13636 3 DYILKVEELNYNYSD-GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKG-LMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 510 ILQVNILFGSIMKKEFYEQVLEACALLPDLEQLPKGDQTEIGERGVNISG--------------GQQHRVSLARAVYSGA 575
Cdd:PRK13636 81 RESVGMVFQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGiehlkdkpthclsfGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74136409 576 DIYLLDDPLSAVDvHVGKQLFEKVIGSLGLLKNKTRILVTHNLTLLP-QMDLIVVMESGRIAQMGTYQELLSK 647
Cdd:PRK13636 161 KVLVLDEPTAGLD-PMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1064-1265 |
2.01e-10 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 62.37 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCL----------FRI----VERAggkiiidgidiSTIGLHDLRGKlNI-- 1127
Cdd:COG1136 23 ALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILggldrptsgeVLIdgqdISSL-----------SERELARLRRR-HIgf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1128 IPQHPVLFSG-------TLQMNLDPLNKYSDSKlwEALELchLKEFvqSLPEKLRHEISEggenLSMGQRQLVCLARALL 1200
Cdd:COG1136 91 VFQFFNLLPEltalenvALPLLLAGVSRKERRE--RAREL--LERV--GLGDRLDHRPSQ----LSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 1201 RKTKILILDEATASIDFETDKLVQTTIR---KEFsDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEA 1265
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRelnREL-GTTIVMVTHDPELAARADRVIRLRDGRIVSDER 227
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1065-1294 |
2.10e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.53 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQTHGEEKIGIVGRTGAGKSTL-SNCLFRIVERAGGKIIidgidistiglhdLRGKLNIIPQHPVLFSGTLQMNL 1143
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLiSAMLGELPPRSDASVV-------------IRGTVAYVPQVSWIFNATVRDNI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1144 DPLNKYSDSKLWEALELCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLV 1223
Cdd:PLN03130 700 LFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQV 779
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74136409 1224 -QTTIRKEFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQNLIRQKGLFYEMTTDAGITQESGTEKK 1294
Cdd:PLN03130 780 fDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENAGKMEEYVEENG 851
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1062-1261 |
2.10e-10 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 62.75 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1062 GL-ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLF--------RIVeraggkiiidgidistiglhdLRGKlNIIP--- 1129
Cdd:COG0411 16 GLvAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITgfyrptsgRIL---------------------FDGR-DITGlpp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1130 ------------QHPVLFSG-----------------TLQMNLDPLNKYSDS------KLWEALELCHLkefvqslpEKL 1174
Cdd:COG0411 74 hriarlgiartfQNPRLFPEltvlenvlvaaharlgrGLLAALLRLPRARREereareRAEELLERVGL--------ADR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1175 RHEISEggeNLSMGQRQLVCLARALLRKTKILILDEATA--SIDfETDKLVQT--TIRKEFsDCTILTIAHRLQSIID-S 1249
Cdd:COG0411 146 ADEPAG---NLSYGQQRRLEIARALATEPKLLLLDEPAAglNPE-ETEELAELirRLRDER-GITILLIEHDMDLVMGlA 220
|
250
....*....|..
gi 74136409 1250 DRVLVLDSGSIV 1261
Cdd:COG0411 221 DRIVVLDFGRVI 232
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
450-618 |
2.46e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 62.49 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 450 LKDLNIKIPEGALVAVVGQVGSGKSSMLSAIlGEMEKLTGVVQRKGSVAY---------------------VSQQAWIQN 508
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRMNDLNPEVTITGSIVYnghniysprtdtvdlrkeigmVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 509 CILQVNILFGSIMKKEFYEQVLEAcALLPDLEQLPKGDQTE--IGERGVNISGGQQHRVSLARAVYSGADIYLLDDPLSA 586
Cdd:PRK14239 100 MSIYENVVYGLRLKGIKDKQVLDE-AVEKSLKGASIWDEVKdrLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSA 178
|
170 180 190
....*....|....*....|....*....|...
gi 74136409 587 VD-VHVGKqlFEKVIgsLGLLKNKTRILVTHNL 618
Cdd:PRK14239 179 LDpISAGK--IEETL--LGLKDDYTMLLVTRSM 207
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
433-669 |
2.49e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 63.56 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDA--TYSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILG--------------EMEKLTG---VVQR 493
Cdd:COG1135 2 IELENLskTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLlerptsgsvlvdgvDLTALSErelRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 494 KgSVAYVSQQAwiqncilqvNIL-----FGSIM---------KKEFYEQVLEacaLLpDLeqlpkgdqTEIGERG----V 555
Cdd:COG1135 82 R-KIGMIFQHF---------NLLssrtvAENVAlpleiagvpKAEIRKRVAE---LL-EL--------VGLSDKAdaypS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 556 NISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGKQLfekvigsLGLLK--NK----TRILVTHnltllpQMDLI-- 627
Cdd:COG1135 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSI-------LDLLKdiNRelglTIVLITH------EMDVVrr 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 74136409 628 -----VVMESGRIAQMGTYQELLSK-----TRNLtnLHQVISEEEKAHALKR 669
Cdd:COG1135 207 icdrvAVLENGRIVEQGPVLDVFANpqselTRRF--LPTVLNDELPEELLAR 256
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1063-1272 |
2.74e-10 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 62.66 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1063 LALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIG---LHDLRGK--------LNIIPQH 1131
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKkismvfqsFALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1132 PVLFSGTLQMNLDPLNKYS-DSKLWEALELCHLKEFVQSLPEKLrheiseggenlSMGQRQLVCLARALLRKTKILILDE 1210
Cdd:cd03294 118 TVLENVAFGLEVQGVPRAErEERAAEALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74136409 1211 ATASIDfetdklvqTTIRKEFSDC----------TILTIAHRLQSIID-SDRVLVLDSGSIVEFEAPQNLIRQ 1272
Cdd:cd03294 187 AFSALD--------PLIRREMQDEllrlqaelqkTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
446-636 |
2.87e-10 |
|
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: 60.13 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 446 GMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAilgemekLTGVVQR-KGSVaYVSQQAwiqncilqvnILFGSIMKKE 524
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKI-------LSGLYKPdSGEI-LVDGKE----------VSFASPRDAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 525 fyeqvleacallpdleqlpkgdqteigERGVNI----SGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGKQLFeKVI 600
Cdd:cd03216 74 ---------------------------RAGIAMvyqlSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLF-KVI 125
|
170 180 190
....*....|....*....|....*....|....*..
gi 74136409 601 GSLGlLKNKTRILVTHNLTLLPQM-DLIVVMESGRIA 636
Cdd:cd03216 126 RRLR-AQGVAVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
448-657 |
2.95e-10 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 62.44 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 448 PVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVV-------------QRKGSVAYVSQQ-----AWIqnc 509
Cdd:COG4559 15 TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVrlngrplaawspwELARRRAVLPQHsslafPFT--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 510 ILQVnILFG----SIMKKEFYEQVLEACALLpDLEQLpkgdqteiGERGVN-ISGGQQHRVSLARA-------VYSGADI 577
Cdd:COG4559 92 VEEV-VALGraphGSSAAQDRQIVREALALV-GLAHL--------AGRSYQtLSGGEQQRVQLARVlaqlwepVDGGPRW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 578 YLLDDPLSAVDVHvgKQLfekviGSLGLLKNKTR-----ILVTHNLTLLPQM-DLIVVMESGRIAQMGTYQELLSKtrnl 651
Cdd:COG4559 162 LFLDEPTSALDLA--HQH-----AVLRLARQLARrgggvVAVLHDLNLAAQYaDRILLLHQGRLVAQGTPEEVLTD---- 230
|
....*.
gi 74136409 652 TNLHQV 657
Cdd:COG4559 231 ELLERV 236
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
774-942 |
3.70e-10 |
|
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: 62.58 E-value: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 774 IYGILGLIKGLFVCSGAYVITrgsLAASRTMY---VQLLNNVLHLPIQFFETNSTGQIISRFTKDI--------FIIDMR 842
Cdd:cd18557 41 ILLAIYLLQSVFTFVRYYLFN---IAGERIVArlrRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTsvlqsavtDNLSQL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 843 LHYYLRLwvnctLDVIGTILVIIGALPLFILGIIPSVFFYFSIQRYYVassRQIRRLTGASRSPVISHFSETLSGVSTIR 922
Cdd:cd18557 118 LRNILQV-----IGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYI---RKLSKEVQDALAKAGQVAEESLSNIRTVR 189
|
170 180
....*....|....*....|
gi 74136409 923 AFGHQQRFIQQYKEVVNENL 942
Cdd:cd18557 190 SFSAEEKEIRRYSEALDRSY 209
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1064-1272 |
4.31e-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: 63.67 E-value: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCL------------FRI----VERAGGKIIIDGIDISTIGLhdLRGKLNI 1127
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIagvleptsgevnVRVgdewVDMTKPGPDGRGRAKRYIGI--LHQEYDL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1128 IPQHPVLFSGTLQMNLDPLNKYSDSKLWEALELCHLKE-FVQSLPEKLRHEISEGgenlsmgQRQLVCLARALLRKTKIL 1206
Cdd:TIGR03269 377 YPHRTVLDNLTEAIGLELPDELARMKAVITLKMVGFDEeKAEEILDKYPDELSEG-------ERHRVALAQVLIKEPRIV 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1207 ILDEATASIDFETDKLVQTTI---RKEFSDcTILTIAHRLQSIID-SDRVLVLDSGSIVEFEAPQNLIRQ 1272
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSIlkaREEMEQ-TFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1065-1262 |
5.76e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 61.63 E-value: 5.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCL------------FRIVERAGGKIIIDGIDISTIGL--HDLRGKLNiiPQ 1130
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLvglespsqgnvsWRGEPLAKLNRAQRKAFRRDIQMvfQDSISAVN--PR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1131 HPVLFSgtLQMNLDPLNKYSDS-KLWEALELCHLKEFVQSLPEKLRHEiseggenLSMGQRQLVCLARALLRKTKILILD 1209
Cdd:PRK10419 106 KTVREI--IREPLRHLLSLDKAeRLARASEMLRAVDLDDSVLDKRPPQ-------LSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 74136409 1210 EATASID--FETDKLVQTTIRKEFSDCTILTIAHRLqSIID--SDRVLVLDSGSIVE 1262
Cdd:PRK10419 177 EAVSNLDlvLQAGVIRLLKKLQQQFGTACLFITHDL-RLVErfCQRVMVMDNGQIVE 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1047-1269 |
6.00e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 61.65 E-value: 6.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1047 VVEFINYQARYRDELGL-ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKL 1125
Cdd:PRK13642 4 ILEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1126 NIIPQHP--VLFSGTLQMNL-----------DPLNKYSDsklwEALELCHLKEFVQSLPEKLrheiseggenlSMGQRQL 1192
Cdd:PRK13642 84 GMVFQNPdnQFVGATVEDDVafgmenqgiprEEMIKRVD----EALLAVNMLDFKTREPARL-----------SGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74136409 1193 VCLARALLRKTKILILDEATASIDFETDKLVQTTIR--KEFSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQNL 1269
Cdd:PRK13642 149 VAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHeiKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1064-1264 |
6.33e-10 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 60.62 E-value: 6.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRI-------VERAGGKIIIDGIdisTIGLH-DLRGKLNIIpqhpvlF 1135
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIyppdsgtVTVRGRVSSLLGL---GGGFNpELTGRENIY------L 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1136 SGTLqMNLDPlnKYSDSKLWEALELCHLKEFVQsLPEKlrheiseggeNLSMGQRQLVCLARALLRKTKILILDEATASI 1215
Cdd:cd03220 108 NGRL-LGLSR--KEIDEKIDEIIEFSELGDFID-LPVK----------TYSSGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 74136409 1216 DFETDKLVQTTIRKEFSDCTILTIA-HRLQSIID-SDRVLVLDSGSIVEFE 1264
Cdd:cd03220 174 DAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1064-1279 |
6.85e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.01 E-value: 6.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCL----------FRIVERAGGKIIIDGIDISTIGLhdLRGKLNIIPQHPV 1133
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILsgnyqpdagsILIDGQEMRFASTTAALAAGVAI--IYQELHLVPEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1134 ---LFSGTLQMNLDPLNKySDSKLWEALELCHLKEFVQslPE-KLRHeiseggenLSMGQRQLVCLARALLRKTKILILD 1209
Cdd:PRK11288 97 aenLYLGQLPHKGGIVNR-RLLNYEAREQLEHLGVDID--PDtPLKY--------LSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74136409 1210 EATASIDF-ETDKL--VQTTIRKEfsDCTILTIAHRLQSIID-SDRVLVLDSGSIVE-FEAPQNLIRQKgLFYEM 1279
Cdd:PRK11288 166 EPTSSLSArEIEQLfrVIRELRAE--GRVILYVSHRMEEIFAlCDAITVFKDGRYVAtFDDMAQVDRDQ-LVQAM 237
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
433-588 |
8.00e-10 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 60.11 E-value: 8.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWnKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQ---------RKGSVAYVSQQ 503
Cdd:cd03292 1 IEFINVTKTY-PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRvngqdvsdlRGRAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 504 AWIqncILQVNIL------FGSIM---------KKEFYEQVLEACALLpdleqlpkGDQTEIGERGVNISGGQQHRVSLA 568
Cdd:cd03292 80 IGV---VFQDFRLlpdrnvYENVAfalevtgvpPREIRKRVPAALELV--------GLSHKHRALPAELSGGEQQRVAIA 148
|
170 180
....*....|....*....|
gi 74136409 569 RAVYSGADIYLLDDPLSAVD 588
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLD 168
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
449-635 |
8.33e-10 |
|
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: 59.99 E-value: 8.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 449 VLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSvayvSQQAWIQNcilqvniLFG------SIMK 522
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK----PLDIAARN-------RIGylpeerGLYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 523 KEfyeQVLEACALLPDLEQLPKGD----------QTEIGE----RGVNISGGQQHRVSLARAVYSGADIYLLDDPLSAVD 588
Cdd:cd03269 84 KM---KVIDQLVYLAQLKGLKKEEarrridewleRLELSEyankRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 74136409 589 VhVGKQLFEKVIGSLgLLKNKTRILVTHNLTLLPQM-DLIVVMESGRI 635
Cdd:cd03269 161 P-VNVELLKDVIREL-ARAGKTVILSTHQMELVEELcDRVLLLNKGRA 206
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
429-670 |
8.43e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 61.26 E-value: 8.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 429 GDHAIEFTDATYSWNKTG----MPVLKDLNIKIPEGALVAVVGQVGSGKSSM---LSAIL--------------GEMEKL 487
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALLipsegkvyvdgldtSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 488 TGVVQRKGSVaYVSQQAWIQNCILQVNILFG----SIMKKEFYEQVLEAcallpdleqLPKGDQTEIGERGVN-ISGGQQ 562
Cdd:PRK13633 81 WDIRNKAGMV-FQNPDNQIVATIVEEDVAFGpenlGIPPEEIRERVDES---------LKKVGMYEYRRHAPHlLSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 563 HRVSLARAVYSGADIYLLDDPLSAVDvHVGKQLFEKVIGSLGLLKNKTRILVTHNLTLLPQMDLIVVMESGRIAQMGTYQ 642
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLD-PSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPK 229
|
250 260
....*....|....*....|....*....
gi 74136409 643 ELLSKTRNLTNLH-QVISEEEKAHALKRA 670
Cdd:PRK13633 230 EIFKEVEMMKKIGlDVPQVTELAYELKKE 258
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
429-583 |
8.58e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.77 E-value: 8.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 429 GDHAIEFTDATYSWNktGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRkGS---VAYVSQQAw 505
Cdd:COG0488 312 GKKVLELEGLSKSYG--DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GEtvkIGYFDQHQ- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 506 iqncilqvnilfgsimkKEFYEQ--VLEAcallpdLEQL-PKGDQTEI----------GER-----GVnISGGQQHRVSL 567
Cdd:COG0488 388 -----------------EELDPDktVLDE------LRDGaPGGTEQEVrgylgrflfsGDDafkpvGV-LSGGEKARLAL 443
|
170
....*....|....*.
gi 74136409 568 ARAVYSGADIYLLDDP 583
Cdd:COG0488 444 AKLLLSPPNVLLLDEP 459
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1065-1270 |
8.83e-10 |
|
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: 60.43 E-value: 8.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGgkiiidgidistiGLHDLRGK-----------LNIIPQHPV 1133
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDS-------------GKILLNGKditnlppekrdISYVPQNYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1134 LFSG-TLQMNLD-PLNKYSDSKLwealelcHLKEFVQSLPEKL--RHEISEGGENLSMGQRQLVCLARALLRKTKILILD 1209
Cdd:cd03299 82 LFPHmTVYKNIAyGLKKRKVDKK-------EIERKVLEIAEMLgiDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74136409 1210 EATASIDFET-DKLVQ--TTIRKEFsDCTILTIAHRLQSI-IDSDRVLVLDSGSIVEFEAPQNLI 1270
Cdd:cd03299 155 EPFSALDVRTkEKLREelKKIRKEF-GVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
432-646 |
9.18e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 61.38 E-value: 9.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 432 AIEFTDATYSWNKtGMPV----LKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKG-SVAYVSQQAWI 506
Cdd:PRK13641 2 SIKFENVDYIYSP-GTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyHITPETGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 507 QNCILQVNILFGSIMKKEFYEQVLEACALLPD-------------LEQLPK-GDQTEIGERG-VNISGGQQHRVSLARAV 571
Cdd:PRK13641 81 KKLRKKVSLVFQFPEAQLFENTVLKDVEFGPKnfgfsedeakekaLKWLKKvGLSEDLISKSpFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 572 YSGADIYLLDDPLSAVDVHVGKQLFEkvigslgLLKN-----KTRILVTHNLTLLPQ-MDLIVVMESGRIAQMGTYQELL 645
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQ-------LFKDyqkagHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIF 233
|
.
gi 74136409 646 S 646
Cdd:PRK13641 234 S 234
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1048-1260 |
9.18e-10 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 59.85 E-value: 9.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1048 VEFINYQARYRDELglALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVE--RAGGKIIIDGIDISTIGLHDLRGKL 1125
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEpdSGTIIIDGLKLTDDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1126 NIIPQHPVLFSgtlqmNLDPLNKYSDSKLW--------------EALELCHLKEFVQSLPEKlrheiseggenLSMGQRQ 1191
Cdd:cd03262 79 GMVFQQFNLFP-----HLTVLENITLAPIKvkgmskaeaeeralELLEKVGLADKADAYPAQ-----------LSGGQQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74136409 1192 LVCLARALLRKTKILILDEATASIDFETDKLVQTTIRK-EFSDCTILTIAHRLQSIID-SDRVLVLDSGSI 1260
Cdd:cd03262 143 RVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
446-616 |
9.53e-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: 59.81 E-value: 9.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 446 GMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSVAYVSQQAWIQNC--ILQVNILFGSIMKK 523
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLlyLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 524 E---FY------EQVLEACAL--LPDLEQLPKGdqteigergvNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVG 592
Cdd:cd03231 92 EnlrFWhadhsdEQVEEALARvgLNGFEDRPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180
....*....|....*....|....
gi 74136409 593 KQLFEKVIGSLGllKNKTRILVTH 616
Cdd:cd03231 162 ARFAEAMAGHCA--RGGMVVLTTH 183
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
446-617 |
9.60e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 59.89 E-value: 9.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 446 GMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKG----------SVAYVSQQAWIQNcILQV-- 513
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddpdvaeACHYLGHRNAMKP-ALTVae 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 514 NILFGSIMKKEFYEQVLEA-CAL-LPDLEQLPKGdqteigergvNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHv 591
Cdd:PRK13539 93 NLEFWAAFLGGEELDIAAAlEAVgLAPLAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA- 161
|
170 180
....*....|....*....|....*.
gi 74136409 592 GKQLFEKVIgSLGLLKNKTRILVTHN 617
Cdd:PRK13539 162 AVALFAELI-RAHLAQGGIVIAATHI 186
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1065-1273 |
9.98e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 60.83 E-value: 9.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVE------RAGGKIIIDGIDISTIGLHDLRGKLNIIPQHPVLFSG- 1137
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPHl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1138 TLQMNLD-PLNKYSDSKLWEALELCHLKEFVQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRKTKILILDEATASID 1216
Cdd:PRK14246 106 SIYDNIAyPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74136409 1217 FETDKLVQTTIRKEFSDCTILTIAHRLQSIID-SDRVLVLDSGSIVE-------FEAPQNLIRQK 1273
Cdd:PRK14246 186 IVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEwgssneiFTSPKNELTEK 250
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
448-649 |
1.04e-09 |
|
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: 61.61 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 448 PVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILG-------------------------EMEKLtgvvqRKGSVAYVSQ 502
Cdd:COG0444 19 KAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpppgitsgeilfdgedllklsekELRKI-----RGREIQMIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 503 QAW--------IQNCILQVNILFGSIMKKEFYEQVLEACAL--LPDLE--------QLpkgdqteigergvniSGGQQHR 564
Cdd:COG0444 94 DPMtslnpvmtVGDQIAEPLRIHGGLSKAEARERAIELLERvgLPDPErrldryphEL---------------SGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 565 VSLARAVYSGADIYLLDDPLSAVDVHVGKQLfekvigsLGLLK------NKTRILVTHNLTLLPQM-DLIVVMESGRIAQ 637
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQI-------LNLLKdlqrelGLAILFITHDLGVVAEIaDRVAVMYAGRIVE 231
|
250
....*....|..
gi 74136409 638 MGTYQELLSKTR 649
Cdd:COG0444 232 EGPVEELFENPR 243
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
449-650 |
1.08e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 60.70 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 449 VLKDLNIKIPEGALVAVVGQVGSGKSSMLSAI-----LGEMEKLTG-------------VVQRKGSVAYVSQqawIQNCI 510
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGevyldgqdifkmdVIELRRRVQMVFQ---IPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 511 ------------LQVNILFGSimKKEFYEQVLEAcallpdLE--QLPKGDQTEIGERGVNISGGQQHRVSLARAVYSGAD 576
Cdd:PRK14247 95 pnlsifenvalgLKLNRLVKS--KKELQERVRWA------LEkaQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 577 IYLLDDPLSAVD-VHVGK--QLFekvigsLGLLKNKTRILVTHnltlLPQM-----DLIVVMESGRIAQMGTYQELLSKT 648
Cdd:PRK14247 167 VLLADEPTANLDpENTAKieSLF------LELKKDMTIVLVTH----FPQQaarisDYVAFLYKGQIVEWGPTREVFTNP 236
|
..
gi 74136409 649 RN 650
Cdd:PRK14247 237 RH 238
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
774-942 |
1.20e-09 |
|
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: 61.02 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 774 IYGILGLIKGLF--VCSGAYVITRGSLAasRTMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDMRLHYYLRLWV 851
Cdd:cd18572 41 LLLLLSVLSGLFsgLRGGCFSYAGTRLV--RRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 852 NCTLDVIGTILVI------IGALPLFILGIIPSVFFYFSiqRYYVASSRQIRRLTGASRSPVishfSETLSGVSTIRAFG 925
Cdd:cd18572 119 RNLVQLVGGLAFMfslswrLTLLAFITVPVIALITKVYG--RYYRKLSKEIQDALAEANQVA----EEALSNIRTVRSFA 192
|
170
....*....|....*..
gi 74136409 926 HQQRFIQQYKEVVNENL 942
Cdd:cd18572 193 TEEREARRYERALDKAL 209
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
433-643 |
1.49e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 62.57 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWnkTGMPVL-KDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSVAY-VSQQAWIQNCI 510
Cdd:PLN03073 509 ISFSDASFGY--PGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMaVFSQHHVDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 511 LQVNILFgsIMKKEF---YEQVLEAcallpdleqlpkgdqtEIGERGVN----------ISGGQQHRVSLARAVYSGADI 577
Cdd:PLN03073 587 LSSNPLL--YMMRCFpgvPEQKLRA----------------HLGSFGVTgnlalqpmytLSGGQKSRVAFAKITFKKPHI 648
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 578 YLLDDPLSAVDVHVgkqlFEKVIGSLGLLKNKTrILVTHNLTLLP-QMDLIVVMESGRIAQM-GTYQE 643
Cdd:PLN03073 649 LLLDEPSNHLDLDA----VEALIQGLVLFQGGV-LMVSHDEHLISgSVDELWVVSEGKVTPFhGTFHD 711
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
774-940 |
1.61e-09 |
|
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: 60.57 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 774 IYGILGLikGLFVCSGAYVITRGSLAA--SRTMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDM----RLHYYL 847
Cdd:cd18577 52 YFVYLGI--GSFVLSYIQTACWTITGErqARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDgigeKLGLLI 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 848 RlwvNCTLDVIGTI----------LVIIGALPLFilgIIPSVFFYFSIQRYyvaSSRQIRRLTGASrspviSHFSETLSG 917
Cdd:cd18577 130 Q---SLSTFIAGFIiafiyswkltLVLLATLPLI---AIVGGIMGKLLSKY---TKKEQEAYAKAG-----SIAEEALSS 195
|
170 180
....*....|....*....|...
gi 74136409 918 VSTIRAFGHQQRFIQQYKEVVNE 940
Cdd:cd18577 196 IRTVKAFGGEEKEIKRYSKALEK 218
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
449-639 |
1.65e-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: 59.08 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 449 VLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEME-KLTgvvqrKGSVAYVSQqawiqncilqvnilfgSIMKKEFYE 527
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyEVT-----EGEILFKGE----------------DITDLPPEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 528 QVLEACALLPdleQLPkgdqTEIGE-------RGVN--ISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVhVGKQLFEK 598
Cdd:cd03217 74 RARLGIFLAF---QYP----PEIPGvknadflRYVNegFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI-DALRLVAE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 74136409 599 VIGSLgLLKNKTRILVTHNLTLLPQM--DLIVVMESGRIAQMG 639
Cdd:cd03217 146 VINKL-REEGKSVLIITHYQRLLDYIkpDRVHVLYDGRIVKSG 187
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
447-616 |
1.68e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.59 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 447 MPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLtgvvQRKGSVAyVSQQAWIQNCILQVNILfgsiMKKEFY 526
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGT----PVAGCVD-VPDNQFGREASLIDAIG----RKGDFK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 527 E--QVLEACALlpdleqlpkGDQTEIGERGVNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGKQLFEKViGSLG 604
Cdd:COG2401 114 DavELLNAVGL---------SDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNL-QKLA 183
|
170
....*....|..
gi 74136409 605 LLKNKTRILVTH 616
Cdd:COG2401 184 RRAGITLVVATH 195
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
777-966 |
1.91e-09 |
|
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: 60.52 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 777 ILGLIKGLFVCSGAYVITRGSLAASRTMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDMRLHYYLRLWVNCTLD 856
Cdd:cd18542 47 GVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 857 VIGTILVIIG---ALPLFILGIIP-----SVFFYFSIQRYYVASSRQIRRLTgasrspviSHFSETLSGVSTIRAFGHQQ 928
Cdd:cd18542 127 FIGALIIMFSinwKLTLISLAIIPfialfSYVFFKKVRPAFEEIREQEGELN--------TVLQENLTGVRVVKAFARED 198
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 74136409 929 RFIQQYKEvVNENlvcFYN-NVISNRWLSVR---LEFLGNLM 966
Cdd:cd18542 199 YEIEKFDK-ENEE---YRDlNIKLAKLLAKYwplMDFLSGLQ 236
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
450-644 |
2.00e-09 |
|
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: 59.31 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 450 LKDLNIKIPEGALVAVVGQVGSGKSSMLSaILGEMEKLTG---------VVQRKGSV----AYVSQQ--------AWiQN 508
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIK-MLTTLLKPTSgratvaghdVVREPREVrrriGIVFQDlsvddeltGW-EN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 509 CILQVNIL-FGSIMKKEFYEQVLEACALLpdleqlpkgdqtEIGERGV-NISGGQQHRVSLARAVYSGADIYLLDDPLSA 586
Cdd:cd03265 94 LYIHARLYgVPGAERRERIDELLDFVGLL------------EAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 74136409 587 VDVHVGKQLFEkVIGSLGLLKNKTRILVTHNLTLLPQM-DLIVVMESGRIAQMGTYQEL 644
Cdd:cd03265 162 LDPQTRAHVWE-YIEKLKEEFGMTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGTPEEL 219
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
449-640 |
2.09e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 59.64 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 449 VLKDLNIKIPEGALVAVVGQVGSGKSSMLSAI-LGEM--------------------EKLTGVVQRKgsVAYVSQQ--AW 505
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMprsgtlniagnhfdfsktpsDKAIRELRRN--VGMVFQQynLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 506 -----IQNCI-LQVNILfgSIMKKEFYEQVLEacaLLPDLEQLPKGDQTEIgergvNISGGQQHRVSLARAVYSGADIYL 579
Cdd:PRK11124 95 phltvQQNLIeAPCRVL--GLSKDQALARAEK---LLERLRLKPYADRFPL-----HLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74136409 580 LDDPLSAVDVHVGKQLFeKVIGSL---GLlknkTRILVTHNLTLLPQMDLIVV-MESGRIAQMGT 640
Cdd:PRK11124 165 FDEPTAALDPEITAQIV-SIIRELaetGI----TQVIVTHEVEVARKTASRVVyMENGHIVEQGD 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
433-650 |
2.30e-09 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 59.38 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNKTGMpvlkDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVV-------------QRKgsVAY 499
Cdd:COG3840 2 LRLDDLTYRYGDFPL----RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIlwngqdltalppaERP--VSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 500 VSQQawiQN-----CILQvNILFGsimkkefyeqvleacaLLPDLeQLPKGDQTEIGE--RGVNI-----------SGGQ 561
Cdd:COG3840 76 LFQE---NNlfphlTVAQ-NIGLG----------------LRPGL-KLTAEQRAQVEQalERVGLaglldrlpgqlSGGQ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 562 QHRVSLARAVYSGADIYLLDDPLSAVDV---HVGKQLFEKVIGSLGLlknkTRILVTHNLT-LLPQMDLIVVMESGRIAQ 637
Cdd:COG3840 135 RQRVALARCLVRKRPILLLDEPFSALDPalrQEMLDLVDELCRERGL----TVLMVTHDPEdAARIADRVLLVADGRIAA 210
|
250
....*....|...
gi 74136409 638 MGTYQELLSKTRN 650
Cdd:COG3840 211 DGPTAALLDGEPP 223
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
450-654 |
2.32e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 60.11 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 450 LKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSvAYVSQQAWiqNCILQVNILFGSIMKKEFYEQV 529
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-LLTAENVW--NLRRKIGMVFQNPDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 530 LEACAL------LPDLEQLPKGDQTEIG--------ERGVNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDvHVGKQL 595
Cdd:PRK13642 100 EDDVAFgmenqgIPREEMIKRVDEALLAvnmldfktREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLD-PTGRQE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 74136409 596 FEKVIGSLGLLKNKTRILVTHNLTLLPQMDLIVVMESGRIAQMGTYQELLSKTRNLTNL 654
Cdd:PRK13642 179 IMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMVEI 237
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
769-957 |
2.84e-09 |
|
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: 59.75 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 769 SNKLNIYGILGLIKGLFVCS------GAYVITRGSLAASRTMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDMR 842
Cdd:cd18551 30 SAGGSSGGLLALLVALFLLQavlsalSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLREL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 843 LHYYLRLWVNCTLDVIGTI-----------LVIIGALPLFILGIIPsvfFYFSIQRYYVASSRQIRRLTGAsrspvishF 911
Cdd:cd18551 110 ITSGLPQLVTGVLTVVGAVvlmflldwvltLVTLAVVPLAFLIILP---LGRRIRKASKRAQDALGELSAA--------L 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 74136409 912 SETLSGVSTIRAFGHQQRFIQQYKEVVNEnlvCFYNNVISNRWLSV 957
Cdd:cd18551 179 ERALSAIRTVKASNAEERETKRGGEAAER---LYRAGLKAAKIEAL 221
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
769-966 |
2.90e-09 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 59.83 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 769 SNKLNIYGI----LGLIKGLFVCSGAYVITRGSLAASRTMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDMRLH 844
Cdd:cd18555 38 LNLLNVLGIgiliLFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLFRANSNVYIRQILSN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 845 YYLRLWVNCTLDVIGTILVIIGALPL----FILGIIPSVFFYFSIQRYYVASSRQIrrltgASRSPVISHFSETLSGVST 920
Cdd:cd18555 118 QVISLIIDLLLLVIYLIYMLYYSPLLtlivLLLGLLIVLLLLLTRKKIKKLNQEEI-----VAQTKVQSYLTETLYGIET 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 74136409 921 IRAFGHQQRFIQQYKEVVNENLVCF-----YNNVISNrwLSVRLEFLGNLM 966
Cdd:cd18555 193 IKSLGSEKNIYKKWENLFKKQLKAFkkkerLSNILNS--ISSSIQFIAPLL 241
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1064-1263 |
2.99e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 59.40 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLH-------DLRGKLNIIPQHPVLFS 1136
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYsprtdtvDLRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1137 GTLQMNLD---PLNKYSD-SKLWEALElchlKEFVQ-SLPEKLRHEISEGGENLSMGQRQLVCLARALLRKTKILILDEA 1211
Cdd:PRK14239 100 MSIYENVVyglRLKGIKDkQVLDEAVE----KSLKGaSIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 74136409 1212 TASIDFETDKLVQTTIRKEFSDCTILTIAHRLQ--SIIdSDRVLVLDSGSIVEF 1263
Cdd:PRK14239 176 TSALDPISAGKIEETLLGLKDDYTMLLVTRSMQqaSRI-SDRTGFFLDGDLIEY 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1064-1267 |
3.08e-09 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 61.24 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERA--GGKIIIDGIDISTIGLHDLRGKLNIIPQHPvlFS----- 1136
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEgeIRFDGQDLDGLSRRALRPLRRRMQVVFQDP--FGslspr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1137 -----------GTLQMNLDPLNKysDSKLWEALElchlkEfVQsLPEKLR----HEiseggenLSMGQRQLVCLARALLR 1201
Cdd:COG4172 379 mtvgqiiaeglRVHGPGLSAAER--RARVAEALE-----E-VG-LDPAARhrypHE-------FSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1202 KTKILILDEATASIdfetDKLVQTTI-------RKEFsDCTILTIAHRLqSIID--SDRVLVLDSGSIVE-------FEA 1265
Cdd:COG4172 443 EPKLLVLDEPTSAL----DVSVQAQIldllrdlQREH-GLAYLFISHDL-AVVRalAHRVMVMKDGKVVEqgpteqvFDA 516
|
..
gi 74136409 1266 PQ 1267
Cdd:COG4172 517 PQ 518
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1065-1246 |
3.18e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 59.28 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVE-------RAGGKIIIDGIDISTIGLHDLRGKLNIIPQHPVLFsg 1137
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevrvEGRVEFFNQNIYERRVNLNRLRRQVSMVHPKPNLF-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1138 tlqmnldPLNKYSDS----KLWEALELCHLKEFVQS------LPEKLRHEISEGGENLSMGQRQLVCLARALLRKTKILI 1207
Cdd:PRK14258 101 -------PMSVYDNVaygvKIVGWRPKLEIDDIVESalkdadLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 74136409 1208 LDEATASID----FETDKLVQTTIRKefSDCTILTIAHRLQSI 1246
Cdd:PRK14258 174 MDEPCFGLDpiasMKVESLIQSLRLR--SELTMVIVSHNLHQV 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1048-1269 |
3.90e-09 |
|
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: 58.50 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1048 VEFINYQARYRDelGLALQDITFQTHGEEKIGIVGRTGAGKSTLsnclFRIV---ERAGGKIIIDGIDISTiGLHDLRGK 1124
Cdd:cd03296 3 IEVRNVSKRFGD--FVALDDVSLDIPSGELVALLGPSGSGKTTL----LRLIaglERPDSGTILFGGEDAT-DVPVQERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1125 LNIIPQHPVLFSG-TLQMNL-----------DPLNKYSDSKLWEALELCHLKEFVQSLPEKLrheiseggenlSMGQRQL 1192
Cdd:cd03296 76 VGFVFQHYALFRHmTVFDNVafglrvkprseRPPEAEIRAKVHELLKLVQLDWLADRYPAQL-----------SGGQRQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1193 VCLARALLRKTKILILDEATASIDFETDKLVQTTIRKEFSDCTILTI--AHRLQSIID-SDRVLVLDSGSIVEFEAPQNL 1269
Cdd:cd03296 145 VALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVfvTHDQEEALEvADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
446-646 |
4.57e-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: 58.22 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 446 GMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEM-----------EKLTGV----VQRKGsVAYVSQQAWI---- 506
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLrptsgsvlfdgEDITGLppheIARLG-IGRTFQIPRLfpel 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 507 ---QNCIL------QVNILFGSIMK--KEFYEQ---VLEACALLPDLEQLPKgdqteigergvNISGGQQHRVSLARAVY 572
Cdd:cd03219 91 tvlENVMVaaqartGSGLLLARARReeREARERaeeLLERVGLADLADRPAG-----------ELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 573 SGADIYLLDDP---LSAVDVHVGKQLFEKvIGSLGLlknkTRILVTHNLTLLpqMDL---IVVMESGRIAQMGTYQELLS 646
Cdd:cd03219 160 TDPKLLLLDEPaagLNPEETEELAELIRE-LRERGI----TVLLVEHDMDVV--MSLadrVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1061-1260 |
4.57e-09 |
|
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: 57.44 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1061 LGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFriveraggkiiidgidistiGLHDLRgklniipqhpvlfSGTLQ 1140
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALF--------------------GLRPPA-------------SGEIT 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1141 MNLDPLNKYSDSKlWEALELCHLkefvqslPEKlRHEisEG-------GENLSMGQR------QLVCLARALLRKTKILI 1207
Cdd:cd03215 59 LDGKPVTRRSPRD-AIRAGIAYV-------PED-RKR--EGlvldlsvAENIALSSLlsggnqQKVVLARWLARDPRVLI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 74136409 1208 LDEATASIDFETDKLVQTTIRkEFSD--CTILTIAHRLQSIID-SDRVLVLDSGSI 1260
Cdd:cd03215 128 LDEPTRGVDVGAKAEIYRLIR-ELADagKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1064-1261 |
5.02e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 58.91 E-value: 5.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDIS--TIGLHDLRGKLNIIPQHP--VLFSGTL 1139
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQYPeyQLFEETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1140 QMNLD--PLN-KYSDS----KLWEALELCHLKefVQSLPEKLRHEiseggenLSMGQRQLVCLARALLRKTKILILDEAT 1212
Cdd:PRK13637 102 EKDIAfgPINlGLSEEeienRVKRAMNIVGLD--YEDYKDKSPFE-------LSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 74136409 1213 ASIDFET--DKLVQ-TTIRKEFsDCTILTIAHRLQSIID-SDRVLVLDSGSIV 1261
Cdd:PRK13637 173 AGLDPKGrdEILNKiKELHKEY-NMTIILVSHSMEDVAKlADRIIVMNKGKCE 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
450-618 |
6.39e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 58.25 E-value: 6.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 450 LKDLNIKIPEGALVAVVGQVGSGKSSMLSAiLGEMEKLTGVVQRKGSVAYVSQQAWIQNC-ILQVNILFGSIMKKE--FY 526
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRC-FNRLNDLIPGFRVEGKVTFHGKNLYAPDVdPVEVRRRIGMVFQKPnpFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 527 EQVLEACALLPDLEQLpKGDQTEIGER------------------GVNISGGQQHRVSLARAVYSGADIYLLDDPLSAVD 588
Cdd:PRK14243 105 KSIYDNIAYGARINGY-KGDMDELVERslrqaalwdevkdklkqsGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALD 183
|
170 180 190
....*....|....*....|....*....|
gi 74136409 589 vHVGKQLFEKVIGSLGllKNKTRILVTHNL 618
Cdd:PRK14243 184 -PISTLRIEELMHELK--EQYTIIIVTHNM 210
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1067-1260 |
6.39e-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: 60.22 E-value: 6.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1067 DITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIG--LHDLRGKLNIIPQH-------PVLFSG 1137
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFINGKPVDIRnpAQAIRAGIAMVPEDrkrhgivPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1138 TlQMNLDPLNKYSD-SKLWEALELCHLKEFVQSLPEKLRHEISEGGeNLSMGQRQLVCLARALLRKTKILILDEATASID 1216
Cdd:TIGR02633 358 K-NITLSVLKSFCFkMRIDAAAELQIIGSAIQRLKVKTASPFLPIG-RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 74136409 1217 ----FETDKLVQTTIRKEFSdctILTIAHRLQSIID-SDRVLVLDSGSI 1260
Cdd:TIGR02633 436 vgakYEIYKLINQLAQEGVA---IIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1064-1270 |
6.85e-09 |
|
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: 6.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCL--------------FRI--------VERAGGKIIIDGIDISTIGL--- 1118
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmdqyeptsgriiYHValcekcgyVERPSKVGEPCPVCGGTLEPeev 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1119 ----------HDLRGKLNIIPQHPVLFSG---TLQMNLDPLNK--YS-DSKLWEALELChlkEFVQslpekLRHEISEGG 1182
Cdd:TIGR03269 95 dfwnlsdklrRRIRKRIAIMLQRTFALYGddtVLDNVLEALEEigYEgKEAVGRAVDLI---EMVQ-----LSHRITHIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1183 ENLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTIRK--EFSDCTILTIAHRLQSIID-SDRVLVLDSGS 1259
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIEDlSDKAIWLENGE 246
|
250
....*....|.
gi 74136409 1260 IVEFEAPQNLI 1270
Cdd:TIGR03269 247 IKEEGTPDEVV 257
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1058-1261 |
7.24e-09 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 57.50 E-value: 7.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1058 RDELGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCL--FRIVERAGGkiiidgidisTIGLHDL------RGKLNIIP 1129
Cdd:cd03298 7 RFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIagFETPQSGRV----------LINGVDVtaappaDRPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1130 QHPVLFSG-TLQMNLD----P---LNKYSDSKLWEALELCHLKEFVQSLPEKLrheiseggenlSMGQRQLVCLARALLR 1201
Cdd:cd03298 77 QENNLFAHlTVEQNVGlglsPglkLTAEDRQAIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVLVR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74136409 1202 KTKILILDEATASID----FETDKLVqTTIRKEfSDCTILTIAHRLQSIID-SDRVLVLDSGSIV 1261
Cdd:cd03298 146 DKPVLLLDEPFAALDpalrAEMLDLV-LDLHAE-TKMTVLMVTHQPEDAKRlAQRVVFLDNGRIA 208
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1080-1273 |
7.54e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 57.93 E-value: 7.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1080 IVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLH-------DLRGKLNIIPQHPVLFSG-TLQMNLD---PLNK 1148
Cdd:PRK14267 35 LMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYspdvdpiEVRREVGMVFQYPNPFPHlTIYDNVAigvKLNG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1149 YSDSK--LWEALELChLKEfvQSLPEKLRHEISEGGENLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTT 1226
Cdd:PRK14267 115 LVKSKkeLDERVEWA-LKK--AALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEEL 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 74136409 1227 IRKEFSDCTILTIAHR-LQSIIDSDRVLVLDSGSIVE-------FEAPQNLIRQK 1273
Cdd:PRK14267 192 LFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEvgptrkvFENPEHELTEK 246
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1069-1261 |
9.31e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 57.28 E-value: 9.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1069 TFQTHGEEKIGIVGRTGAGKSTLSNCL--FRIVERAGGKIIIDGIDISTIGlhdlRGKLNIIPQHPVLFSG-TLQMN--- 1142
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIagFLTPASGSLTLNGQDHTTTPPS----RRPVSMLFQENNLFSHlTVAQNigl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1143 -LDP---LNKYSDSKLWEALELCHLKEFVQSLPEKLrheiseggenlSMGQRQLVCLARALLRKTKILILDEATASID-- 1216
Cdd:PRK10771 95 gLNPglkLNAAQREKLHAIARQMGIEDLLARLPGQL-----------SGGQRQRVALARCLVREQPILLLDEPFSALDpa 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 74136409 1217 --FETDKLVQTTIRKEfsDCTILTIAHRLQsiiDS----DRVLVLDSGSIV 1261
Cdd:PRK10771 164 lrQEMLTLVSQVCQER--QLTLLMVSHSLE---DAariaPRSLVVADGRIA 209
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1064-1268 |
9.87e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.48 E-value: 9.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIG---LHDLRGKLNIIPQHPVlfsgtlq 1140
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPY------- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1141 MNLDPLNKYSDSkLWEAL-------------ELCHLKEFVQSLPE---KLRHEiseggenLSMGQRQLVCLARALLRKTK 1204
Cdd:PRK10261 412 ASLDPRQTVGDS-IMEPLrvhgllpgkaaaaRVAWLLERVGLLPEhawRYPHE-------FSGGQRQRICIARALALNPK 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74136409 1205 ILILDEATASIDFETDKLVQT---TIRKEFSdCTILTIAHRLqSIID--SDRVLVLDSGSIVE-------FEAPQN 1268
Cdd:PRK10261 484 VIIADEAVSALDVSIRGQIINlllDLQRDFG-IAYLFISHDM-AVVEriSHRVAVMYLGQIVEigprravFENPQH 557
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1065-1273 |
1.00e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 58.30 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQTHGEEKIGIVGRTGAGKSTLS---NCLFR----IVERAggkIIIDGIDISTIGLHDLRGKLNIIPQHP--VLF 1135
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMqhfNALLKpssgTITIA---GYHITPETGNKNLKKLRKKVSLVFQFPeaQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1136 SGTLQMNLD--PLN-KYSDSKLWEAlELCHLKEFvqSLPEKLrheISEGGENLSMGQRQLVCLARALLRKTKILILDEAT 1212
Cdd:PRK13641 100 ENTVLKDVEfgPKNfGFSEDEAKEK-ALKWLKKV--GLSEDL---ISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74136409 1213 ASIDFETDK-LVQTTIRKEFSDCTILTIAHRLQSIID-SDRVLVLDSGSIVEFEAPQNLIRQK 1273
Cdd:PRK13641 174 AGLDPEGRKeMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
432-645 |
1.02e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 58.69 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 432 AIEFTDATYSWNktGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGsvAYVSQQAWIQNCIL 511
Cdd:PRK13536 41 AIDLAGVSKSYG--DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG--VPVPARARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 512 QVNILFGSiMKKEFY--EQVL-----------EACALLPDLEQLPKgDQTEIGERGVNISGGQQHRVSLARAVYSGADIY 578
Cdd:PRK13536 117 GVVPQFDN-LDLEFTvrENLLvfgryfgmstrEIEAVIPSLLEFAR-LESKADARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 579 LLDDPLSAVDVHVGKQLFEKvIGSLgLLKNKTRILVTHNLTLLPQM-DLIVVMESGRIAQMGTYQELL 645
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWER-LRSL-LARGKTILLTTHFMEEAERLcDRLCVLEAGRKIAEGRPHALI 260
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1064-1261 |
1.14e-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: 57.34 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVeraggkiIIDGIDISTIGLHDLRGKLNIIPQHPVLFS--GTLQM 1141
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLL-------QPTSGEVRVAGLVPWKRRKKFLRRIGVVFGqkTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1142 NLDPLNKYSDSKLWEALELCHLKEFVQSLPE--KLRHEISEGGENLSMGQRQLVCLARALLRKTKILILDEATASIDFET 1219
Cdd:cd03267 109 DLPVIDSFYLLAAIYDLPPARFKKRLDELSEllDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 74136409 1220 DKLVQTTIRKEFSD--CTILTIAHRLQSIID-SDRVLVLDSGSIV 1261
Cdd:cd03267 189 QENIRNFLKEYNRErgTTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1065-1265 |
1.35e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.91 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVeraggkiiidGIDISTIGLHDLR---------GKLNI--IPQHPV 1133
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIV----------PPDSGTLEIGGNPcarltpakaHQLGIylVPQEPL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1134 LFSG-TLQMN-LDPLNKYSDSKLwealelcHLKEFVQSLPEKLRHEISEGgeNLSMGQRQLVCLARALLRKTKILILDEA 1211
Cdd:PRK15439 97 LFPNlSVKENiLFGLPKRQASMQ-------KMKQLLAALGCQLDLDSSAG--SLEVADRQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 74136409 1212 TASID-FETDKLVQtTIRKEFS-DCTILTIAHRLQSIID-SDRVLVLDSGSIVEFEA 1265
Cdd:PRK15439 168 TASLTpAETERLFS-RIRELLAqGVGIVFISHKLPEIRQlADRISVMRDGTIALSGK 223
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1048-1261 |
1.36e-08 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 56.52 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1048 VEFINYQARYRDELglALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIV-----ERAGGKIIIDGIDISTIG-LHDL 1121
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIIlpdsgEVLFDGKPLDIAARNRIGyLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1122 RG---KLNIIPQhpVLFSGTLQ-MNLDPLNKYSDSKLwEALELCHLKEfvqslpEKLrheiseggENLSMGQRQLVCLAR 1197
Cdd:cd03269 79 RGlypKMKVIDQ--LVYLAQLKgLKKEEARRRIDEWL-ERLELSEYAN------KRV--------EELSKGNQQKVQFIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74136409 1198 ALLRKTKILILDEATASIDFETDKLVQTTIRkEFSD--CTILTIAHRLQSIID-SDRVLVLDSGSIV 1261
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPVNVELLKDVIR-ELARagKTVILSTHQMELVEElCDRVLLLNKGRAV 207
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
401-590 |
1.44e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 59.18 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 401 QTKiSLGRLEDFlhtEELLPQN----IETNYI--------GDHAIEFTDATYSWNktGMPVLKDLNIKIPEGALVAVVGQ 468
Cdd:TIGR03719 283 QAK-SKARLARY---EELLSQEfqkrNETAEIyippgprlGDKVIEAENLTKAFG--DKLLIDDLSFKLPPGGIVGVIGP 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 469 VGSGKSSMLSAILGEMEKLTGVVQRKGSV--AYVSQQAwiqncilqvNILFGSimkKEFYEQVLEACallpdleqlpkgD 546
Cdd:TIGR03719 357 NGAGKSTLFRMITGQEQPDSGTIEIGETVklAYVDQSR---------DALDPN---KTVWEEISGGL------------D 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74136409 547 QTEIGERGVN---------------------ISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVH 590
Cdd:TIGR03719 413 IIKLGKREIPsrayvgrfnfkgsdqqkkvgqLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVE 477
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1156-1272 |
1.46e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 58.19 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1156 EALELCHLKEFvqslPEKLRHEISEGgenlsmgQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTIR---KEFs 1232
Cdd:PRK11432 119 EALELVDLAGF----EDRYVDQISGG-------QQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRelqQQF- 186
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 74136409 1233 DCTILTIAH-RLQSIIDSDRVLVLDSGSIVEFEAPQNLIRQ 1272
Cdd:PRK11432 187 NITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
770-966 |
1.46e-08 |
|
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: 57.84 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 770 NKLNIYGI----LGLIKGLFVCSGAYVITRGSLAASRTMYVQLLNNVLHLPIQFFETNSTGQIISRFTkDIF-IIDMRLH 844
Cdd:cd18570 39 NLLNIISIglilLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFN-DANkIREAISS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 845 YYLRLWVNCTLDVIGTILVIIGALPLFILGIIpSVFFYFSIQRYYVASSRQIRRLTGASRSPVISHFSETLSGVSTIRAF 924
Cdd:cd18570 118 TTISLFLDLLMVIISGIILFFYNWKLFLITLL-IIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSL 196
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 74136409 925 GHQQRFIQQYKEVVNEnlvcFYNNVISNRWLSVRLEFLGNLM 966
Cdd:cd18570 197 NAEEQFLKKIEKKFSK----LLKKSFKLGKLSNLQSSIKGLI 234
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1064-1255 |
1.50e-08 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 56.09 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRI-------VERAGGkiiidgidiSTIGLhdlrgklniIPQH----- 1131
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVlrptsgtVRRAGG---------ARVAY---------VPQRsevpd 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1132 --PVLFSGTLQMN-------LDPLNKYSDSKLWEALELCHLKEFvqslpekLRHEISEggenLSMGQRQLVCLARALLRK 1202
Cdd:NF040873 69 slPLTVRDLVAMGrwarrglWRRLTRDDRAAVDDALERVGLADL-------AGRQLGE----LSGGQRQRALLAQGLAQE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 74136409 1203 TKILILDEATASIDFETDKLVQTTIRKEFSD-CTILTIAHRLQSIIDSDRVLVL 1255
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALLAEEHARgATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
777-942 |
1.59e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 57.91 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 777 ILGLIKGLFVCSGAYVITRgslAASRTMY---VQLLNNVLHLPIQFFETNSTGQIISRFTKDIfiidmrlhYYLR-LWVN 852
Cdd:cd18564 62 GIALLRGLASYAGTYLTAL---VGQRVVLdlrRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDV--------GAIQdLLVS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 853 CTLDVIGTILVIIGA----------LPLFILGIIPsvFFYFSIQRYY---VASSRQIRRLTGAsrspVISHFSETLSGVS 919
Cdd:cd18564 131 GVLPLLTNLLTLVGMlgvmfwldwqLALIALAVAP--LLLLAARRFSrriKEASREQRRREGA----LASVAQESLSAIR 204
|
170 180
....*....|....*....|...
gi 74136409 920 TIRAFGHQQRFIQQYKEVVNENL 942
Cdd:cd18564 205 VVQAFGREEHEERRFARENRKSL 227
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
446-620 |
1.67e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 58.99 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 446 GMPVLKDLNIKIPEGALVAVVGQVGSGKSSmLSAILGEMEKLTG---VVQRKGSVAYVSQQAWIQNCILQVNILFG---- 518
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSS-LFRILGELWPVYGgrlTKPAKGKLFYVPQRPYMTLGTLRDQIIYPdsse 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 519 SIMKKEFYEQVLEACALLPDLEQLPkgdQTEIGERGVN-----ISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGK 593
Cdd:TIGR00954 543 DMKRRGLSDKDLEQILDNVQLTHIL---EREGGWSAVQdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEG 619
|
170 180
....*....|....*....|....*....
gi 74136409 594 QLFEkvigslgLLKNK--TRILVTHNLTL 620
Cdd:TIGR00954 620 YMYR-------LCREFgiTLFSVSHRKSL 641
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
446-650 |
1.69e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 57.41 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 446 GMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVvQRKGSVAYVSQQAWIQNCILQVNILFGSIMKK-- 523
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGY-RYSGDVLLGGRSIFNYRDVLEFRRRVGMLFQRpn 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 524 ----EFYEQVL---EACALLP--DLEQLPKGDQTEIG----------ERGVNISGGQQHRVSLARAVYSGADIYLLDDPL 584
Cdd:PRK14271 112 pfpmSIMDNVLagvRAHKLVPrkEFRGVAQARLTEVGlwdavkdrlsDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74136409 585 SAVDVHVGKQLfEKVIGSLGllKNKTRILVTHNLTLLPQM-DLIVVMESGRIAQMGTYQELLSKTRN 650
Cdd:PRK14271 192 SALDPTTTEKI-EEFIRSLA--DRLTVIIVTHNLAQAARIsDRAALFFDGRLVEEGPTEQLFSSPKH 255
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
449-635 |
1.71e-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: 55.52 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 449 VLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGS-VAYVSQQAWIQNCIlqvnilfgsimkkefye 527
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpVTRRSPRDAIRAGI----------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 528 qvleacALLPD--LEQLPKGDQTeIGErgvNI------SGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHvGKQLFEKV 599
Cdd:cd03215 78 ------AYVPEdrKREGLVLDLS-VAE---NIalssllSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG-AKAEIYRL 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 74136409 600 IGSLgLLKNKTRILVTHNLTLLPQM-DLIVVMESGRI 635
Cdd:cd03215 147 IREL-ADAGKAVLLISSELDELLGLcDRILVMYEGRI 182
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1056-1261 |
1.82e-08 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 56.22 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1056 RYRDELG--LALQDITFQTHGEEKIGIVGRTGAGKSTLSNCL---------------FRIVERAGGKIIIDGIDISTIGL 1118
Cdd:cd03266 10 RFRDVKKtvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLagllepdagfatvdgFDVVKEPAEARRRLGFVSDSTGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1119 HD-LRGKLNIipqhpVLFSGTLQMNLDPLNKysdsklwealelcHLKEFVQSLpeKLRHEISEGGENLSMGQRQLVCLAR 1197
Cdd:cd03266 90 YDrLTARENL-----EYFAGLYGLKGDELTA-------------RLEELADRL--GMEELLDRRVGGFSTGMRQKVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74136409 1198 ALLRKTKILILDEATASIDFETDKLVQTTIRKEFSD-CTILTIAHRLQSIID-SDRVLVLDSGSIV 1261
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1080-1266 |
1.98e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 57.03 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1080 IVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDI---STIGLHDL---RGKLNIIPQHPVLFSGTLQMNLDP---LNKYS 1150
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLggrSIFNYRDVlefRRRVGMLFQRPNPFPMSIMDNVLAgvrAHKLV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1151 DSKLWEALELCHLKEFvqSLPEKLRHEISEGGENLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTIRKE 1230
Cdd:PRK14271 132 PRKEFRGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL 209
|
170 180 190
....*....|....*....|....*....|....*..
gi 74136409 1231 FSDCTILTIAHRL-QSIIDSDRVLVLDSGSIVEfEAP 1266
Cdd:PRK14271 210 ADRLTVIIVTHNLaQAARISDRAALFFDGRLVE-EGP 245
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
449-617 |
2.00e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 56.77 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 449 VLKDLNIKIPEGALVAVVGQVGSGKSSMLSAI-----LGEMEKLTGVVQRKGSVAYVSQQAWIQnCILQVNILF---GSI 520
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPIE-VRREVGMVFqypNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 521 MKKEFYEQVleacALLPDLEQLPKGdQTEIGER---------------------GVNISGGQQHRVSLARAVYSGADIYL 579
Cdd:PRK14267 98 PHLTIYDNV----AIGVKLNGLVKS-KKELDERvewalkkaalwdevkdrlndyPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 74136409 580 LDDPLSAVDvHVGKQLFEKVIgsLGLLKNKTRILVTHN 617
Cdd:PRK14267 173 MDEPTANID-PVGTAKIEELL--FELKKEYTIVLVTHS 207
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
433-654 |
2.16e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 57.05 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNK-TGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSvAYVSQQAW------ 505
Cdd:PRK13650 5 IEVKNLTFKYKEdQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD-LLTEENVWdirhki 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 506 ---IQN-------CILQVNILFG----SIMKKEFYEQVLEACALLpdleqlpkgDQTEIGERG-VNISGGQQHRVSLARA 570
Cdd:PRK13650 84 gmvFQNpdnqfvgATVEDDVAFGlenkGIPHEEMKERVNEALELV---------GMQDFKEREpARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 571 VYSGADIYLLDDPLSAVDVHvGKQLFEKVIGSLGLLKNKTRILVTHNLTLLPQMDLIVVMESGRIAQMGTYQELLSKTRN 650
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPE-GRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGND 233
|
....
gi 74136409 651 LTNL 654
Cdd:PRK13650 234 LLQL 237
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
777-934 |
2.61e-08 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 56.72 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 777 ILGLIKGLFVCSGAYVITRGSLAASRTMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDMRLHYYLRLWVNCTLD 856
Cdd:cd18543 47 ALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGNLLTL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 857 VIGTILVIIGALPLFILGIIPSVFFYFSIQRY---YVASSRQIRRLTGAsrspVISHFSETLSGVSTIRAFGHQQRFIQQ 933
Cdd:cd18543 127 VVGLVVMLVLSPPLALVALASLPPLVLVARRFrrrYFPASRRAQDQAGD----LATVVEESVTGIRVVKAFGRERRELDR 202
|
.
gi 74136409 934 Y 934
Cdd:cd18543 203 F 203
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1063-1261 |
2.63e-08 |
|
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: 56.13 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1063 LALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKLNIIPQHPVLFSG----- 1137
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPRKPDQFQKCVAYVRQDDILLPGltvre 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1138 ----TLQMNL-DPLNKYSDSKLWEALELCHLKEfvqslpEKLRHEISEGgenLSMGQRQLVCLARALLRKTKILILDEAT 1212
Cdd:cd03234 101 tltyTAILRLpRKSSDAIRKKRVEDVLLRDLAL------TRIGGNLVKG---ISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 74136409 1213 ASID-FETDKLVQTTIRKEFSDCTILTIAHRLQSIIDS--DRVLVLDSGSIV 1261
Cdd:cd03234 172 SGLDsFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRlfDRILLLSSGEIV 223
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
781-942 |
2.85e-08 |
|
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: 56.71 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 781 IKGLFVCSGAYV-ITRGSLAASR-----TMYV----------QLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDMrlh 844
Cdd:cd18545 36 LSGLLIIALLFLaLNLVNWVASRlriylMAKVgqrilydlrqDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSD--- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 845 yylrLWVNCTLDVIGTILVIIGA----------LPLFILGIIPS-VFFYFSIQRYYVASSRQIRRltgaSRSPVISHFSE 913
Cdd:cd18545 113 ----LLSNGLINLIPDLLTLVGIviimfslnvrLALVTLAVLPLlVLVVFLLRRRARKAWQRVRK----KISNLNAYLHE 184
|
170 180
....*....|....*....|....*....
gi 74136409 914 TLSGVSTIRAFGHQQRFIQQYKEVVNENL 942
Cdd:cd18545 185 SISGIRVIQSFAREDENEEIFDELNRENR 213
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
432-640 |
3.17e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 56.68 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 432 AIEFTDATYSWnKTGMP----VLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKG-SVAYVSQQAWI 506
Cdd:PRK13649 2 GINLQNVSYTY-QAGTPfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtLITSTSKNKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 507 QNCILQVNILFGSIMKKEFYEQVLEACALLP--------DLEQLPK------GDQTEIGERG-VNISGGQQHRVSLARAV 571
Cdd:PRK13649 81 KQIRKKVGLVFQFPESQLFEETVLKDVAFGPqnfgvsqeEAEALAReklalvGISESLFEKNpFELSGGQMRRVAIAGIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74136409 572 YSGADIYLLDDPLSAVDVHVGKQLFE--KVIGSLGLlknkTRILVTHNLTLLPQM-DLIVVMESGRIAQMGT 640
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGRKELMTlfKKLHQSGM----TIVLVTHLMDDVANYaDFVYVLEKGKLVLSGK 228
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1080-1262 |
3.38e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 56.07 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1080 IVGRTGAGKSTLSNCLFRIVE-----RAGGKIIIDGIDISTIGLHDLRGKL-------NIIPQHPVLFSGTLQMNLDPLN 1147
Cdd:PRK14247 34 LMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVqmvfqipNPIPNLSIFENVALGLKLNRLV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1148 KySDSKLWE----ALELCHLKEFVqslpeklRHEISEGGENLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLV 1223
Cdd:PRK14247 114 K-SKKELQErvrwALEKAQLWDEV-------KDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKI 185
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 74136409 1224 QTTIRKEFSDCTILTIAH-RLQSIIDSDRVLVLDSGSIVE 1262
Cdd:PRK14247 186 ESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVE 225
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
446-589 |
3.65e-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: 55.06 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 446 GMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSVAYVSQQAWIQNC--ILQVNILFGSIMKK 523
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENIlyLGHLPGLKPELSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 524 E---FY-----------EQVLEACALLpDLEQLPKGdqteigergvNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDV 589
Cdd:TIGR01189 92 EnlhFWaaihggaqrtiEDALAAVGLT-GFEDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
449-659 |
3.67e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 56.13 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 449 VLKDLNIKIPEGALVAVVGQVGSGKSSML-----------SAILGEMEKLTGVVQRKGSVAyVSQQAWIQNCILQVNILF 517
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLrcinflekpseGSIVVNGQTINLVRDKDGQLK-VADKNQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 518 GSIMKKEFY---EQVLEACALLPDLEQLPKG-------DQTEIGERG-----VNISGGQQHRVSLARAVYSGADIYLLDD 582
Cdd:PRK10619 99 QHFNLWSHMtvlENVMEAPIQVLGLSKQEAReravkylAKVGIDERAqgkypVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74136409 583 PLSAVDVH-VGKQLfeKVIGSLGlLKNKTRILVTHNLTLLPQM-DLIVVMESGRIAQMGTYQELLSKTRNlTNLHQVIS 659
Cdd:PRK10619 179 PTSALDPElVGEVL--RIMQQLA-EEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLFGNPQS-PRLQQFLK 253
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1056-1263 |
3.74e-08 |
|
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: 55.28 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1056 RYRDelGLALQDITFqTHGEEKIGIVGRTGAGKSTLSNCLFRIVEraggkiiidgIDISTIGLHD---------LRGKLN 1126
Cdd:cd03264 9 RYGK--KRALDGVSL-TLGPGMYGLLGPNGAGKTTLMRILATLTP----------PSSGTIRIDGqdvlkqpqkLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1127 IIPQHPvlfsgtlqmnldplNKYSDSKLWEALE-LCHLKEFVQSlpeKLRHEISEGGEN-------------LSMGQRQL 1192
Cdd:cd03264 76 YLPQEF--------------GVYPNFTVREFLDyIAWLKGIPSK---EVKARVDEVLELvnlgdrakkkigsLSGGMRRR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74136409 1193 VCLARALLRKTKILILDEATASIDFETDKLVQTTIRKEFSDCTILTIAHRLQSIIDS-DRVLVLDSGSIVEF 1263
Cdd:cd03264 139 VGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFE 210
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
439-639 |
4.03e-08 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 55.45 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 439 TYSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGsVAYVSQQAWIQNCILQVNILFG 518
Cdd:cd03266 10 RFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG-FDVVKEPAEARRRLGFVSDSTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 519 SIMKKEFYEQV--------LEACALLPDLEQLpkGDQTEIGE----RGVNISGGQQHRVSLARAVYSGADIYLLDDPLSA 586
Cdd:cd03266 89 LYDRLTARENLeyfaglygLKGDELTARLEEL--ADRLGMEElldrRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 74136409 587 VDVHVGKQLFE--KVIGSLGllknKTRILVTHNLTLLPQM-DLIVVMESGRIAQMG 639
Cdd:cd03266 167 LDVMATRALREfiRQLRALG----KCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
451-644 |
4.85e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 56.64 E-value: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 451 KDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKG-SVAYVSQQAW------IQnCILQ---------VN 514
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkDLLGMKDDEWravrsdIQ-MIFQdplaslnprMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 515 IlfGSIM------------KKEFYEQVLEACA---LLPDLeqlpkgdqteIGERGVNISGGQQHRVSLARAVYSGADIYL 579
Cdd:PRK15079 117 I--GEIIaeplrtyhpklsRQEVKDRVKAMMLkvgLLPNL----------INRYPHEFSGGQCQRIGIARALILEPKLII 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74136409 580 LDDPLSAVDVHVGKQ---LFEKVIGSLGLlknkTRILVTHNLTLLPQM-DLIVVMESGRIAQMGTYQEL 644
Cdd:PRK15079 185 CDEPVSALDVSIQAQvvnLLQQLQREMGL----SLIFIAHDLAVVKHIsDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1065-1270 |
5.31e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 55.28 E-value: 5.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHD--LRGkLNIIPQHPVLFS------ 1136
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHAraRRG-IGYLPQEASIFRrlsvyd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1137 ---GTLQMNLDPLNKYSDSKLWEALELCHLKEFVQSLpeklrheisegGENLSMGQRQLVCLARALLRKTKILILDEATA 1213
Cdd:PRK10895 98 nlmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74136409 1214 SID----FETDKLVQtTIRKefSDCTILTIAHRLQSIID-SDRVLVLDSGSIVEFEAPQNLI 1270
Cdd:PRK10895 167 GVDpisvIDIKRIIE-HLRD--SGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEIL 225
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1065-1261 |
5.33e-08 |
|
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: 54.48 E-value: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDIStIGLHDLRGKLNIIPQHPVLFsGTLQmnld 1144
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGRP-LDKRSFRKIIGYVPQDDILH-PTLT---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1145 plnkysdskLWEALELChlkefvqslpEKLRheiseggeNLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQ 1224
Cdd:cd03213 99 ---------VRETLMFA----------AKLR--------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 74136409 1225 TTIRKEFSD-CTILTIAHRLQSIIDS--DRVLVLDSGSIV 1261
Cdd:cd03213 152 SLLRRLADTgRTIICSIHQPSSEIFElfDKLLLLSQGRVI 191
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
815-941 |
6.12e-08 |
|
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: 55.57 E-value: 6.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 815 LPIQFFETNSTGQIISRFTKDI----------------------FIIDMRLhyylrlwvncTLDVIGTILVIIGALPLFI 872
Cdd:cd18546 85 LSLDFHERETSGRIMTRMTSDIdalsellqtglvqlvvslltlvGIAVVLL----------VLDPRLALVALAALPPLAL 154
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74136409 873 LgiipSVFFyfsiQRYYVASSRQIRRLTGAsrspVISHFSETLSGVSTIRAFGHQQRFIQQYKEVVNEN 941
Cdd:cd18546 155 A----TRWF----RRRSSRAYRRARERIAA----VNADLQETLAGIRVVQAFRRERRNAERFAELSDDY 211
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
433-644 |
6.37e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 56.38 E-value: 6.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNktGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVV-------------QRKGSVAY 499
Cdd:PRK11607 20 LEIRNLTKSFD--GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQImldgvdlshvppyQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 500 VSQqAWIQNCILQVNILFG----SIMKKEFYEQVLEACALLpDLEQLPKgdqteigERGVNISGGQQHRVSLARAVYSGA 575
Cdd:PRK11607 98 QSY-ALFPHMTVEQNIAFGlkqdKLPKAEIASRVNEMLGLV-HMQEFAK-------RKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 576 DIYLLDDPLSAVDVHVGKQLFEKVIGSLGLLkNKTRILVTHNLTLLPQM-DLIVVMESGRIAQMGTYQEL 644
Cdd:PRK11607 169 KLLLLDEPMGALDKKLRDRMQLEVVDILERV-GVTCVMVTHDQEEAMTMaGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1065-1258 |
6.97e-08 |
|
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: 52.84 E-value: 6.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQTHGEEKIGIVGRTGAGKSTLsnclfriveraggkiiidgidistiglhdlrgkLNIIPQHPVLFSGTLQmnld 1144
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTL---------------------------------LKLIAGELEPDEGIVT---- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1145 plnkySDSKLwealELCHLkefvqslpeklrheiseggENLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQ 1224
Cdd:cd03221 59 -----WGSTV----KIGYF-------------------EQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALE 110
|
170 180 190
....*....|....*....|....*....|....*..
gi 74136409 1225 TTIrKEFsDCTILTIAH-R--LQSIIdsDRVLVLDSG 1258
Cdd:cd03221 111 EAL-KEY-PGTVILVSHdRyfLDQVA--TKIIELEDG 143
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
433-653 |
7.37e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 55.48 E-value: 7.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNK---TGMPVLKDLNIKIPEGALVAVVGQVGSGKSSM---LSAIL----GEME----------------- 485
Cdd:PRK13651 3 IKVKNIVKIFNKklpTELKALDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALLlpdtGTIEwifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 486 -KLTGVVQRKGS------------VAYVSQQAWIQ--NCILQVNILFGSIM----KKEFYEQVLEACALLP-DLEQLPKG 545
Cdd:PRK13651 83 vLEKLVIQKTRFkkikkikeirrrVGVVFQFAEYQlfEQTIEKDIIFGPVSmgvsKEEAKKRAAKYIELVGlDESYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 546 DqteigergVNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGKQLFEkVIGSLGLlKNKTRILVTHNL-TLLPQM 624
Cdd:PRK13651 163 P--------FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE-IFDNLNK-QGKTIILVTHDLdNVLEWT 232
|
250 260
....*....|....*....|....*....
gi 74136409 625 DLIVVMESGRIAQMGTYQELLSKTRNLTN 653
Cdd:PRK13651 233 KRTIFFKDGKIIKDGDTYDILSDNKFLIE 261
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
448-646 |
7.40e-08 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 55.02 E-value: 7.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 448 PVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAIlgeMEKLTgvvQRKGSVAYVSQQAWiqncilqvnilfgSIMKKEFYE 527
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCF---ARLLT---PQSGTVFLGDKPIS-------------MLSSRQLAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 528 QVleacALLPDLEQLPKG---------------------------------DQTEIGE----RGVNISGGQQHRVSLARA 570
Cdd:PRK11231 77 RL----ALLPQHHLTPEGitvrelvaygrspwlslwgrlsaednarvnqamEQTRINHladrRLTDLSGGQRQRAFLAMV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 571 VYSGADIYLLDDPLSAVDVHVGKQLfekvIGSLGLLKN--KTRILVTHNLTllpQM----DLIVVMESGRIAQMGTYQEL 644
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDINHQVEL----MRLMRELNTqgKTVVTVLHDLN---QAsrycDHLVVLANGHVMAQGTPEEV 225
|
..
gi 74136409 645 LS 646
Cdd:PRK11231 226 MT 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1048-1261 |
7.49e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 55.24 E-value: 7.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1048 VEFINYqaRYRDELGlALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVE--RAGGKIIIDGIDISTIGLHDLRGKL 1125
Cdd:PRK13636 8 VEELNY--NYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKpsSGRILFDGKPIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1126 NIIPQHP--VLFSGTL--QMNLDPLN-KYSDSKLWEALELCHLKEFVQSLPEKLRHEiseggenLSMGQRQLVCLARALL 1200
Cdd:PRK13636 85 GMVFQDPdnQLFSASVyqDVSFGAVNlKLPEDEVRKRVDNALKRTGIEHLKDKPTHC-------LSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74136409 1201 RKTKILILDEATASID----FETDKLVQTTIrKEFsDCTILTIAHRLQSI-IDSDRVLVLDSGSIV 1261
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQ-KEL-GLTIIIATHDIDIVpLYCDNVFVMKEGRVI 221
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1064-1262 |
7.85e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 55.87 E-value: 7.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKII---IDGIDISTIGLHDLRGKLNIIPQHPvLFSGTLQ 1140
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwlgKDLLGMKDDEWRAVRSDIQMIFQDP-LASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1141 MNL-----DPLNKYsdsklWEALELCHLKEFVQSLPEK---LRHEISEGGENLSMGQRQLVCLARALLRKTKILILDEAT 1212
Cdd:PRK15079 115 MTIgeiiaEPLRTY-----HPKLSRQEVKDRVKAMMLKvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 74136409 1213 A----SIDFETDKLVQtTIRKEFsDCTILTIAHRLqSIID--SDRVLVLDSGSIVE 1262
Cdd:PRK15079 190 SaldvSIQAQVVNLLQ-QLQREM-GLSLIFIAHDL-AVVKhiSDRVLVMYLGHAVE 242
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
405-631 |
8.50e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 56.74 E-value: 8.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 405 SLGRLEDF---LHTEELLPQNIET-NYIGDHAIEFTDATYSwNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAI 480
Cdd:COG4178 331 TVDRLAGFeeaLEAADALPEAASRiETSEDGALALEDLTLR-TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 481 LGemekL----TGVVQR--KGSVAYVSQQAWIQNCILQVNILFGSI---MKKEFYEQVLEACAlLPDL-EQLpkgDQTEI 550
Cdd:COG4178 410 AG----LwpygSGRIARpaGARVLFLPQRPYLPLGTLREALLYPATaeaFSDAELREALEAVG-LGHLaERL---DEEAD 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 551 GERGvnISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGKQLFEKVIGSlglLKNKTRILVTHNLTLLPQMDLIVVM 630
Cdd:COG4178 482 WDQV--LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREE---LPGTTVISVGHRSTLAAFHDRVLEL 556
|
.
gi 74136409 631 E 631
Cdd:COG4178 557 T 557
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1065-1264 |
8.52e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 56.61 E-value: 8.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQTHGEEKIGIVGRTGAGKSTlsncLFRI-----------VERAGGKiiidgidisTIGlhdlrgklnIIPQHPV 1133
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKST----LLKIlagelepdsgeVSIPKGL---------RIG---------YLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1134 LFSG-----TLQMNLDPLnkysdSKLWEAL-ELCHLKEFVQSLPEK---LRHEISEGGE--------------------- 1183
Cdd:COG0488 72 LDDDltvldTVLDGDAEL-----RALEAELeELEAKLAEPDEDLERlaeLQEEFEALGGweaearaeeilsglgfpeedl 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1184 -----NLSMGQRQLVCLARALLRKTKILILDEATASIDFEtdklvqtTIR------KEFsDCTILTIAH-R--LQSIidS 1249
Cdd:COG0488 147 drpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLE-------SIEwleeflKNY-PGTVLVVSHdRyfLDRV--A 216
|
250
....*....|....*
gi 74136409 1250 DRVLVLDSGSIVEFE 1264
Cdd:COG0488 217 TRILELDRGKLTLYP 231
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
443-635 |
9.07e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 53.81 E-value: 9.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 443 NKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAI---LGEMEKLTGVV------------QRKGSVAYVSQQAWiQ 507
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIhyngipykefaeKYPGEIIYVSEEDV-H 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 508 NCILQVnilfgsimkkefyEQVLEACALLpdleqlpKGDQTeigERGvnISGGQQHRVSLARAVYSGADIYLLDDPLSAV 587
Cdd:cd03233 95 FPTLTV-------------RETLDFALRC-------KGNEF---VRG--ISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 74136409 588 DVHVGKQLFEKvigslglLKNKTRILVTHNLTLLPQ--------MDLIVVMESGRI 635
Cdd:cd03233 150 DSSTALEILKC-------IRTMADVLKTTTFVSLYQasdeiydlFDKVLVLYEGRQ 198
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1067-1260 |
9.08e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.48 E-value: 9.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1067 DITFQTHGEEKIGIVGRTGAGKSTLSNCLF-----------RIVERAGGKIIIDGIDISTIGL--HDlRGKLNIIPQHPV 1133
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFgaypgrwegeiFIDGKPVKIRNPQQAIAQGIAMvpED-RKRDGIVPVMGV 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1134 LFSGTLQMnldpLNKYSD-SKLWEALELCHLKEFVQSLPEKLRH-EISEGgeNLSMGQRQLVCLARALLRKTKILILDEA 1211
Cdd:PRK13549 359 GKNITLAA----LDRFTGgSRIDDAAELKTILESIQRLKVKTASpELAIA--RLSGGNQQKAVLAKCLLLNPKILILDEP 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 74136409 1212 TASID----FETDKLVQTTIRKEFSdctILTIAHRLQSIID-SDRVLVLDSGSI 1260
Cdd:PRK13549 433 TRGIDvgakYEIYKLINQLVQQGVA---IIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
807-942 |
9.69e-08 |
|
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: 55.11 E-value: 9.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 807 QLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDMrlhyYLRLWVNCTLDVIGTILVIIGA-----LPLFILGIIPSVFF 881
Cdd:cd18541 78 DLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRM----ALGPGILYLVDALFLGVLVLVMmftisPKLTLIALLPLPLL 153
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 882 YFSIQRYyvasSRQIRRLTGASRspviSHFS-------ETLSGVSTIRAFGHQQRFIQQYKEVVNENL 942
Cdd:cd18541 154 ALLVYRL----GKKIHKRFRKVQ----EAFSdlsdrvqESFSGIRVIKAFVQEEAEIERFDKLNEEYV 213
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
433-646 |
1.07e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 54.20 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSWNktGMPVLKDLNIKipEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSVAYVSQQAWIQNCIL- 511
Cdd:PRK10771 2 LKLTDITWLYH--HLPMRFDLTVE--RGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 512 QVNILFGSIM------------------KKEFYEQVLEACALLPDLEQLPkgdqteiGErgvnISGGQQHRVSLARAVYS 573
Cdd:PRK10771 78 QENNLFSHLTvaqniglglnpglklnaaQREKLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 574 GADIYLLDDPLSAVDVHVGKQLfekvigsLGLL------KNKTRILVTHNLT----LLPQMDLIVvmeSGRIAQMGTYQE 643
Cdd:PRK10771 147 EQPILLLDEPFSALDPALRQEM-------LTLVsqvcqeRQLTLLMVSHSLEdaarIAPRSLVVA---DGRIAWDGPTDE 216
|
...
gi 74136409 644 LLS 646
Cdd:PRK10771 217 LLS 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
446-643 |
1.12e-07 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 54.66 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 446 GMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEM-----------EKLTGV----VQRKG--------------S 496
Cdd:COG0411 16 GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYrptsgrilfdgRDITGLpphrIARLGiartfqnprlfpelT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 497 VA---YVSQQAWIQNCILQVNILFGSIMK--KEFYEQVLEACALLpDLEQLpkgdqteIGERGVNISGGQQHRVSLARAV 571
Cdd:COG0411 96 VLenvLVAAHARLGRGLLAALLRLPRARReeREARERAEELLERV-GLADR-------ADEPAGNLSYGQQRRLEIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74136409 572 YSGADIYLLDDP---LSAVDVHVGKQLFEKVIGSLGLlknkTRILVTHNLTLLpqMDL---IVVMESGR-IAQmGTYQE 643
Cdd:COG0411 168 ATEPKLLLLDEPaagLNPEETEELAELIRRLRDERGI----TILLIEHDMDLV--MGLadrIVVLDFGRvIAE-GTPAE 239
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1061-1285 |
1.22e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 55.42 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1061 LGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLR-----------GKLNIIP 1129
Cdd:PRK10070 40 LSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrkkiamvfQSFALMP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1130 QHPVLFSGTLQMNLDPL-NKYSDSKLWEALELCHLKEFVQSLPEKlrheiseggenLSMGQRQLVCLARALLRKTKILIL 1208
Cdd:PRK10070 120 HMTVLDNTAFGMELAGInAEERREKALDALRQVGLENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1209 DEATASIdfetDKLVQTTIRKEFSDC------TILTIAHRL-QSIIDSDRVLVLDSGSIVEFEAPQNLIRQKGLFYEMTT 1281
Cdd:PRK10070 189 DEAFSAL----DPLIRTEMQDELVKLqakhqrTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
....
gi 74136409 1282 DAGI 1285
Cdd:PRK10070 265 FRGV 268
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
450-651 |
1.28e-07 |
|
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: 55.85 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 450 LKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGeMEKLTGVVQRKG-SVAYVSQQAW------IQncilqvnILF----G 518
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGqDLDGLSRRALrplrrrMQ-------VVFqdpfG 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 519 SI---M------------------KKEFYEQVLEAcallpdLEQ--LPKGDQT----EIgergvniSGGQQHRVSLARAV 571
Cdd:COG4172 374 SLsprMtvgqiiaeglrvhgpglsAAERRARVAEA------LEEvgLDPAARHryphEF-------SGGQRQRIAIARAL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 572 YSGADIYLLDDPLSAVDVHVGKQLfekvigsLGLLKN--KTR----ILVTHNLTLLPQM-DLIVVMESGRIAQMGTYQEL 644
Cdd:COG4172 441 ILEPKLLVLDEPTSALDVSVQAQI-------LDLLRDlqREHglayLFISHDLAVVRALaHRVMVMKDGKVVEQGPTEQV 513
|
250
....*....|..
gi 74136409 645 LSK-----TRNL 651
Cdd:COG4172 514 FDApqhpyTRAL 525
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1064-1261 |
1.38e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.95 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGlHDLRGKL--NIIPQH-PVLFSGTLQ 1140
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQLgiGIIYQElSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1141 MNLdPLNKYSDSKLW--EALELCHLKEFVQSLPEK--LRHEISEGGENLSMGQRQLVCLARALLRKTKILILDEATASI- 1215
Cdd:PRK09700 99 ENL-YIGRHLTKKVCgvNIIDWREMRVRAAMMLLRvgLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLt 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 74136409 1216 DFETDKL--VQTTIRKEFSdcTILTIAHRLQSIID-SDRVLVLDSGSIV 1261
Cdd:PRK09700 178 NKEVDYLflIMNQLRKEGT--AIVYISHKLAEIRRiCDRYTVMKDGSSV 224
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1156-1267 |
1.45e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 53.86 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1156 EALELCHLKEFVQSLPEklrheiseggeNLSMGQRQLVCLARALLRKTKILILDEATASIDFE-TDKLVqtTIRKEFSDC 1234
Cdd:PRK11124 124 KLLERLRLKPYADRFPL-----------HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQIV--SIIRELAET 190
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 74136409 1235 TI--------LTIAHRLQSiidsdRVLVLDSGSIVE------FEAPQ 1267
Cdd:PRK11124 191 GItqvivtheVEVARKTAS-----RVVYMENGHIVEqgdascFTQPQ 232
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1064-1262 |
1.50e-07 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 53.37 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVerAGGKIIIDGIDISTIGLHDLRGKLNIIPQHPVLFSG-TLQMN 1142
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLI--KPDSGEITFDGKSYQKNIEALRRIGALIEAPGFYPNlTAREN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1143 LDPLNKY---SDSKLWEALELCHLKEfvqSLPEKLRheiseggeNLSMGQRQLVCLARALLRKTKILILDEATASIDFET 1219
Cdd:cd03268 93 LRLLARLlgiRKKRIDEVLDVVGLKD---SAKKKVK--------GFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 74136409 1220 DKLVQTTIRKEF-SDCTILTIAHRLQSI-IDSDRVLVLDSGSIVE 1262
Cdd:cd03268 162 IKELRELILSLRdQGITVLISSHLLSEIqKVADRIGIINKGKLIE 206
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
774-940 |
1.80e-07 |
|
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: 54.44 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 774 IYGILGlikGLFVCSGAYVITRGSL---AASRT---MYVQLLNNVLHLPIQFFETNSTGQIISRFTKDIFI----IDMRL 843
Cdd:cd18573 43 FALALL---GVFVVGAAANFGRVYLlriAGERIvarLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVvgksLTQNL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 844 HYYLRLwVNCTLDVIGTILVIIGALPLFILGIIP-----SVFFYFSIQRYyvasSRQIRRLTGASRSPVishfSETLSGV 918
Cdd:cd18573 120 SDGLRS-LVSGVGGIGMMLYISPKLTLVMLLVVPpiavgAVFYGRYVRKL----SKQVQDALADATKVA----EERLSNI 190
|
170 180
....*....|....*....|..
gi 74136409 919 STIRAFGHQQRFIQQYKEVVNE 940
Cdd:cd18573 191 RTVRAFAAERKEVERYAKKVDE 212
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1156-1272 |
2.13e-07 |
|
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: 53.39 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1156 EALELCHLKEFVQSLPEKLrheiseggenlSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTIR---KEFS 1232
Cdd:cd03300 113 EALDLVQLEGYANRKPSQL-----------SGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKrlqKELG 181
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 74136409 1233 dCTILTIAH-RLQSIIDSDRVLVLDSGSIVEFEAPQNLIRQ 1272
Cdd:cd03300 182 -ITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
448-646 |
2.26e-07 |
|
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: 55.08 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 448 PVLKDLNIKIPEGALVAVVGQVGSGKS-SMLSaILGEMEKltGVVQRKGSVAY-------VSQQAW-------------- 505
Cdd:COG4172 24 EAVKGVSFDIAAGETLALVGESGSGKSvTALS-ILRLLPD--PAAHPSGSILFdgqdllgLSERELrrirgnriamifqe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 506 ----------IQNCILQVNILFGSIMKKEFYEQVLEACAL--LPDLE--------QLpkgdqteigergvniSGGQQHRV 565
Cdd:COG4172 101 pmtslnplhtIGKQIAEVLRLHRGLSGAAARARALELLERvgIPDPErrldayphQL---------------SGGQRQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 566 SLARAVYSGADIYLLDDPLSAVDVHVGKQLfekvigsLGLLKNKTR------ILVTHNLTLLPQM-DLIVVMESGRIAQM 638
Cdd:COG4172 166 MIAMALANEPDLLIADEPTTALDVTVQAQI-------LDLLKDLQRelgmalLLITHDLGVVRRFaDRVAVMRQGEIVEQ 238
|
....*...
gi 74136409 639 GTYQELLS 646
Cdd:COG4172 239 GPTAELFA 246
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
777-942 |
2.42e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 54.05 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 777 ILGLIKGlfvcsgaYVITRGSLAASRTMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDIfiidMRLHYYLrlwVNCTLD 856
Cdd:cd18563 58 LLGILRG-------RLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDT----DRLQDFL---SDGLPD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 857 VIGTILVIIGA----------LPLFILGIIP-----SVFFYFSIQRYYVASSRQIRRLTgasrspviSHFSETLSGVSTI 921
Cdd:cd18563 124 FLTNILMIIGIgvvlfslnwkLALLVLIPVPlvvwgSYFFWKKIRRLFHRQWRRWSRLN--------SVLNDTLPGIRVV 195
|
170 180
....*....|....*....|.
gi 74136409 922 RAFGHQQRFIQQYKEVVNENL 942
Cdd:cd18563 196 KAFGQEKREIKRFDEANQELL 216
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
463-620 |
2.90e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.86 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 463 VAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKG-SVAYVSQQAWIQNCILQVNILFGSIMkkefyeqvleacaLLPDLE- 540
Cdd:PRK10584 39 IALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqPLHQMDEEARAKLRAKHVGFVFQSFM-------------LIPTLNa 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 541 ----QLP---KGD--------------QTEIGER----GVNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGKQL 595
Cdd:PRK10584 106 lenvELPallRGEssrqsrngakalleQLGLGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
|
170 180
....*....|....*....|....*
gi 74136409 596 FEkVIGSLGLLKNKTRILVTHNLTL 620
Cdd:PRK10584 186 AD-LLFSLNREHGTTLILVTHDLQL 209
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
448-664 |
2.93e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 53.16 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 448 PVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEklTGVVQRKGSVAYVSQQawIQNCILQvNILFGSIMK----- 522
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILP--AGVRQTAGRVLLDGKP--VAPCALR-GRKIATIMQnprsa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 523 ----KEFYEQVLEACA---LLPDLEQLPK-------GDQTEIGER-GVNISGGQQHRVSLARAVYSGADIYLLDDPLSAV 587
Cdd:PRK10418 92 fnplHTMHTHARETCLalgKPADDATLTAaleavglENAARVLKLyPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 588 DVHVGKQ---LFEKVIGS--LGLLknktriLVTHNLTLLPQM-DLIVVMESGRIAQMGTYQELLSK-----TRNLTNLHQ 656
Cdd:PRK10418 172 DVVAQARildLLESIVQKraLGML------LVTHDMGVVARLaDDVAVMSHGRIVEQGDVETLFNApkhavTRSLVSAHL 245
|
....*...
gi 74136409 657 VISEEEKA 664
Cdd:PRK10418 246 ALYGMELA 253
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1156-1269 |
3.07e-07 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 53.95 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1156 EALELCHLKEFVQSLPeklrHEiseggenLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTIR---KEFs 1232
Cdd:COG3842 118 ELLELVGLEGLADRYP----HQ-------LSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRrlqREL- 185
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 74136409 1233 DCTILTIAHrlqsiiD-------SDRVLVLDSGSIVEFEAPQNL 1269
Cdd:COG3842 186 GITFIYVTH------DqeealalADRIAVMNDGRIEQVGTPEEI 223
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
449-618 |
3.16e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 53.12 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 449 VLKDLNIKIPEGALVAVVGQVGSGKSSMLSAI--LGEME---KLTG---------------VVQ-RKgSVAYVSQQAwiq 507
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIpgaRVEGeilldgediydpdvdVVElRR-RVGMVFQKP--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 508 N----CILQvNILFG----SIMKK----EFYEQVLEACALLPDLEqlpkgDQteIGERGVNISGGQQHRVSLARAVysgA 575
Cdd:COG1117 102 NpfpkSIYD-NVAYGlrlhGIKSKseldEIVEESLRKAALWDEVK-----DR--LKKSALGLSGGQQQRLCIARAL---A 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 74136409 576 ---DIYLLDDPLSAVDvHVGKQLFEKVIGSLGllKNKTRILVTHNL 618
Cdd:COG1117 171 vepEVLLMDEPTSALD-PISTAKIEELILELK--KDYTIVIVTHNM 213
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
450-646 |
3.70e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 54.67 E-value: 3.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 450 LKDLNIKIPEGALVAVVGQVGSGKSSMLSAIlgeMEKLTGVVQRKGSVAY------VSQQAWIQNCILQVNILFGSIM-- 521
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNAL---AFRSPKGVKGSGSVLLngmpidAKEMRAISAYVQQDDLFIPTLTvr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 522 -------------------KKEFYEQVLEACALLpdleqlpKGDQTEIGERGV--NISGGQQHRVSLARAVYSGADIYLL 580
Cdd:TIGR00955 118 ehlmfqahlrmprrvtkkeKRERVDEVLQALGLR-------KCANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 581 DDPLSAVDVHVGKQLFeKVIGSLGlLKNKTRILVTHNLT--LLPQMDLIVVMESGRIAQMGTYQELLS 646
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVV-QVLKGLA-QKGKTIICTIHQPSseLFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1184-1261 |
3.74e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 53.17 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1184 NLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLV-QTT--IRKEFSdCTILTIAHRLQSIID-SDRVLVLDSGS 1259
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVlELTekIVEENN-LTTLMVTHNMEQALDyGNRLIMMHEGR 226
|
..
gi 74136409 1260 IV 1261
Cdd:COG1101 227 II 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1064-1268 |
3.98e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 54.33 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIV--ERAGGKIIIDGIDISTIGLHDLRGKLNIIPQHPvlfSGTLQM 1141
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLInsQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDP---NSSLNP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1142 NLDPLnkysdSKLWEALELCHLKEFVQSLPEKLRHEISEGG----------ENLSMGQRQLVCLARALLRKTKILILDEA 1211
Cdd:PRK15134 378 RLNVL-----QIIEEGLRVHQPTLSAAQREQQVIAVMEEVGldpetrhrypAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74136409 1212 TASIdfetDKLVQTTI------RKEFSDCTILTIAHRLQsIIDS--DRVLVLDSGSIVE-------FEAPQN 1268
Cdd:PRK15134 453 TSSL----DKTVQAQIlallksLQQKHQLAYLFISHDLH-VVRAlcHQVIVLRQGEVVEqgdcervFAAPQQ 519
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
449-646 |
4.60e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 52.77 E-value: 4.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 449 VLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGeMEKLTgvvqrKGSVAYVSQ-----------------QAWIQNCIL 511
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVG-LESPS-----QGNVSWRGEplaklnraqrkafrrdiQMVFQDSIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 512 QVNILF--GSIM--------------KKEFYEQVLEACALLP-DLEQLPKgdqteigergvNISGGQQHRVSLARAVYSG 574
Cdd:PRK10419 101 AVNPRKtvREIIreplrhllsldkaeRLARASEMLRAVDLDDsVLDKRPP-----------QLSGGQLQRVCLARALAVE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74136409 575 ADIYLLDDPLSAVDVHVGKQlfekVIGSLGLLKNKTRI---LVTHNLTLLPQM-DLIVVMESGRIAQMGTYQELLS 646
Cdd:PRK10419 170 PKLLILDEAVSNLDLVLQAG----VIRLLKKLQQQFGTaclFITHDLRLVERFcQRVMVMDNGQIVETQPVGDKLT 241
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
121-363 |
4.61e-07 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 53.17 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 121 VALFKVFADILSFTSPLIMKQMIIFCEHSSDFG--WNgYGYAMALFVVV-FLQTLILQRYqcfnmltSAKVKTAV-NGL- 195
Cdd:cd18548 4 APLFKLLEVLLELLLPTLMADIIDEGIANGDLSyiLR-TGLLMLLLALLgLIAGILAGYF-------AAKASQGFgRDLr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 196 --IYKKALLLSNVSRQKFSTGEIINLMSADAQQLMDLTAN-LNLLWSAPFQILMAIYLLWQ---ELGPAVLAGVAVLVFV 269
Cdd:cd18548 76 kdLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMlLRMLVRAPIMLIGAIIMAFRinpKLALILLVAIPILALV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 270 IpinALAATKIKKLKKSQRKNKDKQIKLLKEILHGIKILKLYAWEPSYKNKIIKIRDQELEFQKSARYLTVFSMLTLTci 349
Cdd:cd18548 156 V---FLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMM-- 230
|
250
....*....|....
gi 74136409 350 pFLVSLATLCVYFL 363
Cdd:cd18548 231 -LIMNLAIVAILWF 243
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1064-1259 |
4.73e-07 |
|
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: 52.05 E-value: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFR---------IVERAGGKIIIDGIDISTIglHDLRGK--------LN 1126
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnylpdsgsiLVRHDGGWVDLAQASPREI--LALRRRtigyvsqfLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1127 IIPQHPvlfsgTLQMNLDPLNKYSDSKLwEALE-----LCHLKefvqsLPEKLrHEIS----EGGEnlsmgqRQLVCLAR 1197
Cdd:COG4778 104 VIPRVS-----ALDVVAEPLLERGVDRE-EARArarelLARLN-----LPERL-WDLPpatfSGGE------QQRVNIAR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74136409 1198 ALLRKTKILILDEATASIDFET-DKLVQTTIRKEFSDCTILTIAHRLqSIID--SDRVLVLDSGS 1259
Cdd:COG4778 166 GFIADPPLLLLDEPTASLDAANrAVVVELIEEAKARGTAIIGIFHDE-EVREavADRVVDVTPFS 229
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1064-1263 |
4.97e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 53.19 E-value: 4.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTI------GLHDLRG-KLNIIPQHPVlfs 1136
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNGREIlnlpekELNKLRAeQISMIFQDPM--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1137 gtlqMNLDPLNKYSDsKLWEALELcH--------LKEFVQSL-----PEKlRHEISEGGENLSMGQRQLVCLARALLRKT 1203
Cdd:PRK09473 108 ----TSLNPYMRVGE-QLMEVLML-HkgmskaeaFEESVRMLdavkmPEA-RKRMKMYPHEFSGGMRQRVMIAMALLCRP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 1204 KILILDEATASIDFEtdklVQTTI-------RKEFsDCTILTIAHRLQSIIDS-DRVLVLDSGSIVEF 1263
Cdd:PRK09473 181 KLLIADEPTTALDVT----VQAQImtllnelKREF-NTAIIMITHDLGVVAGIcDKVLVMYAGRTMEY 243
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
446-640 |
5.21e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 53.31 E-value: 5.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 446 GMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGeMEKLTG--------VV------QRkgSVAYVsqqawIQNCIL 511
Cdd:PRK11650 16 KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAG-LERITSgeiwiggrVVnelepaDR--DIAMV-----FQNYAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 512 ----QV--NILFG----SIMKKEFYEQVLEACALLpDLEQL----PKgdqteigergvNISGGQQHRVSLARAVYSGADI 577
Cdd:PRK11650 88 yphmSVreNMAYGlkirGMPKAEIEERVAEAARIL-ELEPLldrkPR-----------ELSGGQRQRVAMGRAIVREPAV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74136409 578 YLLDDPLSAVD----VHVGKQLfEKVIGSLGllknKTRILVTHN----LTLlpqMDLIVVMESGRIAQMGT 640
Cdd:PRK11650 156 FLFDEPLSNLDaklrVQMRLEI-QRLHRRLK----TTSLYVTHDqveaMTL---ADRVVVMNGGVAEQIGT 218
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
768-940 |
5.82e-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: 52.87 E-value: 5.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 768 RSNKLNIYGILGLIKGLFVCSGA------YVITRGSLAASRTMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDIfiidM 841
Cdd:cd18576 29 GGDTASLNQIALLLLGLFLLQAVfsffriYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDV----T 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 842 RLHYYLRLWVnctLDVIGTILVIIGA----------LPLFILGIIPSVFFYFSIqryyvaSSRQIRRLTGA-----SRSP 906
Cdd:cd18576 105 QIQDTLTTTL---AEFLRQILTLIGGvvllffiswkLTLLMLATVPVVVLVAVL------FGRRIRKLSKKvqdelAEAN 175
|
170 180 190
....*....|....*....|....*....|....
gi 74136409 907 VIShfSETLSGVSTIRAFGHQQRFIQQYKEVVNE 940
Cdd:cd18576 176 TIV--EETLQGIRVVKAFTREDYEIERYRKALER 207
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1064-1275 |
8.53e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 52.11 E-value: 8.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKLNIIPQHP--VLFSGTLQM 1141
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1142 NL--DPLNKYSDS-----KLWEALELCHLKEFVQSLPeklrheiseggENLSMGQRQLVCLARALLRKTKILILDEATAS 1214
Cdd:PRK13652 99 DIafGPINLGLDEetvahRVSSALHMLGLEELRDRVP-----------HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74136409 1215 IDFETDKLVQTTIRK--EFSDCTILTIAHRLQSIID-SDRVLVLDSGSIVEFEAPQNLIRQKGL 1275
Cdd:PRK13652 168 LDPQGVKELIDFLNDlpETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1047-1273 |
9.30e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 52.05 E-value: 9.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1047 VVEFINYQARYRDELGlALQDITFQTHGEEKIGIVGRTGAGKSTL---SNCLFrIVERAGGKIIIDGIDISTIglHDLRG 1123
Cdd:PRK13647 4 IIEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLllhLNGIY-LPQRGRVKVMGREVNAENE--KWVRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1124 KLNIIPQHP--VLFSGT---------LQMNLDPlnKYSDSKLWEALELCHLKEFVQSLPEklrheiseggeNLSMGQRQL 1192
Cdd:PRK13647 80 KVGLVFQDPddQVFSSTvwddvafgpVNMGLDK--DEVERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1193 VCLARALLRKTKILILDEATASIDfETDKLVQTTIRKEFSD--CTILTIAHRLQSIID-SDRVLVLDSGSIVEFEAPQNL 1269
Cdd:PRK13647 147 VAIAGVLAMDPDVIVLDEPMAYLD-PRGQETLMEILDRLHNqgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLL 225
|
....
gi 74136409 1270 IRQK 1273
Cdd:PRK13647 226 TDED 229
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1067-1261 |
1.04e-06 |
|
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: 51.14 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1067 DITFQTHgEEKIGIVGRTGAGKSTLSNCLfriveraggkiiidgidistIGLHDL-RGKLNIipQHPVLFSGTLQMNLDP 1145
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCI--------------------AGLEKPdGGTIVL--NGTVLFDSRKKINLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1146 ---------------------------LNKYSDSKLW----EALELCHLKEFVQSLPEKLrheiseggenlSMGQRQLVC 1194
Cdd:cd03297 73 qqrkiglvfqqyalfphlnvrenlafgLKRKRNREDRisvdELLDLLGLDHLLNRYPAQL-----------SGGEKQRVA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74136409 1195 LARALLRKTKILILDEATASIDFET-DKLVQ--TTIRKEFSDCTILtIAHRLQSIID-SDRVLVLDSGSIV 1261
Cdd:cd03297 142 LARALAAQPELLLLDEPFSALDRALrLQLLPelKQIKKNLNIPVIF-VTHDLSEAEYlADRIVVMEDGRLQ 211
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
448-588 |
1.11e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.72 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 448 PVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQ------RKGSVAYVSQQAWI-------------QN 508
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILferqsiKKDLCTYQKQLCFVghrsginpyltlrEN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 509 CILQVNILFGSImkkefyeQVLEACAL--LPDLEQLPKGdqteigergvNISGGQQHRVSLARAVYSGADIYLLDDPLSA 586
Cdd:PRK13540 95 CLYDIHFSPGAV-------GITELCRLfsLEHLIDYPCG----------LLSSGQKRQVALLRLWMSKAKLWLLDEPLVA 157
|
..
gi 74136409 587 VD 588
Cdd:PRK13540 158 LD 159
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1156-1269 |
1.18e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 52.26 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1156 EALELCHLKEFVQSLPEklrheiseggeNLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTI----RKef 1231
Cdd:PRK09452 127 EALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELkalqRK-- 193
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 74136409 1232 SDCTILTIAH-RLQSIIDSDRVLVLDSGSIVE-------FEAPQNL 1269
Cdd:PRK09452 194 LGITFVFVTHdQEEALTMSDRIVVMRDGRIEQdgtpreiYEEPKNL 239
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1064-1293 |
1.21e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 52.16 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFqTHGEEKI-GIVGRTGAGKSTLSNCL---------------FRIVERAGGKIIIDGIDISTI-GLHDLRGKLN 1126
Cdd:PRK13631 41 ALNNISY-TFEKNKIyFIIGNSGSGKSTLVTHFnglikskygtiqvgdIYIGDKKNNHELITNPYSKKIkNFKELRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1127 IIPQHP--VLFSGTLQMNL--DPLN----KYSDSKLWEA-LELCHLKE-FVQSLPEKLrheiseggenlSMGQRQLVCLA 1196
Cdd:PRK13631 120 MVFQFPeyQLFKDTIEKDImfGPVAlgvkKSEAKKLAKFyLNKMGLDDsYLERSPFGL-----------SGGQKRRVAIA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1197 RALLRKTKILILDEATASIDFETDK-LVQTTIRKEFSDCTILTIAHRLQSIID-SDRVLVLDSGSIVEFEAPqnlirqkg 1274
Cdd:PRK13631 189 GILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTP-------- 260
|
250
....*....|....*....
gi 74136409 1275 lfYEMTTDAGITQESGTEK 1293
Cdd:PRK13631 261 --YEIFTDQHIINSTSIQV 277
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1185-1258 |
1.29e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.70 E-value: 1.29e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74136409 1185 LSMGQRQLVCLARALLRKTKILILDEAT-ASIDFETDKLVQtTIRK-EFSDCTILTIAHRLQSIID-SDRVLVLDSG 1258
Cdd:PRK10762 142 LSIGEQQMVEIAKVLSFESKVIIMDEPTdALTDTETESLFR-VIRElKSQGRGIVYISHRLKEIFEiCDDVTVFRDG 217
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1064-1261 |
1.36e-06 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 51.14 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGgkiiidgidiSTIGL--HDLRG-------KLNI--IPQHP 1132
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRS----------GSIRFdgEDITGlpphriaRLGIgyVPEGR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1133 VLFSG-T----LQMNLDPLNKYSDSKlwEALELCH-----LKEFVQSLpeklrheiseGGeNLSMGQRQLVCLARALLRK 1202
Cdd:COG0410 88 RIFPSlTveenLLLGAYARRDRAEVR--ADLERVYelfprLKERRRQR----------AG-TLSGGEQQMLAIGRALMSR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 1203 TKILILDEATA----SIdfeTDKLVQT--TIRKEfsDCTILTI---AHRLQSIidSDRVLVLDSGSIV 1261
Cdd:COG0410 155 PKLLLLDEPSLglapLI---VEEIFEIirRLNRE--GVTILLVeqnARFALEI--ADRAYVLERGRIV 215
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
433-672 |
1.41e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 52.11 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTD--ATYSWNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGeMEKLTGvvqrkGSVaYV--------SQ 502
Cdd:PRK11153 2 IELKNisKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINL-LERPTS-----GRV-LVdgqdltalSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 503 QAWIQ-----NCILQ-VNIL-----FGSIM---------KKEFYEQVLEACAL--LPDL-EQLPKgdqteigergvNISG 559
Cdd:PRK11153 75 KELRKarrqiGMIFQhFNLLssrtvFDNVAlplelagtpKAEIKARVTELLELvgLSDKaDRYPA-----------QLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 560 GQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGKQLfekvigsLGLLK--NK----TRILVTHnltllpQMDLI------ 627
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSI-------LELLKdiNRelglTIVLITH------EMDVVkricdr 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 74136409 628 -VVMESGRIAQMGTYQELLSK-----TRNLtnLHQVISEEEKAHALKRASA 672
Cdd:PRK11153 211 vAVIDAGRLVEQGTVSEVFSHpkhplTREF--IQSTLHLDLPEDYLARLQA 259
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
774-940 |
1.48e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 51.68 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 774 IYGILGLIKGLFVCSGAYVITRGSLAASRTMYVQLLNNVLHLPIQFF--ETNSTGQIISRFTKDIF----IIDMRLhyyL 847
Cdd:cd18578 57 MFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFddPENSTGALTSRLSTDASdvrgLVGDRL---G 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 848 RLWVNCTLDVIGTI----------LVIIGALPLFILgiipSVFFYFSIQRYYVASSRQIRRLTGasrspviSHFSETLSG 917
Cdd:cd18578 134 LILQAIVTLVAGLIiafvygwklaLVGLATVPLLLL----AGYLRMRLLSGFEEKNKKAYEESS-------KIASEAVSN 202
|
170 180
....*....|....*....|...
gi 74136409 918 VSTIRAFGHQQRFIQQYKEVVNE 940
Cdd:cd18578 203 IRTVASLTLEDYFLEKYEEALEE 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
557-653 |
1.48e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.40 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 557 ISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGKQLfekvigsLGLLK------NKTRILVTHNLTLLPQM-DLIVV 629
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQI-------LQLLRelqqelNMGLLFITHNLSIVRKLaDRVAV 229
|
90 100
....*....|....*....|....*....
gi 74136409 630 MESGRIAQMGTYQELLSK-----TRNLTN 653
Cdd:PRK15134 230 MQNGRCVEQNRAATLFSApthpyTQKLLN 258
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1019-1264 |
1.50e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 52.37 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1019 RVCEYENMDKEAPWIMSRRPPLQWPN-----KGVVEFINYQARYRDELglALQDITFQTHGEEKIGIVGRTGAGKSTLSN 1093
Cdd:COG0488 282 RIKALEKLEREEPPRRDKTVEIRFPPperlgKKVLELEGLSKSYGDKT--LLDDLSLRIDRGDRIGLIGPNGAGKSTLLK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1094 CLfriveraggkiiidgidistIG-LHDLRGKLNI--------IPQHpvlfsgtlQMNLDPlnkysDSKLWEAL------ 1158
Cdd:COG0488 360 LL--------------------AGeLEPDSGTVKLgetvkigyFDQH--------QEELDP-----DKTVLDELrdgapg 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1159 --ELcHLKEFVQSL---PEKLRHEISeggeNLSMGQRQLVCLARALLRKTKILILDEATASIDFET-----DKLvqttir 1228
Cdd:COG0488 407 gtEQ-EVRGYLGRFlfsGDDAFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETlealeEAL------ 475
|
250 260 270
....*....|....*....|....*....|....*....
gi 74136409 1229 KEFsDCTILTIAH-R--LQSIidSDRVLVLDSGSIVEFE 1264
Cdd:COG0488 476 DDF-PGTVLLVSHdRyfLDRV--ATRILEFEDGGVREYP 511
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
116-382 |
1.92e-06 |
|
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: 51.02 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 116 SVLIQVALFKVFADILsftsplimkQMIIFCEHSSDFGWngygYAMALFVVVFLQTL-ILQRYQCFNMlTSAKVktaVNG 194
Cdd:cd18557 8 SSAAQLLLPYLIGRLI---------DTIIKGGDLDVLNE----LALILLAIYLLQSVfTFVRYYLFNI-AGERI---VAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 195 LiykKALLLSNVSRQ------KFSTGEIINLMSADAQQLMD-LTANLNLLWSAPFQILMAIYLL----WQeLGPAVLAgv 263
Cdd:cd18557 71 L---RRDLFSSLLRQeiaffdKHKTGELTSRLSSDTSVLQSaVTDNLSQLLRNILQVIGGLIILfilsWK-LTLVLLL-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 264 avlvfVIPINALAAT----KIKKLKKSQRKNKDKQIKLLKEILHGIKILKLYAWEP----SYKNKIIKIRDqelEFQKSA 335
Cdd:cd18557 145 -----VIPLLLIASKiygrYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEkeirRYSEALDRSYR---LARKKA 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 74136409 336 RYLTVFSMLTLtcipFLVSLATLCVYFLldeGNILTATKVFTSMSLF 382
Cdd:cd18557 217 LANALFQGITS----LLIYLSLLLVLWY---GGYLVLSGQLTVGELT 256
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
247-647 |
2.03e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.90 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 247 AIYLLWqeLGPAVLAGVAV-LVFVIPINALAATKIKKLKKSQRKNKDKQIKLLKEILHGIKILKL------YAWEPSYKN 319
Cdd:PRK10522 139 AAYLAW--LSPKMLLVTAIwMAVTIWGGFVLVARVYKHMATLRETEDKLYNDYQTVLEGRKELTLnreraeYVFENEYEP 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 320 KIIKIRDQELE---FQKSARYLTVFSMLTLTCIPFlvslatlcvYFLLDEGNILTATKVFTSMSLFnILRIPLFE----L 392
Cdd:PRK10522 217 DAQEYRHHIIRadtFHLSAVNWSNIMMLGAIGLVF---------YMANSLGWADTNVAATYSLTLL-FLRTPLLSavgaL 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 393 PTVISTvvqtKISLGRLEDFlhteELLPQNIE---TNYIGD-HAIEFTDATYSWNKTGMPVlKDLNIKIPEGALVAVVGQ 468
Cdd:PRK10522 287 PTLLSA----QVAFNKLNKL----ALAPYKAEfprPQAFPDwQTLELRNVTFAYQDNGFSV-GPINLTIKRGELLFLIGG 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 469 VGSGKS--SMLsailgemekLTGVVQ-RKGS-------VAYVSQQAWIQncilqvniLFGSIMkKEFY--EQVLEACALL 536
Cdd:PRK10522 358 NGSGKStlAML---------LTGLYQpQSGEilldgkpVTAEQPEDYRK--------LFSAVF-TDFHlfDQLLGPEGKP 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 537 PD-------LEQLPKGDQTEI-GERGVNI--SGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVgKQLFEKVIgsLGLL 606
Cdd:PRK10522 420 ANpalvekwLERLKMAHKLELeDGRISNLklSKGQKKRLALLLALAEERDILLLDEWAADQDPHF-RREFYQVL--LPLL 496
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 74136409 607 K--NKTRILVTHNLTLLPQMDLIVVMESGRIAQM-GTYQELLSK 647
Cdd:PRK10522 497 QemGKTIFAISHDDHYFIHADRLLEMRNGQLSELtGEERDAASR 540
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1185-1268 |
2.37e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 50.42 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1185 LSMGQRQLVCLARALLRKTKILILDEATASIDF-ETDKlVQTTIRKEFSDCTILTIAHRLQ--SIIdSDRVLVLDSGSIV 1261
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPiSTAK-IEELILELKKDYTIVIVTHNMQqaARV-SDYTAFFYLGELV 232
|
90
....*....|....
gi 74136409 1262 E-------FEAPQN 1268
Cdd:COG1117 233 EfgpteqiFTNPKD 246
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1056-1287 |
2.37e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 50.78 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1056 RYRDELGLALQDITFQTHGeeKIGIVGRTGAGKSTLSNCLFRIV--ERAGGKIIIDGIDISTIGLHDLRGKLNIIPQHP- 1132
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSP--VTGLVGANGCGKSTLFMNLSGLLrpQKGAVLWQGKPLDYSKRGLLALRQQVATVFQDPe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1133 -----------VLFSgtlQMNLDPLNKYSDSKLWEALELCHLKEFVQSLPEKLRHeiseggenlsmGQRQLVCLARALLR 1201
Cdd:PRK13638 88 qqifytdidsdIAFS---LRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSH-----------GQKKRVAIAGALVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1202 KTKILILDEATASIDFETDKLVQTTIRKEFSDCTILTI-AHRLQSIID-SDRVLVLDSGSIVEFEAPQNLIRQKglfyEM 1279
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFACT----EA 229
|
....*...
gi 74136409 1280 TTDAGITQ 1287
Cdd:PRK13638 230 MEQAGLTQ 237
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1064-1269 |
2.47e-06 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 51.37 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHdlRGKLNIIPQHPVLFSG-TLQMN 1142
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY--QRPINMMFQSYALFPHmTVEQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1143 L------DPLNKYS-DSKLWEALELCHLKEFVQSLPEKLrheiseggenlSMGQRQLVCLARALLRKTKILILDEATASI 1215
Cdd:PRK11607 112 IafglkqDKLPKAEiASRVNEMLGLVHMQEFAKRKPHQL-----------SGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74136409 1216 dfetDKLVQTTIRKEFSD------CTILTIAH-RLQSIIDSDRVLVLDSGSIVEFEAPQNL 1269
Cdd:PRK11607 181 ----DKKLRDRMQLEVVDilervgVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
791-966 |
2.65e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 50.64 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 791 YVITRGSLAASRTMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDMRLHYYLRLWVN-CTLDVIGTILVIIG-AL 868
Cdd:cd18568 64 YLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFQENQKIRRFLTRSALTTILDlLMVFIYLGLMFYYNlQL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 869 PLFILGIIP-SVFFYFSIQRYYVASSRQIRRLTGASRspviSHFSETLSGVSTIRAFGHQQRFIQQYKEVVNENLvcfyN 947
Cdd:cd18568 144 TLIVLAFIPlYVLLTLLSSPKLKRNSREIFQANAEQQ----SFLVEALTGIATIKALAAERPIRWRWENKFAKAL----N 215
|
170
....*....|....*....
gi 74136409 948 NVISNRWLSVRLEFLGNLM 966
Cdd:cd18568 216 TRFRGQKLSIVLQLISSLI 234
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1078-1291 |
2.96e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 50.40 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1078 IGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKLNIIPQHPVLFSGtlqMNLDPLNKYSDS---KL 1154
Cdd:PRK11231 31 TALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEG---ITVRELVAYGRSpwlSL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1155 W------------EALELCHLKEFVQslpeklrHEISEggenLSMGQRQLVCLARALLRKTKILILDEATASIDF----E 1218
Cdd:PRK11231 108 WgrlsaednarvnQAMEQTRINHLAD-------RRLTD----LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDInhqvE 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 1219 TDKLVQttirkEFSDC--TILTIAHRL-QSIIDSDRVLVLDSGSIVEFEAPQNLIRQKGLFYEMTTDAGITQE--SGT 1291
Cdd:PRK11231 177 LMRLMR-----ELNTQgkTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAEIHPEpvSGT 249
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
450-665 |
2.96e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.20 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 450 LKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSVAYVSQQAWIQNCILQV-NILFGSIMKKEFYEQ 528
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTGIeNIEFKMLCMGFKRKE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 529 VLeacALLPDLEQLpkgdqTEIGE---RGV-NISGGQQHRVSLARAVYSGADIYLLDDPLSavdvhVGKQLF-EKVIGSL 603
Cdd:PRK13546 120 IK---AMTPKIIEF-----SELGEfiyQPVkKYSSGMRAKLGFSINITVNPDILVIDEALS-----VGDQTFaQKCLDKI 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74136409 604 GLLK--NKTRILVTHNLTLLPQM-DLIVVMESGRIAQMGTYQELLSKTRNLTNLHQVISEEEKAH 665
Cdd:PRK13546 187 YEFKeqNKTIFFVSHNLGQVRQFcTKIAWIEGGKLKDYGELDDVLPKYEAFLNDFKKKSKAEQKE 251
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1047-1270 |
3.05e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 50.57 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1047 VVEFINYQARYRDELglALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGgkiiidgidiSTIGL-------- 1118
Cdd:PRK13537 7 PIDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDA----------GSISLcgepvpsr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1119 -HDLRGKLNIIPQHPvlfsgtlqmNLDPLNKYSDSKL----WEALELCHLKEFVQSLPE--KLRHEISEGGENLSMGQRQ 1191
Cdd:PRK13537 75 aRHARQRVGVVPQFD---------NLDPDFTVRENLLvfgrYFGLSAAAARALVPPLLEfaKLENKADAKVGELSGGMKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1192 LVCLARALLRKTKILILDEATASIDFETDKLVQTTIRKEFSDC-TILTIAH------RLqsiidSDRVLVLDSGSIVEFE 1264
Cdd:PRK13537 146 RLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGkTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEG 220
|
....*.
gi 74136409 1265 APQNLI 1270
Cdd:PRK13537 221 APHALI 226
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
450-630 |
3.16e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.86 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 450 LKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQR----KGSVAYVSQqawiqnciLQVNILFGsimkkef 525
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISFLpkfsRNKLIFIDQ--------LQFLIDVG------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 526 yeqvleacallpdLEQLPkgdqteIGERGVNISGGQQHRVSLARAVYSGAD--IYLLDDPLSAVDvHVGKQLFEKVIGSL 603
Cdd:cd03238 76 -------------LGYLT------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH-QQDINQLLEVIKGL 135
|
170 180
....*....|....*....|....*..
gi 74136409 604 GLLKNkTRILVTHNLTLLPQMDLIVVM 630
Cdd:cd03238 136 IDLGN-TVILIEHNLDVLSSADWIIDF 161
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1065-1255 |
4.27e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 49.33 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQ-THGEEKIgIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKLNIIPQHPVLFSGTLQMNL 1143
Cdd:PRK10247 23 LNNISFSlRAGEFKL-ITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1144 ----DPLNKYSDSKLWEAlelcHLKEFvqSLPEK-LRHEISEggenLSMGQRQLVCLARALLRKTKILILDEATASIDFE 1218
Cdd:PRK10247 102 ifpwQIRNQQPDPAIFLD----DLERF--ALPDTiLTKNIAE----LSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 74136409 1219 TDKLVQTTIRKEFSDCTI--LTIAHRLQSIIDSDRVLVL 1255
Cdd:PRK10247 172 NKHNVNEIIHRYVREQNIavLWVTHDKDEINHADKVITL 210
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1064-1272 |
4.27e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 50.12 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIG----LHDLRGKLNIIPQHP--VLFSG 1137
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKPVRKKVGVVFQFPesQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1138 TL--QMNLDPLN-----KYSDSKLWEALELCHL-KEFVQSLPEKlrheiseggenLSMGQRQLVCLARALLRKTKILILD 1209
Cdd:PRK13643 101 TVlkDVAFGPQNfgipkEKAEKIAAEKLEMVGLaDEFWEKSPFE-----------LSGGQMRRVAIAGILAMEPEVLVLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 1210 EATASID----FETDKLVQTTIRkefSDCTILTIAHRLQSIID-SDRVLVLDSGSIVEFEAPQNLIRQ 1272
Cdd:PRK13643 170 EPTAGLDpkarIEMMQLFESIHQ---SGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1064-1269 |
4.58e-06 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 50.46 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLfriverAggkiiidgidistiGLHDL-RGKL---------------NI 1127
Cdd:COG3839 18 ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMI------A--------------GLEDPtSGEIliggrdvtdlppkdrNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1128 --IPQHPVLF-SGTLQMNLD-PL--NKYS----DSKLWEALELCHLKEFVQSLPEklrheiseggeNLSMGQRQLVCLAR 1197
Cdd:COG3839 78 amVFQSYALYpHMTVYENIAfPLklRKVPkaeiDRRVREAAELLGLEDLLDRKPK-----------QLSGGQRQRVALGR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1198 ALLRKTKILILDEATASIDFetdKL-VQTtiRKEFSD-------CTI---------LTIAhrlqsiidsDRVLVLDSGSI 1260
Cdd:COG3839 147 ALVREPKVFLLDEPLSNLDA---KLrVEM--RAEIKRlhrrlgtTTIyvthdqveaMTLA---------DRIAVMNDGRI 212
|
....*....
gi 74136409 1261 VEFEAPQNL 1269
Cdd:COG3839 213 QQVGTPEEL 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1185-1267 |
4.70e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 49.36 E-value: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1185 LSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTIRKEFSDC-TILTIAHRLQSIID-SDRVLVLDSGSIVE 1262
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDvADRAIFMDQGRIVE 224
|
90
....*....|..
gi 74136409 1263 -------FEAPQ 1267
Cdd:PRK11264 225 qgpakalFADPQ 236
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
460-634 |
4.92e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 51.03 E-value: 4.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 460 GALVAVVGQVGSGKSSMLSAILGEMEK--LTGVV---QRKGSVAYVSQQAWIQncilQVNILFGSIMKKEfyeqVLEACA 534
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGnnFTGTIlanNRKPTKQILKRTGFVT----QDDILYPHLTVRE----TLVFCS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 535 LLPDLEQLPKGDQTEIGE---------------------RGvnISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGK 593
Cdd:PLN03211 166 LLRLPKSLTKQEKILVAEsviselgltkcentiignsfiRG--ISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAY 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 74136409 594 QLfekvIGSLGLLKNKTRILVT---HNLTLLPQM-DLIVVMESGR 634
Cdd:PLN03211 244 RL----VLTLGSLAQKGKTIVTsmhQPSSRVYQMfDSVLVLSEGR 284
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
558-649 |
5.03e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.96 E-value: 5.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 558 SGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGKQ---LFEKVIGSLGLlknkTRILVTHNLTLLPQM-DLIVVMESG 633
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQvlnLMMDLQQELGL----SYVFISHDLSVVEHIaDEVMVMYLG 231
|
90
....*....|....*.
gi 74136409 634 RIAQMGTYQELLSKTR 649
Cdd:PRK11308 232 RCVEKGTKEQIFNNPR 247
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1064-1246 |
5.97e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 49.50 E-value: 5.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLrgkLNIIPQH-------PVLFS 1136
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSeevdwsfPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1137 GTLQMN-------LDPLNKYSDSKLWEALELCHLKEFvqslpeklRH-EISEggenLSMGQRQLVCLARALLRKTKILIL 1208
Cdd:PRK15056 99 DVVMMGryghmgwLRRAKKRDRQIVTAALARVDMVEF--------RHrQIGE----LSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 74136409 1209 DEATASIDFETDKLVQTTIRkEFSD--CTILTIAHRLQSI 1246
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLR-ELRDegKTMLVSTHNLGSV 205
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
457-617 |
6.93e-06 |
|
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: 48.94 E-value: 6.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 457 IPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKG-SVAYVSQQAwIQNCILQVNILFGSIMKkEFYEQVLEACAL 535
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYI-KADYEGTVRDLLSSITK-DFYTHPYFKTEI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 536 LPDLeQLPKgdqteIGERGVN-ISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHvGKQLFEKVIGSLGLLKNKTRILV 614
Cdd:cd03237 100 AKPL-QIEQ-----ILDREVPeLSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE-QRLMASKVIRRFAENNEKTAFVV 172
|
...
gi 74136409 615 THN 617
Cdd:cd03237 173 EHD 175
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1184-1292 |
7.09e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.31 E-value: 7.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1184 NLSMGQRQLVCLARALLRKTKILILDEATASI-DFETDKLVqtTIRKEFS--DCTILTIAHRLQSIID-SDRVLVLDSGS 1259
Cdd:PRK13549 143 NLGLGQQQLVEIAKALNKQARLLILDEPTASLtESETAVLL--DIIRDLKahGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
90 100 110
....*....|....*....|....*....|...
gi 74136409 1260 IVEFEAPQNlirqkglfyeMTTDAGITQESGTE 1292
Cdd:PRK13549 221 HIGTRPAAG----------MTEDDIITMMVGRE 243
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
779-940 |
7.20e-06 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 49.26 E-value: 7.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 779 GLIKGLFVCSGAYVITRgslaasrtMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDIFI----IDMRLHYYLRLWVNCt 854
Cdd:cd18590 54 GLRGGLFMCTLSRLNLR--------LRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLmsrsVALNANVLLRSLVKT- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 855 ldvIGTILVIIGALPLFILGIIPSVFFYFSIQRYYVASSRQIRRLTGASRSPVISHFSETLSGVSTIRAFGHQQRFIQQY 934
Cdd:cd18590 125 ---LGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRY 201
|
....*.
gi 74136409 935 KEVVNE 940
Cdd:cd18590 202 SEALER 207
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
433-599 |
7.32e-06 |
|
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: 47.53 E-value: 7.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 433 IEFTDATYSwNKTGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQR--KGSVAYVSQQAWIQNci 510
Cdd:cd03223 1 IELENLSLA-TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpeGEDLLFLPQRPYLPL-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 511 lqvnilfGSIMkkefyEQVLeacallpdleqLPKGDqteigergvNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVH 590
Cdd:cd03223 78 -------GTLR-----EQLI-----------YPWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
|
....*....
gi 74136409 591 VGKQLFEKV 599
Cdd:cd03223 126 SEDRLYQLL 134
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1063-1244 |
8.49e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 49.01 E-value: 8.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1063 LALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFR---IVERAGGKIIIDGIDISTIGLH----DLRGKLNIIPQHPVLF 1135
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndLIPGFRVEGKVTFHGKNLYAPDvdpvEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1136 SGTL-------------QMNLDPLNKYS--DSKLWEALElchlkefvqslpEKLRheisEGGENLSMGQRQLVCLARALL 1200
Cdd:PRK14243 104 PKSIydniaygaringyKGDMDELVERSlrQAALWDEVK------------DKLK----QSGLSLSGGQQQRLCIARAIA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 74136409 1201 RKTKILILDEATASIDFETDKLVQTTIRKEFSDCTILTIAHRLQ 1244
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQ 211
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
452-595 |
8.86e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 47.88 E-value: 8.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 452 DLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQ------RKGSVAYVSQQAWI--QNCILQV-----NILFG 518
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwqgepiRRQRDEYHQDLLYLghQPGIKTEltaleNLRFY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 519 SIMKKEFYEQVLEAcAL----LPDLEQLPKGdqteigergvNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGKQ 594
Cdd:PRK13538 99 QRLHGPGDDEALWE-ALaqvgLAGFEDVPVR----------QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVAR 167
|
.
gi 74136409 595 L 595
Cdd:PRK13538 168 L 168
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1185-1260 |
9.69e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 48.86 E-value: 9.69e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74136409 1185 LSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTIR--KEFSDCTILTIAHRLQSIID-SDRVLVLDSGSI 1260
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDYALRyCERIVALRQGHV 231
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
558-644 |
9.87e-06 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 49.34 E-value: 9.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 558 SGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGKQ---LFEKVIGSLGLlknkTRILVTHNLTLLPQM-DLIVVMESG 633
Cdd:COG4608 159 SGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQvlnLLEDLQDELGL----TYLFISHDLSVVRHIsDRVAVMYLG 234
|
90
....*....|.
gi 74136409 634 RIAQMGTYQEL 644
Cdd:COG4608 235 KIVEIAPRDEL 245
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1047-1270 |
1.00e-05 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 48.55 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1047 VVEFINYQARYRDELglALQDITFQTHGEEKIGIVGRTGAGKSTLSNCL--FRIVERAGGKIIIDGIDISTIGLHDLRGK 1124
Cdd:PRK09493 1 MIEFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITSGDLIVDGLKVNDPKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1125 LNIIPQHPVLFSgtlQMN------LDPLNKYSDSKLwEALELChlKEFVQS--LPEKLRHEISEggenLSMGQRQLVCLA 1196
Cdd:PRK09493 79 AGMVFQQFYLFP---HLTalenvmFGPLRVRGASKE-EAEKQA--RELLAKvgLAERAHHYPSE----LSGGQQQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1197 RALLRKTKILILDEATASIDFETDKLVQTTIR---KEFSDCTILT----IAHRLQSiidsdRVLVLDSGSIVEFEAPQNL 1269
Cdd:PRK09493 149 RALAVKPKLMLFDEPTSALDPELRHEVLKVMQdlaEEGMTMVIVTheigFAEKVAS-----RLIFIDKGRIAEDGDPQVL 223
|
.
gi 74136409 1270 I 1270
Cdd:PRK09493 224 I 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1065-1273 |
1.10e-05 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 48.61 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQTHGEEKIGIVGRTGAGKSTLsncLfriveRAGGKIIIDGIDISTIGLHDLRG--------KLNIIPQHPVL-F 1135
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTL---L-----RALSGELSPDSGEVRLNGRPLADwspaelarRRAVLPQHSSLsF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1136 SGTLQ----MNLDPL---NKYSDSKLWEALELCHLKEFVQ-SLPEklrheiseggenLSMGQRQLVCLARALLR------ 1201
Cdd:PRK13548 90 PFTVEevvaMGRAPHglsRAEDDALVAAALAQVDLAHLAGrDYPQ------------LSGGEQQRVQLARVLAQlwepdg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1202 KTKILILDEATASIDfetdkLV--QTTIR--KEFSD---CTILTIAHRL-QSIIDSDRVLVLDSGSIVEFEAPQNLIRQK 1273
Cdd:PRK13548 158 PPRWLLLDEPTSALD-----LAhqHHVLRlaRQLAHergLAVIVVLHDLnLAARYADRIVLLHQGRLVADGTPAEVLTPE 232
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1064-1272 |
1.16e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 48.15 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRI-------VERaggkiiidgidISTI--------GLH-DLRGKLNI 1127
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGIleptsgrVEV-----------NGRVsallelgaGFHpELTGRENI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1128 IpqhpvlFSGTLqMNLDPlnKYSDSKLWEALELCHLKEFVqSLPEKlrheiseggeNLSMGQRqlvclAR-----ALLRK 1202
Cdd:COG1134 110 Y------LNGRL-LGLSR--KEIDEKFDEIVEFAELGDFI-DQPVK----------TYSSGMR-----ARlafavATAVD 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 1203 TKILILDEATASIDFE-----TDKLvqttirKEFSD--CTILTIAHRLQSIID-SDRVLVLDSGSIVEFEAPQNLIRQ 1272
Cdd:COG1134 165 PDILLVDEVLAVGDAAfqkkcLARI------RELREsgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1048-1273 |
1.21e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 49.06 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1048 VEFINYQARYRDELglALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVeraggkiiidGIDISTIGLHDL------ 1121
Cdd:PRK13536 42 IDLAGVSKSYGDKA--VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMT----------SPDAGKITVLGVpvpara 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1122 ---RGKLNIIPQHPVL-FSGTLQMNLDPLNKY--SDSKLWEALeLCHLKEFVQsLPEKLRHEISEggenLSMGQRQLVCL 1195
Cdd:PRK13536 110 rlaRARIGVVPQFDNLdLEFTVRENLLVFGRYfgMSTREIEAV-IPSLLEFAR-LESKADARVSD----LSGGMKRRLTL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1196 ARALLRKTKILILDEATASIDFETDKLVQTTIRKEFSDC-TILTIAH------RLqsiidSDRVLVLDSGSIVEFEAPQN 1268
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGkTILLTTHfmeeaeRL-----CDRLCVLEAGRKIAEGRPHA 258
|
....*
gi 74136409 1269 LIRQK 1273
Cdd:PRK13536 259 LIDEH 263
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1064-1272 |
1.23e-05 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 48.99 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLsncLfRIV---ERAGGkiiidgidiSTIGLHDLRGKLNIIP---------QH 1131
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTL---L-RIIaglETPDS---------GRIVLNGRDLFTNLPPrerrvgfvfQH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1132 PVLFSgtlQMN-----------LDPLNKYSDSKLWEALELCHLKEFVQSLPEklrheiseggeNLSMGQRQLVCLARALL 1200
Cdd:COG1118 84 YALFP---HMTvaeniafglrvRPPSKAEIRARVEELLELVQLEGLADRYPS-----------QLSGGQRQRVALARALA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1201 RKTKILILDEATASIDFEtdklVQTTIRKEFSD------CTILTIAH------RLqsiidSDRVLVLDSGSIVEFEAPQN 1268
Cdd:COG1118 150 VEPEVLLLDEPFGALDAK----VRKELRRWLRRlhdelgGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDE 220
|
....
gi 74136409 1269 LIRQ 1272
Cdd:COG1118 221 VYDR 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1183-1275 |
1.32e-05 |
|
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: 48.94 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1183 ENLSMGQRQLVCLARALLRKTKILILDEATASIDFETdK------LVQttIRKEFsDCTILTIAH------RLqsiidSD 1250
Cdd:COG4148 132 ATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR-KaeilpyLER--LRDEL-DIPILYVSHsldevaRL-----AD 202
|
90 100
....*....|....*....|....*
gi 74136409 1251 RVLVLDSGSIVEFEAPQNLIRQKGL 1275
Cdd:COG4148 203 HVVLLEQGRVVASGPLAEVLSRPDL 227
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1071-1256 |
1.44e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.42 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1071 QTHGEEKIGIVGRTGAGKSTLSNCLFRIVEraggkiiidgidiSTIGLHDLRGKLNIIPQH-PVLFSGTLQMNLDPLN-K 1148
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLK-------------PDEGEVDPELKISYKPQYiKPDYDGTVEDLLRSITdD 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1149 YSDSKLWEalelchlkEFVQ--SLPEKLRHEISEggenLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTT 1226
Cdd:PRK13409 428 LGSSYYKS--------EIIKplQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKA 495
|
170 180 190
....*....|....*....|....*....|....
gi 74136409 1227 IRK--EFSDCTILTIAHRLQsIID--SDRVLVLD 1256
Cdd:PRK13409 496 IRRiaEEREATALVVDHDIY-MIDyiSDRLMVFE 528
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1065-1272 |
1.47e-05 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 48.93 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQTHGEEKIGIVGRTGAGKSTLsnclFRIVERAGGKIIIDGIDIST--IGLHDLRGKLNIIPQHPVLFSG-TLQM 1141
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTL----LRIIAGLEHQTSGHIRFHGTdvSRLHARDRKVGFVFQHYALFRHmTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1142 NLD-----------PLNKYSDSKLWEALELCHLKEFVQSLPEKLrheiseggenlSMGQRQLVCLARALLRKTKILILDE 1210
Cdd:PRK10851 94 NIAfgltvlprrerPNAAAIKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74136409 1211 ATASIDFETDKLVQTTIRK--EFSDCTILTIAHRLQSIID-SDRVLVLDSGSIVEFEAPQNLIRQ 1272
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQlhEELKFTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQVWRE 227
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1065-1242 |
1.56e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 49.36 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQTHGEEKIGIVGRTGAGKSTLsnclFRIVERAGGKIIIDGIDIStiglhdlRGKLNIIPQHPVLFSGTLQ---- 1140
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSL----FRILGELWPVYGGRLTKPA-------KGKLFYVPQRPYMTLGTLRdqii 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1141 --MNLDPLNK--YSDSKLWEALELCHLKEFVQSlpeklrheisEGG--------ENLSMGQRQLVCLARALLRKTKILIL 1208
Cdd:TIGR00954 537 ypDSSEDMKRrgLSDKDLEQILDNVQLTHILER----------EGGwsavqdwmDVLSGGEKQRIAMARLFYHKPQFAIL 606
|
170 180 190
....*....|....*....|....*....|....*.
gi 74136409 1209 DEATA--SIDFEtDKLVQTTIRKEFsdcTILTIAHR 1242
Cdd:TIGR00954 607 DECTSavSVDVE-GYMYRLCREFGI---TLFSVSHR 638
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
815-943 |
1.60e-05 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 48.22 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 815 LPIQFFETNSTGQIISRFTKDIFIIDMRLHYYLRLWVNCTLDVIGT--ILVII-GALPLFILGIIPsVFFYFSIqrYY-- 889
Cdd:cd18549 88 LSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSfiILLTInVPLTLIVFALLP-LMIIFTI--YFnk 164
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 890 --VASSRQIRRLTGAsrspVISHFSETLSGVSTIRAFG----HQQRFiqqykEVVNENLV 943
Cdd:cd18549 165 kmKKAFRRVREKIGE----INAQLEDSLSGIRVVKAFAneeyEIEKF-----DEGNDRFL 215
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1080-1264 |
1.67e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 47.65 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1080 IVGRTGAGKSTLSNCLFRIVERAggkiiidgidiSTIGLHDLrgKLNIIPQHPVLFSgtlqmNLDPLNKYSDSKlwEALE 1159
Cdd:COG2401 61 IVGASGSGKSTLLRLLAGALKGT-----------PVAGCVDV--PDNQFGREASLID-----AIGRKGDFKDAV--ELLN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1160 LCHLKEfVQSLPEKLRHeiseggenLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTIRKEFSDC--TIL 1237
Cdd:COG2401 121 AVGLSD-AVLWLRRFKE--------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAgiTLV 191
|
170 180
....*....|....*....|....*....
gi 74136409 1238 TIAHR--LQSIIDSDRVLVLDSGSIVEFE 1264
Cdd:COG2401 192 VATHHydVIDDLQPDLLIFVGYGGVPEEK 220
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
798-942 |
2.00e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 47.84 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 798 LAASRTMYVQLLNNV----LHLPIQFFETNSTGQIISRFT-----KDIFIIDMrlhyylrlwVNCTLDVIGTILVII--- 865
Cdd:cd18567 67 LYLSTSLNLQWTSNLfrhlLRLPLSYFEKRHLGDIVSRFGsldeiQQTLTTGF---------VEALLDGLMAILTLVmmf 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 866 ---GALPLFILGiipSVFFYFSIQryyVASSRQIRRLT------GASRSpviSHFSETLSGVSTIRAFGHQQ----RFIQ 932
Cdd:cd18567 138 lysPKLALIVLA---AVALYALLR---LALYPPLRRATeeqivaSAKEQ---SHFLETIRGIQTIKLFGREAereaRWLN 208
|
170
....*....|
gi 74136409 933 QYKEVVNENL 942
Cdd:cd18567 209 LLVDAINADI 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
446-643 |
2.02e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 47.40 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 446 GMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGS-VAYVSQQAWIQN---CIlQVNILFGS-- 519
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdISTLKPEIYRQQvsyCA-QTPTLFGDtv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 520 ----IMKKEFYEQVLEACALLPDLEQ--LPKgdqtEIGERGVN-ISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHvG 592
Cdd:PRK10247 98 ydnlIFPWQIRNQQPDPAIFLDDLERfaLPD----TILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDES-N 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 74136409 593 KQLFEKVIGSLGLLKNKTRILVTHNLTLLPQMDLIVVMESgriaQMGTYQE 643
Cdd:PRK10247 173 KHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQP----HAGEMQE 219
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
557-649 |
2.06e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 48.20 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 557 ISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGKQLFEKVIgSLGLLKNKTRILVTHNLTLLPQM-DLIVVMESGRI 635
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLL-ELQQKENMALVLITHDLALVAEAaHKIIVMYAGQV 232
|
90
....*....|....
gi 74136409 636 AQMGTYQELLSKTR 649
Cdd:PRK11022 233 VETGKAHDIFRAPR 246
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
759-942 |
2.13e-05 |
|
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: 48.01 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 759 NDFTEWKQIRSNKLNIYgILGLIkGLFVCSGAYVITRG---SLAASRTMY---VQLLNNVLHLPIQFFETNSTGQIISRF 832
Cdd:cd18780 28 NHSGSGGEEALRALNQA-VLILL-GVVLIGSIATFLRSwlfTLAGERVVArlrKRLFSAIIAQEIAFFDVTRTGELLNRL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 833 TKDIFIIDMRLHYYLRLWVNCTLDVIGTI---LVIIGALPLFILGIIPSVFFYFSIQRYYVassRQIRRLTGASRSPVIS 909
Cdd:cd18780 106 SSDTQVLQNAVTVNLSMLLRYLVQIIGGLvfmFTTSWKLTLVMLSVVPPLSIGAVIYGKYV---RKLSKKFQDALAAAST 182
|
170 180 190
....*....|....*....|....*....|...
gi 74136409 910 HFSETLSGVSTIRAFGHQQRFIQQYKEVVNENL 942
Cdd:cd18780 183 VAEESISNIRTVRSFAKETKEVSRYSEKINESY 215
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1184-1261 |
2.19e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 48.16 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1184 NLSMGQRQLVCLARALLRKTKILILDEATASIDFetdkLVQTTIRkEF-------SDCTILTIAHRLQSIID-SDRVLVL 1255
Cdd:COG4586 154 QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDV----VSKEAIR-EFlkeynreRGTTILLTSHDMDDIEAlCDRVIVI 228
|
....*.
gi 74136409 1256 DSGSIV 1261
Cdd:COG4586 229 DHGRII 234
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
446-588 |
2.28e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 47.20 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 446 GMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVV---------------QRKGsVAYVSQQAwiqnci 510
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllplharARRG-IGYLPQEA------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 511 lqvnilfgSIMKK-EFYEQVLEACALLPDLEQLPKGDQT-EIGER----------GVNISGGQQHRVSLARAVYSGADIY 578
Cdd:PRK10895 88 --------SIFRRlSVYDNLMAVLQIRDDLSAEQREDRAnELMEEfhiehlrdsmGQSLSGGERRRVEIARALAANPKFI 159
|
170
....*....|
gi 74136409 579 LLDDPLSAVD 588
Cdd:PRK10895 160 LLDEPFAGVD 169
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1065-1256 |
2.90e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 47.03 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVerAGGKIIIDGIDISTIGLhdLRGKLNIIPQHPVLFSGTlqMNLD 1144
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLV--APDEGVIKRNGKLRIGY--VPQKLYLDTTLPLTVNRF--LRLR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1145 PLNKYSDskLWEALELCHLKEFVQSLPEKLrheisEGGENlsmgqrQLVCLARALLRKTKILILDEATASIDFET----- 1219
Cdd:PRK09544 94 PGTKKED--ILPALKRVQAGHLIDAPMQKL-----SGGET------QRVLLARALLNRPQLLVLDEPTQGVDVNGqvaly 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 74136409 1220 DKLVQttIRKEFsDCTILTIAHRLQSII-DSDRVLVLD 1256
Cdd:PRK09544 161 DLIDQ--LRREL-DCAVLMVSHDLHLVMaKTDEVLCLN 195
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
447-644 |
3.44e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.31 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 447 MPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQ--------RKGSVAYVSQQ-------------AW 505
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmllrrRSRQVIELSEQsaaqmrhvrgadmAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 506 I-QNCILQVNILFG-------SI-----MKKEfyEQVLEACALLpDLEQLPKGdQTEIGERGVNISGGQQHRVSLARAVY 572
Cdd:PRK10261 109 IfQEPMTSLNPVFTvgeqiaeSIrlhqgASRE--EAMVEAKRML-DQVRIPEA-QTILSRYPHQLSGGMRQRVMIAMALS 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 573 SGADIYLLDDPLSAVDVHVGKQLFE--KVIG---SLGLlknktrILVTHNLTLLPQM-DLIVVMESGRIAQMGTYQEL 644
Cdd:PRK10261 185 CRPAVLIADEPTTALDVTIQAQILQliKVLQkemSMGV------IFITHDMGVVAEIaDRVLVMYQGEAVETGSVEQI 256
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1065-1283 |
3.55e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 48.18 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDL----RGKLNIIPQHPVLFSG-TL 1139
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLSHlTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1140 QMNLDPLNKYSDSKLWEALELCHlkEFVQSLpeKLRHEISEGGENLSMGQRQLVCLARALLRKTKILILDEATASIDFET 1219
Cdd:PRK10535 104 AQNVEVPAVYAGLERKQRLLRAQ--ELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHS 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74136409 1220 DKLVQtTIRKEFSD--CTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQNLIRQKGLFYEMTTDA 1283
Cdd:PRK10535 180 GEEVM-AILHQLRDrgHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVNVAGGTEPVVNTA 244
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1073-1256 |
3.57e-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: 48.24 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1073 HGEEKIGIVGRTGAGKSTLSNCLFRIVEraggkiiidgidiSTIGLHDLRGKLNIIPQHPV-LFSGTLQMNLDPLNK--Y 1149
Cdd:COG1245 364 REGEVLGIVGPNGIGKTTFAKILAGVLK-------------PDEGEVDEDLKISYKPQYISpDYDGTVEEFLRSANTddF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1150 SDSKLWEalelchlkEFVQSLP-EKLRH-EISEggenLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTI 1227
Cdd:COG1245 431 GSSYYKT--------EIIKPLGlEKLLDkNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 498
|
170 180 190
....*....|....*....|....*....|...
gi 74136409 1228 RK--EFSDCTILTIAHRLQsIID--SDRVLVLD 1256
Cdd:COG1245 499 RRfaENRGKTAMVVDHDIY-LIDyiSDRLMVFE 530
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
807-943 |
3.98e-05 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 47.03 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 807 QLLNNVLHLPIQFFETNSTGQIISRFTKDI-FIIDMRLHYYLRLWVNCT--LDVIGTILVIIGALPLFILGIIPsvfFYF 883
Cdd:cd18554 84 DLFDHLQKLSLRYYANNRSGEIISRVINDVeQTKDFITTGLMNIWLDMItiIIAICIMLVLNPKLTFVSLVIFP---FYI 160
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 884 SIQRYYVASSRQIRRLTGASRSPVISHFSETLSGVSTIRAFGHQQRFIQQYKEVVNENLV 943
Cdd:cd18554 161 LAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLT 220
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
450-628 |
4.17e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 46.84 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 450 LKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGE--MEKLTGVVQRKGSVAYVSQQAWIQNCIlQVN------------- 514
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPalARRLHLKKEQPGNHDRIEGLEHIDKVI-VIDqspigrtprsnpa 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 515 ----------ILFGSIMK-KEFYEQVL------------------EACALLPDLEQLPKGDQT---------EIGERGVN 556
Cdd:cd03271 90 tytgvfdeirELFCEVCKgKRYNRETLevrykgksiadvldmtveEALEFFENIPKIARKLQTlcdvglgyiKLGQPATT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74136409 557 ISGGQQHRVSLARAVY---SGADIYLLDDPLSAVDVHVGKQLFEkVIGSLGLLKNkTRILVTHNLTLLPQMDLIV 628
Cdd:cd03271 170 LSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLE-VLQRLVDKGN-TVVVIEHNLDVIKCADWII 242
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
456-627 |
4.24e-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: 47.86 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 456 KIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSVAYVSQqaWIQNCI-LQVNILFGSIMKKE-----FYEQV 529
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQ--YISPDYdGTVEEFLRSANTDDfgssyYKTEI 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 530 LEACALLPDLEQLPKgdqteigergvNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDV----HVGkqlfeKVIGSLGL 605
Cdd:COG1245 440 IKPLGLEKLLDKNVK-----------DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVA-----KAIRRFAE 503
|
170 180
....*....|....*....|..
gi 74136409 606 LKNKTRILVTHNLTLlpqMDLI 627
Cdd:COG1245 504 NRGKTAMVVDHDIYL---IDYI 522
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1185-1216 |
4.39e-05 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 47.53 E-value: 4.39e-05
10 20 30
....*....|....*....|....*....|..
gi 74136409 1185 LSMGQRQLVCLARALLRKTKILILDEATASID 1216
Cdd:PRK09536 140 LSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
446-603 |
4.50e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.69 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 446 GMPVLKDLNIKIPEGALVAVVGQVGSGKSSMlsailgeMEKLTGVVQR-KGSVAYV-----------SQQAWIQ------ 507
Cdd:PRK10762 16 GVKALSGAALNVYPGRVMALVGENGAGKSTM-------MKVLTGIYTRdAGSILYLgkevtfngpksSQEAGIGiihqel 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 508 NCILQV----NIL--------FGSIMKKEFYEqvlEACALLPDLeQLPKGDQTEIGErgvnISGGQQHRVSLARAVYSGA 575
Cdd:PRK10762 89 NLIPQLtiaeNIFlgrefvnrFGRIDWKKMYA---EADKLLARL-NLRFSSDKLVGE----LSIGEQQMVEIAKVLSFES 160
|
170 180
....*....|....*....|....*...
gi 74136409 576 DIYLLDDPLSAVDVHVGKQLFeKVIGSL 603
Cdd:PRK10762 161 KVIIMDEPTDALTDTETESLF-RVIREL 187
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
448-635 |
5.14e-05 |
|
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: 46.17 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 448 PVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSVAYVSQQAWIQncilQVNILFGSIMKKEFYE 527
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLR----RIGVVFGQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 528 QVLEACALLPDLEQLPKG----------DQTEIGE------RgvNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVhV 591
Cdd:cd03267 111 PVIDSFYLLAAIYDLPPArfkkrldelsELLDLEElldtpvR--QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV-V 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 74136409 592 GKQLFEKVIGSLGLLKNKTRILVTHNLTLLPQM-DLIVVMESGRI 635
Cdd:cd03267 188 AQENIRNFLKEYNRERGTTVLLTSHYMKDIEALaRRVLVIDKGRL 232
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
777-957 |
5.17e-05 |
|
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: 46.62 E-value: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 777 ILGLIKGLFVCSGAYVITRGSLAASRTMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDMRLHYYLRLWVNCTLD 856
Cdd:cd18548 47 LLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 857 VIGTI-----------LVIIGALPLFILGIIpsVFFYFSIqRYYVASSRQIRRLTGASRspvishfsETLSGVSTIRAFG 925
Cdd:cd18548 127 LIGAIimafrinpklaLILLVAIPILALVVF--LIMKKAI-PLFKKVQKKLDRLNRVVR--------ENLTGIRVIRAFN 195
|
170 180 190
....*....|....*....|....*....|..
gi 74136409 926 HQQRFIQQYKEvVNENLvcFYNNVISNRWLSV 957
Cdd:cd18548 196 REDYEEERFDK-ANDDL--TDTSLKAGRLMAL 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1064-1268 |
5.32e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.54 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDG-------------IDISTIGLHDLRG-KLNIIP 1129
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvielSEQSAAQMRHVRGaDMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1130 QHPVlfsgtlqMNLDPL---------------NKYSDSKLWEA---LELCHLKEfVQSLPEKLRHEiseggenLSMGQRQ 1191
Cdd:PRK10261 111 QEPM-------TSLNPVftvgeqiaesirlhqGASREEAMVEAkrmLDQVRIPE-AQTILSRYPHQ-------LSGGMRQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1192 LVCLARALLRKTKILILDEATASIDFETDKLVQTTIR---KEFSDCTILtIAHRLQSIID-SDRVLVLDSGSIVE----- 1262
Cdd:PRK10261 176 RVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlqKEMSMGVIF-ITHDMGVVAEiADRVLVMYQGEAVEtgsve 254
|
....*...
gi 74136409 1263 --FEAPQN 1268
Cdd:PRK10261 255 qiFHAPQH 262
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
457-627 |
5.52e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.50 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 457 IPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSVAY------VSQQAWIQNCILQVNILFGSIMkkeFYEQVL 530
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYkpqyikPDYDGTVEDLLRSITDDLGSSY---YKSEII 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 531 EACALlpdleqlpkgdqTEIGERGVN-ISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVhvgkqlfE------KVIGSL 603
Cdd:PRK13409 439 KPLQL------------ERLLDKNVKdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV-------EqrlavaKAIRRI 499
|
170 180
....*....|....*....|....
gi 74136409 604 GLLKNKTRILVTHNLTLlpqMDLI 627
Cdd:PRK13409 500 AEEREATALVVDHDIYM---IDYI 520
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
118-312 |
5.97e-05 |
|
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: 46.65 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 118 LIQVALFKVFADILSFTSPLIMKQMI--IFCEHSSDFGWngyGYAMALFVVVFLQ--TLILQRYqcFNMLTSAKVKTAVN 193
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLddIFVEKDLEALL---LVPLAIIGLFLLRglASYLQTY--LMAYVGQRVVRDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 194 GLIYKKALLLSnVSR-QKFSTGEIINLMSADAQQLMD-LTANLNLLWSAPFQIL----MAIYLLWQelgpavLAGVAVLV 267
Cdd:cd18552 76 NDLFDKLLRLP-LSFfDRNSSGDLISRITNDVNQVQNaLTSALTVLVRDPLTVIgllgVLFYLDWK------LTLIALVV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 74136409 268 FviPINALAATKI-KKLKKSQRKNKDKQ---IKLLKEILHGIKILKLYA 312
Cdd:cd18552 149 L--PLAALPIRRIgKRLRKISRRSQESMgdlTSVLQETLSGIRVVKAFG 195
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1185-1263 |
6.41e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.79 E-value: 6.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1185 LSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQT---TIRKEFsDCTILTIAHRLQSIID-SDRVLVLDSGSI 1260
Cdd:PRK11144 129 LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPyleRLAREI-NIPILYVSHSLDEILRlADRVVVLEQGKV 207
|
...
gi 74136409 1261 VEF 1263
Cdd:PRK11144 208 KAF 210
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
452-643 |
7.24e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.41 E-value: 7.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 452 DLNIKIPEGALVAVVGQVGSGKSSMLSAILG-----------------EMEKLTGVVQRKGSVAYVSQQAWI-QNCILQV 513
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGltrpqkgrivlngrvlfDAEKGICLPPEKRRIGYVFQDARLfPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 514 NILFGsiMKKEFYEQVLEACALL---PDLEQLPkgdqteigergVNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVH 590
Cdd:PRK11144 96 NLRYG--MAKSMVAQFDKIVALLgiePLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 591 VGKQL---FEKVIGSLgllknKTRIL-VTHNL-TLLPQMDLIVVMESGRIAQMGTYQE 643
Cdd:PRK11144 163 RKRELlpyLERLAREI-----NIPILyVSHSLdEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
449-639 |
7.26e-05 |
|
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: 45.26 E-value: 7.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 449 VLKDLNIKIPEGaLVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGS------------VAYVSQQ------------- 503
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrrIGYLPQEfgvypnftvrefl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 504 ---AWIQNcilqvnilfgsIMKKEFYEQVLEACALLpDLEQLPKgdqTEIGErgvnISGGQQHRVSLARAVYSGADIYLL 580
Cdd:cd03264 94 dyiAWLKG-----------IPSKEVKARVDEVLELV-NLGDRAK---KKIGS----LSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 581 DDPLSAVDVhVGKQLFEKVIGSLGllKNKTRILVTHNLTLLPQM-DLIVVMESGRIAQMG 639
Cdd:cd03264 155 DEPTAGLDP-EERIRFRNLLSELG--EDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1185-1275 |
8.10e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.01 E-value: 8.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1185 LSMGQRQLVCLARALLRKTKILILDEATASIDFEtdklVQTTI-------RKEFsDCTILTIAHRLqSIID--SDRVLVL 1255
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVS----VQAQIlqllrelQQEL-NMGLLFITHNL-SIVRklADRVAVM 230
|
90 100
....*....|....*....|....*..
gi 74136409 1256 DSGSIVE-------FEAPQNLIRQKGL 1275
Cdd:PRK15134 231 QNGRCVEqnraatlFSAPTHPYTQKLL 257
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1185-1267 |
8.19e-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: 46.99 E-value: 8.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1185 LSMGQRQLVCLARALLRKTKILILDEATASIDfetdklvqTTIRKEfsdctILTIAHRLQ-----SII----D------- 1248
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALD--------VTVQAQ-----ILDLLKDLQrelgmALLlithDlgvvrrf 223
|
90 100
....*....|....*....|....*.
gi 74136409 1249 SDRVLVLDSGSIVE-------FEAPQ 1267
Cdd:COG4172 224 ADRVAVMRQGEIVEqgptaelFAAPQ 249
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1163-1263 |
9.54e-05 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 44.94 E-value: 9.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1163 LKEFVQSLPEKLR--HEISEGGENLSMGQRQLVCLARALLRKTKILILDEATASIdfetDKLVQTTIRKEFS------DC 1234
Cdd:cd03301 107 IDERVREVAELLQieHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNL----DAKLRVQMRAELKrlqqrlGT 182
|
90 100 110
....*....|....*....|....*....|
gi 74136409 1235 TILTIAH-RLQSIIDSDRVLVLDSGSIVEF 1263
Cdd:cd03301 183 TTIYVTHdQVEAMTMADRIAVMNDGQIQQI 212
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
452-644 |
1.03e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 45.87 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 452 DLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKlTGVVqrKGSVAYVSQQawiqncIL-------------QVNILFG 518
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAA-NGRI--GGSATFNGRE------ILnlpekelnklraeQISMIFQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 519 SIMKK-EFYEQVLEAcalLPDLEQLPKG-DQTEIGERGVNI--------------------SGGQQHRVSLARAVYSGAD 576
Cdd:PRK09473 105 DPMTSlNPYMRVGEQ---LMEVLMLHKGmSKAEAFEESVRMldavkmpearkrmkmyphefSGGMRQRVMIAMALLCRPK 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74136409 577 IYLLDDPLSAVDVHVGKQLFEkvigSLGLLK---NKTRILVTHNLTLLPQM-DLIVVMESGRIAQMGTYQEL 644
Cdd:PRK09473 182 LLIADEPTTALDVTVQAQIMT----LLNELKrefNTAIIMITHDLGVVAGIcDKVLVMYAGRTMEYGNARDV 249
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1185-1260 |
1.04e-04 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 45.44 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1185 LSMGQRQLVCLARALLRKTKILILDEATASID----FETDKLVQTTIRKE-FsdcTILTIAHRL-QSIIDSDRVLVLDSG 1258
Cdd:PRK11247 134 LSGGQKQRVALARALIHRPGLLLLDEPLGALDaltrIEMQDLIESLWQQHgF---TVLLVTHDVsEAVAMADRVLLIEEG 210
|
..
gi 74136409 1259 SI 1260
Cdd:PRK11247 211 KI 212
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
460-639 |
1.15e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 45.30 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 460 GALVAVVGQVGSGKSSMLSAILGEMEKLTGVV---QRKGSV-------------------AYVSQQAwIQNCILQV---- 513
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrMRDGQLrdlyalseaerrrllrtewGFVHQHP-RDGLRMQVsagg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 514 NI---LFGSIMKKefYEQVLE-ACALLPDLEQlpkgDQTEIGERGVNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDV 589
Cdd:PRK11701 111 NIgerLMAVGARH--YGDIRAtAGDWLERVEI----DAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 74136409 590 HVGKQLfekvigsLGLLKNKTR------ILVTHNLT---LLPqmDLIVVMESGRIAQMG 639
Cdd:PRK11701 185 SVQARL-------LDLLRGLVRelglavVIVTHDLAvarLLA--HRLLVMKQGRVVESG 234
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1184-1265 |
1.22e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 46.16 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1184 NLSMGQRQLVCLARALLRKTKILILDEATASID----FEtdklVQTTIRkEFSD--CTILTIAHRLQSIID-SDRVLVLD 1256
Cdd:COG1129 394 NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgakAE----IYRLIR-ELAAegKAVIVISSELPELLGlSDRILVMR 468
|
90
....*....|
gi 74136409 1257 SGSIV-EFEA 1265
Cdd:COG1129 469 EGRIVgELDR 478
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
447-621 |
1.42e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.89 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 447 MPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAI----LGEMEKLT--GVVQRKGSVAYVSqqawiqncilqvnilfgsi 520
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIglalGGAQSATRrrSGVKAGCIVAAVS------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 521 mkkefyeqvLEACALLPDLeqlpkgdqteigergvniSGGQQHRVSLARAV----YSGADIYLLDDPLSAVDVHVGKQLF 596
Cdd:cd03227 69 ---------AELIFTRLQL------------------SGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALA 121
|
170 180
....*....|....*....|....*
gi 74136409 597 EKVIGSlgLLKNKTRILVTHNLTLL 621
Cdd:cd03227 122 EAILEH--LVKGAQVIVITHLPELA 144
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1067-1260 |
1.49e-04 |
|
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: 46.55 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1067 DITFqtHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTiGLHDLRGKLNIIPQHPVLFSGTLQMNLDPL 1146
Cdd:TIGR01257 950 NITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHLTVAEHILF 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1147 NKYSDSKLWEALELchlkEFVQSLPEK-LRHEISEGGENLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQT 1225
Cdd:TIGR01257 1027 YAQLKGRSWEEAQL----EMEAMLEDTgLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
|
170 180 190
....*....|....*....|....*....|....*.
gi 74136409 1226 TIRKEFSDCTILTIAHRL-QSIIDSDRVLVLDSGSI 1260
Cdd:TIGR01257 1103 LLLKYRSGRTIIMSTHHMdEADLLGDRIAIISQGRL 1138
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
401-589 |
1.58e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.88 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 401 QTKiSLGRLEDFlhtEELLPQN----IETNYI--------GDHAIEFTDATYSWnktGMPVL-KDLNIKIPEGALVAVVG 467
Cdd:PRK11819 285 QAK-SKARLARY---EELLSEEyqkrNETNEIfippgprlGDKVIEAENLSKSF---GDRLLiDDLSFSLPPGGIVGIIG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 468 QVGSGKSSMLSAILGEMEKLTGVVqRKGS---VAYVSQQ-AWIQNcilqvnilfgsimKKEFYEQVLEacallpdleqlp 543
Cdd:PRK11819 358 PNGAGKSTLFKMITGQEQPDSGTI-KIGEtvkLAYVDQSrDALDP-------------NKTVWEEISG------------ 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 544 kG-DQTEIGERGVN---------------------ISGGQQHRVSLARAVYSGADIYLLDDPLSAVDV 589
Cdd:PRK11819 412 -GlDIIKVGNREIPsrayvgrfnfkggdqqkkvgvLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1048-1271 |
1.60e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 45.01 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1048 VEFInYQARYRDElGLALQDI--TFQTHGeeKIGIVGRTGAGKSTLS---NCLFRIVERAGgkiiidgidisTIG----- 1117
Cdd:PRK13634 8 VEHR-YQYKTPFE-RRALYDVnvSIPSGS--YVAIIGHTGSGKSTLLqhlNGLLQPTSGTV-----------TIGervit 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1118 -------LHDLRGKLNIIPQHP--VLFSGTLQMNL--DPLNkYSDSKLwEALELChlKEFVQ--SLPEKLRHeisEGGEN 1184
Cdd:PRK13634 73 agkknkkLKPLRKKVGIVFQFPehQLFEETVEKDIcfGPMN-FGVSEE-DAKQKA--REMIElvGLPEELLA---RSPFE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1185 LSMGQRQLVCLARALLRKTKILILDEATASID----------FEtdklvqtTIRKEfSDCTILTIAHRLQSIID-SDRVL 1253
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDpkgrkemmemFY-------KLHKE-KGLTTVLVTHSMEDAARyADQIV 217
|
250
....*....|....*...
gi 74136409 1254 VLDSGSIVEFEAPQNLIR 1271
Cdd:PRK13634 218 VMHKGTVFLQGTPREIFA 235
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1065-1272 |
1.66e-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: 44.05 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCL-----FRIVERAGGKIIIDGIDISTiglhDLRGKLNII--PQHPVLFSG 1137
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTImghpkYEVTEGEILFKGEDITDLPP----EERARLGIFlaFQYPPEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1138 TlqmnldplnkysdsklwealelcHLKEFVQSLpeklrheisegGENLSMGQRQLVCLARALLRKTKILILDEATASIDF 1217
Cdd:cd03217 92 V-----------------------KNADFLRYV-----------NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 1218 ETDKLVQTTIRKEFS-DCTILTIAH--RLQSIIDSDRVLVLDSGSIVEfEAPQNLIRQ 1272
Cdd:cd03217 138 DALRLVAEVINKLREeGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVK-SGDKELALE 194
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
777-936 |
1.73e-04 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 44.99 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 777 ILGLIK-GLFVCSGayviTRG---SLAASRtMYVQLLN----NVLHLPIQFFETNSTGQIISRFTKDIFI----IDMRLH 844
Cdd:cd18784 41 IMGLLAiASSVAAG----IRGglfTLAMAR-LNIRIRNllfrSIVSQEIGFFDTVKTGDITSRLTSDTTTmsdtVSLNLN 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 845 YYLRLWVNctldVIGTILVIIG---ALPLFILGIIPSVFFYFSIQ-RYYVASSRQIR-RLTGASrspviSHFSETLSGVS 919
Cdd:cd18784 116 IFLRSLVK----AIGVIVFMFKlswQLSLVTLIGLPLIAIVSKVYgDYYKKLSKAVQdSLAKAN-----EVAEETISSIR 186
|
170
....*....|....*..
gi 74136409 920 TIRAFGHQQRFIQQYKE 936
Cdd:cd18784 187 TVRSFANEDGEANRYSE 203
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1184-1269 |
1.78e-04 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 44.71 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1184 NLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTIRK--EFSDCTILTIAHRLqSIID--SDRVLVLDSGS 1259
Cdd:cd03237 115 ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRfaENNEKTAFVVEHDI-IMIDylADRLIVFEGEP 193
|
90
....*....|..
gi 74136409 1260 IVEFEA--PQNL 1269
Cdd:cd03237 194 SVNGVAnpPQSL 205
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
448-645 |
1.80e-04 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 44.46 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 448 PVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAIlgemeklTGVVQ----------------------RKGsVAYVSQQAW 505
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMI-------VGLVKpdsgkilldgqditklpmhkraRLG-IGYLPQEAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 506 I-------QN--CILQvnilfgsIMKKEFYEQVLEACALLPDLEQLPKGDQteigeRGVNISGGQQHRVSLARAVYSGAD 576
Cdd:cd03218 86 IfrkltveENilAVLE-------IRGLSKKEREEKLEELLEEFHITHLRKS-----KASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 577 IYLLDDPLSAVD-VHVG------KQLFEKVIGslgllknktrILVT-HNL-TLLPQMDLIVVMESGRIAQMGTYQELL 645
Cdd:cd03218 154 FLLLDEPFAGVDpIAVQdiqkiiKILKDRGIG----------VLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1184-1262 |
1.86e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.55 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1184 NLSMGQRQLVCLARALLRKTKILILDEATASI-DFETDKLVQttIRKEFSD--CTILTIAHRLQSIID-SDRVLVLDSGS 1259
Cdd:NF040905 139 DIGVGKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLD--LLLELKAqgITSIIISHKLNEIRRvADSITVLRDGR 216
|
...
gi 74136409 1260 IVE 1262
Cdd:NF040905 217 TIE 219
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1063-1258 |
2.04e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 44.60 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1063 LALQDITFQTHGEEKIGIVGRTGAGKSTLSNCL--F------RIVERAGGKIIIDGIDISTIGLhdLRGKLNI------- 1127
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLtgFykptggTILLRGQHIEGLPGHQIARMGV--VRTFQHVrlfremt 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1128 ------IPQH----PVLFSGTLQMnldPLNKYSDSklwEALELC-HLKEFVQSLPEKLRheisEGGeNLSMGQRQLVCLA 1196
Cdd:PRK11300 97 vienllVAQHqqlkTGLFSGLLKT---PAFRRAES---EALDRAaTWLERVGLLEHANR----QAG-NLAYGQQRRLEIA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74136409 1197 RALLRKTKILILDEATASID-FETDKLVQ--TTIRKEFsDCTILTIAHRLQSIID-SDRVLVLDSG 1258
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNpKETKELDEliAELRNEH-NVTVLLIEHDMKLVMGiSDRIYVVNQG 230
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
555-631 |
2.07e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 43.71 E-value: 2.07e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 555 VNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHvGKQLFEKVIGSLGLLKNKTRILVTHNLTLLPQM-DLIVVME 631
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIE-QRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLsDRIHVFE 146
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1058-1228 |
2.08e-04 |
|
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: 43.89 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1058 RDELGLaLQDITFQTHGEEKIGIVGRTGAGKSTLsnclFRIVEraggkiiidgidistiGLhdlrgklniipQHPVlfSG 1137
Cdd:TIGR01189 10 RGERML-FEGLSFTLNAGEALQVTGPNGIGKTTL----LRILA----------------GL-----------LRPD--SG 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1138 TLQMNLDPLNKYSDSKLWEALELCHLKEFVQSLP--EKLR--HEISEGGEN---------------------LSMGQRQL 1192
Cdd:TIGR01189 56 EVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSalENLHfwAAIHGGAQRtiedalaavgltgfedlpaaqLSAGQQRR 135
|
170 180 190
....*....|....*....|....*....|....*.
gi 74136409 1193 VCLARALLRKTKILILDEATASIDFETDKLVQTTIR 1228
Cdd:TIGR01189 136 LALARLWLSRRPLWILDEPTTALDKAGVALLAGLLR 171
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
785-936 |
2.12e-04 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 44.77 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 785 FVCSGAYVITRGSLaaSRTMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDifIIDMR----------LHYYLR------ 848
Cdd:cd18589 54 FVCDLIYNITMSRI--HSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTD--TEDMSeslsenlsllMWYLARglflfi 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 849 --LWVNCTLdvigTILVIIGaLPLFILgiIPSVffyfsIQRYYVASSRQIRR-LTGASRSPVishfsETLSGVSTIRAFG 925
Cdd:cd18589 130 fmLWLSPKL----ALLTALG-LPLLLL--VPKF-----VGKFQQSLAVQVQKsLARANQVAV-----ETFSAMKTVRSFA 192
|
170
....*....|.
gi 74136409 926 HQQRFIQQYKE 936
Cdd:cd18589 193 NEEGEAQRYRQ 203
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
558-683 |
2.13e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.62 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 558 SGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGKQLfekvigSLGLLK-NKTRILVTHNLTLLPQM--DLIVVMESGR 634
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWL------ETYLLKwPKTFIVVSHAREFLNTVvtDILHLHGQKL 419
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74136409 635 IAQMGTYqELLSKTR--NLTNLHQVISEEEKAHA------------LKRASAVNSRTRPKDKI 683
Cdd:PLN03073 420 VTYKGDY-DTFERTReeQLKNQQKAFESNERSRShmqafidkfrynAKRASLVQSRIKALDRL 481
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1047-1273 |
2.20e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 44.68 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1047 VVEFINYQARYRDELgLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVE--RAGGKIIIDGIDISTIGLHDLRGK 1124
Cdd:PRK13639 1 ILETRDLKYSYPDGT-EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKptSGEVLIKGEPIKYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1125 LNIIPQHP--VLFSGTLQMNL--DPLNkysdsklweaLELCHlKEFVQSLPEKLRHEISEGGEN-----LSMGQRQLVCL 1195
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVafGPLN----------LGLSK-EEVEKRVKEALKAVGMEGFENkpphhLSGGQKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1196 ARALLRKTKILILDEATASIdfetDKLVQTTIRKEFSD-----CTILTIAHRLQSI-IDSDRVLVLDSGSIVEFEAPQNL 1269
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGL----DPMGASQIMKLLYDlnkegITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
....
gi 74136409 1270 IRQK 1273
Cdd:PRK13639 225 FSDI 228
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1080-1282 |
2.42e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 44.61 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1080 IVGRTGAGKST---LSNCLfrIVERAGGKIIIDGIDISTIG----LHDLRGKLNIIPQHP--VLFSGTLQMNL--DPLNK 1148
Cdd:PRK13645 42 VIGTTGSGKSTmiqLTNGL--IISETGQTIVGDYAIPANLKkikeVKRLRKEIGLVFQFPeyQLFQETIEKDIafGPVNL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1149 YSDS-----KLWEALELCHL-KEFVQSLPEKLrheiseggenlSMGQRQLVCLARALLRKTKILILDEATASID--FETD 1220
Cdd:PRK13645 120 GENKqeaykKVPELLKLVQLpEDYVKRSPFEL-----------SGGQKRRVALAGIIAMDGNTLVLDEPTGGLDpkGEED 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74136409 1221 KL-VQTTIRKEFSDcTILTIAHRLQSIID-SDRVLVLDSGSIVEFEAPQNLIRQKGLFYEMTTD 1282
Cdd:PRK13645 189 FInLFERLNKEYKK-RIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEIFSNQELLTKIEID 251
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1066-1262 |
2.65e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.16 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1066 QDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGgkiiidgidistiGLHDLRGKlNIIPQHPV------------ 1133
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAG-------------GEIRLNGK-DISPRSPLdavkkgmayite 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1134 ------LFSG-TLQMNLDPLNKYSDSKLWEALELCHLKEfVQSLPEKLR-------HEISEGGENLSMGQRQLVCLARAL 1199
Cdd:PRK09700 346 srrdngFFPNfSIAQNMAISRSLKDGGYKGAMGLFHEVD-EQRTAENQRellalkcHSVNQNITELSGGNQQKVLISKWL 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74136409 1200 LRKTKILILDEATASIDFETDKLVQTTIRKEFSDC-TILTIAHRLQSIID-SDRVLVLDSGSIVE 1262
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGkVILMVSSELPEIITvCDRIAVFCEGRLTQ 489
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
777-940 |
3.09e-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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 44.40 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 777 ILGLIkGLFVCSGAYVITRGSLAAS---RTMY---VQLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDMRlhyylrlw 850
Cdd:cd18550 42 ALGMV-AVAVASALLGVVQTYLSARigqGVMYdlrVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSV-------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 851 VNCTL-DVIGTILVIIGA----------LPLFILGIIPsvFFYFSIQRYyvasSRQIRRLTGAS---RSPVISHFSETLS 916
Cdd:cd18550 113 VTGTLtSVVSNVVTLVATlvamlaldwrLALLSLVLLP--LFVLPTRRV----GRRRRKLTREQqekLAELNSIMQETLS 186
|
170 180
....*....|....*....|....*.
gi 74136409 917 --GVSTIRAFGHQQRFIQQYKEVVNE 940
Cdd:cd18550 187 vsGALLVKLFGREDDEAARFARRSRE 212
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
450-619 |
3.50e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.88 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 450 LKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSVAYVSQQAWIQNCILQV-NILFGSIMKKEFYEQ 528
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGIeNIELKGLMMGLTKEK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 529 VLEACALLPDLEQLPKGdqteIGERGVNISGGQQHRVSLARAVYSGADIYLLDDPLSavdvhVGKQLF-EKVIGSLGLLK 607
Cdd:PRK13545 120 IKEIIPEIIEFADIGKF----IYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALS-----VGDQTFtKKCLDKMNEFK 190
|
170
....*....|....
gi 74136409 608 N--KTRILVTHNLT 619
Cdd:PRK13545 191 EqgKTIFFISHSLS 204
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
801-940 |
3.65e-04 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 44.07 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 801 SRTMYVQLLNNVLHLPIQFFETNSTGQIISRFTKDI--------FIIDMRLHyylrlwvNCTLDV--IGTILVIIGALPL 870
Cdd:cd18574 74 AARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVqefkssfkQCVSQGLR-------SVTQTVgcVVSLYLISPKLTL 146
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 871 FILGIIPSVFFYFSIqryYVASSRQIRRLTGASRSPVISHFSETLSGVSTIRAFGHQQRFIQQYKEVVNE 940
Cdd:cd18574 147 LLLVIVPVVVLVGTL---YGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEK 213
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
556-630 |
4.07e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.80 E-value: 4.07e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 556 NISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVhvgKQLFE--KVIGSLGllKNKTRILVTHNLTLLPQM-DLIVVM 630
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI---RQRLNvaRLIRELA--EGKYVLVVEHDLAVLDYLaDNVHIA 284
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
450-655 |
4.17e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 43.62 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 450 LKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQ------RKGSVAYVSQQ------------------AW 505
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLiddhplHFGDYSYRSQRirmifqdpstslnprqriSQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 506 IQNCILQVNILFGSIMKKEFYEQVLEACALLPD-LEQLPKGdqteigergvnISGGQQHRVSLARAVYSGADIYLLDDPL 584
Cdd:PRK15112 109 ILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDhASYYPHM-----------LAPGQKQRLGLARALILRPKVIIADEAL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 585 SAVDVHVGKQLfekvIGSLGLLKNK---TRILVTHNLTLLPQM-DLIVVMESGRIAQMGTYQELLSK-----TRNLTNLH 655
Cdd:PRK15112 178 ASLDMSMRSQL----INLMLELQEKqgiSYIYVTQHLGMMKHIsDQVLVMHQGEVVERGSTADVLASplhelTKRLIAGH 253
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
449-646 |
4.74e-04 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 43.33 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 449 VLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSVAYVSQQAWI---------------QNCILQV 513
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKImreavaivpegrrvfSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 514 NILFGSIM--KKEFYEQVLEACALLPDLeqlpkgdQTEIGERGVNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHV 591
Cdd:PRK11614 100 NLAMGGFFaeRDQFQERIKWVYELFPRL-------HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 592 GKQLFEKV--IGSLGLlknkTRILVTHNLT-LLPQMDLIVVMESGRIAQMGTYQELLS 646
Cdd:PRK11614 173 IQQIFDTIeqLREQGM----TIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1064-1273 |
6.31e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 43.23 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLS---NCLFRiveraggkiiidgIDISTIGLHDL--------------RGKLN 1126
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIqniNALLK-------------PTTGTVTVDDItithktkdkyirpvRKRIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1127 IIPQHP--VLFSGTLQ-----------MNLDPLNKYSDSKLweaLELCHLKEFVQSLPEKlrheiseggenLSMGQRQLV 1193
Cdd:PRK13646 89 MVFQFPesQLFEDTVEreiifgpknfkMNLDEVKNYAHRLL---MDLGFSRDVMSQSPFQ-----------MSGGQMRKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1194 CLARALLRKTKILILDEATASIDFETDKLVQTTIRK--EFSDCTILTIAHRLQSIID-SDRVLVLDSGSIVEFEAPQNLI 1270
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELF 234
|
...
gi 74136409 1271 RQK 1273
Cdd:PRK13646 235 KDK 237
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
446-621 |
6.41e-04 |
|
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: 43.12 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 446 GMPVLKDlnikipeGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSVAYVsqqawiqncilqVNILFGSIMKkEF 525
Cdd:cd03236 19 RLPVPRE-------GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEI------------LDEFRGSELQ-NY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 526 YEQVLEA---CALLPD-LEQLPKG----------------------DQTEIG---ERGV-NISGGQQHRVSLARAVYSGA 575
Cdd:cd03236 79 FTKLLEGdvkVIVKPQyVDLIPKAvkgkvgellkkkdergkldelvDQLELRhvlDRNIdQLSGGELQRVAIAAALARDA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 74136409 576 DIYLLDDPLSAVDVhvgKQLFEKVIGSLGLLKNKTRILVT-HNLTLL 621
Cdd:cd03236 159 DFYFFDEPSSYLDI---KQRLNAARLIRELAEDDNYVLVVeHDLAVL 202
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1065-1216 |
6.78e-04 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 42.88 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQTHGEEKIGIVGRTGAGKSTLsnclfriveraggkiiidgidistigLHdLRGKLNIIPQHPVLFSGTlqmnld 1144
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTL--------------------------LH-LLGGLDTPTSGDVIFNGQ------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1145 PLNKYSDSKLWEAL--ELCHLKEFVQSLPE---------------KLRHEISE---------GGEN--------LSMGQR 1190
Cdd:PRK11629 72 PMSKLSSAAKAELRnqKLGFIYQFHHLLPDftalenvamplligkKKPAEINSralemlaavGLEHranhrpseLSGGER 151
|
170 180
....*....|....*....|....*.
gi 74136409 1191 QLVCLARALLRKTKILILDEATASID 1216
Cdd:PRK11629 152 QRVAIARALVNNPRLVLADEPTGNLD 177
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1184-1267 |
6.82e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.84 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1184 NLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTIRKEFSD-CTILTIAHRLQSIID-SDRVLVLDSGSIV 1261
Cdd:PRK10762 395 LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEgLSIILVSSEMPEVLGmSDRILVMHEGRIS 474
|
....*..
gi 74136409 1262 -EFEAPQ 1267
Cdd:PRK10762 475 gEFTREQ 481
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1064-1272 |
7.05e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 7.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGgkiiidgidiSTIGLH---------------------DLR 1122
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSA----------GTITLHgkkinnhnaneainhgfalvtEER 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1123 GKLNIIPQHPVLFSgTLQMNLDplnKYSDSklWEALELCHLKEFVQSLPEKLR-----HEISEGgeNLSMGQRQLVCLAR 1197
Cdd:PRK10982 333 RSTGIYAYLDIGFN-SLISNIR---NYKNK--VGLLDNSRMKSDTQWVIDSMRvktpgHRTQIG--SLSGGNQQKVIIGR 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1198 ALLRKTKILILDEATASID----FETDKLVQTTIRKefsDCTILTIAHRLQSIID-SDRVLVLDSG---SIVEF-EAPQN 1268
Cdd:PRK10982 405 WLLTQPEILMLDEPTRGIDvgakFEIYQLIAELAKK---DKGIIIISSEMPELLGiTDRILVMSNGlvaGIVDTkTTTQN 481
|
....
gi 74136409 1269 LIRQ 1272
Cdd:PRK10982 482 EILR 485
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
557-645 |
7.42e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 43.26 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 557 ISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGKQLFEKvIGSLgLLKNKTRILVTHNLTLLPQM-DLIVVMESGR- 634
Cdd:PRK13537 139 LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWER-LRSL-LARGKTILLTTHFMEEAERLcDRLCVIEEGRk 216
|
90
....*....|.
gi 74136409 635 IAQmGTYQELL 645
Cdd:PRK13537 217 IAE-GAPHALI 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
543-635 |
7.50e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.84 E-value: 7.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 543 PKGDQTeIGergvNISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGKQLFEkvigslglLKNKTR------ILVTH 616
Cdd:PRK10762 387 PSMEQA-IG----LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQ--------LINQFKaeglsiILVSS 453
|
90 100
....*....|....*....|
gi 74136409 617 NLTLLPQM-DLIVVMESGRI 635
Cdd:PRK10762 454 EMPEVLGMsDRILVMHEGRI 473
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1065-1267 |
7.57e-04 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 42.42 E-value: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQTHGEEKIGIVGRTGAGKSTL------------------SNCLFRIVERAggkiiidgidistigLHDLRG-KL 1125
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLlgllagldrptsgtvrlaGQDLFALDEDA---------------RARLRArHV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1126 NIIPQHPVLFsGTLQMnLD----PLNKYSDSKLWE-ALELchLKEfVqSLPEKLRHEISEggenLSMGQRQLVCLARALL 1200
Cdd:COG4181 93 GFVFQSFQLL-PTLTA-LEnvmlPLELAGRRDARArARAL--LER-V-GLGHRLDHYPAQ----LSGGEQQRVALARAFA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1201 RKTKILILDEATASIDFETDKLVQT---TIRKEfSDCTILTIAHRLQSIIDSDRVLVLDSGSIVEFEAPQ 1267
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDllfELNRE-RGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAAT 231
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1065-1267 |
7.91e-04 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 42.80 E-value: 7.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCL----------FRIVERAggkiiidgidISTIGLHDLRGKLNIIPQHPVL 1134
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLtgeltpssgeVRLNGRP----------LAAWSPWELARRRAVLPQHSSL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1135 -FSGTLQ----MNLDPLNKYSDSKLW---EALELC---HLKE-FVQSLpeklrheiSeGGEnlsmgqRQLVCLARALL-- 1200
Cdd:COG4559 87 aFPFTVEevvaLGRAPHGSSAAQDRQivrEALALVglaHLAGrSYQTL--------S-GGE------QQRVQLARVLAql 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1201 -----RKTKILILDEATASIDFetdKLVQTTIR--KEFSD--CTILTIAHrlqsiiD-------SDRVLVLDSGSIVEFE 1264
Cdd:COG4559 152 wepvdGGPRWLFLDEPTSALDL---AHQHAVLRlaRQLARrgGGVVAVLH------DlnlaaqyADRILLLHQGRLVAQG 222
|
...
gi 74136409 1265 APQ 1267
Cdd:COG4559 223 TPE 225
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1184-1258 |
8.59e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.56 E-value: 8.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1184 NLSMGQRQLVCLARALLRKTKILILDEATASIdfeTDKLVQ---TTIRK-EFSDCTILTIAHRLQSIID-SDRVLVLDSG 1258
Cdd:PRK10982 134 TLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL---TEKEVNhlfTIIRKlKERGCGIVYISHKMEEIFQlCDEITILRDG 210
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1184-1292 |
8.76e-04 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 43.66 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1184 NLSMGQRQLVCLARALLRKTKILILDEATASI-DFETDKLVQTTIRKEFSDCTILTIAHRLQSIID-SDRVLVLDSGSIV 1261
Cdd:TIGR02633 141 DYGGGQQQLVEIAKALNKQARLLILDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
90 100 110
....*....|....*....|....*....|.
gi 74136409 1262 EFEAPQNlirqkglfyeMTTDAGITQESGTE 1292
Cdd:TIGR02633 221 ATKDMST----------MSEDDIITMMVGRE 241
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
774-929 |
1.01e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 42.52 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 774 IYGILGLIKGLFVCSGAYVITRGSL---AASRT---MYVQLLNNVLHLPIQFFETNSTGQIISRFTKDIFIIDmrlhyyl 847
Cdd:cd18778 39 LLGLALLLLGAYLLRALLNFLRIYLnhvAEQKVvadLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVE------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 848 RLWVNCTLDVIGTILVIIGALPLFI--------LGIIPSVFFYFSIqRYYVASSRQIRRLTGASRSPVISHFSETLSGVS 919
Cdd:cd18778 112 RLIADGIPQGITNVLTLVGVAIILFsinpklalLTLIPIPFLALGA-WLYSKKVRPRYRKVREALGELNALLQDNLSGIR 190
|
170
....*....|
gi 74136409 920 TIRAFGHQQR 929
Cdd:cd18778 191 EIQAFGREEE 200
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1184-1228 |
1.02e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 41.78 E-value: 1.02e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 74136409 1184 NLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTIR 1228
Cdd:PRK13539 127 YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIR 171
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1076-1256 |
1.41e-03 |
|
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: 40.43 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1076 EKIGIVGRTGAGKSTLSNCLFRIVERaggkiiidgidistiglhdlrgklniiPQHPVLFsgtlqMNLDPLNKYSDSKLW 1155
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGP---------------------------PGGGVIY-----IDGEDILEEVLDQLL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1156 EALELCHLKEFVQslpeklrheiseggenlsmGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQ-------TTIR 1228
Cdd:smart00382 51 LIIVGGKKASGSG-------------------ELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrlLLLL 111
|
170 180
....*....|....*....|....*...
gi 74136409 1229 KEFSDCTILTIAHRLQSIIDSDRVLVLD 1256
Cdd:smart00382 112 KSEKNLTVILTTNDEKDLGPALLRRRFD 139
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
431-502 |
1.57e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.57 E-value: 1.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74136409 431 HAIEFTDATYSWNktGMPVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQ--RKGSVAYVSQ 502
Cdd:PRK15064 318 NALEVENLTKGFD--NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKwsENANIGYYAQ 389
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1185-1262 |
1.65e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 41.70 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1185 LSMGQRQLVCLARALLRKTKILILDEATASIDFET-DKLVQTTIR-KEFSDCTILTIAHRLQSIID-SDRVLVLDSGSIV 1261
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMrSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVV 229
|
.
gi 74136409 1262 E 1262
Cdd:PRK15112 230 E 230
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1064-1267 |
1.69e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 42.26 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRI---VERAGGKIIIDGIDISTIGLHDLRGKLNIIPQHPVlfsgtlq 1140
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIetpTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNPY------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1141 MNLDPLNKYSDSkLWEALEL------CHLKEFVQSLPEK--LRHEISEGGENL-SMGQRQLVCLARALLRKTKILILDEA 1211
Cdd:PRK11308 103 GSLNPRKKVGQI-LEEPLLIntslsaAERREKALAMMAKvgLRPEHYDRYPHMfSGGQRQRIAIARALMLDPDVVVADEP 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74136409 1212 TASIDFEtdklVQTTIRKEFSD------CTILTIAHRLqSIID--SDRVLVLDSGSIVE-------FEAPQ 1267
Cdd:PRK11308 182 VSALDVS----VQAQVLNLMMDlqqelgLSYVFISHDL-SVVEhiADEVMVMYLGRCVEkgtkeqiFNNPR 247
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1064-1261 |
2.05e-03 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 41.01 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1064 ALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIvERAGGKIIIdgidistIGLHD-----------LRGKLNIIPQ-H 1131
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGI-ERPSAGKIW-------FSGHDitrlknrevpfLRRQIGMIFQdH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1132 PVLFSGTLQMNLD-PLNKYSDS------KLWEALELCHLKEFVQSLPEKlrheiseggenLSMGQRQLVCLARALLRKTK 1204
Cdd:PRK10908 89 HLLMDRTVYDNVAiPLIIAGASgddirrRVSAALDKVGLLDKAKNFPIQ-----------LSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74136409 1205 ILILDEATASIDfetDKLVQTTIR--KEFS--DCTILTIAHRLQSIIDSD-RVLVLDSGSIV 1261
Cdd:PRK10908 158 VLLADEPTGNLD---DALSEGILRlfEEFNrvGVTVLMATHDIGLISRRSyRMLTLSDGHLH 216
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
450-495 |
2.21e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.37 E-value: 2.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 74136409 450 LKDLNIKIPEGALVAVVGQVGSGKSSMLSAIL--GEMEKLTGVVQRKG 495
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLINETLykALARKLNGAKKVPG 672
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1065-1260 |
2.54e-03 |
|
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: 40.99 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1065 LQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDlRGKLNII--PQHPVLFSG-TLQM 1141
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIGylPQEASIFRKlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1142 NLD-------PLNKYSDSKLWEALELCHLkefvqslpEKLRHEIsegGENLSMGQRQLVCLARALLRKTKILILDEATAS 1214
Cdd:cd03218 95 NILavleirgLSKKEREEKLEELLEEFHI--------THLRKSK---ASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 74136409 1215 IDFETDKLVQTTIR--KEfSDCTILTIAHRLQSIID-SDRVLVLDSGSI 1260
Cdd:cd03218 164 VDPIAVQDIQKIIKilKD-RGIGVLITDHNVRETLSiTDRAYIIYEGKV 211
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1048-1262 |
2.62e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.88 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1048 VEFINYQARYRDElGLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCLFRIVERAGGKIIIDGIDISTIGLHDLRGKLNI 1127
Cdd:PRK10522 323 LELRNVTFAYQDN-GFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1128 IPQHPVLFSGTlqmnLDPLNKYSDSKLWEALeLCHLKefvqsLPEKLRHeisEGGE----NLSMGQRQLVCLARALLRKT 1203
Cdd:PRK10522 402 VFTDFHLFDQL----LGPEGKPANPALVEKW-LERLK-----MAHKLEL---EDGRisnlKLSKGQKKRLALLLALAEER 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74136409 1204 KILILDEATASIDfetdklvqTTIRKEF----------SDCTILTIAHRLQSIIDSDRVLVLDSGSIVE 1262
Cdd:PRK10522 469 DILLLDEWAADQD--------PHFRREFyqvllpllqeMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
557-660 |
2.93e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 41.37 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 557 ISGGQQHRVSLARAVYSGADIYLLDDPLSAVDVHVGKQLFEKVIGSLGllKNKTRILVTHNL-TLLPQMDLIVVMESGRI 635
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKA--NNKTVFVITHTMeHVLEVADEVIVMDKGKI 254
|
90 100 110
....*....|....*....|....*....|..
gi 74136409 636 AQMGT-Y-----QELLSKTR-NLTNLHQVISE 660
Cdd:PRK13631 255 LKTGTpYeiftdQHIINSTSiQVPRVIQVIND 286
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1149-1256 |
3.26e-03 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 40.17 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1149 YSDSKLWEALELCHLKEFvQSLPEKlrheiseggeNLSMGQRQLVCLARALLRKTKILILDEATASIDFETDKLVQTTIR 1228
Cdd:PRK13538 105 GDDEALWEALAQVGLAGF-EDVPVR----------QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLA 173
|
90 100 110
....*....|....*....|....*....|
gi 74136409 1229 KEFSD--CTILTIAHRLQSIIDSDRVLVLD 1256
Cdd:PRK13538 174 QHAEQggMVILTTHQDLPVASDKVRKLRLG 203
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1062-1095 |
3.52e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 40.68 E-value: 3.52e-03
10 20 30
....*....|....*....|....*....|....
gi 74136409 1062 GLALQDITFQTHGEEKIGIVGRTGAGKSTLSNCL 1095
Cdd:PRK11701 19 RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNAL 52
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
446-630 |
3.62e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 41.69 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 446 GMPVLKdlnikipEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSVAYVSQQawiqncilqvnilF-GSIMKKE 524
Cdd:COG1245 92 GLPVPK-------KGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSWDEVLKR-------------FrGTELQDY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 525 F---YEQVLEAcALLPD-LEQLP---KGDQTEI----GERGV-------------------NISGGQQHRVSLARAVYSG 574
Cdd:COG1245 152 FkklANGEIKV-AHKPQyVDLIPkvfKGTVRELlekvDERGKldelaeklglenildrdisELSGGELQRVAIAAALLRD 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 74136409 575 ADIYLLDDPLSAVDVhvgKQLFE--KVIGSLgLLKNKTRILVTHNLTLLPQM-DLIVVM 630
Cdd:COG1245 231 ADFYFFDEPSSYLDI---YQRLNvaRLIREL-AEEGKYVLVVEHDLAILDYLaDYVHIL 285
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
123-409 |
3.74e-03 |
|
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: 40.86 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 123 LFKVFADILSFTSPLIMKQMIIFCEHSSDFGWNGYGYAMALFVVVFLQTLI--LQRYQCFNmlTSAKVKTAVNGLIYKKA 200
Cdd:cd18541 6 LFLILVDLLQLLIPRIIGRAIDALTAGTLTASQLLRYALLILLLALLIGIFrfLWRYLIFG--ASRRIEYDLRNDLFAHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 201 LLLSNVSRQKFSTGEIINLMSADAQQLMDLTAN-LNLLWSAPFQILMAIYLLWQeLGPaVLAGVAVLVFviPINALAATK 279
Cdd:cd18541 84 LTLSPSFYQKNRTGDLMARATNDLNAVRMALGPgILYLVDALFLGVLVLVMMFT-ISP-KLTLIALLPL--PLLALLVYR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 280 I-KKLKKSQRKNKDKQIKL---LKEILHGIKILKLYAWEPSYKNKIIKIRDqelEFQKSARYLTVFSMLTLTCIPFLVSL 355
Cdd:cd18541 160 LgKKIHKRFRKVQEAFSDLsdrVQESFSGIRVIKAFVQEEAEIERFDKLNE---EYVEKNLRLARVDALFFPLIGLLIGL 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74136409 356 ATLCVYF----LLDEGNI----LTAtkvFTSMslFNILRIPLFELPTVISTVVQTKISLGRL 409
Cdd:cd18541 237 SFLIVLWyggrLVIRGTItlgdLVA---FNSY--LGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
1078-1097 |
3.75e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 40.90 E-value: 3.75e-03
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1185-1269 |
4.18e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 41.17 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1185 LSMGQRQLVCLARALLRKTKILILDEATASIdfetDKLVQTTIRKEFS------DCTILTIAH-RLQSIIDSDRVLVLDS 1257
Cdd:PRK11000 134 LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL----DAALRVQMRIEISrlhkrlGRTMIYVTHdQVEAMTLADKIVVLDA 209
|
90
....*....|..
gi 74136409 1258 GSIVEFEAPQNL 1269
Cdd:PRK11000 210 GRVAQVGKPLEL 221
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
448-636 |
4.38e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.25 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 448 PVLKDLNIKIPEGALVAVVGQVGSGKSSMLSAILGEMEKLTGVVQRKGSV--------------AYVSQQAWIQNCILQV 513
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKinnhnaneainhgfALVTEERRSTGIYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 514 NILFGSIMKKefYEQVLEACALLPDLE--------------QLPkGDQTEIGergvNISGGQQHRVSLARAVYSGADIYL 579
Cdd:PRK10982 342 DIGFNSLISN--IRNYKNKVGLLDNSRmksdtqwvidsmrvKTP-GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILM 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 74136409 580 LDDPLSAVDVHVGKQLFEkVIGSLGlLKNKTRILVTHNL-TLLPQMDLIVVMESGRIA 636
Cdd:PRK10982 415 LDEPTRGIDVGAKFEIYQ-LIAELA-KKDKGIIIISSEMpELLGITDRILVMSNGLVA 470
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1157-1270 |
5.95e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.56 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1157 ALELCHL------KEFVQSLPeklrHEISEGgenlsmgQRQLVCLARALLRKTKILILDEATASIDFETdklvQTTIRKE 1230
Cdd:PRK15093 136 AIELLHRvgikdhKDAMRSFP----YELTEG-------ECQKVMIAIALANQPRLLIADEPTNAMEPTT----QAQIFRL 200
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 74136409 1231 FS------DCTILTIAHRLQSIID-SDRVLVLDSGSIVEFEAPQNLI 1270
Cdd:PRK15093 201 LTrlnqnnNTTILLISHDLQMLSQwADKINVLYCGQTVETAPSKELV 247
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
812-929 |
6.58e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 40.24 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 812 VLHLPIQFFETNSTGQIISRFTKDI-----FIIDMrlhyyLR--LWVNCTLDVIGTILVIIGA-LPLFILGIIPSVF--- 880
Cdd:cd18565 97 VQRLDMAFFEDRQTGDLMSVLNNDVnqlerFLDDG-----ANsiIRVVVTVLGIGAILFYLNWqLALVALLPVPLIIagt 171
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 74136409 881 FYFS--IQRYYvassRQIRRLTGAsrspVISHFSETLSGVSTIRAFGHQQR 929
Cdd:cd18565 172 YWFQrrIEPRY----RAVREAVGD----LNARLENNLSGIAVIKAFTAEDF 214
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1156-1216 |
8.14e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.49 E-value: 8.14e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74136409 1156 EALELCHLKEFVQSLPEklrheiseggeNLSMGQRQLVCLARALLRKTKILILDEATASID 1216
Cdd:NF033858 380 EMLERFDLADVADALPD-----------SLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1080-1216 |
9.05e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.13 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74136409 1080 IVGRTGAGKSTLSNCLFriveraggkiiidgidISTIGLHDLRGKLN-----IIPQHPVLFSGTLQMNLDPLNKYSDSKL 1154
Cdd:cd03240 27 IVGQNGAGKTTIIEALK----------------YALTGELPPNSKGGahdpkLIREGEVRAQVKLAFENANGKKYTITRS 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74136409 1155 WEALE---LCHLKEFVQSLPEKLrheiseggENLSMGQRQLVC------LARALLRKTKILILDEATASID 1216
Cdd:cd03240 91 LAILEnviFCHQGESNWPLLDMR--------GRCSGGEKVLASliirlaLAETFGSNCGILALDEPTTNLD 153
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
1077-1097 |
9.55e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 37.21 E-value: 9.55e-03
|
| |
