|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-1522 |
0e+00 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 2538.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 7 SGELGSKFWDSNLTVYTNTPDLTPCFQNSLLAWVPCIYLWAALPCYLFYLRHHRLGYIVLSCLSRLKTALGVLLWCISWV 86
Cdd:TIGR00957 2 SADGSDPLWDWNVTWHTSNPDFTKCFQNTVLAWVPCFYLWVCFPCYFLYLSRHDRGYIQMTHLNKTKTALGFLLWIVCWA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 87 DLFYSFHGLVHGSSPAPVFFITPLLVGITMLLATLLIQYERLRGVRSSGVLIIFWLLCVICAIIPFRSKILLALAEGKIL 166
Cdd:TIGR00957 82 DLFYSFWERSHGRAPAPVFLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALVCALAILRSKILLALKEDAIV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 167 DPFRFTTFYIYFALVLCAFILSCFQEKPPLFSPENLDTNPCPEASAGFFSRLSFWWFTKLAILGYRRPLEDSDLWSLSEE 246
Cdd:TIGR00957 162 DPFRDTTFYIYFALVLSQLVLSCFSDKSPLFSETNHDPNPCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 247 DCSHKVVQRLLEAWQKQQTQ-ASGPQTAALEPK------------IAGEDEVLLKARP-KTKKPSFLRALVRTFTSSLLM 312
Cdd:TIGR00957 242 DTSEMVVPVLVENWKKECKKtRKQPVSAVYGKKdpskpkgssqldANEEVEALIVKSPhKPRKPSLFKVLYKTFGPYFLM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 313 GACFKLIQDLLSFINPQLLSILIRFISDPTAPTWWGFLLAGLMFVSSTMQTLILHQHYHCIFVMALRIRTAIIGVIYRKA 392
Cdd:TIGR00957 322 SFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 393 LTITNSVKREYTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNGAVSMKM 472
Cdd:TIGR00957 402 LVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKT 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 473 KTYQVQQMKFKDSRIKLMSEILNGIKVLKLYAWEPTFLEQVEGIRQSELQLLRKGAYLQAISTFIWVCTPFMVTLITLGV 552
Cdd:TIGR00957 482 KTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAV 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 553 YVCVDKNNVLDAEKAFVSLSLFNILKIPLNLLPQLISGMTQTSVSLKRIQDFLNQDELDPQCVERKTISPGR--AITIHN 630
Cdd:TIGR00957 562 YVTVDENNILDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEgnSITVHN 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 631 GTFSWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSVAYVPQQAWIQNCTLQENVLF 710
Cdd:TIGR00957 642 ATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILF 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 711 GQPMNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFD 790
Cdd:TIGR00957 722 GKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 791 QVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQITEMGHYSELLQHDGSFANFLRNYAPDENQEANE----GVLQH 866
Cdd:TIGR00957 802 HVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQGHLEdswtALVSG 881
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 867 ANEEVLLLEDTLSthtdLTDTepaiyeVRKQFMREMSSLSSEGEGQNRpvlkrYTSSLEKEVPATQTKETGALIKEEIAE 946
Cdd:TIGR00957 882 EGKEAKLIENGML----VTDV------VGKQLQRQLSASSSDSGDQSR-----HHGSSAELQKAEAKEETWKLMEADKAQ 946
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 947 TGNVKLSVYWDYAKSVGLCTTLFICLLYAGQNAVAIGANVWLSAWTNDVEEHGQQNNTSVRLGVYATLGILQGLLVMLSA 1026
Cdd:TIGR00957 947 TGQVELSVYWDYMKAIGLFITFLSIFLFVCNHVSALASNYWLSLWTDDPMVNGTQNNTSLRLSVYGALGILQGFAVFGYS 1026
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1027 FTMVVGAIQAARLLHTALLHNQIRAPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLFNSFYTSISTIVVIVASTPL 1106
Cdd:TIGR00957 1027 MAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPI 1106
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1107 FCVVVLPLAVFYGFVQRFYVATSRQLKRLESVSRSPIFSHFSETVTGTSVIRAYGRVQDFKVLSDAKVDSNQKTTYPYIA 1186
Cdd:TIGR00957 1107 AAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIV 1186
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1187 SNRWLGVHVEFVGNCVVLFSALFAVIGRNSLNPGLVGLSVSYALQVTLSLNWMIRTLSDLESNIIAVERVKEYSKTETEA 1266
Cdd:TIGR00957 1187 ANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEA 1266
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1267 PWVLESNRAPEGWPRSGVVEFRNYSVRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFID 1346
Cdd:TIGR00957 1267 PWQIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIID 1346
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1347 GLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQ 1426
Cdd:TIGR00957 1347 GLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQ 1426
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1427 RQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNL 1506
Cdd:TIGR00957 1427 RQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNL 1506
|
1530
....*....|....*.
gi 1937891448 1507 IAAGGIFYGMAKDAGL 1522
Cdd:TIGR00957 1507 LQQRGIFYSMAKDAGL 1522
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
207-1523 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 1052.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 207 CPEASAGFFSRLSFWWFTKLAILGYRRPLEDSDLWSLSEEDCSHKVVQRLLEAWQKQQTQAsgpqtaalepkiagedevl 286
Cdd:PLN03130 227 CPERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKKP------------------- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 287 lkarpktkKPSFLRALVRTFTSSLLMGACFKLIQDLLSFINPQLLSILIRFISDpTAPTWWGFLLAGLMFVSSTMQTLIL 366
Cdd:PLN03130 288 --------KPWLLRALNNSLGGRFWLGGFFKIGNDLSQFVGPLLLNLLLESMQN-GEPAWIGYIYAFSIFVGVVLGVLCE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 367 HQHYHCIFVMALRIRTAIIGVIYRKALTITNSVKREYTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQI 446
Cdd:PLN03130 359 AQYFQNVMRVGFRLRSTLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQ 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 447 LGPSALAGVAVIVLLIPLNGAVSMKMKTYQVQQMKFKDSRIKLMSEILNGIKVLKLYAWEPTFLEQVEGIRQSELQLLRK 526
Cdd:PLN03130 439 LGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRK 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 527 GAYLQAISTFIWVCTPFMVTLITLGVYVCVdkNNVLDAEKAFVSLSLFNILKIPLNLLPQLISGMTQTSVSLKRIQDFLN 606
Cdd:PLN03130 519 AQLLSAFNSFILNSIPVLVTVVSFGVFTLL--GGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLL 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 607 QDE--LDPQcverKTISPGR-AITIHNGTFSW-SKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEG 682
Cdd:PLN03130 597 AEErvLLPN----PPLEPGLpAISIKNGYFSWdSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSD 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 683 A-VSVKGSVAYVPQQAWIQNCTLQENVLFGQPMNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLA 761
Cdd:PLN03130 673 AsVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMA 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 762 RAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGPEgvLAGKTRVLVTHGISFLPQTDFIIVLADGQITEMGHYSELLQHD 841
Cdd:PLN03130 753 RAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDE--LRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNG 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 842 GSFANFLRNYAPDENQEANEGvlqhaneevllledtlSTHTDLTDTEPAIYEVRKQFMREMSSLSSEGEGQNrpvlkryt 921
Cdd:PLN03130 831 PLFQKLMENAGKMEEYVEENG----------------EEEDDQTSSKPVANGNANNLKKDSSSKKKSKEGKS-------- 886
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 922 sslekevpatqtketgALIKEEIAETGNVKLSVYWDYAKSVG---LCTTLFICllYAGQNAVAIGANVWLSAWTNDV--E 996
Cdd:PLN03130 887 ----------------VLIKQEERETGVVSWKVLERYKNALGgawVVMILFLC--YVLTEVFRVSSSTWLSEWTDQGtpK 948
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 997 EHGqqnnTSVRLGVYATLGILQGLLVMLSAFTMVVGAIQAARLLHTALLHNQIRAPQSFFDTTPSGRILNRFSKDIYVID 1076
Cdd:PLN03130 949 THG----PLFYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDID 1024
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1077 EVLAPTILMLFNSFYTSISTIVVI--VASTPLFCVVVLpLAVFYGfVQRFYVATSRQLKRLESVSRSPIFSHFSETVTGT 1154
Cdd:PLN03130 1025 RNVAVFVNMFLGQIFQLLSTFVLIgiVSTISLWAIMPL-LVLFYG-AYLYYQSTAREVKRLDSITRSPVYAQFGEALNGL 1102
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1155 SVIRAYGRVQDFKVLSDAKVDSNQKTTYPYIASNRWLGVHVEFVGNCVVLFSALFAVIGR-NSLNP----GLVGLSVSYA 1229
Cdd:PLN03130 1103 STIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMQNgRAENQaafaSTMGLLLSYA 1182
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1230 LQVTLSLNWMIRTLSDLESNIIAVERVKEYSKTETEAPWVLESNRAPEGWPRSGVVEFRNYSVRYRPGLELVLKNLTLHV 1309
Cdd:PLN03130 1183 LNITSLLTAVLRLASLAENSLNAVERVGTYIDLPSEAPLVIENNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEI 1262
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1310 QGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSDE 1389
Cdd:PLN03130 1263 SPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDA 1342
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1390 DIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFE 1469
Cdd:PLN03130 1343 DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFK 1422
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*
gi 1937891448 1470 DCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIA-AGGIFYGMAKDAGLA 1523
Cdd:PLN03130 1423 SCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSnEGSAFSKMVQSTGAA 1477
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
196-1523 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 1002.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 196 LFSPENLDT----------NPCPEASAGFFSRLSFWWFTKLAILGYRRPLEDSDLWSLSEEDCSHKVVQRLLEAWQKQQT 265
Cdd:PLN03232 206 ILNNESLDNveydalrggeNICPERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEESR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 266 qasgpqtaalepkiagedevllkaRPKtkkPSFLRALVRTFTSSLLMGACFKLIQDLLSFINPQLLSILIRFISDPTaPT 345
Cdd:PLN03232 286 ------------------------RPK---PWLLRALNNSLGGRFWLGGIFKIGHDLSQFVGPVILSHLLQSMQEGD-PA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 346 WWGFLLAGLMFVSSTMQTLILHQHYHCIFVMALRIRTAIIGVIYRKALTITNSVKREYTVGEMVNLMSVDAQRFMDVSPF 425
Cdd:PLN03232 338 WVGYVYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQ 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 426 INLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNGAVSMKMKTYQVQQMKFKDSRIKLMSEILNGIKVLKLYAW 505
Cdd:PLN03232 418 LHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAW 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 506 EPTFLEQVEGIRQSELQLLRKGAYLQAISTFIWVCTPFMVTLITLGVYVCVDKNnvLDAEKAFVSLSLFNILKIPLNLLP 585
Cdd:PLN03232 498 EKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGVFVLLGGD--LTPARAFTSLSLFAVLRSPLNMLP 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 586 QLISGMTQTSVSLKRIQD-FLNQDELDPQcveRKTISPGR-AITIHNGTFSW-SKDLPPTLHSLNIQIPKGALVAVVGPV 662
Cdd:PLN03232 576 NLLSQVVNANVSLQRIEElLLSEERILAQ---NPPLQPGApAISIKNGYFSWdSKTSKPTLSDINLEIPVGSLVAIVGGT 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 663 GCGKSSLVSALLGEMEKLEGA-VSVKGSVAYVPQQAWIQNCTLQENVLFGQPMNPKRYQQALETCALLADLDVLPGGDQT 741
Cdd:PLN03232 653 GEGKTSLISAMLGELSHAETSsVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLT 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 742 EIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGPEgvLAGKTRVLVTHGISFLPQTDFII 821
Cdd:PLN03232 733 EIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDE--LKGKTRVLVTNQLHFLPLMDRII 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 822 VLADGQITEMGHYSELLQHDGSFANFLRNYAP-DENQEANEGvlqhaNEEVLLLEDTLSTHTdltdtepaiyevrkqfmr 900
Cdd:PLN03232 811 LVSEGMIKEEGTFAELSKSGSLFKKLMENAGKmDATQEVNTN-----DENILKLGPTVTIDV------------------ 867
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 901 EMSSLSSEGEGQNRPVLkrytsslekevpatqtketgaLIKEEIAETGNVKLSVYWDYAKSVG---LCTTLFICllYAGQ 977
Cdd:PLN03232 868 SERNLGSTKQGKRGRSV---------------------LVKQEERETGIISWNVLMRYNKAVGglwVVMILLVC--YLTT 924
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 978 NAVAIGANVWLSAWTNdveehgQQNNTSVRLG----VYATLGILQGLLVMLSAFTMVVGAIQAARLLHTALLHNQIRAPQ 1053
Cdd:PLN03232 925 EVLRVSSSTWLSIWTD------QSTPKSYSPGfyivVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPM 998
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1054 SFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLFNSFYTSISTIVVIVASTPLFCVVVLPLAVFYGFVQRFYVATSRQLK 1133
Cdd:PLN03232 999 LFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVR 1078
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1134 RLESVSRSPIFSHFSETVTGTSVIRAYGRVQDFKVLSDAKVDSNQKTTYPYIASNRWLGVHVEFVGNCVVLFSALFAVIG 1213
Cdd:PLN03232 1079 RLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLR 1158
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1214 RNSLN-----PGLVGLSVSYALQVTLSLNWMIRTLSDLESNIIAVERVKEYSKTETEAPWVLESNRAPEGWPRSGVVEFR 1288
Cdd:PLN03232 1159 NGNAEnqagfASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRGSIKFE 1238
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1289 NYSVRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTIIPQD 1368
Cdd:PLN03232 1239 DVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQS 1318
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1369 PILFSGTLRMNLDPFGRYSDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEA 1448
Cdd:PLN03232 1319 PVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEA 1398
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 1449 TAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIA-AGGIFYGMAKDAGLA 1523
Cdd:PLN03232 1399 TASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSrDTSAFFRMVHSTGPA 1474
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
291-1521 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 819.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 291 PKTKKPSFLRALVRTFTSSLLMGACFKLIQDLLSFINPQLLSILIRFISDPTApTW-WGFLLAGLMFVSSTMQTLILHQH 369
Cdd:PTZ00243 227 PTPKRLSLLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFLDADNA-TWgRGLGLVLTLFLTQLIQSVCLHRF 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 370 YHCIFVMALRIRTAIIGVIYRKALTITN-SVKR-EYTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQIL 447
Cdd:PTZ00243 306 YYISIRCGLQYRSALNALIFEKCFTISSkSLAQpDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLV 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 448 GPSALAGVAVIVLLIPLNGAVSMKMKTYQVQQMKFKDSRIKLMSEILNGIKVLKLYAWEPTFLEQVEGIRQSELQLLRKG 527
Cdd:PTZ00243 386 GWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDV 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 528 AYLQAISTFIWVCTPFMVTLITLGVYVCVdkNNVLDAEKAFVSLSLFNILKIPLNLLPQLISGMTQTSVSLKRIQDFLNQ 607
Cdd:PTZ00243 466 QLARVATSFVNNATPTLMIAVVFTVYYLL--GHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLEC 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 608 DELD----------------------------------------PQCVERKTISPGRAI-----------------TIHN 630
Cdd:PTZ00243 544 DNATcstvqdmeeywreqrehstacqlaavlenvdvtafvpvklPRAPKVKTSLLSRALrmlcceqcrptkrhpspSVVV 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 631 GTFSWSK--------------------------------------DLPPT--LHSLNIQIPKGALVAVVGPVGCGKSSLV 670
Cdd:PTZ00243 624 EDTDYGSpssasrhiveggtgggheatptsersaktpkmktddffELEPKvlLRDVSVSVPRGKLTVVLGATGSGKSTLL 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 671 SALLGEMEKLEGAVSVKGSVAYVPQQAWIQNCTLQENVLFGQPMNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINL 750
Cdd:PTZ00243 704 QSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNL 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 751 SGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIgpEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQITE 830
Cdd:PTZ00243 784 SGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECF--LGALAGKTRVLATHQVHVVPRADYVVALGDGRVEF 861
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 831 MGHYSELLQhdGSFANFLRNyAPDENQEANEGvlqHANEEVLlledtlsthtdltdtepaiyevrkqfmrEMSSLSSEGE 910
Cdd:PTZ00243 862 SGSSADFMR--TSLYATLAA-ELKENKDSKEG---DADAEVA----------------------------EVDAAPGGAV 907
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 911 GQNRPVLKRyTSSLEKEVPATQTKETGALIKEEIAETGNVKLSVYWDYAKSV-GLCTTLFICLLYAGQNAVAIGANVWLS 989
Cdd:PTZ00243 908 DHEPPVAKQ-EGNAEGGDGAALDAAAGRLMTREEKASGSVPWSTYVAYLRFCgGLHAAGFVLATFAVTELVTVSSGVWLS 986
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 990 AWTNDVEEHGQQNNTSVRLGVYATLGILQGLLVMLSAFTMVVGaiqaARLLHTALLHNQIRAPQSFFDTTPSGRILNRFS 1069
Cdd:PTZ00243 987 MWSTRSFKLSAATYLYVYLGIVLLGTFSVPLRFFLSYEAMRRG----SRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFS 1062
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1070 KDIYVIDEVLAPTILMLFNSFYTSISTIVVIVASTPLFCVVVLPLAVFYGFVQRFYVATSRQLKRLESVSRSPIFSHFSE 1149
Cdd:PTZ00243 1063 RDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEE 1142
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1150 TVTGTSVIRAYGRVQdfKVLSDA--KVDSNQKTTYPYIASNRWLGVHVEFVGNCVVLFSALFAVIGR----NSLNPGLVG 1223
Cdd:PTZ00243 1143 ALQGSATITAYGKAH--LVMQEAlrRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIGVIGTmlraTSQEIGLVS 1220
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1224 LSVSYALQVTLSLNWMIRTLSDLESNIIAVERVKEYS--------------------KTETEAP----WVLESNRAPEGW 1279
Cdd:PTZ00243 1221 LSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTdevphedmpeldeevdalerRTGMAADvtgtVVIEPASPTSAA 1300
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1280 PR---SGVVEFRNYSVRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLH 1356
Cdd:PTZ00243 1301 PHpvqAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLR 1380
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1357 DLRSQLTIIPQDPILFSGTLRMNLDPFGRYSDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARAL 1436
Cdd:PTZ00243 1381 ELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARAL 1460
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1437 LRK-SRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLI-AAGGIFY 1514
Cdd:PTZ00243 1461 LKKgSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVmNRQSIFH 1540
|
....*..
gi 1937891448 1515 GMAKDAG 1521
Cdd:PTZ00243 1541 SMVEALG 1547
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
208-1513 |
0e+00 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 596.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 208 PEASAGFFSRLSFWWFTKLAILGYRRPLEDSDLWSLSEEDCSHKVVQRLLEAWQKQQTQASgpqtaalepkiagedevll 287
Cdd:TIGR01271 5 PVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASAK------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 288 karpktKKPSFLRALVRTFTSSLLMGACFKLIQDLLSFINPQLLS-ILIRFISDPTAPTWWGFLLA---GLMFVsstMQT 363
Cdd:TIGR01271 66 ------KNPKLLNALRRCFFWRFVFYGILLYFGEATKAVQPLLLGrIIASYDPFNAPEREIAYYLAlglCLLFI---VRT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 364 LILHQHYHCIFVMALRIRTAIIGVIYRKALTITNSVKREYTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFL 443
Cdd:TIGR01271 137 LLLHPAIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 444 WQILGPSALAGVAVIVLLIPLNGAVSMKMKTYQVQQMKFKDSRIKLMSEILNGIKVLKLYAWEPTFLEQVEGIRQSELQL 523
Cdd:TIGR01271 217 WELLEVNGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 524 LRKGAYLQAISTFIWVCTPFMVTLITLGVYVCVdKNNVLdaEKAFVSLSLFNILKIPLNL-LPQLISGMTQTSVSLKRIQ 602
Cdd:TIGR01271 297 TRKIAYLRYFYSSAFFFSGFFVVFLSVVPYALI-KGIIL--RRIFTTISYCIVLRMTVTRqFPGAIQTWYDSLGAITKIQ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 603 DFLNQDELdpQCVERKTISpgRAITIHNGTFSW--------------------------------SKDLPPTLHSLNIQI 650
Cdd:TIGR01271 374 DFLCKEEY--KTLEYNLTT--TEVEMVNVTASWdegigelfekikqnnkarkqpngddglffsnfSLYVTPVLKNISFKL 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 651 PKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSVAYVPQQAWIQNCTLQENVLFGQPMNPKRYQQALETCALLA 730
Cdd:TIGR01271 450 EKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEE 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 731 DLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGPegVLAGKTRVLVTHG 810
Cdd:TIGR01271 530 DIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCK--LMSNKTRILVTSK 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 811 ISFLPQTDFIIVLADGQITEMGHYSEL--LQHDGS--------FANF------------LRNYAPDEN------------ 856
Cdd:TIGR01271 608 LEHLKKADKILLLHEGVCYFYGTFSELqaKRPDFSslllgleaFDNFsaerrnsiltetLRRVSIDGDstvfsgpetikq 687
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 857 -----------------------------------QEANEGVLQHANEEVLLLEDTLSTHTDLTD----------TEPAI 891
Cdd:TIGR01271 688 sfkqpppefaekrkqsiilnpiasarkfsfvqmgpQKAQATTIEDAVREPSERKFSLVPEDEQGEeslprgnqyhHGLQH 767
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 892 YEVRKQFMREMSSLSSEGEGQNRpvlkRYTSSLEKEVPATQT---------------KETGALIKEEIAETG-------- 948
Cdd:TIGR01271 768 QAQRRQSVLQLMTHSNRGENRRE----QLQTSFRKKSSITQQnelaseldiysrrlsKDSVYEISEEINEEDlkecfade 843
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 949 --NVKLSVYWD-YAKSV----GLCTTLFICLLYAGQNAVAIGANVWL-----SAWTNDVEEHGQQNNTSVRLGVYAT--- 1013
Cdd:TIGR01271 844 reNVFETTTWNtYLRYIttnrNLVFVLIFCLVIFLAEVAASLLGLWLitdnpSAPNYVDQQHANASSPDVQKPVIITpts 923
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1014 --------LGILQGLLVM--LSAFTMVVGAIQAARLLHTALLHNQIRAPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTI 1083
Cdd:TIGR01271 924 ayyifyiyVGTADSVLALgfFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTL 1003
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1084 LMLFNSFYTSISTIVVIVASTPLFCVVVLPLAVFYGFVQRFYVATSRQLKRLESVSRSPIFSHFSETVTGTSVIRAYGRV 1163
Cdd:TIGR01271 1004 FDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQ 1083
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1164 QDFKVLSDAKVDSNQKTTYPYIASNRWLGVHVEFVgnCVVLFSAL-FAVIGRNSLNPGLVGLSVSYALQVTLSLNWMIRT 1242
Cdd:TIGR01271 1084 SYFETLFHKALNLHTANWFLYLSTLRWFQMRIDII--FVFFFIAVtFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNS 1161
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1243 LSDLESNIIAVERVKEYSKTETEAP--------------WVLESNRAPEGWPRSGVVEFRNYSVRYRPGLELVLKNLTLH 1308
Cdd:TIGR01271 1162 SIDVDGLMRSVSRVFKFIDLPQEEPrpsggggkyqlstvLVIENPHAQKCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFS 1241
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1309 VQGGEKVGIVGRTGAGKSSMTLCLFRILeAAEGEIFIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSD 1388
Cdd:TIGR01271 1242 VEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSD 1320
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1389 EDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQF 1468
Cdd:TIGR01271 1321 EEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSF 1400
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|....*
gi 1937891448 1469 EDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIF 1513
Cdd:TIGR01271 1401 SNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
313-601 |
2.10e-162 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350039 [Multi-domain] Cd Length: 290 Bit Score: 491.21 E-value: 2.10e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 313 GACFKLIQDLLSFINPQLLSILIRFISDPTAPTWWGFLLAGLMFVSSTMQTLILHQHYHCIFVMALRIRTAIIGVIYRKA 392
Cdd:cd18595 2 AALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 393 LTITNSVKREYTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNGAVSMKM 472
Cdd:cd18595 82 LRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 473 KTYQVQQMKFKDSRIKLMSEILNGIKVLKLYAWEPTFLEQVEGIRQSELQLLRKGAYLQAISTFIWVCTPFMVTLITLGV 552
Cdd:cd18595 162 KKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFAT 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1937891448 553 YVCVDKNNVLDAEKAFVSLSLFNILKIPLNLLPQLISGMTQTSVSLKRI 601
Cdd:cd18595 242 YVLSDPDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
967-1260 |
1.53e-155 |
|
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: 473.50 E-value: 1.53e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 967 TLFICLLYAGQNAVAIGANVWLSAWTND--VEEHGQQNNTSVRLGVYATLGILQGLLVMLSAFTMVVGAIQAARLLHTAL 1044
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDpaLNGTQDTEQRDYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1045 LHNQIRAPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLFNSFYTSISTIVVIVASTPLFCVVVLPLAVFYGFVQRF 1124
Cdd:cd18603 81 LHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1125 YVATSRQLKRLESVSRSPIFSHFSETVTGTSVIRAYGRVQDFKVLSDAKVDSNQKTTYPYIASNRWLGVHVEFVGNCVVL 1204
Cdd:cd18603 161 YVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 1205 FSALFAVIGRNSLNPGLVGLSVSYALQVTLSLNWMIRTLSDLESNIIAVERVKEYS 1260
Cdd:cd18603 241 FAALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEYS 296
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1283-1503 |
6.13e-134 |
|
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: 412.27 E-value: 6.13e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1283 GVVEFRNYSVRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQL 1362
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1363 TIIPQDPILFSGTLRMNLDPFGRYSDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRV 1442
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937891448 1443 LVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSP 1503
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
313-601 |
2.17e-115 |
|
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: 364.88 E-value: 2.17e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 313 GACFKLIQDLLSFINPQLLSILIRFISD-PTAPTWWGFLLAGLMFVSSTMQTLILHQHYHCIFVMALRIRTAIIGVIYRK 391
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSyPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 392 ALTITNSVKREYTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNGAVSMK 471
Cdd:cd18579 82 ALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 472 MKTYQVQQMKFKDSRIKLMSEILNGIKVLKLYAWEPTFLEQVEGIRQSELQLLRKGAYLQAISTFIWVCTPFMVTLITLG 551
Cdd:cd18579 162 ISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1937891448 552 VYVCVDknNVLDAEKAFVSLSLFNILKIPLNLLPQLISGMTQTSVSLKRI 601
Cdd:cd18579 242 TYVLLG--NPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1008-1518 |
3.55e-114 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 372.58 E-value: 3.55e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1008 LGVYATLGILQGLLVMLSAFTMVVGAIQAARLLHTALLHNQIRAPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLF 1087
Cdd:COG1132 64 LLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1088 NSFYTSISTIVVIVASTPLFCVVVLPLAVFYGFVQRFYVATSRQLKRLESVSRSPIFSHFSETVTGTSVIRAYGRVQDFK 1167
Cdd:COG1132 144 RSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREEREL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1168 VLSDAKVDSNQKTTYPYIASNRWLGVHVEFVGNCVVLFSALFAV--IGRNSLNPGLVGLSVSYALQVTLSLNWMIRTLSD 1245
Cdd:COG1132 224 ERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGllVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQ 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1246 LESNIIAVERVKEYSKTETEapwVLESNRAPEGWPRSGVVEFRNYSVRYRPGlELVLKNLTLHVQGGEKVGIVGRTGAGK 1325
Cdd:COG1132 304 LQRALASAERIFELLDEPPE---IPDPPGAVPLPPVRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1326 SSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDpFGR--YSDEDIWRTLELSHLSAF 1403
Cdd:COG1132 380 STLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIR-YGRpdATDEEVEEAAKAAQAHEF 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1404 VSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTI 1483
Cdd:COG1132 459 IEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTI 538
|
490 500 510
....*....|....*....|....*....|....*
gi 1937891448 1484 MDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGMAK 1518
Cdd:COG1132 539 RNADRILVLDDGRIVEQGTHEELLARGGLYARLYR 573
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
626-827 |
2.20e-113 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 355.62 E-value: 2.20e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWSKD---LPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSVAYVPQQAWIQNC 702
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 703 TLQENVLFGQPMNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDS 782
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1937891448 783 HVAKHIFDQVIGPEGvLAGKTRVLVTHGISFLPQTDFIIVLADGQ 827
Cdd:cd03250 161 HVGRHIFENCILGLL-LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
968-1260 |
2.90e-105 |
|
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: 337.17 E-value: 2.90e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 968 LFICLLYAGQNAVAIGANVWLSAWTNDVEEHGQQNNTSvRLGVYATLGIL-QGLLVMLSAFTMVVGAIQAARLLHTALLH 1046
Cdd:cd18580 2 LLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGY-YLGVYAALLVLaSVLLVLLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1047 NQIRAPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLFNSFYTSISTIVVIVASTPLFCVVVLPLAVFYGFVQRFYV 1126
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1127 ATSRQLKRLESVSRSPIFSHFSETVTGTSVIRAYGRVQDFKVLSDAKVDSNQKTTYPYIASNRWLGVHVEFVGNCVVLFS 1206
Cdd:cd18580 161 RTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALVV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1937891448 1207 ALFAVIGRNSLNPGLVGLSVSYALQVTLSLNWMIRTLSDLESNIIAVERVKEYS 1260
Cdd:cd18580 241 ALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1279-1503 |
4.65e-103 |
|
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: 327.45 E-value: 4.65e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1279 WPRSGVVEFRNYSVRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDL 1358
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1359 RSQLTIIPQDPILFSGTLRMNLDPFGRYSDEDIWRTLELshlsafvssqptgldfqcSEGGDNLSVGQRQLVCLARALLR 1438
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALRV------------------SEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937891448 1439 KSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSP 1503
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
967-1260 |
3.74e-97 |
|
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: 314.41 E-value: 3.74e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 967 TLFICLLYAGQnAVAIGANVWLSAWTNDveEHGQQNNTSVrlGVYATLGILQGLLVMLSAFTMVVGAIQAARLLHTALLH 1046
Cdd:cd18606 2 PLLLLLLILSQ-FAQVFTNLWLSFWTED--FFGLSQGFYI--GIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1047 NQIRAPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLFNSFYTSISTIVVIVASTPLFCVVVLPLAVFYGFVQRFYV 1126
Cdd:cd18606 77 RVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1127 ATSRQLKRLESVSRSPIFSHFSETVTGTSVIRAYGRVQDFKVLSDAKVDSNQKTTYPYIASNRWLGVHVEFVGNCVVLFS 1206
Cdd:cd18606 157 ASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLLVLIV 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1937891448 1207 ALFAVIGRNSLNPGLVGLSVSYALQVTLSLNWMIRTLSDLESNIIAVERVKEYS 1260
Cdd:cd18606 237 ALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
968-1260 |
7.82e-91 |
|
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: 296.69 E-value: 7.82e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 968 LFICLLYAGQNAVAIGANVWLSAWTNDVEEHGQQNNTSVR----LGVYATLGILQGLLVMLSAFTMVVGAIQAARLLHTA 1043
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEVSvlyyLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1044 LLHNQIRAPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLFNSFYTSISTIVVIVASTPLFCVVVLPLAVFYGFVQR 1123
Cdd:cd18604 82 LLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1124 FYVATSRQLKRLESVSRSPIFSHFSETVTGTSVIRAYGRVQDFKVLSDAKVDSNQKTTYPYIASNRWLGVHVEFVGNCVV 1203
Cdd:cd18604 162 LYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFS 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1937891448 1204 LFSALFAVIGRnSLNPGLVGLSVSYALQVTLSLNWMIRTLSDLESNIIAVERVKEYS 1260
Cdd:cd18604 242 FATAALLVYGP-GIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1009-1518 |
3.59e-89 |
|
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: 306.38 E-value: 3.59e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1009 GVYATLGILQGLLVMLSAFTMVVGAIQAARLLHT----------ALLHNQIRAPQSFFDTTPSGRILNRFSkDIYVIDEV 1078
Cdd:COG2274 190 QDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLgqridlrlssRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREF 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1079 LA-PTILMLFNSFYTSISTIVVIVASTPLFCVVVLPLAVFYG---FVQRFYVATSRQlkrlESVSRSPIFSHFSETVTGT 1154
Cdd:COG2274 269 LTgSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLlglLFQPRLRRLSRE----ESEASAKRQSLLVETLRGI 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1155 SVIRAYG----RVQDFKVLSDAKVDSNQKTTYPYIASNRWLGVhVEFVGNCVVLFSALFAVIGrNSLNPG-LVGlSVSYA 1229
Cdd:COG2274 345 ETIKALGaesrFRRRWENLLAKYLNARFKLRRLSNLLSTLSGL-LQQLATVALLWLGAYLVID-GQLTLGqLIA-FNILS 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1230 LQVTLSLNWMIRTLSDLESNIIAVERVKEYSKTETEAPwvleSNRAPEGWPR-SGVVEFRNYSVRYRPGLELVLKNLTLH 1308
Cdd:COG2274 422 GRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPERE----EGRSKLSLPRlKGDIELENVSFRYPGDSPPVLDNISLT 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1309 VQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNL---DPfgR 1385
Cdd:COG2274 498 IKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDP--D 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1386 YSDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIR 1465
Cdd:COG2274 576 ATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLR 655
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 1466 TQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGMAK 1518
Cdd:COG2274 656 RLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
314-601 |
4.51e-87 |
|
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: 286.70 E-value: 4.51e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 314 ACFKLIQDLLSFINPQLLSILIRFISDPTA-PTWWGFLLAGLMFVSSTMQTLILHQHYHCIFVMALRIRTAIIGVIYRKA 392
Cdd:cd18596 3 ALLAVLSSVLSFAPPFFLNRLLRYLEDPGEdATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 393 LTI-------------------TNSVKREYTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSALA 453
Cdd:cd18596 83 LRRrdksgssksseskkkdkeeDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 454 GVAVIVLLIPLNGAVSMKMKTYQVQQMKFKDSRIKLMSEILNGIKVLKLYAWEPTFLEQVEGIRQSELQLLRKGAYLQAI 533
Cdd:cd18596 163 GLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937891448 534 STFIWVCTPFMVTLITLGVYVCVDKNNvLDAEKAFVSLSLFNILKIPLNLLPQLISGMTQTSVSLKRI 601
Cdd:cd18596 243 LSLLWFLIPILVTVVTFATYTLVMGQE-LTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
316-601 |
1.62e-86 |
|
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: 284.11 E-value: 1.62e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 316 FKLIQDLLSFINPQLLSILIRFISDPTAPTWWGFLLAGLMFVSSTMQTLILHQHYHCIFVMALRIRTAIIGVIYRKALTI 395
Cdd:cd18559 5 IKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 396 TNSVKREYTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNGAVSMKMKTY 475
Cdd:cd18559 85 PISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 476 QVQQMKFKDSRIKLMSEILNGIKVLKLYAWEPTFLEQVEGIRQSELQLLRKGAYLQAISTFIWVCTPFMVTLITLGVYVC 555
Cdd:cd18559 165 KRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVS 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1937891448 556 VDKNNVLDAEKAFVSLSLFNILKIPLNLLPQLISGMTQTSVSLKRI 601
Cdd:cd18559 245 RHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
967-1260 |
6.82e-85 |
|
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: 280.26 E-value: 6.82e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 967 TLFICLLYAGQNAVAIGANVWLSAWTNDVEEHG-----------QQNNTSVRLGVYATLGILQGLLVMLSAFTMVVGAIQ 1035
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADWTEANHDVAsvvfnitssslEDDEVSYYISVYAGLSLGAVILSLVTNLAGELAGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1036 AARLLHTALLHNQIRAPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLFNSFYTSISTIVVIVASTPLFCVVVLPLA 1115
Cdd:cd18602 81 AARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1116 VFYGFVQRFYVATSRQLKRLESVSRSPIFSHFSETVTGTSVIRAYGRVQDFKVLSDAKVDSNQKTTYPYIASNRWLGVHV 1195
Cdd:cd18602 161 IVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937891448 1196 EFVGNCVVLFSALFAVIG--RNSLNPGLVGLSVSYALQVTLSLNWMIRTLSDLESNIIAVERVKEYS 1260
Cdd:cd18602 241 DYLGAVIVFLAALSSLTAalAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
316-601 |
3.99e-80 |
|
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: 265.95 E-value: 3.99e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 316 FKLIQDLLSFINPQLLSILIRFISDPTAPTWWGFLLAGLMFVSSTMQTlILHQHYHciFVMA---LRIRTAIIGVIYRKA 392
Cdd:cd18598 5 LKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGA-LLSSHYN--FQMNkvsLKVRAALVTAVYRKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 393 LTITNSVKREYTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNGAVSMKM 472
Cdd:cd18598 82 LRVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 473 KTYQVQQMKFKDSRIKLMSEILNGIKVLKLYAWEPTFLEQVEGIRQSELQLLRKGAYLQAISTFIWVCTPFMVTLITLGV 552
Cdd:cd18598 162 GALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTPVLISILTFAT 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1937891448 553 YVCVdkNNVLDAEKAFVSLSLFNILKIPLNLLPQLISGMTQTSVSLKRI 601
Cdd:cd18598 242 YVLM--GNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1283-1508 |
3.49e-79 |
|
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: 262.15 E-value: 3.49e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1283 GVVEFRNYSVRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQL 1362
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1363 TIIPQDPILFSGTLRMNLDPFGRYSDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRV 1442
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 1443 LVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIA 1508
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLA 243
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
968-1259 |
4.18e-78 |
|
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: 260.54 E-value: 4.18e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 968 LFICLLYAGQNAvaigANVWLSAWTNDvEEHGQQNNTSVR----LGVYATLGILQGLLVMLSAFTMVVGAIQAARLLHTA 1043
Cdd:cd18605 6 LSLILMQASRNL----IDFWLSYWVSH-SNNSFFNFINDSfnffLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1044 LLHNQIRAPQSFFDTTPSGRILNRFSKDIYVIDEVLaPTILMLF-NSFYTSISTIVVIVASTPLFCVVVLPLAVFYGFVQ 1122
Cdd:cd18605 81 LLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSL-PFILNILlAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1123 RFYVATSRQLKRLESVSRSPIFSHFSETVTGTSVIRAYGRVQDFKVLSDAKVDSNQKTTYPYIASNRWLGVHVEFVGNCV 1202
Cdd:cd18605 160 RYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVLI 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1203 VLFSALFAVIGRN---SLNPGLVGLSVSYALQVTLSLNWMIRTLSDLESNIIAVERVKEY 1259
Cdd:cd18605 240 VTFVALTAVVQHFfglSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQY 299
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
312-601 |
2.89e-75 |
|
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: 251.99 E-value: 2.89e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 312 MGACFKLIQDLLSFINPQLLSILIRFISD-----PTAPTWWGFLLAGLMFVSSTMQTLILHQHYHCIFVMALRIRTAIIG 386
Cdd:cd18597 1 LAGLLKLLADVLQVLSPLLLKYLINFVEDaylggPPPSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 387 VIYRKALTITNSVKREYTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNG 466
Cdd:cd18597 81 AIYRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 467 AVSMKMKTYQVQQMKFKDSRIKLMSEILNGIKVLKLYAWEPTFLEQVEGIRQSELQLLRKGAYLQAISTFIWVCTPFMVT 546
Cdd:cd18597 161 FLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLAS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1937891448 547 LITLGVYVCVdkNNVLDAEKAFVSLSLFNILKIPLNLLPQLISGMTQTSVSLKRI 601
Cdd:cd18597 241 MLSFITYYAT--GHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
298-849 |
5.54e-75 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 261.25 E-value: 5.54e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 298 FLRALVRTFTSSLLMGACFKLIQDLLSFINPQLLSILIRFI---SDPTAPTWWGFLLAGLMFVSSTMQTLilhqHYHCIF 374
Cdd:COG1132 11 RLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALlagGDLSALLLLLLLLLGLALLRALLSYL----QRYLLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 375 VMALRIRTAIIGVIYRKALTITNSVKREYTVGEMVNLMSVDAQRFMD-VSPFINLLWSAPLQVILAIYFLWQILGPSALA 453
Cdd:COG1132 87 RLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQfLAHGLPQLVRSVVTLIGALVVLFVIDWRLALI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 454 GVAVIVLLIPLNGAVSMKMKTYQVQQMKFKDSRIKLMSEILNGIKVLKLYAWEPT----FLEQVEGIRQSELQLLRKGAY 529
Cdd:COG1132 167 VLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERelerFREANEELRRANLRAARLSAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 530 LQAISTFIWVCTPFMVTL----------ITLGVYVcvdknnvldaekAFVSLSLFniLKIPLNLLPQLISGMTQTSVSLK 599
Cdd:COG1132 247 FFPLMELLGNLGLALVLLvggllvlsgsLTVGDLV------------AFILYLLR--LFGPLRQLANVLNQLQRALASAE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 600 RIQDFLNQDELDPQCVERKTISPGR-AITIHNGTFSWSKDlPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEME 678
Cdd:COG1132 313 RIFELLDEPPEIPDPPGAVPLPPVRgEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 679 KLEGAVSVKG-------------SVAYVPQQAWIQNCTLQENVLFGqpmNPKRYQQALETCALLADLDV----LPGGDQT 741
Cdd:COG1132 392 PTSGRILIDGvdirdltleslrrQIGVVPQDTFLFSGTIRENIRYG---RPDATDEEVEEAAKAAQAHEfieaLPDGYDT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 742 EIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVigpEGVLAGKTRVLVTHGISFLPQTDFII 821
Cdd:COG1132 469 VVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEAL---ERLMKGRTTIVIAHRLSTIRNADRIL 545
|
570 580
....*....|....*....|....*...
gi 1937891448 822 VLADGQITEMGHYSELLQHDGSFANFLR 849
Cdd:COG1132 546 VLDDGRIVEQGTHEELLARGGLYARLYR 573
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
288-850 |
4.91e-71 |
|
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: 253.60 E-value: 4.91e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 288 KARPKTKKPSFLRALVRTFTSSLLMGACFKLIQDLLSFINPQLLSILI-RFISDPTAPTWW----GFLLAGLM-FVSSTM 361
Cdd:COG2274 136 KRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIdRVLPNQDLSTLWvlaiGLLLALLFeGLLRLL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 362 QTLILhqhyhciFVMALRIRTAIIGVIYRKALTITNSVKREYTVGEMVN-LMSVDA-QRFMdVSPFINLLWSAPlQVILA 439
Cdd:COG2274 216 RSYLL-------LRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASrFRDVESiREFL-TGSLLTALLDLL-FVLIF 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 440 IYFLWQILGPSALAGVAVIVLLIPLNGAVSMKMKTYQVQQMKFKDSRIKLMSEILNGIKVLKLYAWEPTFLEQVEGI--- 516
Cdd:COG2274 287 LIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLlak 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 517 -RQSELQLLRKGAYLQAISTFIWVCTPfmVTLITLGVYVcvdknnVLDAEkafvsLSL-----FNILKI----PLNLLPQ 586
Cdd:COG2274 367 yLNARFKLRRLSNLLSTLSGLLQQLAT--VALLWLGAYL------VIDGQ-----LTLgqliaFNILSGrflaPVAQLIG 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 587 LISGMTQTSVSLKRIQDFLNQdELDPQcVERKTISPGR---AITIHNGTFSWSKDLPPTLHSLNIQIPKGALVAVVGPVG 663
Cdd:COG2274 434 LLQRFQDAKIALERLDDILDL-PPERE-EGRSKLSLPRlkgDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSG 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 664 CGKSSLVSALLGEMEKLEGAVSVKG-------------SVAYVPQQAWIQNCTLQENVLFGQP-MNPKRYQQALETCALL 729
Cdd:COG2274 512 SGKSTLLKLLLGLYEPTSGRILIDGidlrqidpaslrrQIGVVLQDVFLFSGTIRENITLGDPdATDEEIIEAARLAGLH 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 730 ADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVigpEGVLAGKTRVLVTH 809
Cdd:COG2274 592 DFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENL---RRLLKGRTVIIIAH 668
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1937891448 810 GISFLPQTDFIIVLADGQITEMGHYSELLQHDGSFANFLRN 850
Cdd:COG2274 669 RLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
313-601 |
5.50e-71 |
|
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: 240.60 E-value: 5.50e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 313 GACFKLIQDLLSFINPQLLSILIRFISDPTAPTWW------------------GFLLAGLMFVSSTMQTLILHQHYHCIF 374
Cdd:cd18591 2 GGILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNstdklsvsyvtveeffsnGYVLAVILFLALLLQATFSQASYHIVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 375 VMALRIRTAIIGVIYRKALTIT--NSVKREYTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSAL 452
Cdd:cd18591 82 REGIRLKTALQAMIYEKALRLSswNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 453 AGVAVIVLLIPLNGAVSMKMKTYQVQQMKFKDSRIKLMSEILNGIKVLKLYAWEPTFLEQVEGIRQSELQLLRKGAYLQA 532
Cdd:cd18591 162 IGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWS 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937891448 533 ISTFIWVCTPFMVTLITLGVYVCVdKNNVLDAEKAFVSLSLFNILKIPLNLLPQLISGMTQTSVSLKRI 601
Cdd:cd18591 242 LMTFLTQASPILVTLVTFGLYPYL-EGEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
626-826 |
2.88e-69 |
|
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: 231.84 E-value: 2.88e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWSKDLPpTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAV-----------------SVKG 688
Cdd:cd03290 1 VQVTNGYFSWGSGLA-TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 689 SVAYVPQQAWIQNCTLQENVLFGQPMNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDA 768
Cdd:cd03290 80 SVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 769 NIFLLDDPLSAVDSHVAKHIFDqvigpEGVLA-----GKTRVLVTHGISFLPQTDFIIVLADG 826
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQ-----EGILKflqddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1263-1511 |
4.25e-68 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 240.82 E-value: 4.25e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1263 ETEAPWVLESNRAPEgWPRSGVVEFRNYSVRYrPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGE 1342
Cdd:COG4988 316 DAPEPAAPAGTAPLP-AAGPPSIELEDVSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1343 IFIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDpFGR--YSDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGD 1420
Cdd:COG4988 394 ILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLR-LGRpdASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGR 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1421 NLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEF 1500
Cdd:COG4988 473 GLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQ 552
|
250
....*....|.
gi 1937891448 1501 DSPVNLIAAGG 1511
Cdd:COG4988 553 GTHEELLAKNG 563
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1283-1511 |
1.22e-67 |
|
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: 227.88 E-value: 1.22e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1283 GVVEFRNYSVRYRPGlELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQL 1362
Cdd:cd03254 1 GEIEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1363 TIIPQDPILFSGTLRMNLDpFGR--YSDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKS 1440
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIR-LGRpnATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937891448 1441 RVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGG 1511
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
963-1260 |
2.82e-66 |
|
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: 227.06 E-value: 2.82e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 963 GLCTTLFICLLYAGQNAVAIGANVWLSAWTNDVEEHGQ--QNNTSVRLG-------------VYATLGILQGLLVMLSAF 1027
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGSGNTTnnVDNSTVDSGnisdnpdlnfyqlVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1028 TMVVGAIQAARLLHTALLHNQIRAPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLFNSFYTSISTIVVIVASTPLF 1107
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1108 CVVVLPLAVFYGFVQRFYVATSRQLKRLESVSRSPIFSHFSETVTGTSVIRAYGRVQDFKVLSDAKVDSNQKTTYPYIAS 1187
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 1188 NRWLGVHVEFVGNCVVLFSALFAVIGRNSLNPGLVGLSVSYALQVTLSLNWMIRTLSDLESNIIAVERVKEYS 1260
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
316-602 |
7.23e-66 |
|
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: 225.20 E-value: 7.23e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 316 FKLIQDLLSFINPQLLSILIR-FISDPTAPTWWGFLLAGLMFVSSTMQTLILHQHYHCIFVMALRIRTAIIGVIYRKALT 394
Cdd:cd18594 5 LLFLEESLKIVQPLLLGRLVAyFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTLK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 395 ITNSVKREYTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNGAVSMKMKT 474
Cdd:cd18594 85 LSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 475 YQVQQMKFKDSRIKLMSEILNGIKVLKLYAWEPTFLEQVEGIRQSELQLLRKGAYLQAISTFIWVCTPFMVTLITLGVYV 554
Cdd:cd18594 165 YRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYV 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1937891448 555 CVdkNNVLDAEKAFVSLSLFNILKIPLNL-LPQLISGMTQTSVSLKRIQ 602
Cdd:cd18594 245 LT--GNTLTARKVFTVISLLNALRMTITRfFPESIQTLSESRVSLKRIQ 291
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
313-601 |
1.45e-63 |
|
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: 218.63 E-value: 1.45e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 313 GACFKLIQDLLSFINPQLLSILIRFISDP--TAPTWWGFLLAGLMFVSSTMQTLILHQHYHCIFVMALRIRTAIIGVIYR 390
Cdd:cd18593 2 LGIFLFLEEAIRVVQPIFLGKLIRYFEGNgsSISLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIYR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 391 KALTITNSVKREYTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNGAVSM 470
Cdd:cd18593 82 KALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 471 KMKTYQVQQMKFKDSRIKLMSEILNGIKVLKLYAWEPTFLEQVEGIRQSELQLLRKGAYLQAISTFIWVCTPFMVTLITL 550
Cdd:cd18593 162 LFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLTF 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 551 GVYVCVDknNVLDAEKAFVSLSLFNILKIPLNL-LPQLISGMTQTSVSLKRI 601
Cdd:cd18593 242 LAYILLG--NILTAERVFVTMALYNAVRLTMTLfFPFAIQFGSELSVSIRRI 291
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1014-1513 |
2.15e-63 |
|
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: 227.29 E-value: 2.15e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1014 LGILQGLLVMLSAFTMVVGAIQAARLLHTALLHNQIRAPQSFFDTTPSGRILNRFSKDI-----YVID----------EV 1078
Cdd:TIGR02203 63 LAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSeqvasAATDafivlvretlTV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1079 LAPTILMLFNSFYTSistivvivastpLFCVVVLPLAVFygfvqrfyvATSRQLKRLESVSRSPIFSH------FSETVT 1152
Cdd:TIGR02203 143 IGLFIVLLYYSWQLT------------LIVVVMLPVLSI---------LMRRVSKRLRRISKEIQNSMgqvttvAEETLQ 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1153 GTSVIRAYG----RVQDFKVLSDAKVDSNQKTTYPYIASNRWLGVhVEFVGNCVVLFSALFAViGRNSLNPGLVGLSVSY 1228
Cdd:TIGR02203 202 GYRVVKLFGgqayETRRFDAVSNRNRRLAMKMTSAGSISSPITQL-IASLALAVVLFIALFQA-QAGSLTAGDFTAFITA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1229 ALQVTLSLNWMIRTLSDLESNIIAVERVKEYSKTETEAPwvlESNRAPEgwpRS-GVVEFRNYSVRYRPGLELVLKNLTL 1307
Cdd:TIGR02203 280 MIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKD---TGTRAIE---RArGDVEFRNVTFRYPGRDRPALDSISL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1308 HVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLdPFGR-- 1385
Cdd:TIGR02203 354 VIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNI-AYGRte 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1386 -YSDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTI 1464
Cdd:TIGR02203 433 qADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAAL 512
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1937891448 1465 RTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIF 1513
Cdd:TIGR02203 513 ERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLY 561
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1285-1516 |
3.02e-63 |
|
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: 215.17 E-value: 3.02e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTI 1364
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1365 IPQDPILFSGTLRMNLdPFGRY--SDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRV 1442
Cdd:cd03251 81 VSQDVFLFNDTVAENI-AYGRPgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937891448 1443 LVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGM 1516
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1285-1495 |
4.92e-62 |
|
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: 209.16 E-value: 4.92e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTI 1364
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1365 IPQDPILFSGTLRMNLdpfgrysdediwrtlelshlsafvssqptgldfqcseggdnLSVGQRQLVCLARALLRKSRVLV 1444
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1937891448 1445 LDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKG 1495
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
963-1260 |
8.02e-62 |
|
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: 214.49 E-value: 8.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 963 GLCTTLFICLLYAGQNAVAIGANVWLSAWTN-----DVEEHGQQNNTSVR-----------LGVYATLGILQGLLVMLSA 1026
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANleeklNDTTDRVQGENSTNvdiedldrdfnLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1027 FTMVVGAIQAARLLHTALLHNQIRAPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLFNSFYTSISTIVVIVASTPL 1106
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1107 FCVVVLPLAVFYGFVQRFYVATSRQLKRLESVSRSPIFSHFSETVTGTSVIRAYGRVQDFKVLSDAKVDSNQKTTYPYIA 1186
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937891448 1187 SNRWLGVHVEFVgnC-----VVLFSALFAvigRNSLNPGLVGLSVSYALQVTLSLNWMIRTLSDLESNIIAVERVKEYS 1260
Cdd:cd18601 241 TSRWLAVRLDAL--CalfvtVVAFGSLFL---AESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEYS 314
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1061-1518 |
1.15e-61 |
|
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: 221.95 E-value: 1.15e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1061 SGRILNRFSKDIYVIDE----VLAPTIlmlfnsfytsiSTIVVIVASTPLFCVVVLPLAVFYG------------FVQRF 1124
Cdd:COG4987 111 SGDLLNRLVADVDALDNlylrVLLPLL-----------VALLVILAAVAFLAFFSPALALVLAlglllaglllplLAARL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1125 YVATSRQLKRLESVSRSpifsHFSETVTGTSVIRAYGRVQDFK---VLSDAKVDSNQKTtypyIASNRWLGvhvEFVGNC 1201
Cdd:COG4987 180 GRRAGRRLAAARAALRA----RLTDLLQGAAELAAYGALDRALarlDAAEARLAAAQRR----LARLSALA---QALLQL 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1202 VVLFSALFAVI------GRNSLNPGLVGLSVSYALQVTLSLNWMIRTLSDLESNIIAVERVKEYSKTETEAPwvleSNRA 1275
Cdd:COG4987 249 AAGLAVVAVLWlaaplvAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPPAVT----EPAE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1276 PEGWPRSGVVEFRNYSVRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGL 1355
Cdd:COG4987 325 PAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDE 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1356 HDLRSQLTIIPQDPILFSGTLRMNL---DPfgRYSDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCL 1432
Cdd:COG4987 405 DDLRRRIAVVPQRPHLFDTTLRENLrlaRP--DATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLAL 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1433 ARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGI 1512
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGR 562
|
....*.
gi 1937891448 1513 FYGMAK 1518
Cdd:COG4987 563 YRQLYQ 568
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
968-1260 |
2.49e-61 |
|
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: 212.07 E-value: 2.49e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 968 LFICLLYAgqnavAIGANVWLSAWTNDvEEHGQQNNTSVRLGVYATLGILQGLLVMLSAFTMVVGAIQAARLLHTALLHN 1047
Cdd:cd18559 7 LVLCNHVF-----SGPSNLWLLLWFDD-PVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1048 QIRAPQSFFDTTPSGRILNRFSKDIYVIDEvLAPTILMLFN-SFYTSISTIVVIVASTPLFcVVVLPLAVFYGFVQRFYV 1126
Cdd:cd18559 81 ALRSPISFFERTPSGELVNLFSKDLDRVDS-MAPQVIKMWMgPLQNVIGLYLLILLAGPMA-AVGIPLGLLYVPVNRVYA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1127 ATSRQLKRLESVSRSPIFSHFSETVTGTSVIRAYGRVQDFKVLSDAKVDsNQKTTYPYIASNRWLGVHVEFVGNCVVLFS 1206
Cdd:cd18559 159 ASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVRLWCVGPCIVLFA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1937891448 1207 ALFAVIGRNSLNpGLVGLSVSYALQVTLSLNWMIRTLSDLESNIIAVERVKEYS 1260
Cdd:cd18559 238 SFFAYVSRHSLA-GLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1285-1516 |
5.06e-58 |
|
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: 200.53 E-value: 5.06e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYRPGLElVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTI 1364
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1365 IPQDPILFSGTLRMNLDpFGRY--SDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRV 1442
Cdd:cd03253 80 VPQDTVLFNDTIGYNIR-YGRPdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937891448 1443 LVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGM 1516
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1285-1518 |
1.61e-57 |
|
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: 198.92 E-value: 1.61e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRY--RPGLElVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQL 1362
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1363 TIIPQDPILFSGTLRMNLDpFGRYS--DEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKS 1440
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIR-YGKPDatDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937891448 1441 RVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGMAK 1518
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVK 236
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1283-1498 |
2.66e-56 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 194.73 E-value: 2.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1283 GVVEFRNYSVRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQL 1362
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1363 TIIPQDPILFSGTLRMNLDPFGRY-SDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSR 1441
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937891448 1442 VLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKG-VVA 1498
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGrIVA 218
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1202-1516 |
5.35e-56 |
|
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: 206.21 E-value: 5.35e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1202 VVLFSALFAVIGRNSLnpGLVGLSVSYALQVTLSLNWM------IRT-LSDLEsniiavervkEYSKTETEAPWVLESNR 1274
Cdd:COG5265 280 MMLMAAQGVVAGTMTV--GDFVLVNAYLIQLYIPLNFLgfvyreIRQaLADME----------RMFDLLDQPPEVADAPD 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1275 APEGWPRSGVVEFRNYSVRYRPGLElVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIG 1354
Cdd:COG5265 348 APPLVVGGGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVT 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1355 LHDLRSQLTIIPQDPILFSGTLRMNLdpfgRY-----SDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQL 1429
Cdd:COG5265 427 QASLRAAIGIVPQDTVLFNDTIAYNI----AYgrpdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQR 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1430 VCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAA 1509
Cdd:COG5265 503 VAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQ 582
|
....*..
gi 1937891448 1510 GGIFYGM 1516
Cdd:COG5265 583 GGLYAQM 589
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1283-1513 |
1.29e-55 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 195.07 E-value: 1.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1283 GVVEFRNYSVRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAaEGEIFIDGLNVAHIGLHDLRSQL 1362
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1363 TIIPQDPILFSGTLRMNLDPFGRYSDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRV 1442
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937891448 1443 LVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIF 1513
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
422-849 |
5.71e-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: 202.30 E-value: 5.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 422 VSPFInllwSAPLQVILAIYFLWQILGPSAL---AGVAVIVLLIPLNGAVSMKMKTYQVQQMKfKDSRIKLMsEILNGIK 498
Cdd:COG4987 133 LLPLL----VALLVILAAVAFLAFFSPALALvlaLGLLLAGLLLPLLAARLGRRAGRRLAAAR-AALRARLT-DLLQGAA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 499 VLKLYAWEPTFLEQVEGIRQSELQLLRKGAYLQAISTFIwvcTPFMVTLITLGV-YVCVD--KNNVLDAEK----AFVSL 571
Cdd:COG4987 207 ELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQAL---LQLAAGLAVVAVlWLAAPlvAAGALSGPLlallVLAAL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 572 SLFNILkiplNLLPQLISGMTQTSVSLKRIQDFLNQDELDPQCVERKTISPGRAITIHNGTFSWSKDLPPTLHSLNIQIP 651
Cdd:COG4987 284 ALFEAL----APLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLP 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 652 KGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-------------SVAYVPQQAWIQNCTLQENVLFGQPM-NPK 717
Cdd:COG4987 360 PGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlrdldeddlrrRIAVVPQRPHLFDTTLRENLRLARPDaTDE 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 718 RYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIgpeG 797
Cdd:COG4987 440 ELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLL---E 516
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 798 VLAGKTRVLVTHGISFLPQTDFIIVLADGQITEMGHYSELLQHDGSFANFLR 849
Cdd:COG4987 517 ALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
318-601 |
7.31e-55 |
|
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: 193.16 E-value: 7.31e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 318 LIQDLLSFINPQ-LLSILIRFISDPTAPTWWGFLLAGLMFVSSTMQTLILHQHYHCIFVMALRIRTAIIGVIYRKALTIt 396
Cdd:cd18592 7 LISLIFGFIGPTiLIRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYKKILRL- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 397 NSVKrEYTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNGAVSMKMKTYQ 476
Cdd:cd18592 86 RSLG-DKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 477 VQQMKFKDSRIKLMSEILNGIKVLKLYAWEPTFLEQVEGIRQSELQLLRKGAYLQAISTFIWVCTPFMVTLITLGVYVCV 556
Cdd:cd18592 165 RKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFLAHVAL 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1937891448 557 DKNnvLDAEKAFVSLSLFNILKIPLNLLPQLISGMTQTSVSLKRI 601
Cdd:cd18592 245 GND--LTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
299-842 |
3.14e-53 |
|
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: 196.90 E-value: 3.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 299 LRALVRTFTSSLLMGACFKLIQDLL----SFINPQLLSILIRFISDPTAPTWWGFLLAGLMFVsstmQTLILHQHYHCIF 374
Cdd:COG4988 8 LKRLARGARRWLALAVLLGLLSGLLiiaqAWLLASLLAGLIIGGAPLSALLPLLGLLLAVLLL----RALLAWLRERAAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 375 VMALRIRTAIIGVIYRKALTITNSVKREYTVGEMVNLMS--VDAqrfMD--VSPFINLLWSA---PLQVILAIYFLwqil 447
Cdd:COG4988 84 RAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTegVEA---LDgyFARYLPQLFLAalvPLLILVAVFPL---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 448 gpSALAGV--AVIVLLIPLNGA-VSMKMKTYQVQQMKfkdsRIKLMS----EILNGIKVLKLYAWEPTFLEQV----EGI 516
Cdd:COG4988 157 --DWLSGLilLVTAPLIPLFMIlVGKGAAKASRRQWR----ALARLSghflDRLRGLTTLKLFGRAKAEAERIaeasEDF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 517 RQSELQLLRkgayLQAISTFIwvcTPFMVTL-ITLG-VYVCVdknNVLDAekafvSLSLFNILKIpLNLLP-------QL 587
Cdd:COG4988 231 RKRTMKVLR----VAFLSSAV---LEFFASLsIALVaVYIGF---RLLGG-----SLTLFAALFV-LLLAPefflplrDL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 588 IS----GMTQTSVSlKRIQDFLNQDELDPQCVERKTISPGR-AITIHNGTFSWSKDlPPTLHSLNIQIPKGALVAVVGPV 662
Cdd:COG4988 295 GSfyhaRANGIAAA-EKIFALLDAPEPAAPAGTAPLPAAGPpSIELEDVSFSYPGG-RPALDGLSLTIPPGERVALVGPS 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 663 GCGKSSLVSALLGEMEKLEGAVSVKG-------------SVAYVPQQAWIQNCTLQENVLFGQP-MNPKRYQQALETCAL 728
Cdd:COG4988 373 GAGKSTLLNLLLGFLPPYSGSILINGvdlsdldpaswrrQIAWVPQNPYLFAGTIRENLRLGRPdASDEELEAALEAAGL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 729 LADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVigpEGVLAGKTRVLVT 808
Cdd:COG4988 453 DEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQAL---RRLAKGRTVILIT 529
|
570 580 590
....*....|....*....|....*....|....
gi 1937891448 809 HGISFLPQTDFIIVLADGQITEMGHYSELLQHDG 842
Cdd:COG4988 530 HRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1285-1514 |
1.02e-50 |
|
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: 179.60 E-value: 1.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTI 1364
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1365 IPQDPILFSGTLRMNL---DPfgRYSDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSR 1441
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 1442 VLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFY 1514
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1012-1516 |
1.72e-50 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 189.54 E-value: 1.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1012 ATLGILQGLLVMLSAftmvVGAIQAARllhTALLHNQIRAPQSFFDTTPSGRILNRFSKDIYVIDEV---LAPTIL---- 1084
Cdd:PRK10790 79 AGLHYAQSLLFNRAA----VGVVQQLR---TDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLyvtVVATVLrsaa 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1085 ----MLFNSFytSISTIVVIVASTpLFCVVVLPLAVFygfvQRFYVATSRQLKRLesvsRSPIFSHFSETVTGTSVIRAY 1160
Cdd:PRK10790 152 ligaMLVAMF--SLDWRMALVAIM-IFPAVLVVMVIY----QRYSTPIVRRVRAY----LADINDGFNEVINGMSVIQQF 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1161 GRVQDF-KVLSDAkvdSNQKttypYIASNRWLGVHVEFVGNCVVLFSA-----LFAVIGRNSlnPGLVGLSVSYALQVTL 1234
Cdd:PRK10790 221 RQQARFgERMGEA---SRSH----YMARMQTLRLDGFLLRPLLSLFSAlilcgLLMLFGFSA--SGTIEVGVLYAFISYL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1235 S-LNWMIRTL----SDLESNIIAVERVKEyskteteapwVLESNRAPEGWP----RSGVVEFRNYSVRYRPGlELVLKNL 1305
Cdd:PRK10790 292 GrLNEPLIELttqqSMLQQAVVAGERVFE----------LMDGPRQQYGNDdrplQSGRIDIDNVSFAYRDD-NLVLQNI 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1306 TLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLdPFGR 1385
Cdd:PRK10790 361 NLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANV-TLGR 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1386 -YSDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTI 1464
Cdd:PRK10790 440 dISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL 519
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 1465 RTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGM 1516
Cdd:PRK10790 520 AAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQM 571
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1016-1518 |
2.43e-49 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 188.24 E-value: 2.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1016 ILQGLLVMLSAfTMVVGAIQAA---RLLhtallhnqiRAPQSFFDTTPSGRILNRFSKdIYVIDEVLAPTIL-MLFNSFY 1091
Cdd:TIGR03797 194 LAQSLAVLRLE-TRMDASLQAAvwdRLL---------RLPVSFFRQYSTGDLASRAMG-ISQIRRILSGSTLtTLLSGIF 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1092 TSISTIVVIVASTPL------FCVVVLPLAVFYGFVQRFYVatsRQLKRLESvsrsPIFSHFSETVTGTSVIRAYGrvqd 1165
Cdd:TIGR03797 263 ALLNLGLMFYYSWKLalvavaLALVAIAVTLVLGLLQVRKE---RRLLELSG----KISGLTVQLINGISKLRVAG---- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1166 fkvlsdAKVDSNQKTTYPYiASNRWLGVHVEFVGNCVVLFSA---------LFAVIGRNSLNPGL-VGLSVSYAL---QV 1232
Cdd:TIGR03797 332 ------AENRAFARWAKLF-SRQRKLELSAQRIENLLTVFNAvlpvltsaaLFAAAISLLGGAGLsLGSFLAFNTafgSF 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1233 TLSLNWMIRTLSDLESNIIAVERVKEYSKTETEApwvlESNRAPEGwPRSGVVEFRNYSVRYRPGLELVLKNLTLHVQGG 1312
Cdd:TIGR03797 405 SGAVTQLSNTLISILAVIPLWERAKPILEALPEV----DEAKTDPG-KLSGAIEVDRVTFRYRPDGPLILDDVSLQIEPG 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1313 EKVGIVGRTGAGKSSmtlcLFRIL---EAAE-GEIFIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSD 1388
Cdd:TIGR03797 480 EFVAIVGPSGSGKST----LLRLLlgfETPEsGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTL 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1389 EDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQf 1468
Cdd:TIGR03797 556 DEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL- 634
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1469 eDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGMAK 1518
Cdd:TIGR03797 635 -KVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLAR 683
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
641-851 |
3.90e-48 |
|
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: 173.89 E-value: 3.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSVAYVPQQAWIQNCTLQENVLFGQPMNPKRYQ 720
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 721 QALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGPegVLA 800
Cdd:cd03291 131 SVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCK--LMA 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1937891448 801 GKTRVLVTHGISFLPQTDFIIVLADGQITEMGHYSELLQHDGSFANFLRNY 851
Cdd:cd03291 209 NKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGY 259
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1027-1516 |
1.22e-47 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 183.38 E-value: 1.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1027 FTMVVGAIQAArlLHTALLHNQIRAPQSFFDTTPSGRILNRFSKDIYVIDEVLAPT---------------ILMLFNSFY 1091
Cdd:TIGR00958 225 FNYTMARINLR--IREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNvnvllrnlvmllgllGFMLWLSPR 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1092 TSISTIVvivaSTPLfcvvVLPLAVFYGfvqRFYVATSRQLKrlESVSRSPIFSHfsETVTGTSVIRAYG----RVQDFK 1167
Cdd:TIGR00958 303 LTMVTLI----NLPL----VFLAEKVFG---KRYQLLSEELQ--EAVAKANQVAE--EALSGMRTVRSFAaeegEASRFK 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1168 V-LSDAKvDSNQKTTYPYIA---SNRWLGVHVeFVGncvVLFSALFAVIgRNSLNPGLVGLSVSYALQVTLSLNWMIRTL 1243
Cdd:TIGR00958 368 EaLEETL-QLNKRKALAYAGylwTTSVLGMLI-QVL---VLYYGGQLVL-TGKVSSGNLVSFLLYQEQLGEAVRVLSYVY 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1244 SDLESNIIAVERVKEYSKTETEAPwvLESNRAPEgwPRSGVVEFRNYSVRY--RPGLeLVLKNLTLHVQGGEKVGIVGRT 1321
Cdd:TIGR00958 442 SGMMQAVGASEKVFEYLDRKPNIP--LTGTLAPL--NLEGLIEFQDVSFSYpnRPDV-PVLKGLTFTLHPGEVVALVGPS 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1322 GAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLdPFG--RYSDEDIWRTLELSH 1399
Cdd:TIGR00958 517 GSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENI-AYGltDTPDEEIMAAAKAAN 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1400 LSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTirTQFEDCTVLTIAHR 1479
Cdd:TIGR00958 596 AHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHR 673
|
490 500 510
....*....|....*....|....*....|....*..
gi 1937891448 1480 LNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGM 1516
Cdd:TIGR00958 674 LSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1255-1523 |
1.53e-46 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 177.85 E-value: 1.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1255 RVKEYSKTETEAPWVLESNRAPEGWPRSGVVEFRNYSVRY---RPGLElvlkNLTLHVQGGEKVGIVGRTGAGKSSMTLC 1331
Cdd:PRK13657 305 KLEEFFEVEDAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYdnsRQGVE----DVSFEAKPGQTVAIVGPTGAGKSTLINL 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1332 LFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDpFGR--YSDEDIWRTLELSHLSAFVSSQPT 1409
Cdd:PRK13657 381 LQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIR-VGRpdATDEEMRAAAERAQAHDFIERKPD 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1410 GLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRV 1489
Cdd:PRK13657 460 GYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRI 539
|
250 260 270
....*....|....*....|....*....|....
gi 1937891448 1490 LVLDKGVVAEFDSPVNLIAAGGIFYGMAKDAGLA 1523
Cdd:PRK13657 540 LVFDNGRVVESGSFDELVARGGRFAALLRAQGML 573
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1283-1513 |
4.44e-46 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 176.36 E-value: 4.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1283 GVVEFRNYSVRYrPGLE-LVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQ 1361
Cdd:PRK11176 340 GDIEFRNVTFTY-PGKEvPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1362 LTIIPQDPILFSGTLRMNLD--PFGRYSDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRK 1439
Cdd:PRK11176 419 VALVSQNVHLFNDTIANNIAyaRTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRD 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937891448 1440 SRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIF 1513
Cdd:PRK11176 499 SPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVY 572
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1264-1492 |
1.47e-44 |
|
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: 170.55 E-value: 1.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1264 TEAPWVLESNRAPEGWPRSGVVEFRNYSVRYrPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEI 1343
Cdd:TIGR02857 301 LDAAPRPLAGKAPVTAAPASSLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSI 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1344 FIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDpFGR--YSDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDN 1421
Cdd:TIGR02857 380 AVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIR-LARpdASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAG 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937891448 1422 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVL 1492
Cdd:TIGR02857 459 LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1016-1514 |
1.34e-43 |
|
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: 171.08 E-value: 1.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1016 ILQGLLVMLSAFTMVVGAIQAARLLHTALLHNQIRAPQSFFDTTPSGRILNRFSkDIYVIDEVLAPTILMLFNSFYTSIS 1095
Cdd:TIGR01193 207 IIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFT-DASSIIDALASTILSLFLDMWILVI 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1096 T-IVVIVASTPLFCVVVLPLAVF----YGFVQRFYVATSRQLKRLESVSRSPIfshfsETVTGTSVIRAYGRVQDFKVLS 1170
Cdd:TIGR01193 286 VgLFLVRQNMLLFLLSLLSIPVYaviiILFKRTFNKLNHDAMQANAVLNSSII-----EDLNGIETIKSLTSEAERYSKI 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1171 DAKVDSNQKTTYPYIASN---RWLGVHVEFVGNCVVLFSALFAVIgRNSLNpglVGLSVSYALQVTLSLNWM---IRTLS 1244
Cdd:TIGR01193 361 DSEFGDYLNKSFKYQKADqgqQAIKAVTKLILNVVILWTGAYLVM-RGKLT---LGQLITFNALLSYFLTPLeniINLQP 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1245 DLESNIIAVERVKEYSKTETEapwVLESNRAPEGWPRSGVVEFRNYSVRYRPGLElVLKNLTLHVQGGEKVGIVGRTGAG 1324
Cdd:TIGR01193 437 KLQAARVANNRLNEVYLVDSE---FINKKKRTELNNLNGDIVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSG 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1325 KSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGR--YSDEDIWRTLELSHLSA 1402
Cdd:TIGR01193 513 KSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKenVSQDEIWAACEIAEIKD 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1403 FVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIrTQFEDCTVLTIAHRLNT 1482
Cdd:TIGR01193 593 DIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNL-LNLQDKTIIFVAHRLSV 671
|
490 500 510
....*....|....*....|....*....|..
gi 1937891448 1483 IMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFY 1514
Cdd:TIGR01193 672 AKQSDKIIVLDHGKIIEQGSHDELLDRNGFYA 703
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
626-846 |
1.82e-43 |
|
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: 158.55 E-value: 1.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-------------SVAY 692
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslrrQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 693 VPQQAWIQNCTLQENVLFGQP-MNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIF 771
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPgATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937891448 772 LLDDPLSAVDSHVAKHIFDQVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQITEMGHYSELLQHDGSFAN 846
Cdd:cd03251 161 ILDEATSALDTESERLVQAAL---ERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAK 232
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
968-1236 |
4.10e-42 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 155.88 E-value: 4.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 968 LFICLLYAGQNAVAIGANVWLSAWTNDVEEHGQQN--NTSVRLGVYATLGILQGLLVMLSAFTMVVGAIQAARLLHTALL 1045
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLLPDGDPEtqALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1046 HNQIRAPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLFNSFYTSISTIVVIVASTPLFCVVVLPLAVFYGFVQRFY 1125
Cdd:pfam00664 82 KKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1126 VATSRQLKRLESVSRSPIFSHFSETVTGTSVIRAYGRVQDFKVLSDAKVDSNQKTTYPYIASNRWLGVHVEFVGNCVVLF 1205
Cdd:pfam00664 162 AKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYAL 241
|
250 260 270
....*....|....*....|....*....|...
gi 1937891448 1206 SALFAV--IGRNSLNPGLVGLSVSYALQVTLSL 1236
Cdd:pfam00664 242 ALWFGAylVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1283-1497 |
6.27e-42 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 153.78 E-value: 6.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1283 GVVEFRNYSVRY--RPGlELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRS 1360
Cdd:cd03248 10 GIVKFQNVTFAYptRPD-TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1361 QLTIIPQDPILFSGTLRMNLD-PFGRYSDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRK 1439
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937891448 1440 SRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVV 1497
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
299-849 |
4.38e-41 |
|
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: 162.82 E-value: 4.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 299 LRALVRTFTSSLLMGacfkLIQDLLSFINPQLLSILI-RFISDPTAPTWWGflLAGLMFVSSTMQTLILHQHYHCIFVMA 377
Cdd:TIGR03797 131 LRGARRDLLAILAMG----LLGTLLGMLVPIATGILIgTAIPDADRSLLVQ--IALALLAAAVGAAAFQLAQSLAVLRLE 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 378 LRIRTAIIGVIYRKALTITNSVKREYTVGEMVN-LMSVDA-QRFMDVSPFINLLwsaplQVILAIYFLWQIL---GPSAL 452
Cdd:TIGR03797 205 TRMDASLQAAVWDRLLRLPVSFFRQYSTGDLASrAMGISQiRRILSGSTLTTLL-----SGIFALLNLGLMFyysWKLAL 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 453 AGVAVIVLLIPLNGAVSMKMKTYQVQQMKFKDSRIKLMSEILNGIKVLK--------LYAWEPTFLEQVE---GIRQSEL 521
Cdd:TIGR03797 280 VAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRvagaenraFARWAKLFSRQRKlelSAQRIEN 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 522 QLLRKGAYLQAIST--FIWVCT-PFMVTLITLGVYVcvdknnvldaekAFVSLslfnilkiplnlLPQLISGMTQTSVSL 598
Cdd:TIGR03797 360 LLTVFNAVLPVLTSaaLFAAAIsLLGGAGLSLGSFL------------AFNTA------------FGSFSGAVTQLSNTL 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 599 ----------KRIQDFLnqdELDPQCVERKTiSPGR---AITIHNGTFSWSKDLPPTLHSLNIQIPKGALVAVVGPVGCG 665
Cdd:TIGR03797 416 isilaviplwERAKPIL---EALPEVDEAKT-DPGKlsgAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSG 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 666 KSSLVSALLGeMEKLEgavsvKGSVAY-------------------VPQQAWIQNCTLQENVLFGQPMNPKRYQQALETC 726
Cdd:TIGR03797 492 KSTLLRLLLG-FETPE-----SGSVFYdgqdlagldvqavrrqlgvVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMA 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 727 ALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVakhifdQVIGPEGVLAGK-TRV 805
Cdd:TIGR03797 566 GLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRT------QAIVSESLERLKvTRI 639
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1937891448 806 LVTHGISFLPQTDFIIVLADGQITEMGHYSELLQHDGSFANFLR 849
Cdd:TIGR03797 640 VIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLAR 683
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
601-850 |
8.47e-41 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 160.40 E-value: 8.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 601 IQDFLNQDELDPQcVERKTISPGRAITIH-NGTFSWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMeK 679
Cdd:PRK11174 324 LVTFLETPLAHPQ-QGEKELASNDPVTIEaEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-P 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 680 LEGAVSVKG------SVAYVPQQ-AWI-QN-----CTLQENVLFGQP-MNPKRYQQALETCALLADLDVLPGGDQTEIGE 745
Cdd:PRK11174 402 YQGSLKINGielrelDPESWRKHlSWVgQNpqlphGTLRDNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIGD 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 746 KGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLAD 825
Cdd:PRK11174 482 QAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQAL---NAASRRQTTLMVTHQLEDLAQWDQIWVMQD 558
|
250 260
....*....|....*....|....*
gi 1937891448 826 GQITEMGHYSELLQHDGSFANFLRN 850
Cdd:PRK11174 559 GQIVQQGDYAELSQAGGLFATLLAH 583
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
626-845 |
2.29e-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: 149.69 E-value: 2.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWSKDLPpTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-------------SVAY 692
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 693 VPQQAWIQNCTLQENVLFGqpmNPKRYQQALETCALLADLD----VLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDA 768
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYG---RPDATDEEVIEAAKAAQIHdkimRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937891448 769 NIFLLDDPLSAVDSHVAKHIFDQVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQITEMGHYSELLQHDGSFA 845
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAAL---RDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYA 230
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
375-845 |
2.89e-40 |
|
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: 158.73 E-value: 2.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 375 VMALRIRtaiigvIYRKALTITNSVKREYTVGEMVNLMSVDA-QRFMDVSPFINLLWSAPLQVILAIYFL----WQIlgp 449
Cdd:TIGR02203 86 VRDIRVR------MFEKLLGLPVSFFDRQPTGTLLSRITFDSeQVASAATDAFIVLVRETLTVIGLFIVLlyysWQL--- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 450 salaGVAVIVLLIPLNGAVSMKMKTYQVQQMKFKDSRIKLM---SEILNGIKVLKLYAWEPTFLEQVEGIRQSELQLLRK 526
Cdd:TIGR02203 157 ----TLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTtvaEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 527 GAYLQAISTfiwvctPFMVTLITLGVYVCV------DKNNVLDAeKAFVSLSLFNILKI-PLNLLPQLISGMTQTSVSLK 599
Cdd:TIGR02203 233 MTSAGSISS------PITQLIASLALAVVLfialfqAQAGSLTA-GDFTAFITAMIALIrPLKSLTNVNAPMQRGLAAAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 600 RIQDFLNQdeldPQCVERKTISPGRA---ITIHNGTFSWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGE 676
Cdd:TIGR02203 306 SLFTLLDS----PPEKDTGTRAIERArgdVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRF 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 677 MEKLEGAV-------------SVKGSVAYVPQQAWIQNCTLQENVLFGQP--MNPKRYQQALETCALLADLDVLPGGDQT 741
Cdd:TIGR02203 382 YEPDSGQIlldghdladytlaSLRRQVALVSQDVVLFNDTIANNIAYGRTeqADRAEIERALAAAYAQDFVDKLPLGLDT 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 742 EIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVigpEGVLAGKTRVLVTHGISFLPQTDFII 821
Cdd:TIGR02203 462 PIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAAL---ERLMQGRTTLVIAHRLSTIEKADRIV 538
|
490 500
....*....|....*....|....
gi 1937891448 822 VLADGQITEMGHYSELLQHDGSFA 845
Cdd:TIGR02203 539 VMDDGRIVERGTHNELLARNGLYA 562
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
626-842 |
1.58e-39 |
|
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: 146.99 E-value: 1.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWSKDLPpTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAV-------------SVKGSVAY 692
Cdd:cd03254 3 IEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgidirdisrkSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 693 VPQQAWIQNCTLQENVLFGQPMNP-KRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIF 771
Cdd:cd03254 82 VLQDTFLFSGTIMENIRLGRPNATdEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937891448 772 LLDDPLSAVDSHVAKHIFDQVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQITEMGHYSELLQHDG 842
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEAL---EKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1302-1516 |
4.26e-39 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 155.39 E-value: 4.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1302 LKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILeAAEGEIFIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNL- 1380
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVl 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1381 --DPfgRYSDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDD 1458
Cdd:PRK11174 445 lgNP--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQ 522
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937891448 1459 LIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGM 1516
Cdd:PRK11174 523 LVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
626-827 |
2.12e-38 |
|
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: 141.37 E-value: 2.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-------------SVAY 692
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 693 VPQQAWIQNCTLQENVLfgqpmnpkryqqaletcalladldvlpggdqteigekginlSGGQRQRVSLARAVYSDANIFL 772
Cdd:cd03228 81 VPQDPFLFSGTIRENIL-----------------------------------------SGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1937891448 773 LDDPLSAVDSHVAKHIFDQVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQ 827
Cdd:cd03228 120 LDEATSALDPETEALILEAL---RALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
618-823 |
6.76e-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: 150.51 E-value: 6.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 618 KTISPGRAITIHNGTFSWsKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG--------- 688
Cdd:TIGR02857 314 VTAAPASSLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadad 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 689 ----SVAYVPQQAWIQNCTLQENVLFGQP-MNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARA 763
Cdd:TIGR02857 393 swrdQIAWVPQHPFLFAGTIAENIRLARPdASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARA 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 764 VYSDANIFLLDDPLSAVDSHVAKHIFDQVigpEGVLAGKTRVLVTHGISFLPQTDFIIVL 823
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEAL---RALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
625-828 |
2.62e-37 |
|
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: 140.42 E-value: 2.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 625 AITIHNGTFSWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-------------SVA 691
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 692 YVPQQAWIQNCTLQENVLFGQPM-NPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANI 770
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937891448 771 FLLDDPLSAVDSHVAKHIFDQVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQI 828
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERL---RQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1061-1480 |
5.89e-37 |
|
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: 147.89 E-value: 5.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1061 SGRILNRFSKDIYVIDEVLAPTILMLFNSFYTSISTIVVI-VASTPLFCVVVLPLAVFYGFVQRFYVATSRQLKRLESVS 1139
Cdd:TIGR02868 109 RGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIaVLSVPAALILAAGLLLAGFVAPLVSLRAARAAEQALARL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1140 RSPIFSHFSETVTGTSVIRAYGRVQDFKvlsDAKVDSNQKTTYPYIASNRWLGVH---VEFVGNCVVLFSALFAV--IGR 1214
Cdd:TIGR02868 189 RGELAAQLTDALDGAAELVASGALPAAL---AQVEEADRELTRAERRAAAATALGaalTLLAAGLAVLGALWAGGpaVAD 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1215 NSLNPGLVGLSVSYALQVTLSLNWMIRTLSDLESNIIAVERVKEYskTETEAPWVLESNRAPEGWPRSGV-VEFRNYSVR 1293
Cdd:TIGR02868 266 GRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEV--LDAAGPVAEGSAPAAGAVGLGKPtLELRDLSAG 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1294 YrPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTIIPQDPILFS 1373
Cdd:TIGR02868 344 Y-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFD 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1374 GTLRMNLDpFGR--YSDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAA 1451
Cdd:TIGR02868 423 TTVRENLR-LARpdATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEH 501
|
410 420
....*....|....*....|....*....
gi 1937891448 1452 IDLETDDLIQGTIRTQFEDCTVLTIAHRL 1480
Cdd:TIGR02868 502 LDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
626-850 |
8.36e-37 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 139.60 E-value: 8.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSW-SKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS-------------VA 691
Cdd:cd03249 1 IEFKNVSFRYpSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 692 YVPQQAWIQNCTLQENVLFGQPmnpKRYQQALETCALLADLD----VLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSD 767
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKP---DATDEEVEEAAKKANIHdfimSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 768 ANIFLLDDPLSAVDSHVAKHI---FDQVIGpegvlaGKTRVLVTHGISFLPQTDFIIVLADGQITEMGHYSELLQHDGSF 844
Cdd:cd03249 158 PKILLLDEATSALDAESEKLVqeaLDRAMK------GRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVY 231
|
....*.
gi 1937891448 845 ANFLRN 850
Cdd:cd03249 232 AKLVKA 237
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1285-1508 |
3.74e-36 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 137.08 E-value: 3.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYRPGlELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTI 1364
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1365 IPQDPI--LFSGTLR-------MNLdpfgRYSDEDIWR----TLELSHLSAFVSSQPtgldfqcseggDNLSVGQRQLVC 1431
Cdd:COG1122 80 VFQNPDdqLFAPTVEedvafgpENL----GLPREEIRErveeALELVGLEHLADRPP-----------HELSGGQKQRVA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937891448 1432 LARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT-QFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSPVNLIA 1508
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAELaDRVIVLDDGRIVADGTPREVFS 223
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
968-1256 |
4.28e-36 |
|
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: 140.32 E-value: 4.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 968 LFICLLYAGQNAVAIGANVWLSAWTNDVEEHGQQNNTSVRLGV-----------YATLGILQGLLVM--LSAFTMVVGAI 1034
Cdd:cd18600 20 LILCLVIFAIEVAASLVGLWLLRSQADRVNTTRPESSSNTYAVivtftssyyvfYIYVGVADSLLAMgfFRGLPLVHTLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1035 QAARLLHTALLHNQIRAPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLFNSFYTSISTIVVIVASTPLFCVVVLPL 1114
Cdd:cd18600 100 TVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVVSILQPYIFLATVPV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1115 AVFYGFVQRFYVATSRQLKRLESVSRSPIFSHFSETVTGTSVIRAYGRVQDFKVLSDAKVDSNQKTTYPYIASNRWLGVH 1194
Cdd:cd18600 180 IIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMR 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 1195 VEFVgnCVVLFSAL-FAVIGRNSLNPGLVGLSVSYALQVTLSLNWMIRTLSDLESNIIAVERV 1256
Cdd:cd18600 260 IEMI--FVIFFTAVtFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRI 320
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1286-1497 |
6.91e-35 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 131.57 E-value: 6.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1286 EFRNYSVRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTII 1365
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1366 PQDPILFSGTLRMNLdpfgrysdediwrtlelshlsafvssqptgldfqcseggdnLSVGQRQLVCLARALLRKSRVLVL 1445
Cdd:cd03246 82 PQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 1446 DEATAAIDLETDDLIQGTI-RTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVV 1497
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIaALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
377-809 |
2.30e-34 |
|
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: 139.80 E-value: 2.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 377 ALRIRTAIIGVIYRKALTITNSVKREYTVGEMVNLMSVDAQRFMD-----VSPFINLLWSAPLQVILAIYFLWQiLGPSA 451
Cdd:TIGR02868 81 ALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDlyvrvIVPAGVALVVGAAAVAAIAVLSVP-AALIL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 452 LAGVAVIVLLIPLNGAVSMKMKTYQVQQmkfkdSRIKLMSEI---LNGIKVLKLYAWEPTFLEQVEGIRQSELQLLRKGA 528
Cdd:TIGR02868 160 AAGLLLAGFVAPLVSLRAARAAEQALAR-----LRGELAAQLtdaLDGAAELVASGALPAALAQVEEADRELTRAERRAA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 529 YLQAIST--FIWVCTPFMVTLITLGVyvcvdkNNVLD--------AEKAFVSLSLFNilkiPLNLLPQLISGMTQTSVSL 598
Cdd:TIGR02868 235 AATALGAalTLLAAGLAVLGALWAGG------PAVADgrlapvtlAVLVLLPLAAFE----AFAALPAAAQQLTRVRAAA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 599 KRIqdflnqDELDPQCVERKTISPGRA---------ITIHNGTFSWSKDlPPTLHSLNIQIPKGALVAVVGPVGCGKSSL 669
Cdd:TIGR02868 305 ERI------VEVLDAAGPVAEGSAPAAgavglgkptLELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKSTL 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 670 VSALLGEMEKLEGAVSVKGS-------------VAYVPQQAWIQNCTLQENVLFGQP-MNPKRYQQALETCALLADLDVL 735
Cdd:TIGR02868 378 LATLAGLLDPLQGEVTLDGVpvssldqdevrrrVSVCAQDAHLFDTTVRENLRLARPdATDEELWAALERVGLADWLRAL 457
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937891448 736 PGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIgpeGVLAGKTRVLVTH 809
Cdd:TIGR02868 458 PDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLL---AALSGRTVVLITH 528
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
427-845 |
4.21e-34 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 141.42 E-value: 4.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 427 NLLWSAPLQVILAIYFLWQILG-----PSALAGVAVIVLL--IPLNGAVSMKMKTYQVQQMKFKDSRIKLMSEILNGIKV 499
Cdd:TIGR01846 250 NFLTGSALTVVLDLLFVVVFLAvmffySPTLTGVVIGSLVcyALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIET 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 500 LKLYAWEPTFL----EQVEGIRQSELQLLRKGAYLQAISTFIWVCTpfMVTLITLGVYVcvdknnVLDAEKAFVSLSLFN 575
Cdd:TIGR01846 330 IKATATEPQFQnrwdRQLAAYVAASFRVTNLGNIAGQAIELIQKLT--FAILLWFGAHL------VIGGALSPGQLVAFN 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 576 ILK----IPLNLLPQLISGMTQTSVSLKRIQDFLNQdeldpqcvERKTISPGRA--------ITIHNGTFSWSKDLPPTL 643
Cdd:TIGR01846 402 MLAgrvtQPVLRLAQLWQDFQQTGIALERLGDILNS--------PTEPRSAGLAalpelrgaITFENIRFRYAPDSPEVL 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 644 HSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSVAYVPQQAWIQ---NCTLQENVLFGQPM------ 714
Cdd:TIGR01846 474 SNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRrqmGVVLQENVLFSRSIrdnial 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 715 -NPKRYQQALETCALLAD----LDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIF 789
Cdd:TIGR01846 554 cNPGAPFEHVIHAAKLAGahdfISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIM 633
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 790 DQVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQITEMGHYSELLQHDGSFA 845
Cdd:TIGR01846 634 RNM---REICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYA 686
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
626-833 |
4.60e-34 |
|
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: 131.08 E-value: 4.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-------------SVAY 692
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 693 VPQQAWIQNCTLQENV-LFGQpMNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIF 771
Cdd:cd03244 83 IPQDPVLFSGTIRSNLdPFGE-YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 772 LLDDPLSAVDSHVAKHIFdQVIGPEgvLAGKTRVLVTHGISFLPQTDFIIVLADGQITEMGH 833
Cdd:cd03244 162 VLDEATASVDPETDALIQ-KTIREA--FKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1280-1514 |
6.28e-34 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 139.19 E-value: 6.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1280 PRSGVVEFRNYSVRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLR 1359
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1360 SQLTIIPQDPILFSGTLRMNL---DPfgRYSDEDIWRTLELSHLSAFVsSQPTGLDFQCSEGGDNLSVGQRQLVCLARAL 1436
Cdd:PRK11160 414 QAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLEKLL-EDDKGLNAWLGEGGRQLSGGEQRRLGIARAL 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937891448 1437 LRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFY 1514
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYY 568
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
267-849 |
1.92e-33 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 139.31 E-value: 1.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 267 ASGPQTAALEPKIAGEDEVLLKARPKT------KKPSFLRALVRTFTSSLlMGACFKLIQDLLsFINPQLL-----SILI 335
Cdd:TIGR03796 104 ALGPRTVSLEEFDESFTGVVLTFEPGPefqkggRKPSLLRALWRRLRGSR-GALLYLLLAGLL-LVLPGLVipafsQIFV 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 336 RFISDPTAPTWWGFLLAGlMFVSSTMQTLIlhQHYHCIFVMALRIRTAI---IGVIYRK-ALTITNSVKReYTvGEMVNL 411
Cdd:TIGR03796 182 DEILVQGRQDWLRPLLLG-MGLTALLQGVL--TWLQLYYLRRLEIKLAVgmsARFLWHIlRLPVRFFAQR-HA-GDIASR 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 412 MSVDAQrfmdVSPFIN-LLWSAPLQVILAI-YFLWQILGPSALAGVAVIVLLIPLnGAVSMKMKTYQVQQMKFKDSRIKL 489
Cdd:TIGR03796 257 VQLNDQ----VAEFLSgQLATTALDAVMLVfYALLMLLYDPVLTLIGIAFAAINV-LALQLVSRRRVDANRRLQQDAGKL 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 490 MSEILNGIKV---LKLYAWEPTFLEQVEGIR----QSELQLLRKGAYLQAISTFIwvcTPFMVTLI-TLGVYVCVDKNNV 561
Cdd:TIGR03796 332 TGVAISGLQSietLKASGLESDFFSRWAGYQakllNAQQELGVLTQILGVLPTLL---TSLNSALIlVVGGLRVMEGQLT 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 562 LDAEKAFVSLsLFNILKiPLNLLPQLISGMTQTSVSLKRIQDFLNQdELDPQCVERKTIS-----PGR---AITIHNGTF 633
Cdd:TIGR03796 409 IGMLVAFQSL-MSSFLE-PVNNLVGFGGTLQELEGDLNRLDDVLRN-PVDPLLEEPEGSAatsepPRRlsgYVELRNITF 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 634 SWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-------------SVAYVPQQAWIQ 700
Cdd:TIGR03796 486 GYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGipreeiprevlanSVAMVDQDIFLF 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 701 NCTLQENV-LFGQPMNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSA 779
Cdd:TIGR03796 566 EGTVRDNLtLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSA 645
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 780 VDSHVAKHIfDQVIGPEGVlagkTRVLVTHGISFLPQTDFIIVLADGQITEMGHYSELLQHDGSFANFLR 849
Cdd:TIGR03796 646 LDPETEKII-DDNLRRRGC----TCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARLIR 710
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
310-577 |
9.64e-33 |
|
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: 128.91 E-value: 9.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 310 LLMGACFKLIQDLLSFINPQLLSILIRFISDPTAPTWWGF-LLAGLMFVSSTMQTLILHQHYHCIFVMALRIRTAIIGVI 388
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALnVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 389 YRKALTITNSVKREYTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPS-ALAGVAVIVLLIPLNGA 467
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKlTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 468 VSMKMKTYQVQQMKFKDSRIKLMSEILNGIKVLKLYAWEPTFLEQVEGIRQSELQLLRKGAYLQAIS-TFIWVCTPFMVT 546
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSfGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|.
gi 1937891448 547 LITLGVYVCVDKNNvLDAEKAFVSLSLFNIL 577
Cdd:pfam00664 241 LALWFGAYLVISGE-LSVGDLVAFLSLFAQL 270
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
625-851 |
5.15e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 125.97 E-value: 5.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 625 AITIHNGTFSWSKDlpPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG--------SVAYVPQQ 696
Cdd:COG1121 6 AIELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 697 A---WIQNCTLQENVLFG--------QPMNPKRYQQALEtcaLLADLDVLPGGDQTeIGEkginLSGGQRQRVSLARAVY 765
Cdd:COG1121 84 AevdWDFPITVRDVVLMGrygrrglfRRPSRADREAVDE---ALERVGLEDLADRP-IGE----LSGGQQQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 766 SDANIFLLDDPLSAVDSHVAKHIFDqvigpegVLA-----GKTRVLVTHGISFLPQ-TDFIIVLADGQITEmGHYSELLQ 839
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYE-------LLRelrreGKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPPEEVLT 227
|
250
....*....|..
gi 1937891448 840 HDgsfaNFLRNY 851
Cdd:COG1121 228 PE----NLSRAY 235
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1285-1495 |
9.31e-32 |
|
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: 122.81 E-value: 9.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGlHDLRSQLTI 1364
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1365 IPQDPILFSGTLRMNLdpfgrysdediwrtlelshlsafvssqptgldfqcsegGDNLSVGQRQLVCLARALLRKSRVLV 1444
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1937891448 1445 LDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKG 1495
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENG 172
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1286-1495 |
2.12e-31 |
|
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: 122.96 E-value: 2.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1286 EFRNYSVRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTII 1365
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1366 PQDP------------ILFsGTLRMNLDPfgrysdEDIWR----TLELSHLSAFVSSQPtgldfqcseggDNLSVGQRQL 1429
Cdd:cd03225 81 FQNPddqffgptveeeVAF-GLENLGLPE------EEIEErveeALELVGLEGLRDRSP-----------FTLSGGQKQR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937891448 1430 VCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT-QFEDCTVLTIAHRLNTIMDY-NRVLVLDKG 1495
Cdd:cd03225 143 VAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLELaDRVIVLEDG 210
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
626-846 |
2.62e-31 |
|
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: 123.75 E-value: 2.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSVAYVPQQAWIQ---NC 702
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRrqvGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 703 TLQENVLFGQPM-------NPKRYQQALETCALLAD----LDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIF 771
Cdd:cd03252 81 VLQENVLFNRSIrdnialaDPGMSMERVIEAAKLAGahdfISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937891448 772 LLDDPLSAVDSHvAKHIFDQVIgpEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQITEMGHYSELLQHDGSFAN 846
Cdd:cd03252 161 IFDEATSALDYE-SEHAIMRNM--HDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAY 232
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1284-1511 |
1.45e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 121.73 E-value: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSmtlcLFR----ILEAAEGEIFIDGLNVAHiglhdLR 1359
Cdd:COG1121 6 AIELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKST----LLKailgLLPPTSGTVRLFGKPPRR-----AR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1360 SQLTIIPQD-------PILFSGTLRMNLDP----FGRYSDED---IWRTLELSHLSAFvSSQPTGldfqcseggdNLSVG 1425
Cdd:COG1121 75 RRIGYVPQRaevdwdfPITVRDVVLMGRYGrrglFRRPSRADreaVDEALERVGLEDL-ADRPIG----------ELSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1426 QRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT-QFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVA----- 1498
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREYfDRVLLLNRGLVAhgppe 223
|
250
....*....|...
gi 1937891448 1499 EFDSPVNLIAAGG 1511
Cdd:COG1121 224 EVLTPENLSRAYG 236
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
422-849 |
2.55e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 128.40 E-value: 2.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 422 VSPFInllwsAPLQVILAIYFLWQILGPSA---LAGVAVIVLLI-PL--------NGAVSMKMK-TYQVQqmkfkdsrik 488
Cdd:PRK11160 138 ISPLV-----AALVVILVLTIGLSFFDLTLaltLGGILLLLLLLlPLlfyrlgkkPGQDLTHLRaQYRVQ---------- 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 489 lMSEILNGIKVLKLYAWEPTFLEQvegIRQSELQLL---RKGAYLQAISTFIWV-CTPFMVTLITlgvYVCVD--KNNV- 561
Cdd:PRK11160 203 -LTEWLQGQAELTLFGAEDRYRQQ---LEQTEQQWLaaqRRQANLTGLSQALMIlANGLTVVLML---WLAAGgvGGNAq 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 562 ---LDAEKAFVSLSLFNILkIPLNLLPQLISgmtQTSVSLKRIQDFLNQdELDPQCVERKTISPGR-AITIHNGTFSWSK 637
Cdd:PRK11160 276 pgaLIALFVFAALAAFEAL-MPVAGAFQHLG---QVIASARRINEITEQ-KPEVTFPTTSTAAADQvSLTLNNVSFTYPD 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 638 DLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-------------SVAYVPQQAWIQNCTL 704
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqpiadyseaalrqAISVVSQRVHLFSATL 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 705 QENVLFGQP-MNPKRYQQALETCALLADLDVLPGGDqTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSH 783
Cdd:PRK11160 431 RDNLLLAAPnASDEALIEVLQQVGLEKLLEDDKGLN-AWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAE 509
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 784 VAKHIFDQVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQITEMGHYSELLQHDGSFANFLR 849
Cdd:PRK11160 510 TERQILELL---AEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1286-1495 |
3.08e-30 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 117.73 E-value: 3.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1286 EFRNYSVRYRPGLelVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTII 1365
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1366 PQdpilfsgtlrmnldpfgrysdediwrtlelshlsafvssqptgldfqcseggdnLSVGQRQLVCLARALLRKSRVLVL 1445
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 1446 DEATAAIDLETDDLIQGTIRTQFED-CTVLTIAHRLNTIMDY-NRVLVLDKG 1495
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1284-1503 |
4.72e-30 |
|
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: 120.53 E-value: 4.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYRPGLelVLKNLTLHVQGGEKVGIVGRTGAGKSsmTL--CLFRILEAAEGEIFIDGLNVAHIGLHDLRSQ 1361
Cdd:COG1120 1 MLEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKS--TLlrALAGLLKPSSGEVLLDGRDLASLSRRELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1362 LTIIPQDPIL-FSGTLR----M----NLDPFGRYSDED---IWRTLELSHLSAFvSSQPTgldfqcseggDNLSVGQRQL 1429
Cdd:COG1120 77 IAYVPQEPPApFGLTVRelvaLgrypHLGLFGRPSAEDreaVEEALERTGLEHL-ADRPV----------DELSGGERQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937891448 1430 VCLARALLRKSRVLVLDEATAAIDL----ETDDLIQGTIRTQfeDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSP 1503
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARER--GRTVVMVLHDLNLAARYaDRLVLLKDGRIVAQGPP 222
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1302-1450 |
1.85e-29 |
|
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: 115.05 E-value: 1.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1302 LKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTIIPQDPILFSGT-----L 1376
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLtvrenL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937891448 1377 RMNLDPFGRYSDEDIWRTLE-LSHLsafvsSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATA 1450
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEaLEKL-----GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
618-863 |
1.99e-29 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 125.60 E-value: 1.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 618 KTISPGR---AITIHngTFSWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAV---------- 684
Cdd:PRK10789 305 EPVPEGRgelDVNIR--QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhdipltkl 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 685 ---SVKGSVAYVPQQAWIQNCTLQENVLFGqpmNPKRYQQALETCALLA----DLDVLPGGDQTEIGEKGINLSGGQRQR 757
Cdd:PRK10789 383 qldSWRSRLAVVSQTPFLFSDTVANNIALG---RPDATQQEIEHVARLAsvhdDILRLPQGYDTEVGERGVMLSGGQKQR 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 758 VSLARAVYSDANIFLLDDPLSAVDSHVAKHIFdQVIGPEGvlAGKTRVLVTHGISFLPQTDFIIVLADGQITEMGHYSEL 837
Cdd:PRK10789 460 ISIARALLLNAEILILDDALSAVDGRTEHQIL-HNLRQWG--EGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQL 536
|
250 260 270
....*....|....*....|....*....|
gi 1937891448 838 LQHDGSFANFLR----NYAPDENQEANEGV 863
Cdd:PRK10789 537 AQQSGWYRDMYRyqqlEAALDDAPEIREEA 566
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1286-1498 |
3.22e-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: 116.86 E-value: 3.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1286 EFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAhiglhDLRSQLTII 1365
Cdd:cd03235 1 EVEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE-----KERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1366 PQD-------PILFSGTLRMNLDP----FGRYSDED---IWRTLELSHLSAFVSSQPtgldfqcseggDNLSVGQRQLVC 1431
Cdd:cd03235 74 PQRrsidrdfPISVRDVVLMGLYGhkglFRRLSKADkakVDEALERVGLSELADRQI-----------GELSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937891448 1432 LARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT-QFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVA 1498
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYfDRVLLLNRTVVA 211
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
438-1493 |
3.27e-29 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 127.45 E-value: 3.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 438 LAIYFlWQILGPSALA-GVAVIVLLIPLNGAV-SMKMKTYQVQQMKFKDSRIKLMSEILNGIKVLKLYAWEPTFLEQVEG 515
Cdd:PTZ00265 186 LGLYI-WSLFKNARLTlCITCVFPLIYICGVIcNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 516 IRQSELQLLRKGAYLQA-----ISTFIWVCTPFMV---TLITLGVYVCVDKNNvlDAEKAFVSLSLFNILkIPLNLLPQL 587
Cdd:PTZ00265 265 SEKLYSKYILKANFMESlhigmINGFILASYAFGFwygTRIIISDLSNQQPNN--DFHGGSVISILLGVL-ISMFMLTII 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 588 ISGMTQTSVSLK---RIQDFLNQDELDPQCVERKTISPGRAITIHNGTFSWS--KDLPpTLHSLNIQIPKGALVAVVGPV 662
Cdd:PTZ00265 342 LPNITEYMKSLEatnSLYEIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYDtrKDVE-IYKDLNFTLTEGKTYAFVGES 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 663 GCGKSSLVSALLGEMEKLEGAVSVKGS--------------VAYVPQQAWIQNCTLQENVLFG----------------- 711
Cdd:PTZ00265 421 GCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwrskIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyned 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 712 --------------------------QPMNPKRYQQALETCALLADLDV---------------LPGGDQTEIGEKGINL 750
Cdd:PTZ00265 501 gndsqenknkrnscrakcagdlndmsNTTDSNELIEMRKNYQTIKDSEVvdvskkvlihdfvsaLPDKYETLVGSNASKL 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 751 SGGQRQRVSLARAVYSDANIFLLDDPLSAVDS---HVAKHIFDQVIGPEGvlagKTRVLVTHGISFLPQTDFIIVLAD-- 825
Cdd:PTZ00265 581 SGGQKQRISIARAIIRNPKILILDEATSSLDNkseYLVQKTINNLKGNEN----RITIIIAHRLSTIRYANTIFVLSNre 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 826 -GQITEMGHYSELLQHDgSFANFLRNYAPDENQEANEGVLQHANEEVLLLEDtlSTHTDLTDTEPAIYEVRKQFMREMSS 904
Cdd:PTZ00265 657 rGSTVDVDIIGEDPTKD-NKENNNKNNKDDNNNNNNNNNNKINNAGSYIIEQ--GTHDALMKNKNGIYYTMINNQKVSSK 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 905 LSSEGEGQNRPVLKR--YTSSlEKEVPATQTKETGALIKEEIAETGNVKLS----------------------------- 953
Cdd:PTZ00265 734 KSSNNDNDKDSDMKSsaYKDS-ERGYDPDEMNGNSKHENESASNKKSCKMSdenasennaggklpflrnlfkrkpkapnn 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 954 ---VY---WDYAKSVglcTTLFICLLYAG--QNAVAIGANVWLSAWTNDVEEHGQQNNTSVRLGVYATLGILQGLLVmlS 1025
Cdd:PTZ00265 813 lriVYreiFSYKKDV---TIIALSILVAGglYPVFALLYAKYVSTLFDFANLEANSNKYSLYILVIAIAMFISETLK--N 887
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1026 AFTMVVGAiQAARLLHTALLHNQIRAPQSFFDT---TPsGRILNRFSKDIYVIDEVLAPTILmLFNSFytsistIVVIVA 1102
Cdd:PTZ00265 888 YYNNVIGE-KVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHINRDVHLLKTGLVNNIV-IFTHF------IVLFLV 958
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1103 STPL---FCVVVLPLAVFYGFVQ------RFYVATSRQLKRLESVSRSPIFSHFS-------------ETVTGTSVIRAY 1160
Cdd:PTZ00265 959 SMVMsfyFCPIVAAVLTGTYFIFmrvfaiRARLTANKDVEKKEINQPGTVFAYNSddeifkdpsfliqEAFYNMNTVIIY 1038
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1161 GRVQDFKVLSDAKVDSNQKTTYPYIASNR------------------WLGVHVEFVGNCVV--LFSALFAVIGRNSLNPG 1220
Cdd:PTZ00265 1039 GLEDYFCNLIEKAIDYSNKGQKRKTLVNSmlwgfsqsaqlfinsfayWFGSFLIRRGTILVddFMKSLFTFLFTGSYAGK 1118
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1221 LVGL---SVSYALQVTLSLNWMIR-TLSDLESNiiAVERVKEYSKTEteapwvlesnrapegwprsGVVEFRNYSVRY-- 1294
Cdd:PTZ00265 1119 LMSLkgdSENAKLSFEKYYPLIIRkSNIDVRDN--GGIRIKNKNDIK-------------------GKIEIMDVNFRYis 1177
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1295 RPGLElVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFR---------ILEAAE------------------------- 1340
Cdd:PTZ00265 1178 RPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydlkndhhIVFKNEhtndmtneqdyqgdeeqnvgmknvn 1256
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1341 --------------------GEIFIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDpFGR--YSDEDIWRTLELS 1398
Cdd:PTZ00265 1257 efsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FGKedATREDVKRACKFA 1335
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1399 HLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIR--TQFEDCTVLTI 1476
Cdd:PTZ00265 1336 AIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdiKDKADKTIITI 1415
|
1290
....*....|....*..
gi 1937891448 1477 AHRLNTIMDYNRVLVLD 1493
Cdd:PTZ00265 1416 AHRIASIKRSDKIVVFN 1432
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1284-1509 |
1.09e-28 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 122.32 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAA---EGEIFIDGLNVAHIGLHDLRS 1360
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1361 QLTIIPQDP------------ILFsgTLRmNLDPFGRYSDEDIWRTLELSHLSAFVSSQPtgldfqcseggDNLSVGQRQ 1428
Cdd:COG1123 84 RIGMVFQDPmtqlnpvtvgdqIAE--ALE-NLGLSRAEARARVLELLEAVGLERRLDRYP-----------HQLSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1429 LVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIR--TQFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSPVN 1505
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEE 229
|
....
gi 1937891448 1506 LIAA 1509
Cdd:COG1123 230 ILAA 233
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
567-849 |
1.27e-28 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 123.15 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 567 AFVSLSLFNILKiplnlLPQLISGMTQTSVSLKRIQDFLNQDELDPQCVER-KTISPGR---AITIHNGTFSWSKDlPPT 642
Cdd:PRK13657 277 AFVGFATLLIGR-----LDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPpGAIDLGRvkgAVEFDDVSFSYDNS-RQG 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-------------SVAYVPQQAWIQNCTLQENVL 709
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirtvtraslrrNIAVVFQDAGLFNRSIEDNIR 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 710 FGQP-MNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHI 788
Cdd:PRK13657 431 VGRPdATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKV 510
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937891448 789 FDQVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQITEMGHYSELLQHDGSFANFLR 849
Cdd:PRK13657 511 KAAL---DELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLR 568
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
586-840 |
1.81e-28 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 122.07 E-value: 1.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 586 QLISGMTQ---TSVSLKRIQDFLNQDELDPQCVERKtiSPGRAITIHNGTFSWSKDLPPTLHSLNIQIPKGALVAVVGPV 662
Cdd:TIGR01842 276 GAIGGWKQfsgARQAYKRLNELLANYPSRDPAMPLP--EPEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 663 GCGKSSLVSALLGEMEKLEGAVSVKG-------------SVAYVPQQAWIQNCTLQENVL-FGQPMNPKRYQQAletcAL 728
Cdd:TIGR01842 354 GSGKSTLARLIVGIWPPTSGSVRLDGadlkqwdretfgkHIGYLPQDVELFPGTVAENIArFGENADPEKIIEA----AK 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 729 LADLD----VLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIgpEGVLAGKTR 804
Cdd:TIGR01842 430 LAGVHelilRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIK--ALKARGITV 507
|
250 260 270
....*....|....*....|....*....|....*.
gi 1937891448 805 VLVTHGISFLPQTDFIIVLADGQITEMGHYSELLQH 840
Cdd:TIGR01842 508 VVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1234-1516 |
3.39e-28 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 121.74 E-value: 3.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1234 LSLNWMIrtlsdlesNIiaVER-VKEYSKTET---EAPWVLESNRA-PEGwprSGVVEFRNYSVRYRPGLELVLKNLTLH 1308
Cdd:PRK10789 271 LALAWMF--------NI--VERgSAAYSRIRAmlaEAPVVKDGSEPvPEG---RGELDVNIRQFTYPQTDHPALENVNFT 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1309 VQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLdPFGR--Y 1386
Cdd:PRK10789 338 LKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNI-ALGRpdA 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1387 SDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT 1466
Cdd:PRK10789 417 TQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQ 496
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1467 QFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGM 1516
Cdd:PRK10789 497 WGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDM 546
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1280-1500 |
4.65e-28 |
|
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: 121.01 E-value: 4.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1280 PR-SGVVEFRNYSVRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDL 1358
Cdd:COG4618 325 PRpKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1359 RSQLTIIPQDPILFSGTLRMNLDPFGRYSDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLR 1438
Cdd:COG4618 405 GRHIGYLPQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 1439 KSRVLVLDEATAAIDLETDDLIQGTIRTQFED-CTVLTIAHRLNTIMDYNRVLVLDKGVVAEF 1500
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAF 547
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
626-828 |
7.01e-28 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 111.54 E-value: 7.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS-------------VAY 692
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 693 VPQQAWIQNCTLQENVLfgqpmnpkryqqaletcalladldvlpggdqteigekginlSGGQRQRVSLARAVYSDANIFL 772
Cdd:cd03246 81 LPQDDELFSGSIAENIL-----------------------------------------SGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 773 LDDPLSAVDSHVAKHIFDQVIGPEgvLAGKTRVLVTHGISFLPQTDFIIVLADGQI 828
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALK--AAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1284-1509 |
1.29e-27 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 119.24 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRY---RPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIG---LHD 1357
Cdd:COG1123 260 LLEVRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1358 LRSQLTIIPQDPilfSGTL--RMN--------LDPFGRYSDEDIW-RTLELshLSAFvssqptGLD--------FQcseg 1418
Cdd:COG1123 340 LRRRVQMVFQDP---YSSLnpRMTvgdiiaepLRLHGLLSRAERReRVAEL--LERV------GLPpdladrypHE---- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1419 gdnLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLetddLIQGTIRTQFED------CTVLTIAHRLNTIMDY-NRVLV 1491
Cdd:COG1123 405 ---LSGGQRQRVAIARALALEPKLLILDEPTSALDV----SVQAQILNLLRDlqrelgLTYLFISHDLAVVRYIaDRVAV 477
|
250
....*....|....*...
gi 1937891448 1492 LDKGVVAEFDSPVNLIAA 1509
Cdd:COG1123 478 MYDGRIVEDGPTEEVFAN 495
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1284-1500 |
1.48e-27 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 112.60 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYRPGLELV--LKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDL--- 1358
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1359 RSQLTIIPQDPILfsgtlrmNLDPfgRYSDED-IWRTLeLSHLSAFVSSQPTGLDFQCSEGGDN-----------LSVGQ 1426
Cdd:cd03257 81 RKEIQMVFQDPMS-------SLNP--RMTIGEqIAEPL-RIHGKLSKKEARKEAVLLLLVGVGLpeevlnrypheLSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937891448 1427 RQLVCLARALLRKSRVLVLDEATAAIDLETD----DLIQgTIRTQFeDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEF 1500
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQaqilDLLK-KLQEEL-GLTLLFITHDLGVVAKIaDRVAVMYAGKIVEE 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
628-812 |
2.87e-27 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 111.09 E-value: 2.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 628 IHNGTFSWSKdlPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG--------SVAYVPQQAWI 699
Cdd:cd03235 2 VEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 700 QNC---TLQENVLFG--QPMNPKRYQQALETCALLADLDVLpggDQTEIGEKGI-NLSGGQRQRVSLARAVYSDANIFLL 773
Cdd:cd03235 80 DRDfpiSVRDVVLMGlyGHKGLFRRLSKADKAKVDEALERV---GLSELADRQIgELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1937891448 774 DDPLSAVDSHVAKHIFDQVIGpegvLA--GKTRVLVTHGIS 812
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRE----LRreGMTILVVTHDLG 193
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
641-832 |
9.39e-27 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 117.16 E-value: 9.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-------------SVAYVPQQAWIQNCTLQEN 707
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGadlsqwdreelgrHIGYLPQDVELFDGTIAEN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 708 V-LFGQPmNPKRYQQAletcALLADL-DV---LPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDS 782
Cdd:COG4618 426 IaRFGDA-DPEKVVAA----AKLAGVhEMilrLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937891448 783 hvakhifdqvigpEGVLA-----------GKTRVLVTHGISFLPQTDFIIVLADGQITEMG 832
Cdd:COG4618 501 -------------EGEAAlaaairalkarGATVVVITHRPSLLAAVDKLLVLRDGRVQAFG 548
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1286-1497 |
1.15e-26 |
|
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: 108.29 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1286 EFRNYSVRYRPGLelVLKNLTLHVQGGEKVGIVGRTGAGKSsmTL--CLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLT 1363
Cdd:cd03214 1 EVENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKS--TLlkTLAGLLKPSSGEILLDGKDLASLSPKELARKIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1364 IIPQdpILfsgtlrmnldpfgrysdediwRTLELSHLSafvssqptglDFQCSEggdnLSVGQRQLVCLARALLRKSRVL 1443
Cdd:cd03214 77 YVPQ--AL---------------------ELLGLAHLA----------DRPFNE----LSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1937891448 1444 VLDEATAAIDL----ETDDLIQGTIRTqfEDCTVLTIAHRLNTIMDY-NRVLVLDKGVV 1497
Cdd:cd03214 120 LLDEPTSHLDIahqiELLELLRRLARE--RGKTVVMVLHDLNLAARYaDRVILLKDGRI 176
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1285-1495 |
1.23e-26 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 108.04 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLH--DLRSQL 1362
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1363 TIIPQDPILFsgtlrmnldpfgrysdediwrtlelSHLSAFvssqptgldfqcseggDN----LSVGQRQLVCLARALLR 1438
Cdd:cd03229 79 GMVFQDFALF-------------------------PHLTVL----------------ENialgLSGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1439 KSRVLVLDEATAAIDLETDDLIQGTIRTQFED--CTVLTIAHRLNTIMDY-NRVLVLDKG 1495
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARLaDRVVVLRDG 177
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1231-1495 |
1.37e-26 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 116.83 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1231 QVTLSLNWMI---RTLSDLESNiiaVERVKEYSkTETEAPWVLESNRAPEGWPRSGVVEFRNYSVRyRPGLELVLKNLTL 1307
Cdd:COG4178 310 QVQGALSWFVdnyQSLAEWRAT---VDRLAGFE-EALEAADALPEAASRIETSEDGALALEDLTLR-TPDGRPLLEDLSL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1308 HVQGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAEGeifidglnvaHIGLHDLRSQLtIIPQDPILFSGTLRMNL--- 1380
Cdd:COG4178 385 SLKPGERLLITGPSGSGKST----LLRAIaglwPYGSG----------RIARPAGARVL-FLPQRPYLPLGTLREALlyp 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1381 DPFGRYSDEDIWRTLELSHLSAFVSSqptgLDfQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLI 1460
Cdd:COG4178 450 ATAEAFSDAELREALEAVGLGHLAER----LD-EEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAAL 524
|
250 260 270
....*....|....*....|....*....|....*.
gi 1937891448 1461 QGTIRTQFEDCTVLTIAHRlNTIMDY-NRVLVLDKG 1495
Cdd:COG4178 525 YQLLREELPGTTVISVGHR-STLAAFhDRVLELTGD 559
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
626-845 |
2.05e-26 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 116.27 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-------------SVAY 692
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdytlaslrnQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 693 VPQQAWIQNCTLQENVLFGQPMNPKRYQqaLETCALLAD----LDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDA 768
Cdd:PRK11176 422 VSQNVHLFNDTIANNIAYARTEQYSREQ--IEEAARMAYamdfINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937891448 769 NIFLLDDPLSAVDSHVAKHIFDQVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQITEMGHYSELLQHDGSFA 845
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAAL---DELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYA 573
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1272-1500 |
2.06e-26 |
|
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: 115.91 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1272 SNRAPEGWPR-SGVVEFRNYSVRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNV 1350
Cdd:TIGR01842 303 SRDPAMPLPEpEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1351 AHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSD-EDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQL 1429
Cdd:TIGR01842 383 KQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADpEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQR 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 1430 VCLARALLRKSRVLVLDEATAAIDLETDD-LIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEF 1500
Cdd:TIGR01842 463 IALARALYGDPKLVVLDEPNSNLDEEGEQaLANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARF 534
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
628-827 |
3.86e-26 |
|
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: 107.94 E-value: 3.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 628 IHNGTFSWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-------------SVAYVP 694
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkelrrKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 695 QQAWIQ--NCTLQENVLFGqPMN--------PKRYQQALETCALLADLDVLPggdqteigekgINLSGGQRQRVSLARAV 764
Cdd:cd03225 82 QNPDDQffGPTVEEEVAFG-LENlglpeeeiEERVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 765 YSDANIFLLDDPLSAVDSHVAKHIFDQVIGpegvL--AGKTRVLVTHGISFL-PQTDFIIVLADGQ 827
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKK----LkaEGKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1285-1499 |
7.68e-26 |
|
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: 107.97 E-value: 7.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYRPGLEL--VLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQL 1362
Cdd:COG1124 2 LEVRNLSVSYGQGGRRvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1363 TIIPQDPIlfsGTL--RMNLD-----PF----GRYSDEDIWRTLELSHL-SAFVSSQPtgldfqcseggDNLSVGQRQLV 1430
Cdd:COG1124 82 QMVFQDPY---ASLhpRHTVDrilaePLrihgLPDREERIAELLEQVGLpPSFLDRYP-----------HQLSGGQRQRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937891448 1431 CLARALLRKSRVLVLDEATAAIDL----ETDDLIQgTIRTQfEDCTVLTIAHRLNTImDY--NRVLVLDKGVVAE 1499
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVsvqaEILNLLK-DLREE-RGLTYLFVSHDLAVV-AHlcDRVAVMQNGRIVE 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
626-823 |
9.15e-26 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 107.17 E-value: 9.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWSKDLPPT--LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG--------SVAYVPQ 695
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepvtgpgpDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 696 QA----WIqncTLQENVLFG---QPMNPK----RYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAV 764
Cdd:cd03293 81 QDallpWL---TVLDNVALGlelQGVPKAeareRAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALARAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937891448 765 YSDANIFLLDDPLSAVDSHVAKHIFDQVIGpegvL---AGKTRVLVTHGIS---FLpqTDFIIVL 823
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTREQLQEELLD----IwreTGKTVLLVTHDIDeavFL--ADRVVVL 205
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
641-845 |
9.30e-26 |
|
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: 114.53 E-value: 9.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAV-------------SVKGSVAYVPQQAWIQNCTLQEN 707
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIlidgqdirdvtqaSLRAAIGIVPQDTVLFNDTIAYN 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 708 VLFGQPMNPkryQQALETCALLADLD----VLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSH 783
Cdd:COG5265 452 IAYGRPDAS---EEEVEAAARAAQIHdfieSLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSR 528
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 784 VAKHIFDQVigpEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQITEMGHYSELLQHDGSFA 845
Cdd:COG5265 529 TERAIQAAL---REVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYA 587
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1284-1499 |
1.08e-25 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 107.28 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRY--RPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLfRILEA-AEGEIFIDGLNVAHI---GLHD 1357
Cdd:cd03258 1 MIELKNVSKVFgdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCI-NGLERpTSGSVLVDGTDLTLLsgkELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1358 LRSQLTIIPQDPILFSG-TLRMNLD-PF------GRYSDEDIWRTLELSHLSAFVSSQPTgldfqcseggdNLSVGQRQL 1429
Cdd:cd03258 80 ARRRIGMIFQHFNLLSSrTVFENVAlPLeiagvpKAEIEERVLELLELVGLEDKADAYPA-----------QLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 1430 VCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT--QFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAE 1499
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRIcDRVAVMEKGEVVE 221
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1286-1503 |
1.24e-25 |
|
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: 107.27 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1286 EFRNYSVRYrPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVA---HIGLHDLRSQL 1362
Cdd:cd03256 2 EVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklkGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1363 TIIPQDPIL----------FSGTL-RMNLDP--FGRYSDEDIWRTLELshLSAFvssqptGLDFQCSEGGDNLSVGQRQL 1429
Cdd:cd03256 81 GMIFQQFNLierlsvlenvLSGRLgRRSTWRslFGLFPKEEKQRALAA--LERV------GLLDKAYQRADQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937891448 1430 VCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIR--TQFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAeFDSP 1503
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLKriNREEGITVIVSLHQVDLAREYaDRIVGLKDGRIV-FDGP 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
621-830 |
4.47e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 106.33 E-value: 4.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 621 SPGRAITIHNGTFSWSKDLPPT--LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG--------SV 690
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvtgpgpDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 691 AYVPQQA----WIqncTLQENVLFGQPMN--PKRY-----QQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVS 759
Cdd:COG1116 83 GVVFQEPallpWL---TVLDNVALGLELRgvPKAErreraRELLELVGLAGFEDAYPH-----------QLSGGMRQRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937891448 760 LARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIgpeGVLA--GKTRVLVTHGIS---FLpqTDFIIVLAD--GQITE 830
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLQDELL---RLWQetGKTVLFVTHDVDeavFL--ADRVVVLSArpGRIVE 221
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1286-1503 |
4.78e-25 |
|
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: 105.71 E-value: 4.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1286 EFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHdLRSQLTII 1365
Cdd:COG4555 3 EVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1366 PQDPILFSG-TLRMNLDPFGR----YSDEDIWRTLELSH---LSAFvssqptgLDFQCSEggdnLSVGQRQLVCLARALL 1437
Cdd:COG4555 80 PDERGLYDRlTVRENIRYFAElyglFDEELKKRIEELIEllgLEEF-------LDRRVGE----LSTGMKKKVALARALV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 1438 RKSRVLVLDEATAAIDLETDDLIQGTIRTQF-EDCTVLTIAHrlntIMD-----YNRVLVLDKGVVAEFDSP 1503
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSH----IMQevealCDRVVILHKGKVVAQGSL 216
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
643-778 |
1.03e-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: 101.57 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-------------SVAYVPQQAWIQN-CTLQENV 708
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslrkEIGYVFQDPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 709 LFGQPMnpKRYQQALETCALLADLDVLPGGDQ--TEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLS 778
Cdd:pfam00005 81 RLGLLL--KGLSKREKDARAEEALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
626-854 |
1.07e-24 |
|
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: 104.69 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWsKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-------------SVAY 692
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 693 VPQQAWI-QNCTLQENV-----LFGQPmNPKRYQQALEtcaLLADLDVLPGG------DQteigekginLSGGQRQRVSL 760
Cdd:cd03295 80 VIQQIGLfPHMTVEENIalvpkLLKWP-KEKIRERADE---LLALVGLDPAEfadrypHE---------LSGGQQQRVGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 761 ARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGPEGVLaGKTRVLVTHGIsflpqtDFIIVLADgQITEMGHySELLQH 840
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQEL-GKTIVFVTHDI------DEAFRLAD-RIAIMKN-GEIVQV 217
|
250
....*....|....
gi 1937891448 841 dGSFANFLRNYAPD 854
Cdd:cd03295 218 -GTPDEILRSPAND 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1285-1497 |
1.37e-24 |
|
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: 102.09 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYRPGLelVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGlHDLRSQLTI 1364
Cdd:cd03230 1 IEVRNLSKRYGKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1365 IPQDPILFSG-TLRMNLDpfgrysdediwrtlelshlsafvssqptgldfqcseggdnLSVGQRQLVCLARALLRKSRVL 1443
Cdd:cd03230 78 LPEEPSLYENlTVRENLK----------------------------------------LSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 1444 VLDEATAAIDLETDDLIQGTIRT-QFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVV 1497
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
646-832 |
2.58e-24 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 102.60 E-value: 2.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 646 LNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-----------SVAYVPQQ-AWIQNCTLQENVLFG-- 711
Cdd:cd03259 19 LSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvtgvpperrNIGMVFQDyALFPHLTVAENIAFGlk 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 712 --QPMNPKRYQQALETCALLADLDVLpggdQTEIGEkginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVA---- 785
Cdd:cd03259 99 lrGVPKAEIRARVRELLELVGLEGLL----NRYPHE----LSGGQQQRVALARALAREPSLLLLDEPLSALDAKLReelr 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1937891448 786 ---KHIFDQvigpegvlAGKTRVLVTHGIS-FLPQTDFIIVLADGQITEMG 832
Cdd:cd03259 171 eelKELQRE--------LGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
376-845 |
2.74e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 110.20 E-value: 2.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 376 MALRIRTAIIGVIYRKALTITNSVKreytVGEMVNLMSVDAQRFMD-VSPFIN-LLWSAPLQVILAIYFLWqiLGPSaLA 453
Cdd:TIGR00958 232 INLRIREDLFRSLLRQDLGFFDENK----TGELTSRLSSDTQTMSRsLSLNVNvLLRNLVMLLGLLGFMLW--LSPR-LT 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 454 GVAVIvlLIPLNGAVSMKMKTY------QVQQMKFKDSRIKLmsEILNGIKVLKLYAWEPTFLEQVEGIRQSELQLLRKG 527
Cdd:TIGR00958 305 MVTLI--NLPLVFLAEKVFGKRyqllseELQEAVAKANQVAE--EALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRK 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 528 AYlqAISTFIWVcTPFMVTLITLGVYVCvDKNNVLDAEKAFVSLSLFNILKIPL--NL--LPQLISGMTQTSVSLKRIQD 603
Cdd:TIGR00958 381 AL--AYAGYLWT-TSVLGMLIQVLVLYY-GGQLVLTGKVSSGNLVSFLLYQEQLgeAVrvLSYVYSGMMQAVGASEKVFE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 604 FLNQDeldPQCVERKTISPGR---AITIHNGTFSW-SKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEK 679
Cdd:TIGR00958 457 YLDRK---PNIPLTGTLAPLNlegLIEFQDVSFSYpNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQP 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 680 LEGAVSVKG-------------SVAYVPQQAWIQNCTLQENVLFGQPMNPKRYQQALETCALLAD-LDVLPGGDQTEIGE 745
Cdd:TIGR00958 534 TGGQVLLDGvplvqydhhylhrQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDfIMEFPNGYDTEVGE 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 746 KGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVakhifDQVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLAD 825
Cdd:TIGR00958 614 KGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC-----EQLLQESRSRASRTVLLIAHRLSTVERADQILVLKK 688
|
490 500
....*....|....*....|
gi 1937891448 826 GQITEMGHYSELLQHDGSFA 845
Cdd:TIGR00958 689 GSVVEMGTHKQLMEDQGCYK 708
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
626-832 |
3.31e-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: 3.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS------------VAYV 693
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 694 PQQAWIQNCTLQENVlfgqpmnpkryqqaletcalladldvlpggdqteigekGINLSGGQRQRVSLARAVYSDANIFLL 773
Cdd:cd03247 81 NQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1937891448 774 DDPLSAVDSHVAKHIFDQVIgpeGVLAGKTRVLVTHGISFLPQTDFIIVLADGQITEMG 832
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIF---EVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1285-1495 |
3.53e-24 |
|
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: 101.78 E-value: 3.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYRPG---LELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGlNVAhiglhdlrsq 1361
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-SIA---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1362 ltIIPQDPILFSGTLRMNLdPFGR-YSDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKS 1440
Cdd:cd03250 70 --YVSQEPWIQNGTIRENI-LFGKpFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937891448 1441 RVLVLDEATAAIDLETDDLIqgtirtqFEDC---------TVLTIAHRLNTIMDYNRVLVLDKG 1495
Cdd:cd03250 147 DIYLLDDPLSAVDAHVGRHI-------FENCilglllnnkTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1285-1503 |
1.02e-23 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 101.49 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYRPGLelVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEA-----AEGEIFIDGLNVAHIGLHD-- 1357
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1358 LRSQLTIIPQDPILFSGTLRMNLDpFG---------RYSDEDIWRTLELSHLSAFVSSQPTGLDfqcseggdnLSVGQRQ 1428
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVA-YGlrlhgiklkEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937891448 1429 LVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNT---IMDYnrVLVLDKGVVAEFDSP 1503
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQaarVADR--TAFLLNGRLVEFGPT 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1285-1501 |
1.13e-23 |
|
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: 100.67 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHdlRSQLTI 1364
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1365 IPQDPILFSG-TLRMNLDpFG---RYSDEDIWRT-----LELSHLSAFVSSQPTGldfqcseggdnLSVGQRQLVCLARA 1435
Cdd:cd03259 77 VFQDYALFPHlTVAENIA-FGlklRGVPKAEIRArvrelLELVGLEGLLNRYPHE-----------LSGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937891448 1436 LLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFE--DCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFD 1501
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEEALALaDRIAVMNEGRIVQVG 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
643-832 |
1.38e-23 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 99.43 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS-------------VAYVPQqawiqnctlqenvl 709
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlaslspkelarkIAYVPQ-------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 710 fgqpmnpkryqqALETCALladldvlpggdqTEIGEKGIN-LSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHI 788
Cdd:cd03214 81 ------------ALELLGL------------AHLADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1937891448 789 FDQVIGpegvLA---GKTRVLVTHGISFLPQ-TDFIIVLADGQITEMG 832
Cdd:cd03214 137 LELLRR----LArerGKTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
618-844 |
1.83e-23 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 107.11 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 618 KTISPGRaITIHNGTFSWSKDlPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG--------- 688
Cdd:PRK10790 334 RPLQSGR-IDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsslshs 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 689 ----SVAYVPQQAWIQNCTLQENVLFGQPMNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAV 764
Cdd:PRK10790 412 vlrqGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVL 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 765 YSDANIFLLDDPLSAVDSHVAKHIfDQVIGpeGVLAGKTRVLVTHGISFLPQTDFIIVLADGQITEMGHYSELLQHDGSF 844
Cdd:PRK10790 492 VQTPQILILDEATANIDSGTEQAI-QQALA--AVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRY 568
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1284-1499 |
2.61e-23 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 100.13 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYRPGLElVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHI---GLHDLRS 1360
Cdd:COG2884 1 MIRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1361 QLTIIPQD-PILFSGTLRMN----LDPFGRySDEDIWR----TLELSHLSAFVSSQPtgldfqcseggDNLSVGQRQLVC 1431
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENvalpLRVTGK-SRKEIRRrvreVLDLVGLSDKAKALP-----------HELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937891448 1432 LARALLRKSRVLVLDEATAAIDLET-DDLIQ--------GTirtqfedcTVLtIA-HRLNTIMDYN-RVLVLDKGVVAE 1499
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETsWEIMElleeinrrGT--------TVL-IAtHDLELVDRMPkRVLELEDGRLVR 217
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1014-1492 |
3.02e-23 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 108.19 E-value: 3.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1014 LGILQGLLVMLSAFTMVVGAIQAARLLHTALLHNQIRAPQSFFDTTPSGRIlnRFSKDIYVidEVLAPTILMLFNSFYTS 1093
Cdd:PTZ00265 106 IGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKL--TSDLDFYL--EQVNAGIGTKFITIFTY 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1094 ISTIVVIV-------ASTPLFCVVVLPLAVFYGFVQRFYVATSRQLKRLESvsrSPIFSHFSETVTGTSVIRAYgrVQDF 1166
Cdd:PTZ00265 182 ASAFLGLYiwslfknARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYN---NNTMSIIEEALVGIRTVVSY--CGEK 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1167 KVLSdaKVDSNQKTTYPYI-ASNRWLGVHVEFVgNCVVLFSALFA-------VIG-------RNSLNPGLVglsVSYALQ 1231
Cdd:PTZ00265 257 TILK--KFNLSEKLYSKYIlKANFMESLHIGMI-NGFILASYAFGfwygtriIISdlsnqqpNNDFHGGSV---ISILLG 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1232 VTLSLNWMIRTLSDLESNIIAVERVKEYSKTETEAPWVlESNRAPEGWPRSGVVEFRNYSVRY--RPGLElVLKNLTLHV 1309
Cdd:PTZ00265 331 VLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLV-ENNDDGKKLKDIKKIQFKNVRFHYdtRKDVE-IYKDLNFTL 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1310 QGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFI-DGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNL-------- 1380
Cdd:PTZ00265 409 TEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslk 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1381 -----------DPFGRYSDEDI------------------------------WRTLELSH---------LSAFVSSQPTG 1410
Cdd:PTZ00265 489 dlealsnyyneDGNDSQENKNKrnscrakcagdlndmsnttdsneliemrknYQTIKDSEvvdvskkvlIHDFVSALPDK 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1411 LDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT--QFEDCTVLTIAHRLNTIMDYNR 1488
Cdd:PTZ00265 569 YETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNlkGNENRITIIIAHRLSTIRYANT 648
|
....
gi 1937891448 1489 VLVL 1492
Cdd:PTZ00265 649 IFVL 652
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1284-1465 |
3.08e-23 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 99.09 E-value: 3.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAEGEIFIDGLNVaHIGLHDLR 1359
Cdd:COG4133 2 MLEAENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTT----LLRILagllPPSAGEVLWNGEPI-RDAREDYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1360 SQLTIIPQDPILFSG-TLRMNLDpF------GRYSDEDIWRTLELSHLSAFvssqptgLDFQCSeggdNLSVGQRQLVCL 1432
Cdd:COG4133 75 RRLAYLGHADGLKPElTVRENLR-FwaalygLRADREAIDEALEAVGLAGL-------ADLPVR----QLSAGQKRRVAL 142
|
170 180 190
....*....|....*....|....*....|...
gi 1937891448 1433 ARALLRKSRVLVLDEATAAIDLETDDLIQGTIR 1465
Cdd:COG4133 143 ARLLLSPAPLWLLDEPFTALDAAGVALLAELIA 175
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
641-828 |
4.09e-23 |
|
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: 99.10 E-value: 4.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSaLLGEMEKL-EGAVSVKG-----------------SVAYVPQQ-AWIQN 701
Cdd:cd03255 18 QALKGVSLSIEKGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVRVDGtdisklsekelaafrrrHIGFVFQSfNLLPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 702 CTLQENVLFGQPMNPK-------RYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLD 774
Cdd:cd03255 97 LTALENVELPLLLAGVpkkerreRAEELLERVGLGDRLNHYPS-----------ELSGGQQQRVAIARALANDPKIILAD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1937891448 775 DPLSAVDSHVAKHIFDqVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQI 828
Cdd:cd03255 166 EPTGNLDSETGKEVME-LLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
625-841 |
4.94e-23 |
|
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: 100.12 E-value: 4.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 625 AITIHNGTFSWSKDlpPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-------------SVA 691
Cdd:COG1120 1 MLEAENLSVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 692 YVPQQ---AWiqNCTLQENVLFG--------QPMNPKRYQ---QALETCAL--LADLDVLpggdqteigekgiNLSGGQR 755
Cdd:COG1120 79 YVPQEppaPF--GLTVRELVALGryphlglfGRPSAEDREaveEALERTGLehLADRPVD-------------ELSGGER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 756 QRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGpegvLA---GKTRVLVTHGISF-LPQTDFIIVLADGQITEM 831
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRR----LArerGRTVVMVLHDLNLaARYADRLVLLKDGRIVAQ 219
|
250
....*....|
gi 1937891448 832 GHYSELLQHD 841
Cdd:COG1120 220 GPPEEVLTPE 229
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1285-1498 |
7.04e-23 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 96.73 E-value: 7.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHD-LRSQLT 1363
Cdd:cd03216 1 LELRGITKRF--GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1364 IIPQdpilfsgtlrmnldpfgrysdediwrtlelshlsafvssqptgldfqcseggdnLSVGQRQLVCLARALLRKSRVL 1443
Cdd:cd03216 79 MVYQ------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937891448 1444 VLDEATAAIDL-ETDDLIQgTIRT-QFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVA 1498
Cdd:cd03216 105 ILDEPTAALTPaEVERLFK-VIRRlRAQGVAVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
641-809 |
1.17e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.92 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG--SVAYVPQQ---AWIQNCTLQENVLFG--QP 713
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRsevPDSLPLTVRDLVAMGrwAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 714 MNPKRY---------QQALEtcAL-LADLDVLPggdqteIGEkginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSH 783
Cdd:NF040873 86 RGLWRRltrddraavDDALE--RVgLADLAGRQ------LGE----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
|
170 180
....*....|....*....|....*.
gi 1937891448 784 VAKHIFDqVIGpEGVLAGKTRVLVTH 809
Cdd:NF040873 154 SRERIIA-LLA-EEHARGATVVVVTH 177
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
626-840 |
4.58e-22 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 96.63 E-value: 4.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWSKDlPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-------------SVAY 692
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkknlrelrrKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 693 VPQQAWIQ--NCTLQENVLFGqPMN--------PKRYQQALETCAL--LADLDVLpggdqteigekgiNLSGGQRQRVSL 760
Cdd:COG1122 80 VFQNPDDQlfAPTVEEDVAFG-PENlglpreeiRERVEEALELVGLehLADRPPH-------------ELSGGQKQRVAI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 761 ARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGpegvL--AGKTRVLVTHGISFLPQ-TDFIIVLADGQITEMGHYSEL 837
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKR----LnkEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREV 221
|
...
gi 1937891448 838 LQH 840
Cdd:COG1122 222 FSD 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1282-1511 |
5.37e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 97.88 E-value: 5.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1282 SGVVEFRNYSVRYRPGLE-LVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRS 1360
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1361 QLTIIPQDPI-LFSGTLRMNLDPFG------RYSD--EDIWRTLELSHLSAFVSSQPTgldfqcseggdNLSVGQRQLVC 1431
Cdd:PRK13650 82 KIGMVFQNPDnQFVGATVEDDVAFGlenkgiPHEEmkERVNEALELVGMQDFKEREPA-----------RLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1432 LARALLRKSRVLVLDEATAAIDLETD-DLIQgTIRTQFED--CTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIA 1508
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRlELIK-TIKGIRDDyqMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
...
gi 1937891448 1509 AGG 1511
Cdd:PRK13650 230 RGN 232
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
643-832 |
5.58e-22 |
|
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: 96.10 E-value: 5.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSAL-----LGEMEKLEGAVSVKGS---------------VAYVPQQAWIQNC 702
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKdiydldvdvlelrrrVGMVFQKPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 703 TLQENVLFGQP---MNPKRY-----QQALETCALLADLDvlpggDQTeigeKGINLSGGQRQRVSLARAVYSDANIFLLD 774
Cdd:cd03260 96 SIYDNVAYGLRlhgIKLKEEldervEEALRKAALWDEVK-----DRL----HALGLSGGQQQRLCLARALANEPEVLLLD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 775 DPLSAVDShVAKHIFDQVIGPegvLAGK-TRVLVTHGisfLPQ----TDFIIVLADGQITEMG 832
Cdd:cd03260 167 EPTSALDP-ISTAKIEELIAE---LKKEyTIVIVTHN---MQQaarvADRTAFLLNGRLVEFG 222
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
633-828 |
1.78e-21 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 94.11 E-value: 1.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 633 FSWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-------------SVAYVPQQ-AW 698
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppewrrQVAYVPQEpAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 699 IQNcTLQENVLF-----GQPMNPKRYQQALEtcALLADLDVLpggdQTEIGEkginLSGGQRQRVSLARAVYSDANIFLL 773
Cdd:COG4619 86 WGG-TVRDNLPFpfqlrERKFDRERALELLE--RLGLPPDIL----DKPVER----LSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 774 DDPLSAVDS----HVAKHIFDQVIGPegvlaGKTRVLVTHGISFLPQ-TDFIIVLADGQI 828
Cdd:COG4619 155 DEPTSALDPentrRVEELLREYLAEE-----GRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
627-829 |
2.07e-21 |
|
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: 93.86 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 627 TIHNGTFSWsKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG----------SVAYVPQQ 696
Cdd:cd03226 1 RIENISFSY-KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 697 AWIQ--NCTLQENVLFGQPMNPKRYQQA---LETCALLADLDVLPggdqteigekgINLSGGQRQRVSLARAVYSDANIF 771
Cdd:cd03226 80 VDYQlfTDSVREELLLGLKELDAGNEQAetvLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1937891448 772 LLDDPLSAVDSHVAKHIFDqVIGpEGVLAGKTRVLVTHGISFLPQT-DFIIVLADGQIT 829
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGE-LIR-ELAAQGKAVIVITHDYEFLAKVcDRVLLLANGAIV 205
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
627-827 |
2.31e-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: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 627 TIHNGTFSWSKdlPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVsvkgsvayvpqqawiqnctlqe 706
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI---------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 707 nVLFGQPMNPKRYQQALETCALLadldvlpggDQteigekginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHvAK 786
Cdd:cd00267 57 -LIDGKDIAKLPLEELRRRIGYV---------PQ---------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA-SR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1937891448 787 HIFDQVIGpEGVLAGKTRVLVTHGISFL-PQTDFIIVLADGQ 827
Cdd:cd00267 117 ERLLELLR-ELAEEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
623-849 |
3.13e-21 |
|
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: 94.98 E-value: 3.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 623 GRAITIHNGTFSWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-SVAYVPQQAWIQN 701
Cdd:cd03288 17 GGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGiDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 702 CT--LQENVLFGQP----MNPK------RYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDAN 769
Cdd:cd03288 97 LSiiLQDPILFSGSirfnLDPEckctddRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 770 IFLLDDPLSAVDShVAKHIFDQVIgpEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQITEMGHYSELL-QHDGSFANFL 848
Cdd:cd03288 177 ILIMDEATASIDM-ATENILQKVV--MTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLV 253
|
.
gi 1937891448 849 R 849
Cdd:cd03288 254 R 254
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
643-839 |
4.56e-21 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 93.97 E-value: 4.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG------------SVAYVPQQAWI-QNCTLQENV- 708
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEPALyPDLTVRENLr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 709 ----LFGQPMN--PKRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDS 782
Cdd:COG1131 96 ffarLYGLPRKeaRERIDELLELFGLTDAADRKVG-----------TLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 783 HVAKHIFDQVIGpegvLA--GKTRVLVTHGISFLPQT-DFIIVLADGQITEMGHYSELLQ 839
Cdd:COG1131 165 EARRELWELLRE----LAaeGKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
643-841 |
4.61e-21 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 93.72 E-value: 4.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS----------------VAYVPQQ-AWIQNCTLQ 705
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrrrMGMLFQSgALFDSLTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 706 ENVLF--------GQPMNPKRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPL 777
Cdd:cd03261 96 ENVAFplrehtrlSEEEIREIVLEKLEAVGLRGAEDLYPA-----------ELSGGMKKRVALARALALDPELLLYDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937891448 778 SAVDShVAKHIFDQVIGPEGVLAGKTRVLVTHGISFLPQT-DFIIVLADGQITEMGHYSELLQHD 841
Cdd:cd03261 165 AGLDP-IASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEELRASD 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
625-873 |
5.02e-21 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 98.82 E-value: 5.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 625 AITIHNGTFSWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLG---EMEKLEGAVSVKG------------- 688
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGrdllelsealrgr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 689 SVAYVPQQAWIQNC--TLQENVLFG---QPMNP----KRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVS 759
Cdd:COG1123 84 RIGMVFQDPMTQLNpvTVGDQIAEAlenLGLSRaearARVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 760 LARAVYSDANIFLLDDPLSAVDSHVAKHIFDqVIGPEGVLAGKTRVLVTHGISFLPQ-TDFIIVLADGQITEMGHYSELL 838
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILD-LLRELQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEIL 231
|
250 260 270
....*....|....*....|....*....|....*
gi 1937891448 839 QHDGSFANflrnyAPDENQEANEGVLQHANEEVLL 873
Cdd:COG1123 232 AAPQALAA-----VPRLGAARGRAAPAAAAAEPLL 261
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
643-830 |
7.92e-21 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 92.80 E-value: 7.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSaLLGEMEKL-EGAVSVKG-----------------SVAYVPQQA-WIQNCT 703
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVLIDGqdisslserelarlrrrHIGFVFQFFnLLPELT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 704 LQENVLF-----GQP--MNPKRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDP 776
Cdd:COG1136 103 ALENVALplllaGVSrkERRERARELLERVGLGDRLDHRPS-----------QLSGGQQQRVAIARALVNRPKLILADEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 777 LSAVDSHVAKHIFDqvigpegVLA------GKTRVLVTHGISFLPQTDFIIVLADGQITE 830
Cdd:COG1136 172 TGNLDSKTGEEVLE-------LLRelnrelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
643-848 |
8.12e-21 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 95.98 E-value: 8.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGemekLE----GAVSVKG------------SVAYVPQQ-AWIQNCTLQ 705
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAG----LEtpdsGRIVLNGrdlftnlpprerRVGFVFQHyALFPHMTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 706 ENVLFGQPMNPKRYQQALETCALLADL-------DVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLS 778
Cdd:COG1118 94 ENIAFGLRVRPPSKAEIRARVEELLELvqleglaDRYPS-----------QLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 779 AVDSHVAK-------HIFDQVigpegvlaGKTRVLVTH------GISflpqtDFIIVLADGQITEMGHYSELLQHDGSF- 844
Cdd:COG1118 163 ALDAKVRKelrrwlrRLHDEL--------GGTTVFVTHdqeealELA-----DRVVVMNQGRIEQVGTPDEVYDRPATPf 229
|
....*
gi 1937891448 845 -ANFL 848
Cdd:COG1118 230 vARFL 234
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1281-1510 |
9.71e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 93.90 E-value: 9.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1281 RSGVVEFRNYSVRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRS 1360
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1361 QLTIIPQDP------------ILFsGTLRMNLDPfgrysdEDIWRTLElshlsafVSSQPTGLDFQCSEGGDNLSVGQRQ 1428
Cdd:PRK13632 84 KIGIIFQNPdnqfigatveddIAF-GLENKKVPP------KKMKDIID-------DLAKKVGMEDYLDKEPQNLSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1429 LVCLARALLRKSRVLVLDEATAAID-LETDDLIQ--GTIRTQfEDCTVLTIAHRLNTIMDYNRVLVLDKGvvaefdspvN 1505
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDpKGKREIKKimVDLRKT-RKKTLISITHDMDEAILADKVIVFSEG---------K 219
|
....*
gi 1937891448 1506 LIAAG 1510
Cdd:PRK13632 220 LIAQG 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
625-840 |
1.09e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 95.53 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 625 AITIHNGTFSWSKDlpPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGemekLE----GAVSVKG-----------S 689
Cdd:COG3839 3 SLELENVSKSYGGV--EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG----LEdptsGEILIGGrdvtdlppkdrN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 690 VAYVPQQ-AWIQNCTLQENVLFGQPMN--PK-----RYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLA 761
Cdd:COG3839 77 IAMVFQSyALYPHMTVYENIAFPLKLRkvPKaeidrRVREAAELLGLEDLLDRKPK-----------QLSGGQRQRVALG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 762 RAVYSDANIFLLDDPLSAVDSHVA-------KHIFDQVigpegvlaGKTRVLVTHGisflpQT------DFIIVLADGQI 828
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLDAKLRvemraeiKRLHRRL--------GTTTIYVTHD-----QVeamtlaDRIAVMNDGRI 212
|
250
....*....|..
gi 1937891448 829 TEMGHYSELLQH 840
Cdd:COG3839 213 QQVGTPEELYDR 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1284-1503 |
1.44e-20 |
|
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: 92.35 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIG---LHDLRS 1360
Cdd:COG1127 5 MIEVRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1361 QLTIIPQDPILFSG-TLRMN----LDPFGRYSDEDI----WRTLELSHLSAFVSSQPtgldfqcSEggdnLSVGQRQLVC 1431
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENvafpLREHTDLSEAEIrelvLEKLELVGLPGAADKMP-------SE----LSGGMRKRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937891448 1432 LARALLRKSRVLVLDEATAAID----LETDDLIQgTIRTQFeDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSP 1503
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDpitsAVIDELIR-ELRDEL-GLTSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTP 226
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1285-1494 |
1.69e-20 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 89.91 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVrYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAEGeifidglnvaHIGLHDlRS 1360
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSS----LFRALaglwPWGSG----------RIGMPE-GE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1361 QLTIIPQDPILFSGTLRMNLdpfgRYSdediWrtlelshlsafvssqptgldfqcsegGDNLSVGQRQLVCLARALLRKS 1440
Cdd:cd03223 65 DLLFLPQRPYLPLGTLREQL----IYP----W--------------------------DDVLSGGEQQRLAFARLLLHKP 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 1441 RVLVLDEATAAIDLETDDLIQGTIRTQFedCTVLTIAHR--LNTImdYNRVLVLDK 1494
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKELG--ITVISVGHRpsLWKF--HDRVLDLDG 162
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1285-1503 |
2.24e-20 |
|
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: 91.79 E-value: 2.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAH---IGLHDLRSQ 1361
Cdd:cd03261 1 IELRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1362 LTIIPQDPILFSG-TLRMN----LDPFGRYSDEDIWR----TLELSHLSAFVSSQPtgldfqcseggDNLSVGQRQLVCL 1432
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENvafpLREHTRLSEEEIREivleKLEAVGLRGAEDLYP-----------AELSGGMKKRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937891448 1433 ARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT--QFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSP 1503
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTP 221
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
626-833 |
2.53e-20 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 90.93 E-value: 2.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-------------SVAY 692
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 693 VPQQAWIQNCTLQENVlfgQPMNpkRYQQALETCALladldvlpggdqtEIGEKGINLSGGQRQRVSLARAVYSDANIFL 772
Cdd:cd03369 87 IPQDPTLFSGTIRSNL---DPFD--EYSDEEIYGAL-------------RVSEGGLNLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937891448 773 LDDPLSAVDSHvAKHIFDQVIGPEgvLAGKTRVLVTHGISFLPQTDFIIVLADGQITEMGH 833
Cdd:cd03369 149 LDEATASIDYA-TDALIQKTIREE--FTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
643-809 |
3.08e-20 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 90.62 E-value: 3.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG------------SVAYVPQQ-AWIQNCTLQENVL 709
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLAYLGHAdGLKPELTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 710 F-----GQPMNPKRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHv 784
Cdd:COG4133 98 FwaalyGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA- 165
|
170 180
....*....|....*....|....*
gi 1937891448 785 AKHIFDQVIGpEGVLAGKTRVLVTH 809
Cdd:COG4133 166 GVALLAELIA-AHLARGGAVLLTTH 189
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1285-1497 |
3.66e-20 |
|
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: 90.63 E-value: 3.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYRPGLE--LVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDL---- 1358
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1359 RSQLTIIPQD----PILfsgTLRMN----LDPFGRYSDEDIWRTLEL-------SHLSAFVSsqptgldfqcseggdNLS 1423
Cdd:cd03255 81 RRHIGFVFQSfnllPDL---TALENvelpLLLAGVPKKERRERAEELlervglgDRLNHYPS---------------ELS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937891448 1424 VGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIR--TQFEDCTVLTIAH--RLNTIMDynRVLVLDKGVV 1497
Cdd:cd03255 143 GGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHdpELAEYAD--RIIELRDGKI 218
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
630-828 |
7.53e-20 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 90.22 E-value: 7.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 630 NGTFSW-SKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS-------------VAYVPQ 695
Cdd:cd03248 16 NVTFAYpTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhskVSLVGQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 696 QAWIQNCTLQENVLFGQPMNP-KRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLD 774
Cdd:cd03248 96 EPVLFARSLQDNIAYGLQSCSfECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 775 DPLSAVDSHvAKHIFDQVI--GPEgvlaGKTRVLVTHGISFLPQTDFIIVLADGQI 828
Cdd:cd03248 176 EATSALDAE-SEQQVQQALydWPE----RRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
632-840 |
1.34e-19 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 89.86 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 632 TFSWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSVAYVPQQAWiQNCTLQenVLFG 711
Cdd:COG1124 10 SYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA-FRRRVQ--MVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 712 QPM---NP-KRYQQALETCALLADLDvlpgGDQTEIGEK----GIN----------LSGGQRQRVSLARAVYSDANIFLL 773
Cdd:COG1124 87 DPYaslHPrHTVDRILAEPLRIHGLP----DREERIAELleqvGLPpsfldryphqLSGGQRQRVAIARALILEPELLLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 774 DDPLSAVDSHVAKHIFDqvigpegVLA------GKTRVLVTHG---ISFLpqTDFIIVLADGQITEMGHYSELLQH 840
Cdd:COG1124 163 DEPTSALDVSVQAEILN-------LLKdlreerGLTYLFVSHDlavVAHL--CDRVAVMQNGRIVEELTVADLLAG 229
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
626-842 |
1.40e-19 |
|
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: 89.92 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWSKdlPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG------------SVAYV 693
Cdd:COG4555 2 IEVENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 694 PQQAWI-QNCTLQENVLF---GQPMNPKRYQQALEtcALLADLDVLPGGDQTeIGEkginLSGGQRQRVSLARAVYSDAN 769
Cdd:COG4555 80 PDERGLyDRLTVRENIRYfaeLYGLFDEELKKRIE--ELIELLGLEEFLDRR-VGE----LSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937891448 770 IFLLDDPLSAVDShVAKHIFDQVI---GPEgvlaGKTRVLVTHGISFLPQT-DFIIVLADGQITEMGHYSELLQHDG 842
Cdd:COG4555 153 VLLLDEPTNGLDV-MARRLLREILralKKE----GKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
641-843 |
1.67e-19 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 89.32 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-----------SVAYVPQQ-AWIQNCTLQENV 708
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedatdvpvqerNVGFVFQHyALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 709 LFGQPMNPK-----------RYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPL 777
Cdd:cd03296 96 AFGLRVKPRserppeaeiraKVHELLKLVQLDWLADRYPA-----------QLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937891448 778 SAVDSHVAKH-------IFDQVigpegvlaGKTRVLVTHGIS-FLPQTDFIIVLADGQITEMGHYSELLQHDGS 843
Cdd:cd03296 165 GALDAKVRKElrrwlrrLHDEL--------HVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYDHPAS 230
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
643-827 |
2.33e-19 |
|
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: 87.24 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG---------------SVAYVPQQ-AWIQNCTLQE 706
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledelpplrrRIGMVFQDfALFPHLTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 707 NVLFGqpmnpkryqqaletcalladldvlpggdqteigekginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVA- 785
Cdd:cd03229 96 NIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRr 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1937891448 786 ------KHIFDQVigpegvlaGKTRVLVTHGISFLPQ-TDFIIVLADGQ 827
Cdd:cd03229 138 evrallKSLQAQL--------GITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
632-832 |
8.17e-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: 87.18 E-value: 8.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 632 TFSWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG----------------SVAYVPQ 695
Cdd:cd03257 10 SFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkirrkEIQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 696 QAwiQNC-----TLQEnvLFGQPM---NPKRYQQALETCALLADLDVlpGGDQTEIGEKGINLSGGQRQRVSLARAVYSD 767
Cdd:cd03257 90 DP--MSSlnprmTIGE--QIAEPLrihGKLSKKEARKEAVLLLLVGV--GLPEEVLNRYPHELSGGQRQRVAIARALALN 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 768 ANIFLLDDPLSAVDSHVAKHIFDqvigpegVLA------GKTRVLVTHGISFLPQ-TDFIIVLADGQITEMG 832
Cdd:cd03257 164 PKLLIADEPTSALDVSVQAQILD-------LLKklqeelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1284-1501 |
9.45e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 91.62 E-value: 9.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYrPGLeLVLKNLTLHVQGGEKVGIVGRTGAGKSsmTL--CLFRILEAAEGEIFIDGLNVAHIGLHD-LRS 1360
Cdd:COG1129 4 LLEMRGISKSF-GGV-KALDGVSLELRPGEVHALLGENGAGKS--TLmkILSGVYQPDSGEILLDGEPVRFRSPRDaQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1361 QLTIIPQDPIL----------FSGTLRMNldpFGRYSdediWRTLE------LSHLsafvssqptGLDFQCSEGGDNLSV 1424
Cdd:COG1129 80 GIAIIHQELNLvpnlsvaeniFLGREPRR---GGLID----WRAMRrrarelLARL---------GLDIDPDTPVGDLSV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1425 GQRQLVCLARALLRKSRVLVLDEATAAIDL-ETDDLIqGTIRT-QFEDCTVLTIAHRLNTIMDY-NRVLVL-DKGVVAEF 1500
Cdd:COG1129 144 AQQQLVEIARALSRDARVLILDEPTASLTErEVERLF-RIIRRlKAQGVAIIYISHRLDEVFEIaDRVTVLrDGRLVGTG 222
|
.
gi 1937891448 1501 D 1501
Cdd:COG1129 223 P 223
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1288-1499 |
1.37e-18 |
|
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: 86.72 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1288 RNYSVRYRpGLeLVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDlRSQLTIIP- 1366
Cdd:cd03219 4 RGLTKRFG-GL-VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE-IARLGIGRt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1367 -QDPILFSG-TLRMNL-----------DPFGRYSDED------IWRTLELSHLSAfVSSQPTGldfqcseggdNLSVGQR 1427
Cdd:cd03219 81 fQIPRLFPElTVLENVmvaaqartgsgLLLARARREErearerAEELLERVGLAD-LADRPAG----------ELSYGQQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 1428 QLVCLARALLRKSRVLVLDEATAAIDL-ETDDLIQgTIRT-QFEDCTVLTIAHRLNTIMDY-NRVLVLDKG-VVAE 1499
Cdd:cd03219 150 RRLEIARALATDPKLLLLDEPAAGLNPeETEELAE-LIRElRERGITVLLVEHDMDVVMSLaDRVTVLDQGrVIAE 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
642-832 |
1.97e-18 |
|
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: 85.38 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 642 TLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-----------SVAYVPQQ-AWIQNCTLQENVL 709
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppkdrDIAMVFQNyALYPHMTVYDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 710 FGQPMN-------PKRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDS 782
Cdd:cd03301 95 FGLKLRkvpkdeiDERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1937891448 783 HVAKHIFDQVIGPEGVLaGKTRVLVTHG-ISFLPQTDFIIVLADGQITEMG 832
Cdd:cd03301 164 KLRVQMRAELKRLQQRL-GTTTIYVTHDqVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
643-828 |
2.33e-18 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 83.99 E-value: 2.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSV------------KGSVAYVPQQA-WIQNCTLQENvl 709
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlgkdikkepeevKRRIGYLPEEPsLYENLTVREN-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 710 fgqpmnpkryqqaletcalladldvlpggdqteigekgINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIF 789
Cdd:cd03230 94 --------------------------------------LKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFW 135
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1937891448 790 DQVIgpEGVLAGKTRVLVTHGISFLPQT-DFIIVLADGQI 828
Cdd:cd03230 136 ELLR--ELKKEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
640-830 |
3.65e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 86.07 E-value: 3.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 640 PPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSV--------AYVPQQ----AWIqncTLQEN 707
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVVFQKdallPWL---NVLDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 708 VLFGQPMN--PK--RYQQALETCALLAdldvLPGGDQTEIGEkginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSH 783
Cdd:COG4525 97 VAFGLRLRgvPKaeRRARAEELLALVG----LADFARRRIWQ----LSGGMRQRVGIARALAADPRFLLMDEPFGALDAL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1937891448 784 VAKHIfdQVIgpegVL-----AGKTRVLVTHGIS---FLpQTDfIIVLAD--GQITE 830
Cdd:COG4525 169 TREQM--QEL----LLdvwqrTGKGVFLITHSVEealFL-ATR-LVVMSPgpGRIVE 217
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1284-1510 |
5.12e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 86.22 E-value: 5.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLT 1363
Cdd:PRK13635 5 IIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1364 IIPQDPI-LFSGT-----LRMNLDPFGRYSDEDIWR---TLELSHLSAFVSSQPTgldfqcseggdNLSVGQRQLVCLAR 1434
Cdd:PRK13635 85 MVFQNPDnQFVGAtvqddVAFGLENIGVPREEMVERvdqALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937891448 1435 ALLRKSRVLVLDEATAAIDLETDDLIQGTIRT--QFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAG 1510
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSG 231
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1280-1501 |
5.45e-18 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 85.53 E-value: 5.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1280 PRSGVVEFRNYSVRYRPGLE--LVLKNLTLHVQGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAEGEIFIDGLNVAHI 1353
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKST----LLRLIagleKPTSGEVLVDGKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1354 GlhdlrSQLTIIPQDPILFsgtlrmnldPfgrysdediWRT--------------------------LELSHLSAFVSSQ 1407
Cdd:COG1116 79 G-----PDRGVVFQEPALL---------P---------WLTvldnvalglelrgvpkaerrerarelLELVGLAGFEDAY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1408 PtgldfqcseggDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLET-----DDLIQgtIRTQfEDCTVLTIAH---- 1478
Cdd:COG1116 136 P-----------HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTrerlqDELLR--LWQE-TGKTVLFVTHdvde 201
|
250 260
....*....|....*....|....*...
gi 1937891448 1479 --RLNtimdyNRVLVLDKG---VVAEFD 1501
Cdd:COG1116 202 avFLA-----DRVVVLSARpgrIVEEID 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
626-839 |
7.18e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.07 E-value: 7.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWSKDlpPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-------------SVAY 692
Cdd:PRK11231 3 LRTENLTVGYGTK--RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 693 VPQQAWI-QNCTLQENVLFGQ-PMNP----------KRYQQALEtcalladldvlpggdQTEIGE----KGINLSGGQRQ 756
Cdd:PRK11231 81 LPQHHLTpEGITVRELVAYGRsPWLSlwgrlsaednARVNQAME---------------QTRINHladrRLTDLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 757 RVSLARAVYSDANIFLLDDPLSAVD-SHVAkhifdQVIGPEGVL--AGKTRVLVTHGISflpQT----DFIIVLADGQIT 829
Cdd:PRK11231 146 RAFLAMVLAQDTPVVLLDEPTTYLDiNHQV-----ELMRLMRELntQGKTVVTVLHDLN---QAsrycDHLVVLANGHVM 217
|
250
....*....|
gi 1937891448 830 EMGHYSELLQ 839
Cdd:PRK11231 218 AQGTPEEVMT 227
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
639-857 |
7.62e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 90.42 E-value: 7.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 639 LPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSAL--LGEMEKLE-----------GAVSVKGSVAYVPQQAWIQNCTLQ 705
Cdd:PLN03232 1248 LPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALfrIVELEKGRimiddcdvakfGLTDLRRVLSIIPQSPVLFSGTVR 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 706 ENVLFGQPMNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVA 785
Cdd:PLN03232 1328 FNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTD 1407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 786 KHIfDQVIGPEgvLAGKTRVLVTHGISFLPQTDFIIVLADGQITEMGHYSELLQHDGS-FANFLRNYAPDENQ 857
Cdd:PLN03232 1408 SLI-QRTIREE--FKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSaFFRMVHSTGPANAQ 1477
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1284-1501 |
1.68e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 87.77 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYrPGLeLVLKNLTLHVQGGEKVGIVGRTGAGKSsmTL--CLFRILEAAEGEIFIDGLNV----------A 1351
Cdd:COG3845 5 ALELRGITKRF-GGV-VANDDVSLTVRPGEIHALLGENGAGKS--TLmkILYGLYQPDSGEILIDGKPVrirsprdaiaL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1352 HIGLhdlrsqltiIPQDPILFSG-TLRMNL------DPFGRYSDEDIWRTL-ELS-------HLSAFVSsqptgldfqcs 1416
Cdd:COG3845 81 GIGM---------VHQHFMLVPNlTVAENIvlglepTKGGRLDRKAARARIrELSerygldvDPDAKVE----------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1417 eggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAI-DLETDDLIQgTIRtQF--EDCTVLTIAHRLNTIMDY-NRVLVL 1492
Cdd:COG3845 141 ----DLSVGEQQRVEILKALYRGARILILDEPTAVLtPQEADELFE-ILR-RLaaEGKSIIFITHKLREVMAIaDRVTVL 214
|
250
....*....|
gi 1937891448 1493 DKG-VVAEFD 1501
Cdd:COG3845 215 RRGkVVGTVD 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1286-1508 |
2.53e-17 |
|
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: 82.48 E-value: 2.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1286 EFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHD-LRSQLTI 1364
Cdd:cd03224 2 EVENLNAGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1365 IPQDPILFSG-TLRMNLDpFGRY--SDEDIWRTLElSHLSAF-----VSSQPTGldfqcseggdNLSVGQRQLVCLARAL 1436
Cdd:cd03224 80 VPEGRRIFPElTVEENLL-LGAYarRRAKRKARLE-RVYELFprlkeRRKQLAG----------TLSGGEQQMLAIARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937891448 1437 LRKSRVLVLDEATA----AIDLETDDLIQgTIRTqfEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSPVNLIA 1508
Cdd:cd03224 148 MSRPKLLLLDEPSEglapKIVEEIFEAIR-ELRD--EGVTILLVEQNARFALEIaDRAYVLERGRVVLEGTAAELLA 221
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1284-1499 |
2.59e-17 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 82.78 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYRPGLELV--LKNLTLHVQGGEKVGIVGRTGAGKSsmTL--CLFRILEAAEGEIFIDGLNVAHIG---LH 1356
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKS--TLlnILGGLDRPTSGEVLIDGQDISSLSereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1357 DLRSQ-LTIIPQD---------------PILFSGTLRmnldpfgRYSDEDIWRTLELSHLSAFVSSQPtgldfqcseggD 1420
Cdd:COG1136 82 RLRRRhIGFVFQFfnllpeltalenvalPLLLAGVSR-------KERRERARELLERVGLGDRLDHRP-----------S 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1421 NLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETD----DLIQGTIRTQfeDCTVLTIAHRLNtIMDY-NRVLVLDKG 1495
Cdd:COG1136 144 QLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGeevlELLRELNREL--GTTIVMVTHDPE-LAARaDRVIRLRDG 220
|
....
gi 1937891448 1496 VVAE 1499
Cdd:COG1136 221 RIVS 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1285-1499 |
3.30e-17 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 84.74 E-value: 3.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYRPGLELV--LKNLTLHVQGGEKVGIVGRTGAGKSsmTL--CLFRiLEAA-EGEIFIDGLNVAHI---GLH 1356
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKS--TLirCINL-LERPtSGSVLVDGVDLTALserELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1357 DLRSQLTIIPQDPILFSG-T--------LRMNldpfgRYSDEDIWR----TLELSHLSAFVSSQPtgldfqcseggDNLS 1423
Cdd:COG1135 79 AARRKIGMIFQHFNLLSSrTvaenvalpLEIA-----GVPKAEIRKrvaeLLELVGLSDKADAYP-----------SQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1424 VGQRQLVCLARALLRKSRVLVLDEATAAIDLETD----DLIQgTIRTQFeDCTVLTIAHRLNTIMDY-NRVLVLDKGVVA 1498
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTrsilDLLK-DINREL-GLTIVLITHEMDVVRRIcDRVAVLENGRIV 220
|
.
gi 1937891448 1499 E 1499
Cdd:COG1135 221 E 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1285-1508 |
3.31e-17 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 82.73 E-value: 3.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYrPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTI 1364
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1365 IPQDPILFSG-TLRMN--LDP-FGRYSDEDI-WRTLELSHLsafVSSQPTGLDFQCSeggDNLSVGQRQLVCLARALLRK 1439
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPkLLKWPKEKIrERADELLAL---VGLDPAEFADRYP---HELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 1440 SRVLVLDEATAAIDLETDDLIQGTIRTQFEDC--TVLTIAHRLN-TIMDYNRVLVLDKGVVAEFDSPVNLIA 1508
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQELgkTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1280-1522 |
3.50e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 83.70 E-value: 3.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1280 PRSGVVEFRNYSVRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRIL---EAAEGEIFIDGLNVAHIGLH 1356
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1357 DLRSQLTIIPQDPI-LFSGTLRMNLDPFGrYSDEDIWRTlELSHLSAFVSSQPTGLDFQCSEGGdNLSVGQRQLVCLARA 1435
Cdd:PRK13640 81 DIREKVGIVFQNPDnQFVGATVGDDVAFG-LENRAVPRP-EMIKIVRDVLADVGMLDYIDSEPA-NLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1436 LLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFED--CTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNliaaggIF 1513
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnnLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVE------IF 231
|
250
....*....|.
gi 1937891448 1514 YG--MAKDAGL 1522
Cdd:PRK13640 232 SKveMLKEIGL 242
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
643-841 |
4.58e-17 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 82.35 E-value: 4.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG----------------SVAYVPQQ-AWIQNCTLQ 705
Cdd:TIGR02315 18 LKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGtditklrgkklrklrrRIGMIFQHyNLIERLTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 706 ENVLFG------------QPMNPKRYQQALEtcaLLADLDVLPGGDQteigeKGINLSGGQRQRVSLARAVYSDANIFLL 773
Cdd:TIGR02315 98 ENVLHGrlgykptwrsllGRFSEEDKERALS---ALERVGLADKAYQ-----RADQLSGGQQQRVAIARALAQQPDLILA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937891448 774 DDPLSAVDSHVAKHIFDQV--IGPEgvlAGKTRVLVTHGISFLPQ-TDFIIVLADGQITEMGHYSELLQHD 841
Cdd:TIGR02315 170 DEPIASLDPKTSKQVMDYLkrINKE---DGITVIINLHQVDLAKKyADRIVGLKAGEIVFDGAPSELDDEV 237
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1285-1503 |
5.16e-17 |
|
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: 81.75 E-value: 5.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYRPGLE--LVLKNLTLHVQGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAEGEIFIDGLNVAhiglhDL 1358
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKST----LLRIIagleRPTSGEVLVDGEPVT-----GP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1359 RSQLTIIPQDPILFS----------GtLRMNLDPFGRySDEDIWRTLELSHLSAFVSSQPtgldfqcseggDNLSVGQRQ 1428
Cdd:cd03293 72 GPDRGYVFQQDALLPwltvldnvalG-LELQGVPKAE-ARERAEELLELVGLSGFENAYP-----------HQLSGGMRQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1429 LVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTI-----RTQFedcTVLTIAHRLN-TIMDYNRVLVLDKG---VVAE 1499
Cdd:cd03293 139 RVALARALAVDPDVLLLDEPFSALDALTREQLQEELldiwrETGK---TVLLVTHDIDeAVFLADRVVVLSARpgrIVAE 215
|
....
gi 1937891448 1500 FDSP 1503
Cdd:cd03293 216 VEVD 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1285-1497 |
5.45e-17 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 81.42 E-value: 5.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNV--AHIGLHDLRSQL 1362
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1363 TIIPQDPILFSgtlRMN------LDP---FGRYSDEDIWRTLELshLsafvssQPTGLDFQCSEGGDNLSVGQRQLVCLA 1433
Cdd:cd03262 79 GMVFQQFNLFP---HLTvlenitLAPikvKGMSKAEAEERALEL--L------EKVGLADKADAYPAQLSGGQQQRVAIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1434 RALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFED-CTVLTIAHRlntiMDY-----NRVLVLDKGVV 1497
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEgMTMVVVTHE----MGFarevaDRVIFMDDGRI 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
643-828 |
8.05e-17 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 81.64 E-value: 8.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG----------------SVAYVPQQ-AWIQNCTLQ 705
Cdd:COG3638 19 LDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGqdvtalrgralrrlrrRIGMIFQQfNLVPRLSVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 706 ENVLFGQ-----------PMNPKR-YQQALEtcaLLADLDVLPGGDQteigeKGINLSGGQRQRVSLARAVYSDANIFLL 773
Cdd:COG3638 99 TNVLAGRlgrtstwrsllGLFPPEdRERALE---ALERVGLADKAYQ-----RADQLSGGQQQRVAIARALVQEPKLILA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 774 DDPLSAVDSHVAKHIFDqvigpegVLA------GKTRVLVTHGISFLPQ-TDFIIVLADGQI 828
Cdd:COG3638 171 DEPVASLDPKTARQVMD-------LLRriaredGITVVVNLHQVDLARRyADRIIGLRDGRV 225
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1302-1498 |
1.01e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.40 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1302 LKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVA--HIGLHDLRSQLTIIPQDP--ILFSGTLR 1377
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1378 MNLdPFG----RYSDEDIwrtlelsHLSAFVSSQPTGLDFQcsEGGD----NLSVGQRQLVCLARALLRKSRVLVLDEAT 1449
Cdd:PRK13637 103 KDI-AFGpinlGLSEEEI-------ENRVKRAMNIVGLDYE--DYKDkspfELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 1450 AAIDLETDDLIQGTIRTQFE--DCTVLTIAHRLNTIMDY-NRVLVLDKGVVA 1498
Cdd:PRK13637 173 AGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKLaDRIIVMNKGKCE 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1300-1508 |
1.07e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 80.95 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1300 LVLKNLT-----------LHVQGGEKVGIVGRTGAGKSsmTLcLFRI---LEAAEGEIFIDGLNVAHIGLHDlRSqLTII 1365
Cdd:COG3840 2 LRLDDLTyrygdfplrfdLTIAAGERVAILGPSGAGKS--TL-LNLIagfLPPDSGRILWNGQDLTALPPAE-RP-VSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1366 PQDPILFSG-TLRMN----LDPFGRYSDED---IWRTLELSHLSAFvssqptgLDFQCSEggdnLSVGQRQLVCLARALL 1437
Cdd:COG3840 77 FQENNLFPHlTVAQNiglgLRPGLKLTAEQraqVEQALERVGLAGL-------LDRLPGQ----LSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 1438 RKSRVLVLDEATAAID----LETDDLIQGTIRTQfeDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSPVNLIA 1508
Cdd:COG3840 146 RKRPILLLDEPFSALDpalrQEMLDLVDELCRER--GLTVLMVTHDPEDAARIaDRVLLVADGRIAADGPTAALLD 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1301-1499 |
1.21e-16 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 81.62 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1301 VLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDlRSQLTI-----IPQdpiLFSG- 1374
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHR-IARLGIartfqNPR---LFPEl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1375 TLRMNL----------------DPFGRYSDEDIWRTLELSHLSAFVssqptGLDFQCSEGGDNLSVGQRQLVCLARALLR 1438
Cdd:COG0411 95 TVLENVlvaaharlgrgllaalLRLPRARREEREARERAEELLERV-----GLADRADEPAGNLSYGQQRRLEIARALAT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 1439 KSRVLVLDEATAAIDL-ETDDLIQgTIRT--QFEDCTVLTIAHRLNTIMDY-NRVLVLDKG-VVAE 1499
Cdd:COG0411 170 EPKLLLLDEPAAGLNPeETEELAE-LIRRlrDERGITILLIEHDMDLVMGLaDRIVVLDFGrVIAE 234
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
641-825 |
1.31e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 80.22 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEmekLEGAVSVKGSV-----------------AYVPQQAWI-QNC 702
Cdd:COG4136 15 PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGT---LSPAFSASGEVllngrrltalpaeqrriGILFQDDLLfPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 703 TLQENVLFGQPMNPKRYQQALETCALLADLDvLPGgdqteIGEKGIN-LSGGQRQRVSLARAVYSDANIFLLDDPLSAVD 781
Cdd:COG4136 92 SVGENLAFALPPTIGRAQRRARVEQALEEAG-LAG-----FADRDPAtLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 782 SHVAKHI----FDQVigpegvlagKTR----VLVTHGISFLPQTDFIIVLAD 825
Cdd:COG4136 166 AALRAQFrefvFEQI---------RQRgipaLLVTHDEEDAPAAGRVLDLGN 208
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1302-1495 |
1.42e-16 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 80.45 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1302 LKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQ----LTIIPQDPILFSGTLR 1377
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1378 MNL---DPFG--RYSdediwRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAI 1452
Cdd:cd03290 97 ENItfgSPFNkqRYK-----AVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1937891448 1453 DLE-TDDLIQGTIRTQFED--CTVLTIAHRLNTIMDYNRVLVLDKG 1495
Cdd:cd03290 172 DIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
643-828 |
1.60e-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: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS----------------VAYVPQQ-AWIQNCTLQ 705
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrrqIGMIFQQfNLIERLSVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 706 ENVLFG------------QPMNPKRYQQALEtcaLLADLDVLPGGDQteigeKGINLSGGQRQRVSLARAVYSDANIFLL 773
Cdd:cd03256 97 ENVLSGrlgrrstwrslfGLFPKEEKQRALA---ALERVGLLDKAYQ-----RADQLSGGQQQRVAIARALMQQPKLILA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 774 DDPLSAVDSHVAKhifdQVIgpeGVLA------GKTRVLVTHGISF-LPQTDFIIVLADGQI 828
Cdd:cd03256 169 DEPVASLDPASSR----QVM---DLLKrinreeGITVIVSLHQVDLaREYADRIVGLKDGRI 223
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
643-830 |
2.60e-16 |
|
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: 79.79 E-value: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGemekLE----GAVSVKG-----------------SVAYVpQQAW--I 699
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAG----LDrptsGTVRLAGqdlfaldedararlrarHVGFV-FQSFqlL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 700 QNCTLQENV-----LFGQPMNPKRYQQALETCALLADLDVLPGGdqteigekginLSGGQRQRVSLARAVYSDANIFLLD 774
Cdd:COG4181 103 PTLTALENVmlpleLAGRRDARARARALLERVGLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAILFAD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 775 DPLSAVDSHVAKHIFDqvigpegvL-------AGKTRVLVTHGISFLPQTDFIIVLADGQITE 830
Cdd:COG4181 172 EPTGNLDAATGEQIID--------LlfelnreRGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1284-1500 |
2.68e-16 |
|
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: 81.64 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYRPGLELV--LKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEA---AEGEIFIDGLNVAHIGLHDL 1358
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1359 R----SQLTIIPQDPilfsgtlrMN-LDP--------------FGRYSDEDIW-RTLEL----------SHLSAFvssqP 1408
Cdd:COG0444 81 RkirgREIQMIFQDP--------MTsLNPvmtvgdqiaeplriHGGLSKAEAReRAIELlervglpdpeRRLDRY----P 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1409 tgldFQcseggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLetddLIQGTI-------RTQFeDCTVLTIAHrln 1481
Cdd:COG0444 149 ----HE-------LSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQAQIlnllkdlQREL-GLAILFITH--- 209
|
250
....*....|....*....
gi 1937891448 1482 timdynrvlvlDKGVVAEF 1500
Cdd:COG0444 210 -----------DLGVVAEI 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1255-1501 |
2.69e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.96 E-value: 2.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1255 RVKEYSKTETEAPWVLESN---RAPEGwPRSG--VVEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSmt 1329
Cdd:COG0488 282 RIKALEKLEREEPPRRDKTveiRFPPP-ERLGkkVLELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKST-- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1330 lcLFRIL----EAAEGEIFIdGLNVaHIG-----LHDLRSQLTIIpqdpilfsgtlrmnlDPFGRYSDEDiwRTLEL-SH 1399
Cdd:COG0488 357 --LLKLLagelEPDSGTVKL-GETV-KIGyfdqhQEELDPDKTVL---------------DELRDGAPGG--TEQEVrGY 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1400 LSAFvssqptglDFqcseGGD-------NLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETddliqgtiRTQFEDC- 1471
Cdd:COG0488 416 LGRF--------LF----SGDdafkpvgVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET--------LEALEEAl 475
|
250 260 270
....*....|....*....|....*....|....*...
gi 1937891448 1472 -----TVLTIAH-R--LNTIMDynRVLVLDKGVVAEFD 1501
Cdd:COG0488 476 ddfpgTVLLVSHdRyfLDRVAT--RILEFEDGGVREYP 511
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1284-1499 |
2.77e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 82.16 E-value: 2.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYRPGLELV--LKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHI---GLHDL 1358
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1359 RSQLTIIPQDPILFSG-------TLRMNLDpfgRYSDEDIWRT----LELSHLSAFVSSQPTgldfqcseggdNLSVGQR 1427
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSrtvfdnvALPLELA---GTPKAEIKARvtelLELVGLSDKADRYPA-----------QLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1428 QLVCLARALLRKSRVLVLDEATAAIDLETD----DLIQGTIRTQfeDCTVLTIAHRlntiMDY-----NRVLVLDKGVVA 1498
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPATTrsilELLKDINREL--GLTIVLITHE----MDVvkricDRVAVIDAGRLV 220
|
.
gi 1937891448 1499 E 1499
Cdd:PRK11153 221 E 221
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
626-840 |
3.01e-16 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 80.55 E-value: 3.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSVAYVPQQAW------- 698
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeirkkvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 699 --IQN-------CTLQENVLFGqPMN--------PKRYQQALETCALLADLDVLPggdqteigekgINLSGGQRQRVSLA 761
Cdd:TIGR04520 81 mvFQNpdnqfvgATVEDDVAFG-LENlgvpreemRKRVDEALKLVGMEDFRDREP-----------HLLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 762 RAVYSDANIFLLDDPLSAVDshvakhifdqvigPEG---VLA---------GKTRVLVTHGISFLPQTDFIIVLADGQIT 829
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLD-------------PKGrkeVLEtirklnkeeGITVISITHDMEEAVLADRVIVMNKGKIV 215
|
250
....*....|.
gi 1937891448 830 EMGHYSELLQH 840
Cdd:TIGR04520 216 AEGTPREIFSQ 226
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1284-1498 |
3.08e-16 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 80.13 E-value: 3.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSmtlcLFRILEA----AEG---EIF---IDGLNV--- 1350
Cdd:COG1119 3 LLELRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKST----LLSLITGdlppTYGndvRLFgerRGGEDVwel 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1351 -AHIGL------HDLRSQLTIIpqDPIL--FSGTLrmnlDPFGRYSDEDI---WRTLELSHLSAFvSSQPTGldfqcseg 1418
Cdd:COG1119 77 rKRIGLvspalqLRFPRDETVL--DVVLsgFFDSI----GLYREPTDEQReraRELLELLGLAHL-ADRPFG-------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1419 gdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT--QFEDCTVLTIAHRLNTIMD-YNRVLVLDKG 1495
Cdd:COG1119 142 --TLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPgITHVLLLKDG 219
|
....
gi 1937891448 1496 -VVA 1498
Cdd:COG1119 220 rVVA 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
625-852 |
3.13e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 80.70 E-value: 3.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 625 AITIHNGTFSWsKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS----------VAYVP 694
Cdd:PRK15056 6 GIVVNDVTVTW-RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 695 QQA---WIQNCTLQENVLFGQPMN------PKRYQQALETCALlADLDVLPGgDQTEIGEkginLSGGQRQRVSLARAVY 765
Cdd:PRK15056 85 QSEevdWSFPVLVEDVVMMGRYGHmgwlrrAKKRDRQIVTAAL-ARVDMVEF-RHRQIGE----LSGGQKKRVFLARAIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 766 SDANIFLLDDPLSAVDSHVAKHIFDQVigPEGVLAGKTRVLVTHGISFLPQ-TDFII-----VLADGQiTEMGHYSELLQ 839
Cdd:PRK15056 159 QQGQVILLDEPFTGVDVKTEARIISLL--RELRDEGKTMLVSTHNLGSVTEfCDYTVmvkgtVLASGP-TETTFTAENLE 235
|
250
....*....|...
gi 1937891448 840 HdgSFANFLRNYA 852
Cdd:PRK15056 236 L--AFSGVLRHVA 246
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1282-1497 |
3.31e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 80.66 E-value: 3.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1282 SGVVEFRNYSVRYRPGLElVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDG--LNVAHIGLHDLR 1359
Cdd:PRK13636 3 DYILKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1360 SQLTIIPQDP--ILFS---------GTLRMNL--DPFGRYSDEDIWRTlELSHLsafvSSQPTgldfQCseggdnLSVGQ 1426
Cdd:PRK13636 82 ESVGMVFQDPdnQLFSasvyqdvsfGAVNLKLpeDEVRKRVDNALKRT-GIEHL----KDKPT----HC------LSFGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937891448 1427 RQLVCLARALLRKSRVLVLDEATAAID-LETDDLIQGTIRTQFE-DCTVLTIAHRLNTIMDY-NRVLVLDKGVV 1497
Cdd:PRK13636 147 KKRVAIAGVLVMEPKVLVLDEPTAGLDpMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYcDNVFVMKEGRV 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1284-1503 |
5.66e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 79.80 E-value: 5.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLT 1363
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1364 IIPQDPI-LFSGT---------LRMNLDPFGRYSdEDIWRTLELSHLSAFVSSQPtgldfqcseggDNLSVGQRQLVCLA 1433
Cdd:PRK13648 87 IVFQNPDnQFVGSivkydvafgLENHAVPYDEMH-RRVSEALKQVDMLERADYEP-----------NALSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 1434 RALLRKSRVLVLDEATAAIDLET-DDLIQGTIRTQFE-DCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSP 1503
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDArQNLLDLVRKVKSEhNITIISITHDLSEAMEADHVIVMNKGTVYKEGTP 226
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
641-828 |
6.82e-16 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 78.22 E-value: 6.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-SVAYVPQQA----------------WIQNCT 703
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqDVSDLRGRAipylrrkigvvfqdfrLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 704 LQENVLF-----GQPMN--PKRYQQALETCALLADLDVLPGGdqteigekginLSGGQRQRVSLARAVYSDANIFLLDDP 776
Cdd:cd03292 95 VYENVAFalevtGVPPReiRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1937891448 777 LSAVDSHVAKHIFDQVigpEGV-LAGKTRVLVTHGISFLPQTDF-IIVLADGQI 828
Cdd:cd03292 164 TGNLDPDTTWEIMNLL---KKInKAGTTVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
647-848 |
7.29e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 78.64 E-value: 7.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 647 NIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-SVAYVP----------QQawiQNC----TLQENVLFG 711
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqDLTALPpaerpvsmlfQE---NNLfphlTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 712 qpMNP---------KRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDS 782
Cdd:COG3840 96 --LRPglkltaeqrAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937891448 783 hvAK-----HIFDQVIGPEGVlagkTRVLVTHGIS-FLPQTDFIIVLADGQITEMGHYSELLQHDGS--FANFL 848
Cdd:COG3840 163 --ALrqemlDLVDELCRERGL----TVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALLDGEPPpaLAAYL 230
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
643-828 |
8.24e-16 |
|
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: 77.96 E-value: 8.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSVAYVPQQAWIQ----------------NCTLQE 706
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElrqkvgmvfqqfnlfpHLTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 707 NVLFG----QPMNPK----RYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLS 778
Cdd:cd03262 96 NITLApikvKGMSKAeaeeRALELLEKVGLADKADAYPA-----------QLSGGQQQRVAIARALAMNPKVMLFDEPTS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 779 AVDSHVAKHIFDQVIGpegvLA--GKTRVLVTHGISFLPQ-TDFIIVLADGQI 828
Cdd:cd03262 165 ALDPELVGEVLDVMKD----LAeeGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
626-833 |
8.43e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 78.17 E-value: 8.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWSKDlPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEmEKL-EGAVSVKG---------SVAY--- 692
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGE-ERPtSGQVLVNGqdlsrlkrrEIPYlrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 693 ----VPQQAW-IQNCTLQENVLFgqPM-----NPKRYQQ----ALETCALLADLDVLPggdqteigekgINLSGGQRQRV 758
Cdd:COG2884 80 rigvVFQDFRlLPDRTVYENVAL--PLrvtgkSRKEIRRrvreVLDLVGLSDKAKALP-----------HELSGGEQQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 759 SLARAVYSDANIFLLDDPLSAVDSHVAKHIFDqvigpegVL-----AGKTRVLVTHGISFLPQTDF-IIVLADGQITEMG 832
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEIME-------LLeeinrRGTTVLIATHDLELVDRMPKrVLELEDGRLVRDE 219
|
.
gi 1937891448 833 H 833
Cdd:COG2884 220 A 220
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
658-840 |
1.01e-15 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 80.23 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 658 VVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-SVAYVPQQ-----------AWIQNCTLQENVLFGQPMN--PK-----R 718
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGeDVTNVPPHlrhinmvfqsyALFPHMTVEENVAFGLKMRkvPRaeikpR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 719 YQQALETCALladldvlpggdQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGPEGV 798
Cdd:TIGR01187 81 VLEALRLVQL-----------EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1937891448 799 LaGKTRVLVTHGIS-FLPQTDFIIVLADGQITEMGHYSELLQH 840
Cdd:TIGR01187 150 L-GITFVFVTHDQEeAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
643-832 |
1.16e-15 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 80.53 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGeMEKL-EGAVSVKG-----------SVAYVPQQ-AWIQNCTLQENVL 709
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAG-FETPdSGRILLDGrdvtglppekrNVGMVFQDyALFPHLTVAENVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 710 FG---QPMNP----KRYQQALETCALLADLDVLPggDQteigekginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDS 782
Cdd:COG3842 100 FGlrmRGVPKaeirARVAELLELVGLEGLADRYP--HQ---------LSGGQQQRVALARALAPEPRVLLLDEPLSALDA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 783 HVA-------KHIFDQVigpegvlaGKTRVLVTH------GISflpqtDFIIVLADGQITEMG 832
Cdd:COG3842 169 KLReemreelRRLQREL--------GITFIYVTHdqeealALA-----DRIAVMNDGRIEQVG 218
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
625-832 |
1.25e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 78.54 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 625 AITIHNgtFSWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSAlLGEMEKLEGAVSVKGSVAYVPQQAWIQNCTL 704
Cdd:PRK14258 7 AIKVNN--LSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQNIYERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 705 Q---------------------ENVLFGQPM---NPK-RYQQALETCALLADL-DVLpggdQTEIGEKGINLSGGQRQRV 758
Cdd:PRK14258 84 NrlrrqvsmvhpkpnlfpmsvyDNVAYGVKIvgwRPKlEIDDIVESALKDADLwDEI----KHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 759 SLARAVYSDANIFLLDDPLSAVDShVAKHIFDQVIGPEGVLAGKTRVLVTHGisfLPQ----TDFIIVLAD-----GQIT 829
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDP-IASMKVESLIQSLRLRSELTMVIVSHN---LHQvsrlSDFTAFFKGnenriGQLV 235
|
...
gi 1937891448 830 EMG 832
Cdd:PRK14258 236 EFG 238
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
643-840 |
1.59e-15 |
|
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: 81.49 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG----------------SVAYVPQQAWIQ-NC--T 703
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkdltklsrrslrelrrRVQMVFQDPYSSlNPrmT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 704 LQENVLFG----QPMNPK----RYQQALETCALLAD-LDVLPGGdqteigekginLSGGQRQRVSLARAVYSDANIFLLD 774
Cdd:COG1123 361 VGDIIAEPlrlhGLLSRAerreRVAELLERVGLPPDlADRYPHE-----------LSGGQRQRVAIARALALEPKLLILD 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 775 DPLSAVDSHVAKHIFDqvigpegVLA------GKTRVLVTHGISFLPQ-TDFIIVLADGQITEMGHYSELLQH 840
Cdd:COG1123 430 EPTSALDVSVQAQILN-------LLRdlqrelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
622-850 |
1.74e-15 |
|
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: 78.45 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 622 PGRAITIHNGTFSWSKDLPPT-----LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-------- 688
Cdd:cd03294 14 PQKAFKLLAKGKSKEEILKKTgqtvgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 689 ---------SVAYVPQQ-AWIQNCTLQENVLFG---QPMNPK----RYQQALETCALLADLDVLPGgdqteigekgiNLS 751
Cdd:cd03294 94 kelrelrrkKISMVFQSfALLPHRTVLENVAFGlevQGVPRAereeRAAEALELVGLEGWEHKYPD-----------ELS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 752 GGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGPEGVLaGKTRVLVTHG-ISFLPQTDFIIVLADGQITE 830
Cdd:cd03294 163 GGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAEL-QKTIVFITHDlDEALRLGDRIAIMKDGRLVQ 241
|
250 260
....*....|....*....|..
gi 1937891448 831 MGHYSELLQH--DGSFANFLRN 850
Cdd:cd03294 242 VGTPEEILTNpaNDYVREFFRG 263
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
310-601 |
1.87e-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: 78.75 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 310 LLMGACFKLIQDLLSFINPQLLSILI-RFISDPTAPTWWgfLLAGLMFVSSTMQTLILHQHYHCIFVMALRIRTAIIGVI 388
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIdDVIPAGDLSLLL--WIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 389 YRKALTITNSVKREYTVGEMVNLMSVDAQRFMD-VSPFINLLWSAPLQVILAIYFL----WQIlgpsALAGVAVIVLLIP 463
Cdd:cd07346 79 FRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNlVSSGLLQLLSDVLTLIGALVILfylnWKL----TLVALLLLPLYVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 464 LNGAVSMKMKTYQVQQMKFKDSRIKLMSEILNGIKVLKLYAWEPT----FLEQVEGIRQSELQLLRKGAYLQAISTFIWV 539
Cdd:cd07346 155 ILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEReierFREANRDLRDANLRAARLSALFSPLIGLLTA 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 540 CTPFMVTL----------ITLGVYVcvdknnvldaekAFvsLSLFNILKIPLNLLPQLISGMTQTSVSLKRI 601
Cdd:cd07346 235 LGTALVLLyggylvlqgsLTIGELV------------AF--LAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
644-828 |
1.91e-15 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 76.95 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 644 HSLNIQIP-KGALVAVVGPVGCGKSSLVSALLGeMEKLE-GAVSVKGS-----------------VAYVPQQ-AWIQNCT 703
Cdd:cd03297 13 FTLKIDFDlNEEVTGIFGASGAGKSTLLRCIAG-LEKPDgGTIVLNGTvlfdsrkkinlppqqrkIGLVFQQyALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 704 LQENVLFGQPMNPKRYQQALETcALLADLDVlpggdqTEIGEKGI-NLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDS 782
Cdd:cd03297 92 VRENLAFGLKRKRNREDRISVD-ELLDLLGL------DHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1937891448 783 HVAKHIFDQVigpEGVLA--GKTRVLVTHGISFLPQ-TDFIIVLADGQI 828
Cdd:cd03297 165 ALRLQLLPEL---KQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRL 210
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1301-1495 |
2.45e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 77.82 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1301 VLKNLTLHVQGGEKVGIVGRTGAGKSSmtlcLFRI----LEAAEGEIFIDGLNVAHIGLHDlRSQLtI--IPQDPILfsG 1374
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKST----LLNAiagsLPPDSGSILIDGKDVTKLPEYK-RAKY-IgrVFQDPMM--G 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1375 T---------------------LRMNLDPfgrySDEDIWR----TLELS---HLSAfvssqPTGLdfqcseggdnLSVGQ 1426
Cdd:COG1101 93 TapsmtieenlalayrrgkrrgLRRGLTK----KRRELFRellaTLGLGlenRLDT-----KVGL----------LSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937891448 1427 RQLVCLARALLRKSRVLVLDEATAAID-------LE-TDDLIQGtirtqfEDCTVLTIAHRLNTIMDY-NRVLVLDKG 1495
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDpktaalvLElTEKIVEE------NNLTTLMVTHNMEQALDYgNRLIMMHEG 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1287-1497 |
3.42e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.49 E-value: 3.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1287 FRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAEGEIFID-GLNVAHiglhdlrsq 1361
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKST----LLKILagelEPDSGEVSIPkGLRIGY--------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1362 ltiIPQDPILFSG-TLRMN-LDPFGRYSdeDIWRTL-ELSHLSAFVSSQP--------------------------TGLD 1412
Cdd:COG0488 66 ---LPQEPPLDDDlTVLDTvLDGDAELR--ALEAELeELEAKLAEPDEDLerlaelqeefealggweaearaeeilSGLG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1413 FQCSEGG---DNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTqfEDCTVLTIAH-R--LNTIMdy 1486
Cdd:COG0488 141 FPEEDLDrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN--YPGTVLVVSHdRyfLDRVA-- 216
|
250
....*....|.
gi 1937891448 1487 NRVLVLDKGVV 1497
Cdd:COG0488 217 TRILELDRGKL 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1276-1509 |
3.66e-15 |
|
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: 80.50 E-value: 3.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1276 PEGWPRSGVVEFRnysvryrpglelVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRiLEAAEGEIFIDGLNVAHIG- 1354
Cdd:COG4172 288 KRGLFRRTVGHVK------------AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGLSr 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1355 --LHDLRSQLTIIPQDPilFsGTL--RMN---------------LDPFGRysDEDIWRTLELSHLSafvssqPTGLD--- 1412
Cdd:COG4172 355 raLRPLRRRMQVVFQDP--F-GSLspRMTvgqiiaeglrvhgpgLSAAER--RARVAEALEEVGLD------PAARHryp 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1413 --FqcseggdnlSVGQRQLVCLARALLRKSRVLVLDEATAAIDLetddliqgTIRTQfedctVLT--------------- 1475
Cdd:COG4172 424 heF---------SGGQRQRIAIARALILEPKLLVLDEPTSALDV--------SVQAQ-----ILDllrdlqrehglaylf 481
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1937891448 1476 IAHRLnTIMDY--NRVLVLDKGVVAE-------FDSPVN-----LIAA 1509
Cdd:COG4172 482 ISHDL-AVVRAlaHRVMVMKDGKVVEqgpteqvFDAPQHpytraLLAA 528
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1284-1507 |
3.69e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 76.67 E-value: 3.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNV--AHIGLHDLRSQ 1361
Cdd:PRK09493 1 MIEFKNVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1362 LTIIPQDPILFSGTLRMNLDPFG--------RYSDEDIWRTLeLSH--LSAFVSSQPtgldfqcSEggdnLSVGQRQLVC 1431
Cdd:PRK09493 79 AGMVFQQFYLFPHLTALENVMFGplrvrgasKEEAEKQAREL-LAKvgLAERAHHYP-------SE----LSGGQQQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937891448 1432 LARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFED-CTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSPVNLI 1507
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLI 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1285-1503 |
3.74e-15 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 76.61 E-value: 3.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSmtlcLFRI---LEAA-EGEIFIDGLNVAHIGLHDlrS 1360
Cdd:cd03296 3 IEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTT----LLRLiagLERPdSGTILFGGEDATDVPVQE--R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1361 QLTIIPQDPILFSG-TLRMNLdPFG--------RYSDEDIWRT----LELSHLSAFVSSQPTgldfqcseggdNLSVGQR 1427
Cdd:cd03296 75 NVGFVFQHYALFRHmTVFDNV-AFGlrvkprseRPPEAEIRAKvhelLKLVQLDWLADRYPA-----------QLSGGQR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937891448 1428 QLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTI--AHRLNTIMDY-NRVLVLDKGVVAEFDSP 1503
Cdd:cd03296 143 QRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVfvTHDQEEALEVaDRVVVMNKGRIEQVGTP 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
641-840 |
3.87e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 76.67 E-value: 3.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSAlLGEMEKLEGA------VSVKGSVA----------YVPQQAWI-QNCT 703
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRC-INKLEEITSGdlivdgLKVNDPKVderlirqeagMVFQQFYLfPHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 704 LQENVLFGqpmnPKR---------YQQALEtcaLLADLdvlpgGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLD 774
Cdd:PRK09493 94 ALENVMFG----PLRvrgaskeeaEKQARE---LLAKV-----GLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937891448 775 DPLSAVDSHVAKHIFD--QVIGPEGVlagkTRVLVTHGISFLPQT-DFIIVLADGQITEMGHYSELLQH 840
Cdd:PRK09493 162 EPTSALDPELRHEVLKvmQDLAEEGM----TMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1306-1503 |
4.13e-15 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 78.23 E-value: 4.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1306 TLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIG---LHDLRSQLTIIPQDPilfSGTL--RMN- 1379
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP---YASLnpRMTv 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1380 -------LDPFGRYSDEDIW-RTLEL--------SHLSAFvssqPtgldfqcSEggdnLSVGQRQLVCLARALLRKSRVL 1443
Cdd:COG4608 115 gdiiaepLRIHGLASKAERReRVAELlelvglrpEHADRY----P-------HE----FSGGQRQRIGIARALALNPKLI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 1444 VLDEATAAIDLEtddlIQGTIRTQFED------CTVLTIAHRLNT---IMDynRVLVLDKGVVAE-------FDSP 1503
Cdd:COG4608 180 VCDEPVSALDVS----IQAQVLNLLEDlqdelgLTYLFISHDLSVvrhISD--RVAVMYLGKIVEiaprdelYARP 249
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1285-1506 |
4.25e-15 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 78.60 E-value: 4.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSsmTLClfRIL----EAAEGEIFIDGLNVAHIGLHDlRs 1360
Cdd:COG3842 6 LELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKT--TLL--RMIagfeTPDSGRILLDGRDVTGLPPEK-R- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1361 QLTIIPQDPILFsgtlrmnldP---------FG----RYSDEDIWR----TLELSHLSAFVSSQPtgldfqcseggDNLS 1423
Cdd:COG3842 78 NVGMVFQDYALF---------PhltvaenvaFGlrmrGVPKAEIRArvaeLLELVGLEGLADRYP-----------HQLS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1424 VGQRQLVCLARALLRKSRVLVLDEATAAIDLETddliqgTIRTQFEdctVLTIAHRLN--TIM------------DynRV 1489
Cdd:COG3842 138 GGQQQRVALARALAPEPRVLLLDEPLSALDAKL------REEMREE---LRRLQRELGitFIYvthdqeealalaD--RI 206
|
250
....*....|....*..
gi 1937891448 1490 LVLDKGVVAEFDSPVNL 1506
Cdd:COG3842 207 AVMNDGRIEQVGTPEEI 223
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
643-832 |
4.94e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 76.80 E-value: 4.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSAL-----LGEMEKLEGAVSVKGSVAYVPQQAWIQ----------------N 701
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPIEvrrevgmvfqypnpfpH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 702 CTLQENVLFGQPMN---------PKRYQQALETCALLADLdvlpggdQTEIGEKGINLSGGQRQRVSLARAVYSDANIFL 772
Cdd:PRK14267 100 LTIYDNVAIGVKLNglvkskkelDERVEWALKKAALWDEV-------KDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937891448 773 LDDPLSAVDSHVAKHIfdqvigPEGVLAGK---TRVLVTHGISFLPQ-TDFIIVLADGQITEMG 832
Cdd:PRK14267 173 MDEPTANIDPVGTAKI------EELLFELKkeyTIVLVTHSPAQAARvSDYVAFLYLGKLIEVG 230
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1285-1507 |
5.03e-15 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 76.22 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYRpglELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAhiGLHDLRSQLTI 1364
Cdd:cd03299 1 LKVENLSKDWK---EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1365 IPQDPILFSGT---------LRMNLDPfgRYSDE----DIWRTLELSHLsafVSSQPTgldfqcseggdNLSVGQRQLVC 1431
Cdd:cd03299 76 VPQNYALFPHMtvykniaygLKKRKVD--KKEIErkvlEIAEMLGIDHL---LNRKPE-----------TLSGGEQQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1432 LARALLRKSRVLVLDEATAAIDLETDDLIQ---GTIRTQFeDCTVLTIAHRLNTI-MDYNRVLVLDKGVVAEFDSPVNLI 1507
Cdd:cd03299 140 IARALVVNPKILLLDEPFSALDVRTKEKLReelKKIRKEF-GVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1284-1508 |
6.40e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.95 E-value: 6.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYRPGLElVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIG-LHDLRSQL 1362
Cdd:PRK13644 1 MIRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1363 TIIPQDPilfsgtlrmNLDPFGRYSDEDI--------WRTLELSHLSAFVSSQpTGLDFQCSEGGDNLSVGQRQLVCLAR 1434
Cdd:PRK13644 80 GIVFQNP---------ETQFVGRTVEEDLafgpenlcLPPIEIRKRVDRALAE-IGLEKYRHRSPKTLSGGQGQCVALAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937891448 1435 ALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDC-TVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIA 1508
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
643-829 |
7.16e-15 |
|
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: 73.62 E-value: 7.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGsvayvpqqawiqnctlqENVLFGqpmNPKRYQQA 722
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG-----------------KEVSFA---SPRDARRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 723 letcalladldvlpggdqteigekGIN----LSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVigpeGV 798
Cdd:cd03216 76 ------------------------GIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVI----RR 127
|
170 180 190
....*....|....*....|....*....|....
gi 1937891448 799 LA--GKTRVLVTHGISFLPQT-DFIIVLADGQIT 829
Cdd:cd03216 128 LRaqGVAVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1289-1499 |
8.56e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.82 E-value: 8.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1289 NYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTIIPQD 1368
Cdd:PRK11231 7 NLTVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1369 PILFSG-TLR----------MNLdpFGRYSDED---IWRTLELSHLSAFVSSQPTgldfqcseggdNLSVGQRQLVCLAR 1434
Cdd:PRK11231 85 HLTPEGiTVRelvaygrspwLSL--WGRLSAEDnarVNQAMEQTRINHLADRRLT-----------DLSGGQRQRAFLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937891448 1435 ALLRKSRVLVLDEATAAIDL----ETDDLIQgtiRTQFEDCTVLTIAHRLNTIMDY-NRVLVLDKG-VVAE 1499
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDInhqvELMRLMR---ELNTQGKTVVTVLHDLNQASRYcDHLVVLANGhVMAQ 219
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1291-1506 |
1.01e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 75.87 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1291 SVRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAEGEifidgLNVAHIGLHDLRSQLTIIP 1366
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKST----LLRLLagleTPSAGE-----LLAGTAPLAEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1367 QDPILFsgtlrmnldPFGRYSD------EDIWRTLELSHLSAfvssqpTGLDFQCSEGGDNLSVGQRQLVCLARALLRKS 1440
Cdd:PRK11247 88 QDARLL---------PWKKVIDnvglglKGQWRDAALQALAA------VGLADRANEWPAALSGGQKQRVALARALIHRP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937891448 1441 RVLVLDEATAAID----LETDDLIQGTIRTQ-FedcTVLTIAHRLN---TIMDynRVLVLDKGVVAeFDSPVNL 1506
Cdd:PRK11247 153 GLLLLDEPLGALDaltrIEMQDLIESLWQQHgF---TVLLVTHDVSeavAMAD--RVLLIEEGKIG-LDLTVDL 220
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
641-841 |
1.03e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.96 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-------------SVAYVPQQAWIQ-NCTLQE 706
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVASVPQDTSLSfEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 707 NVLFGQPMNPKRYQQALETCALLADlDVLPGGDQTEIGEKGI-NLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVA 785
Cdd:PRK09536 97 VVEMGRTPHRSRFDTWTETDRAAVE-RAMERTGVAQFADRPVtSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1937891448 786 KHIFDQVigPEGVLAGKTRVLVTHGISFLPQ-TDFIIVLADGQITEMGHYSELLQHD 841
Cdd:PRK09536 176 VRTLELV--RRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
612-881 |
1.25e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 77.57 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 612 PQCVERKTISPgrAITIHNGTFSWskDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-SV 690
Cdd:PRK11607 8 PQAKTRKALTP--LLEIRNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 691 AYVP-----------QQAWIQNCTLQENVLFG--QPMNPK-----RYQQALETCALladldvlpggdQTEIGEKGINLSG 752
Cdd:PRK11607 84 SHVPpyqrpinmmfqSYALFPHMTVEQNIAFGlkQDKLPKaeiasRVNEMLGLVHM-----------QEFAKRKPHQLSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 753 GQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGP-EGVlaGKTRVLVTHGI-SFLPQTDFIIVLADGQITE 830
Cdd:PRK11607 153 GQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDIlERV--GVTCVMVTHDQeEAMTMAGRIAIMNRGKFVQ 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 831 MGHYSELLQHDGSfanflrNYAPDENQEAN--EGVLQHANEEVLLLEDTLSTH 881
Cdd:PRK11607 231 IGEPEEIYEHPTT------RYSAEFIGSVNvfEGVLKERQEDGLVIDSPGLVH 277
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
641-782 |
1.28e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 75.51 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSVAYVP---------QQAWIQNCTLQENVLFG 711
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPgaergvvfqNEGLLPWRNVQDNVAFG 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937891448 712 QPM----NPKRYQQALEtcaLLADLDvLPGGDQTEIGEkginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDS 782
Cdd:PRK11248 95 LQLagveKMQRLEIAHQ---MLKKVG-LEGAEKRYIWQ----LSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1301-1512 |
1.50e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.57 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1301 VLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTIIPQDPIL---FSG--T 1375
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsfeFDVrqV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1376 LRMNLDP----FGRYSDED---IWRTLELSHLSAFVSsQPTgldfqcseggDNLSVGQRQLVCLARALLRKSRVLVLDEA 1448
Cdd:PRK09536 98 VEMGRTPhrsrFDTWTETDraaVERAMERTGVAQFAD-RPV----------TSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937891448 1449 TAAIDL----ETDDLIQgtiRTQFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSPVNLIAAGGI 1512
Cdd:PRK09536 167 TASLDInhqvRTLELVR---RLVDDGKTAVAAIHDLDLAARYcDELVLLADGRVRAAGPPADVLTADTL 232
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1285-1497 |
1.54e-14 |
|
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: 74.37 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYrPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHigLHD-----LR 1359
Cdd:cd03292 1 IEFINVTKTY-PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSD--LRGraipyLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1360 SQLTIIPQDPILFSG---------TLRMNLDPfGRYSDEDIWRTLELSHLSAFVSSQPTGldfqcseggdnLSVGQRQLV 1430
Cdd:cd03292 78 RKIGVVFQDFRLLPDrnvyenvafALEVTGVP-PREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1431 CLARALLRKSRVLVLDEATAAIDLETDDLIQgTIRTQFED--CTVLTIAHRLNTIMDYN-RVLVLDKGVV 1497
Cdd:cd03292 146 AIARAIVNSPTILIADEPTGNLDPDTTWEIM-NLLKKINKagTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
647-832 |
1.55e-14 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 74.13 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 647 NIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-SVAYVPQQAWIQNCTLQENVLF---------GQPMNP 716
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDqSHTGLAPYQRPVSMLFQENNLFahltvrqniGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 717 -----KRYQQALETCAL---LAD-LDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKH 787
Cdd:TIGR01277 98 glklnAEQQEKVVDAAQqvgIADyLDRLPE-----------QLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1937891448 788 IFdQVIGPEGVLAGKTRVLVTHGISFLPQT-DFIIVLADGQITEMG 832
Cdd:TIGR01277 167 ML-ALVKQLCSERQRTLLMVTHHLSDARAIaSQIAVVSQGKIKVVS 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
646-832 |
1.64e-14 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 74.07 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 646 LNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-SVAYVPQQAWIQNCTLQENVLF---------GQPMN 715
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvDVTAAPPADRPVSMLFQENNLFahltveqnvGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 716 PKRY-----QQALETCAL---LADLDV-LPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAK 786
Cdd:cd03298 97 PGLKltaedRQAIEVALArvgLAGLEKrLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1937891448 787 HIFDQVIGPEGVlAGKTRVLVTHGIS-FLPQTDFIIVLADGQITEMG 832
Cdd:cd03298 166 EMLDLVLDLHAE-TKMTVLMVTHQPEdAKRLAQRVVFLDNGRIAAQG 211
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
643-848 |
1.88e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 74.67 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSAL-LGEMEKlEGAVSVKGS-------------------VAYVPQQ--AWiQ 700
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMPR-SGTLNIAGNhfdfsktpsdkairelrrnVGMVFQQynLW-P 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 701 NCTLQENvLFGQPMN------PKRYQQALEtcaLLADLDVLPGGDQTEIgekgiNLSGGQRQRVSLARAVYSDANIFLLD 774
Cdd:PRK11124 96 HLTVQQN-LIEAPCRvlglskDQALARAEK---LLERLRLKPYADRFPL-----HLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 775 DPLSAVDSHVAKHIFDqvIGPEGVLAGKTRVLVTHGISFLPQT-DFIIVLADGQITEMGHYSELLQ-HDGSFANFL 848
Cdd:PRK11124 167 EPTAALDPEITAQIVS--IIRELAETGITQVIVTHEVEVARKTaSRVVYMENGHIVEQGDASCFTQpQTEAFKNYL 240
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
632-840 |
1.93e-14 |
|
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: 74.54 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 632 TFSWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGeMEK-LEGAVSVKG----------------SVAYVP 694
Cdd:cd03258 10 VFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING-LERpTSGSVLVDGtdltllsgkelrkarrRIGMIF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 695 QQ-AWIQNCTLQENVLF-----GQPMNpKRYQQALETCAL--LADL-DVLPGgdqteigekgiNLSGGQRQRVSLARAVY 765
Cdd:cd03258 89 QHfNLLSSRTVFENVALpleiaGVPKA-EIEERVLELLELvgLEDKaDAYPA-----------QLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 766 SDANIFLLDDPLSAVDSHVAKHIFD------QVIGPegvlagkTRVLVTHGISFLPQ-TDFIIVLADGQITEMGHYSELL 838
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILAllrdinRELGL-------TIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
..
gi 1937891448 839 QH 840
Cdd:cd03258 230 AN 231
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
645-848 |
1.94e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 76.68 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 645 SLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSvaYVPQQAwIQN---C------------TLQENVL 709
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE--DVTHRS-IQQrdiCmvfqsyalfphmSLGENVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 710 FGQPMN--PK-----RYQQALEtcalLADLDvlpgG------DQteigekginLSGGQRQRVSLARAVYSDANIFLLDDP 776
Cdd:PRK11432 101 YGLKMLgvPKeerkqRVKEALE----LVDLA----GfedryvDQ---------ISGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937891448 777 LSAVDSHVAKHIFDQVIGPEGVLaGKTRVLVTHGIS-FLPQTDFIIVLADGQITEMGHYSELLQHDGS--FANFL 848
Cdd:PRK11432 164 LSNLDANLRRSMREKIRELQQQF-NITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQPASrfMASFM 237
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
643-832 |
2.14e-14 |
|
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: 74.20 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-SVAYVP----------QQ-AWIQNCTLQENVLF 710
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkDITNLPphkrpvntvfQNyALFPHLTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 711 GQPMNPKRYQQALETCALLADLDVLPGGDQTEIGEkginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKH--- 787
Cdd:cd03300 96 GLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQ----LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDmql 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1937891448 788 ----IFDQVigpegvlaGKTRVLVTHGIS-FLPQTDFIIVLADGQITEMG 832
Cdd:cd03300 172 elkrLQKEL--------GITFVFVTHDQEeALTMSDRIAVMNKGKIQQIG 213
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1295-1503 |
2.28e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 77.00 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1295 RPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRS----QLTIIPQDPI 1370
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1371 LFSGTLRMNLDPFGrysdediwrtLELSHLS-------AFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVL 1443
Cdd:PRK10070 117 LMPHMTVLDNTAFG----------MELAGINaeerrekALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 1444 VLDEATAAID--LET---DDLIQGTIRTQFedcTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSP 1503
Cdd:PRK10070 187 LMDEAFSALDplIRTemqDELVKLQAKHQR---TIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTP 249
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
643-848 |
2.35e-14 |
|
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: 74.29 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS-----------VAYVPQQ-AWIQNCTLQENVLF 710
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNyALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 711 G----QPMNPKRYQQALETCALLADLDVLpggdqteiGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAK 786
Cdd:cd03299 95 GlkkrKVDKKEIERKVLEIAEMLGIDHLL--------NRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937891448 787 HIFDQV--IGPEgvlAGKTRVLVTHGIS-FLPQTDFIIVLADGQITEMGHYSELLQH--DGSFANFL 848
Cdd:cd03299 167 KLREELkkIRKE---FGVTVLHVTHDFEeAWALADKVAIMLNGKLIQVGKPEEVFKKpkNEFVAEFL 230
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
1008-1256 |
2.40e-14 |
|
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: 75.28 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1008 LGVYATLGILQGLLVMLSAFTMVVGAIQAARLLHTALLHNQIRAPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLF 1087
Cdd:cd07346 42 ALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1088 NSFYTSISTIVVIVASTPLFCVVVLPLAVFYGFVQRFYVATSRQLKRLESVSRSPIFSHFSETVTGTSVIRAYGR----V 1163
Cdd:cd07346 122 SDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAeereI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1164 QDFKVLSDAKVDSNQKTTYPYIASNRWLGVHVEFVGNCVVLFSALFavIGRNSLNPGLVGLSVSYALQVTLSLNWMIRTL 1243
Cdd:cd07346 202 ERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYL--VLQGSLTIGELVAFLAYLGMLFGPIQRLANLY 279
|
250
....*....|...
gi 1937891448 1244 SDLESNIIAVERV 1256
Cdd:cd07346 280 NQLQQALASLERI 292
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1285-1498 |
2.66e-14 |
|
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: 73.56 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYRP--GLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLhDLRSQL 1362
Cdd:cd03266 2 ITADALTKRFRDvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPA-EARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1363 TIIPQDPILFSG-TLRMNLDPFGRYSD----------EDIWRTLELSHLsafvssqptgLDFQCSEggdnLSVGQRQLVC 1431
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYFAGLYGlkgdeltarlEELADRLGMEEL----------LDRRVGG----FSTGMRQKVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937891448 1432 LARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFED-CTVLTIAHRLNTIMDY-NRVLVLDKGVVA 1498
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERLcDRVVVLHRGRVV 215
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
627-832 |
2.72e-14 |
|
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: 72.97 E-value: 2.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 627 TIHNGTFSWSKDLpptLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLG--EMEKLEGAV----------SVKGSVAYVP 694
Cdd:cd03213 12 TVKSSPSKSGKQL---LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVlingrpldkrSFRKIIGYVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 695 qqawiqnctlQENVLFGQpmnpKRYQQALETCALLadldvlpggdqteigeKGInlSGGQRQRVSLARAVYSDANIFLLD 774
Cdd:cd03213 89 ----------QDDILHPT----LTVRETLMFAAKL----------------RGL--SGGERKRVSIALELVSNPSLLFLD 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 775 DPLSAVDSHVAKHIFDQVIGpegvLA--GKTRVLVTHGIS------FlpqtDFIIVLADGQITEMG 832
Cdd:cd03213 137 EPTSGLDSSSALQVMSLLRR----LAdtGRTIICSIHQPSseifelF----DKLLLLSQGRVIYFG 194
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1301-1465 |
3.21e-14 |
|
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: 73.73 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1301 VLKNLTLHVQGGEKVGIVGRTGAGKSS---MTLCLFRileAAEGEIFIDGLNVAHIGLHDlRSQLTII--PQDPILFSG- 1374
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTtfyMIVGLVK---PDSGKILLDGQDITKLPMHK-RARLGIGylPQEASIFRKl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1375 TLRMNLDPF--GRYSDEDIWRT-----LELSHLSAfVSSQPtgldfqcsegGDNLSVGQRQLVCLARALLRKSRVLVLDE 1447
Cdd:cd03218 91 TVEENILAVleIRGLSKKEREEkleelLEEFHITH-LRKSK----------ASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170
....*....|....*...
gi 1937891448 1448 ATAAIDLETDDLIQGTIR 1465
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIK 177
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
643-786 |
4.79e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 75.51 E-value: 4.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS-----------VAYVPQQ-AWIQNCTLQENVLF 710
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQHyALFRHMTVFDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 711 GQPMNPKRYQ-----------QALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSA 779
Cdd:PRK10851 98 GLTVLPRRERpnaaaikakvtQLLEMVQLAHLADRYPA-----------QLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
....*..
gi 1937891448 780 VDSHVAK 786
Cdd:PRK10851 167 LDAQVRK 173
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1301-1501 |
4.85e-14 |
|
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: 72.95 E-value: 4.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1301 VLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGL-HDLRSQLTIIpqDPILFSGTLrMN 1379
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLgGGFNPELTGR--ENIYLNGRL-LG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1380 LDPfgRYSDEDIWRTLELSHLSAFVsSQPTGldfqcseggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDL 1459
Cdd:cd03220 114 LSR--KEIDEKIDEIIEFSELGDFI-DLPVK----------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEK 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1937891448 1460 IQGTIRTQFEDC-TVLTIAHRLNTIMDY-NRVLVLDKGVVAEFD 1501
Cdd:cd03220 181 CQRRLRELLKQGkTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1301-1492 |
7.65e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 71.50 E-value: 7.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1301 VLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGlnvaHIGLHDLRSQLTIIPQDPILFSGTLRMNL 1380
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVPQRSEVPDSLPLTVRDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1381 ----DPFGRYSDED---IWRTLELSHLSAFVSSQPtgldfqcseggDNLSVGQRQLVCLARALLRKSRVLVLDEATAAID 1453
Cdd:NF040873 83 warrGLWRRLTRDDraaVDDALERVGLADLAGRQL-----------GELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1937891448 1454 LETDDLIQGTIRTQFED-CTVLTIAHRLNTIMDYNRVLVL 1492
Cdd:NF040873 152 AESRERIIALLAEEHARgATVVVVTHDLELVRRADPCVLL 191
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1301-1465 |
7.99e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 71.62 E-value: 7.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1301 VLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAhiglhdlrsQLTIIPQDPILFSG------ 1374
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA---------EQRDEPHENILYLGhlpglk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1375 ---TLRMNLD---PFGRYSDEDIWRTLELSHLSAFvSSQPTGldfqcseggdNLSVGQRQLVCLARALLRKSRVLVLDEA 1448
Cdd:TIGR01189 86 pelSALENLHfwaAIHGGAQRTIEDALAAVGLTGF-EDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170
....*....|....*..
gi 1937891448 1449 TAAIDLETDDLIQGTIR 1465
Cdd:TIGR01189 155 TTALDKAGVALLAGLLR 171
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1285-1506 |
9.61e-14 |
|
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: 72.27 E-value: 9.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAEGEIFIDGLNVAHIGLHdlRS 1360
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTT----LLRLIagfeTPTSGEILLDGKDITNLPPH--KR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1361 QLTIIPQDPILFSG-TLRMNLdPFG----RYSDEDIWR----TLELSHLSAFVSSQPtgldfqcseggDNLSVGQRQLVC 1431
Cdd:cd03300 73 PVNTVFQNYALFPHlTVFENI-AFGlrlkKLPKAEIKErvaeALDLVQLEGYANRKP-----------SQLSGGQQQRVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1432 LARALLRKSRVLVLDEATAAID--------LETDDLiQGTIRTQFEDCT-----VLTIAhrlntimdyNRVLVLDKGVVA 1498
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDlklrkdmqLELKRL-QKELGITFVFVThdqeeALTMS---------DRIAVMNKGKIQ 210
|
....*...
gi 1937891448 1499 EFDSPVNL 1506
Cdd:cd03300 211 QIGTPEEI 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1288-1503 |
9.63e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 72.88 E-value: 9.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1288 RNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAEGEIFIDGLNVAHIGLHDLRSQLT 1363
Cdd:PRK13548 6 RNLSVRL--GGRTLLDDVSLTLRPGEVVAILGPNGAGKST----LLRALsgelSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1364 IIPQDPIL-FSGT----LRMNLDPFGRYSDED---IWRTLELSHLSAFVssqptGLDFQcseggdNLSVGQRQLVCLARA 1435
Cdd:PRK13548 80 VLPQHSSLsFPFTveevVAMGRAPHGLSRAEDdalVAAALAQVDLAHLA-----GRDYP------QLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937891448 1436 LLR------KSRVLVLDEATAAIDL----ETDDLIQGtiRTQFEDCTVLTIAHRLN-TIMDYNRVLVLDKGVVAEFDSP 1503
Cdd:PRK13548 149 LAQlwepdgPPRWLLLDEPTSALDLahqhHVLRLARQ--LAHERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTP 225
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
626-841 |
1.04e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 72.81 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWSKDlpPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-SVAYVPQQAWIQNCTL 704
Cdd:COG4604 2 IEIKNVSKRYGGK--VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGlDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 705 --QEN-----------VLFGqpmnpkRY---------------QQALETCAL--LAD--LDvlpggdqteigekgiNLSG 752
Cdd:COG4604 80 lrQENhinsrltvrelVAFG------RFpyskgrltaedreiiDEAIAYLDLedLADryLD---------------ELSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 753 GQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGpegvLA---GKTRVLVTHGISFLPQ-TDFIIVLADGQI 828
Cdd:COG4604 139 GQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRR----LAdelGKTVVIVLHDINFASCyADHIVAMKDGRV 214
|
250
....*....|...
gi 1937891448 829 TEMGHYSELLQHD 841
Cdd:COG4604 215 VAQGTPEEIITPE 227
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
643-839 |
1.07e-13 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 72.84 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-------------SVAYVPQQAWIQ-NCTLQENV 708
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplaawspwelarRRAVLPQHSSLAfPFTVEEVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 709 LFG---QPMNPKRYQQALETCALLADLDVLPGGDQTEigekginLSGGQRQRVSLARA-------VYSDANIFLLDDPLS 778
Cdd:COG4559 97 ALGrapHGSSAAQDRQIVREALALVGLAHLAGRSYQT-------LSGGEQQRVQLARVlaqlwepVDGGPRWLFLDEPTS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 779 AVD-SH------VAKHIFDQVIgpeGVLAgktrvlVTHGisfLPQT----DFIIVLADGQITEMGHYSELLQ 839
Cdd:COG4559 170 ALDlAHqhavlrLARQLARRGG---GVVA------VLHD---LNLAaqyaDRILLLHQGRLVAQGTPEEVLT 229
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
646-834 |
1.07e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 74.68 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 646 LNIQIPKGALVAVVGPVGCGKSSLVSALLG--------------EMEKLEGAvsvKGSVAYVPQQ-AWIQNCTLQENVLF 710
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGleditsgdlfigekRMNDVPPA---ERGVGMVFQSyALYPHLSVAENMSF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 711 G-------QPMNPKRYQQALETCALLADLDVLPGGdqteigekginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD-- 781
Cdd:PRK11000 99 GlklagakKEEINQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaa 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937891448 782 ---------SHVAKHIfdqvigpegvlaGKTRVLVTHG-ISFLPQTDFIIVLADGQITEMG------HY 834
Cdd:PRK11000 168 lrvqmrieiSRLHKRL------------GRTMIYVTHDqVEAMTLADKIVVLDAGRVAQVGkplelyHY 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
641-839 |
1.43e-13 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 71.70 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS--------------VAYVPQ-QAWIQNCTLQ 705
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEgRRIFPELTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 706 ENVLFG-QPMNPKRYQQALEtcALLADLDVLpggdQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDP---LSAVd 781
Cdd:cd03224 94 ENLLLGaYARRRAKRKARLE--RVYELFPRL----KERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPsegLAPK- 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937891448 782 shVAKHIFDQV--IGPEGVlagkTRVLVTHGISF-LPQTDFIIVLADGQITEMGHYSELLQ 839
Cdd:cd03224 167 --IVEEIFEAIreLRDEGV----TILLVEQNARFaLEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1286-1450 |
1.48e-13 |
|
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: 71.94 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1286 EFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDL-RSQLTI 1364
Cdd:COG0410 5 EVENLHAGY--GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1365 IPQDPILFSG-TLRMNLD--PFGRYSDEDIWRTLElshlsaFV----------SSQPTGldfqcseggdNLSVGQRQLVC 1431
Cdd:COG0410 83 VPEGRRIFPSlTVEENLLlgAYARRDRAEVRADLE------RVyelfprlkerRRQRAG----------TLSGGEQQMLA 146
|
170
....*....|....*....
gi 1937891448 1432 LARALLRKSRVLVLDEATA 1450
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSL 165
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
643-828 |
1.64e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 72.40 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGeMEKLEGAVSVKGSVayvPQQAWIQNCTL--QE-----------NVL 709
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG-LETPSAGELLAGTA---PLAEAREDTRLmfQDarllpwkkvidNVG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 710 FGQPMNPK-RYQQALETCALlADldvlpggdqtEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDShVAKHI 788
Cdd:PRK11247 104 LGLKGQWRdAALQALAAVGL-AD----------RANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA-LTRIE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1937891448 789 FDQVIGPEGVLAGKTRVLVTHGIS-FLPQTDFIIVLADGQI 828
Cdd:PRK11247 172 MQDLIESLWQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
625-849 |
1.75e-13 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 71.97 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 625 AITIHNGTFSWSKDlpPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSAL-LGEMEKlEGAVSVKGS-------------- 689
Cdd:COG4161 2 SIQLKNINCFYGSH--QALFDINLECPSGETLVLLGPSGAGKSSLLRVLnLLETPD-SGQLNIAGHqfdfsqkpsekair 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 690 -----VAYVPQQ--AWiQNCTLQENvLFGQPMN---------PKRYQQALETCALLADLDVLPggdqteigekgINLSGG 753
Cdd:COG4161 79 llrqkVGMVFQQynLW-PHLTVMEN-LIEAPCKvlglskeqaREKAMKLLARLRLTDKADRFP-----------LHLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 754 QRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDqvIGPEGVLAGKTRVLVTHGISFLPQT-DFIIVLADGQITEMG 832
Cdd:COG4161 146 QQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVE--IIRELSQTGITQVIVTHEVEFARKVaSQVVYMEKGRIIEQG 223
|
250
....*....|....*...
gi 1937891448 833 HYSELLQ-HDGSFANFLR 849
Cdd:COG4161 224 DASHFTQpQTEAFAHYLS 241
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
1008-1256 |
2.18e-13 |
|
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: 72.44 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1008 LGVYATLGILQGLLVMLSAFTMVVGAIQAARLLHTALLHNQIRAPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLF 1087
Cdd:cd18547 48 LLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1088 NSFYTSISTIVV-IVASTPLFCVVVL--PLAVFY-----GFVQRFYVATSRQLKRLEsvsrspifSHFSETVTGTSVIRA 1159
Cdd:cd18547 128 SSILTIVGTLIMmLYISPLLTLIVLVtvPLSLLVtkfiaKRSQKYFRKQQKALGELN--------GYIEEMISGQKVVKA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1160 YGR----VQDFKVLSDAKVDSNQK------TTYPYIAsnrwlgvhveFVGN----CVVLFSALFAVigRNSLNPGLVGLS 1225
Cdd:cd18547 200 FNReeeaIEEFDEINEELYKASFKaqfysgLLMPIMN----------FINNlgyvLVAVVGGLLVI--NGALTVGVIQAF 267
|
250 260 270
....*....|....*....|....*....|.
gi 1937891448 1226 VSYALQVTLSLNWMIRTLSDLESNIIAVERV 1256
Cdd:cd18547 268 LQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1287-1504 |
3.77e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 71.26 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1287 FRNYSVRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHI---GLHDLRSQLT 1363
Cdd:PRK10419 13 YAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1364 IIPQDPI-----------LFSGTLR--MNLDPFGRYSdediwRTLELshLSAfVSSQPTGLDfQCSEggdNLSVGQRQLV 1430
Cdd:PRK10419 93 MVFQDSIsavnprktvreIIREPLRhlLSLDKAERLA-----RASEM--LRA-VDLDDSVLD-KRPP---QLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1431 CLARALLRKSRVLVLDEATAAIDLetddLIQGTI-------RTQFeDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAE--- 1499
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDL----VLQAGVirllkklQQQF-GTACLFITHDLRLVERFcQRVMVMDNGQIVEtqp 235
|
250
....*....|.
gi 1937891448 1500 ------FDSPV 1504
Cdd:PRK10419 236 vgdkltFSSPA 246
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1297-1516 |
3.81e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 71.56 E-value: 3.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1297 GLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTL 1376
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1377 RMNLDPFGRYSDEDI---WRTLELSHLSAfvSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAID 1453
Cdd:PRK10253 98 VQELVARGRYPHQPLftrWRKEDEEAVTK--AMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1454 LETD----DLIQGTIRTQfeDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSPVNLIAAGGI--FYGM 1516
Cdd:PRK10253 176 ISHQidllELLSELNREK--GYTLAAVLHDLNQACRYaSHLIALREGKIVAQGAPKEIVTAELIerIYGL 243
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1285-1510 |
4.00e-13 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 72.41 E-value: 4.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSmTLclfRIL----EAAEGEIFIDGLNVAHIGLHDlRS 1360
Cdd:COG3839 4 LELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKST-LL---RMIagleDPTSGEILIGGRDVTDLPPKD-RN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1361 qLTIIPQDPILF-SGTLRMNLDpFG----RYSDEDIWR-------TLELSHLsafvssqptgLDFQCSEggdnLSVGQRQ 1428
Cdd:COG3839 77 -IAMVFQSYALYpHMTVYENIA-FPlklrKVPKAEIDRrvreaaeLLGLEDL----------LDRKPKQ----LSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1429 LVCLARALLRKSRVLVLDEATAAID----LETddliqgtiRTQfedctvltIA---HRLNTIMDY------------NRV 1489
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLDaklrVEM--------RAE--------IKrlhRRLGTTTIYvthdqveamtlaDRI 204
|
250 260
....*....|....*....|....*...
gi 1937891448 1490 LVLDKGVVAEFDS-------PVNLIAAG 1510
Cdd:COG3839 205 AVMNDGRIQQVGTpeelydrPANLFVAG 232
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
643-840 |
5.42e-13 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 70.41 E-value: 5.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGemekLE----GAVSVKG---------------SVAYVPQQ------- 696
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINL----LEepdsGTITVDGedltdskkdinklrrKVGMVFQQfnlfphl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 697 -AwIQNCTL-QENVLfGQPmnpkrYQQALETcAL-------LAD-LDVLPGgdqteigekgiNLSGGQRQRVSLARAVYS 766
Cdd:COG1126 93 tV-LENVTLaPIKVK-KMS-----KAEAEER-AMellervgLADkADAYPA-----------QLSGGQQQRVAIARALAM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 767 DANIFLLDDPLSAVDshvakhifdqvigPE---GVLA--------GKTRVLVTHGISFLPQT-DFIIVLADGQITEMGHY 834
Cdd:COG1126 154 EPKVMLFDEPTSALD-------------PElvgEVLDvmrdlakeGMTMVVVTHEMGFAREVaDRVVFMDGGRIVEEGPP 220
|
....*.
gi 1937891448 835 SELLQH 840
Cdd:COG1126 221 EEFFEN 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
643-832 |
5.69e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 72.29 E-value: 5.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-SVAYVPQQAWIQNCTLQ-----------ENVLF 710
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqDITHVPAENRHVNTVFQsyalfphmtvfENVAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 711 GQPMN--PK-----RYQQALETCAL--LADldvlpggdqteigEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD 781
Cdd:PRK09452 110 GLRMQktPAaeitpRVMEALRMVQLeeFAQ-------------RKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 782 SHVAKHIFDQVIGPEGVLaGKTRVLVTHGI-SFLPQTDFIIVLADGQITEMG 832
Cdd:PRK09452 177 YKLRKQMQNELKALQRKL-GITFVFVTHDQeEALTMSDRIVVMRDGRIEQDG 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
643-841 |
6.00e-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: 70.39 E-value: 6.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-SVAYVPQQAWIQnctLQEN--VLFgqpmnpkry 719
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqDITGLSEKELYE---LRRRigMLF--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 720 QQAletcALLADLDV-----LPGGDQTEIGEKGIN----------------------LSGGQRQRVSLARAVYSDANIFL 772
Cdd:COG1127 89 QGG----ALFDSLTVfenvaFPLREHTDLSEAEIRelvleklelvglpgaadkmpseLSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937891448 773 LDDPLSAVDShVAKHIFDQVIgpegvLA-----GKTRVLVTHGISFLPQT-DFIIVLADGQITEMGHYSELLQHD 841
Cdd:COG1127 165 YDEPTAGLDP-ITSAVIDELI-----RElrdelGLTSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTPEELLASD 233
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1287-1494 |
6.63e-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: 71.04 E-value: 6.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1287 FRNYSVRYRPglelVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIfidglnvAHIGlhdlrsQLTIIP 1366
Cdd:cd03291 42 FSNLCLVGAP----VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-------KHSG------RISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1367 QDPILFSGTLRMNLdPFGRYSDEDIWRT-LELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVL 1445
Cdd:cd03291 105 QFSWIMPGTIKENI-IFGVSYDEYRYKSvVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1937891448 1446 DEATAAIDLETDDLIqgtirtqFEDCTVLTIAHRlntimdyNRVLVLDK 1494
Cdd:cd03291 184 DSPFGYLDVFTEKEI-------FESCVCKLMANK-------TRILVTSK 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
643-840 |
1.05e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.40 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAV----SVKgsVAYVPQQawiQ-----NCTLQENVlfgQP 713
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVklgeTVK--IGYFDQH---QeeldpDKTVLDEL---RD 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 714 MNPKRYQQALEtcALLADLDvLPGGDQ-TEIGekgiNLSGGQRQRVSLARAVYSDANIFLLDDP------------LSAV 780
Cdd:COG0488 403 GAPGGTEQEVR--GYLGRFL-FSGDDAfKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPtnhldietlealEEAL 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 781 DShvakhiFdqvigpEGVLagktrVLVTHGISFLPQT-DFIIVLADGQITE-MGHYSELLQH 840
Cdd:COG0488 476 DD------F------PGTV-----LLVSHDRYFLDRVaTRILEFEDGGVREyPGGYDDYLEK 520
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
626-841 |
1.19e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 70.04 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSVaYVPQQAW------- 698
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV-LSEETVWdvrrqvg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 699 --IQN-------CTLQENVLFGQPMN--P-----KRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLAR 762
Cdd:PRK13635 85 mvFQNpdnqfvgATVQDDVAFGLENIgvPreemvERVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 763 AVYSDANIFLLDDPLSAVDShvakhifdqvIGPEGVLA---------GKTRVLVTHGISFLPQTDFIIVLADGQITEMGH 833
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDP----------RGRREVLEtvrqlkeqkGITVLSITHDLDEAAQADRVIVMNKGEILEEGT 223
|
....*...
gi 1937891448 834 YSELLQHD 841
Cdd:PRK13635 224 PEEIFKSG 231
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
643-840 |
1.22e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 69.39 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSAlLGEMEKLE------GAVSVKGSVAYVPQQAWIQNC-------------- 702
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRC-INLLEQPEagtirvGDITIDTARSLSQQKGLIRQLrqhvgfvfqnfnlf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 703 ---TLQENVLFGQPMNPKRYQQALETCA--LLADLDVlpGGDQTEIGEKginLSGGQRQRVSLARAVYSDANIFLLDDPL 777
Cdd:PRK11264 98 phrTVLENIIEGPVIVKGEPKEEATARAreLLAKVGL--AGKETSYPRR---LSGGQQQRVAIARALAMRPEVILFDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 778 SAVDSHVAKHIFDQVIGpegvLA--GKTRVLVTHGISFLPQ-TDFIIVLADGQITEMGHYSELLQH 840
Cdd:PRK11264 173 SALDPELVGEVLNTIRQ----LAqeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
642-809 |
1.22e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 69.42 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 642 TLHSLNIQIPKGALVAVVGPVGCGKSSLVSALlGEMEKLEGAVSVKGSVAY---------------------VPQQAWIQ 700
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRMNDLNPEVTITGSIVYnghniysprtdtvdlrkeigmVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 701 NCTLQENVLFGQPMN----PKRYQQALETCALLADL--DVlpggdQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLD 774
Cdd:PRK14239 99 PMSIYENVVYGLRLKgikdKQVLDEAVEKSLKGASIwdEV-----KDRLHDSALGLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 1937891448 775 DPLSAVDSHVAKHIFDQVIGpegvLAGK-TRVLVTH 809
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLG----LKDDyTMLLVTR 205
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1284-1498 |
1.28e-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: 67.96 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRN--YSVRYRPGL--ELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCL--FRILEAAEGEIFIDGLNvahIGLHD 1357
Cdd:cd03213 3 TLSFRNltVTVKSSPSKsgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRP---LDKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1358 LRSQLTIIPQDPILFsGTLrmnldpfgrysdeDIWRTLELS-HLSafvssqptgldfqcseggdNLSVGQRQLVCLARAL 1436
Cdd:cd03213 80 FRKIIGYVPQDDILH-PTL-------------TVRETLMFAaKLR-------------------GLSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 1437 LRKSRVLVLDEATAAIDLETDDLIQGTIRtQFED--CTVLTIAHRLNTIM--DYNRVLVLDKGVVA 1498
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLR-RLADtgRTIICSIHQPSSEIfeLFDKLLLLSQGRVI 191
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1301-1498 |
1.54e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.01 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1301 VLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGlHDLRSQLTI--IPQDPILFSG-TLR 1377
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT-PAKAHQLGIylVPQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1378 MNLdPFGRYSDEDIWRTLElsHLSAFVSSQptgLDFQCSEGgdNLSVGQRQLVCLARALLRKSRVLVLDEATAAID-LET 1456
Cdd:PRK15439 105 ENI-LFGLPKRQASMQKMK--QLLAALGCQ---LDLDSSAG--SLEVADRQIVEILRGLMRDSRILILDEPTASLTpAET 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1937891448 1457 DDLIQGTIRTQFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVA 1498
Cdd:PRK15439 177 ERLFSRIRELLAQGVGIVFISHKLPEIRQLaDRISVMRDGTIA 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1305-1498 |
1.56e-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: 68.29 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1305 LTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDlrSQLTIIPQDPILFSG-TLRMNLD-- 1381
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFAHlTVEQNVGlg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1382 --PFGRYSDEDIWRTlelshlsaFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAID----LE 1455
Cdd:cd03298 95 lsPGLKLTAEDRQAI--------EVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1937891448 1456 TDDLIQGTIRTQfeDCTVLTIAHRLNTIMD-YNRVLVLDKGVVA 1498
Cdd:cd03298 167 MLDLVLDLHAET--KMTVLMVTHQPEDAKRlAQRVVFLDNGRIA 208
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1304-1493 |
1.58e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.29 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1304 NLTLHVQGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAEGEIFIDGLNVAHIGlHDLRSQLtiipqdpiLFSG----- 1374
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTS----LLRILaglaRPDAGEVLWQGEPIRRQR-DEYHQDL--------LYLGhqpgi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1375 --------TLRMNLDPFGRYSDEDIWRTLELSHLSAFvssqptgLDFQCSeggdNLSVGQRQLVCLARALLRKSRVLVLD 1446
Cdd:PRK13538 86 kteltaleNLRFYQRLHGPGDDEALWEALAQVGLAGF-------EDVPVR----QLSAGQQRRVALARLWLTRAPLWILD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1937891448 1447 EATAAIDLETDDLIQGTIRTQFED--CTVLTIAHRLNTIMDYNRVLVLD 1493
Cdd:PRK13538 155 EPFTAIDKQGVARLEALLAQHAEQggMVILTTHQDLPVASDKVRKLRLG 203
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
647-838 |
1.78e-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: 70.51 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 647 NIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSV-----------------AYVPQQAwiqncTL----- 704
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargiflpphrrriGYVFQEA-----RLfphls 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 705 -QENVLFGQPMNPK-----RYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLS 778
Cdd:COG4148 94 vRGNLLYGRKRAPRaerriSFDEVVELLGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937891448 779 AVDsHVAKH--------IFDQVIGPegVLagktrvLVTHG---ISFLpqTDFIIVLADGQITEMGHYSELL 838
Cdd:COG4148 163 ALD-LARKAeilpylerLRDELDIP--IL------YVSHSldeVARL--ADHVVLLEQGRVVASGPLAEVL 222
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
597-781 |
2.05e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 71.76 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 597 SLKRIQDF---LNQDELDPQCVERKTISPGRAITIHNGTFswskDLP---PTLHSLNIQIPKGALVAVVGPVGCGKSSLV 670
Cdd:COG4178 331 TVDRLAGFeeaLEAADALPEAASRIETSEDGALALEDLTL----RTPdgrPLLEDLSLSLKPGERLLITGPSGSGKSTLL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 671 SALLGemekL----EGAVSV--KGSVAYVPQQAWIQNCTLQENVLFGQP---MNPKRYQQALETCAL--LAD-LDVLPGG 738
Cdd:COG4178 407 RAIAG----LwpygSGRIARpaGARVLFLPQRPYLPLGTLREALLYPATaeaFSDAELREALEAVGLghLAErLDEEADW 482
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1937891448 739 DQTeigekginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD 781
Cdd:COG4178 483 DQV--------LSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1306-1510 |
2.39e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.46 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1306 TLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNvaHIGLHDLRSQLTIIPQDPILFSG-TLRMN----L 1380
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD--HTTTPPSRRPVSMLFQENNLFSHlTVAQNiglgL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1381 DPFGRYSDE------DIWRTLELSHLSAFVSSQptgldfqcseggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAID- 1453
Cdd:PRK10771 97 NPGLKLNAAqreklhAIARQMGIEDLLARLPGQ--------------LSGGQRQRVALARCLVREQPILLLDEPFSALDp 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937891448 1454 ---LETDDLIQGTIRTQfeDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAeFDSPVNLIAAG 1510
Cdd:PRK10771 163 alrQEMLTLVSQVCQER--QLTLLMVSHSLEDAARIaPRSLVVADGRIA-WDGPTDELLSG 220
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1284-1466 |
2.66e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 69.45 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNysVRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHdLRSQLT 1363
Cdd:PRK13537 7 PIDFRN--VEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH-ARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1364 IIPQ----DPILfsgTLRMNLDPFGRYSDediwrtLELSHLSAFVssqPTGLDFQCSEGGDN-----LSVGQRQLVCLAR 1434
Cdd:PRK13537 84 VVPQfdnlDPDF---TVRENLLVFGRYFG------LSAAAARALV---PPLLEFAKLENKADakvgeLSGGMKRRLTLAR 151
|
170 180 190
....*....|....*....|....*....|..
gi 1937891448 1435 ALLRKSRVLVLDEATAAIDLETDDLIQGTIRT 1466
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLDPQARHLMWERLRS 183
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1284-1453 |
2.73e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 68.95 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYRPGLElVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDG--LNVAHIGLHDLRSQ 1361
Cdd:PRK13639 1 ILETRDLKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1362 LTIIPQDP--ILFSGTLR-------MNLdpfgRYSDEDIWR----TLELSHLSAFVSSQPtgldfqcseggDNLSVGQRQ 1428
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEedvafgpLNL----GLSKEEVEKrvkeALKAVGMEGFENKPP-----------HHLSGGQKK 144
|
170 180
....*....|....*....|....*
gi 1937891448 1429 LVCLARALLRKSRVLVLDEATAAID 1453
Cdd:PRK13639 145 RVAIAGILAMKPEIIVLDEPTSGLD 169
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
645-789 |
2.81e-12 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 71.32 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 645 SLNIQIPKGALVAVVGPVGCGKSSLVSaLLGEMEKLEGAVSVK---GSVAYVPQQAWIQNCTLQENVLFgqPMNPKRYQ- 720
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGGRLTKpakGKLFYVPQRPYMTLGTLRDQIIY--PDSSEDMKr 546
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 721 QALETCALLADLDVLPGGD--QTEIGEKGIN-----LSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIF 789
Cdd:TIGR00954 547 RGLSDKDLEQILDNVQLTHilEREGGWSAVQdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMY 622
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1255-1499 |
3.04e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.86 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1255 RVKEYSKTETEAPWVLESNRAPEGWPRSGVVEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFR 1334
Cdd:PRK13536 12 RRLELSPIERKHQGISEAKASIPGSMSTVAIDLAGVSKSY--GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1335 ILEAAEGEIFIDGLNV---AHIGlhdlRSQLTIIPQ-DPILFSGTLRMNLDPFGRYSDEDIwRTLElshlsafvSSQPTG 1410
Cdd:PRK13536 90 MTSPDAGKITVLGVPVparARLA----RARIGVVPQfDNLDLEFTVRENLLVFGRYFGMST-REIE--------AVIPSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1411 LDFQCSEGGDN-----LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQF-EDCTVLTIAHrlntIM 1484
Cdd:PRK13536 157 LEFARLESKADarvsdLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTH----FM 232
|
250 260
....*....|....*....|.
gi 1937891448 1485 DY-----NRVLVLDKGV-VAE 1499
Cdd:PRK13536 233 EEaerlcDRLCVLEAGRkIAE 253
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1289-1500 |
3.46e-12 |
|
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: 67.22 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1289 NYSVRYRPGLelVLKNLTLHVQGGeKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAhIGLHDLRSQLTIIPQD 1368
Cdd:cd03264 5 NLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL-KQPQKLRRRIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1369 PILFSG-TLRMNLDPFG-------RYSDEDIWRTLELSHLSAFVSSQPTGLdfqcseggdnlSVGQRQLVCLARALLRKS 1440
Cdd:cd03264 81 FGVYPNfTVREFLDYIAwlkgipsKEVKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937891448 1441 RVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMD-YNRVLVLDKGVVAEF 1500
Cdd:cd03264 150 SILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFE 210
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
643-841 |
3.64e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 68.26 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-------------SVAYVPQQAWIQ-NCTLQENV 708
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHSSLSfPFTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 709 LFGQ---PMNPKRYQQALETCALLADLDVLPGGDQTEigekginLSGGQRQRVSLARA------VYSDANIFLLDDPLSA 779
Cdd:PRK13548 98 AMGRaphGLSRAEDDALVAAALAQVDLAHLAGRDYPQ-------LSGGEQQRVQLARVlaqlwePDGPPRWLLLDEPTSA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 780 VD-SH------VAKHIFDQviGPEGVLAgktrvlVTHGisfLPQT----DFIIVLADGQITEMGHYSELLQHD 841
Cdd:PRK13548 171 LDlAHqhhvlrLARQLAHE--RGLAVIV------VLHD---LNLAaryaDRIVLLHQGRLVADGTPAEVLTPE 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1284-1508 |
3.70e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 68.58 E-value: 3.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYRPGLEL-VLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQL 1362
Cdd:PRK13642 4 ILEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1363 TIIPQDPI-LFSGTLRMNLDPFGRYSD----EDIWRTLELSHLSAFVssqptgLDFQCSEGGdNLSVGQRQLVCLARALL 1437
Cdd:PRK13642 84 GMVFQNPDnQFVGATVEDDVAFGMENQgiprEEMIKRVDEALLAVNM------LDFKTREPA-RLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937891448 1438 RKSRVLVLDEATAAIDLETDDLIQGTIRtQFED---CTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIA 1508
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIH-EIKEkyqLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
643-790 |
4.05e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 68.12 E-value: 4.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLG----------EMEKLEGAVSVKGSVA-----------YVPQQAWIQN 701
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdksagsHIELLGRTVQREGRLArdirksrantgYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 702 -CTLQENVLFG----QPM--------NPKRYQQALEtcALladldvlpggdqTEIG------EKGINLSGGQRQRVSLAR 762
Cdd:PRK09984 100 rLSVLENVLIGalgsTPFwrtcfswfTREQKQRALQ--AL------------TRVGmvhfahQRVSTLSGGQQQRVAIAR 165
|
170 180
....*....|....*....|....*...
gi 1937891448 763 AVYSDANIFLLDDPLSAVDSHVAKHIFD 790
Cdd:PRK09984 166 ALMQQAKVILADEPIASLDPESARIVMD 193
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1284-1454 |
4.42e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 68.28 E-value: 4.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYS--VRYRPGL------ELVlKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVaHIGL 1355
Cdd:PRK15112 4 LLEVRNLSktFRYRTGWfrrqtvEAV-KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1356 HDLRSQ-LTIIPQDPI-----------LFSGTLRMNLDPFGRYSDEDIWRTL-ELSHLSAFVSSQPtgldfqcseggDNL 1422
Cdd:PRK15112 82 YSYRSQrIRMIFQDPStslnprqrisqILDFPLRLNTDLEPEQREKQIIETLrQVGLLPDHASYYP-----------HML 150
|
170 180 190
....*....|....*....|....*....|..
gi 1937891448 1423 SVGQRQLVCLARALLRKSRVLVLDEATAAIDL 1454
Cdd:PRK15112 151 APGQKQRLGLARALILRPKVIIADEALASLDM 182
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
643-854 |
4.76e-12 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 67.49 E-value: 4.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSVAYVP---QQAWIQNCTLQenvlfgqPMNPKRY 719
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgpdRMVVFQNYSLL-------PWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 720 QQALETCALLADLdvlPGGDQTEIGEKGINL--------------SGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVA 785
Cdd:TIGR01184 74 NIALAVDRVLPDL---SKSERRAIVEEHIALvglteaadkrpgqlSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 786 KHIFDQV--IGPEgvlAGKTRVLVTHGIS---FLpqTDFIIVLADGQITEMGHYSEL----------LQHDGSFANfLRN 850
Cdd:TIGR01184 151 GNLQEELmqIWEE---HRVTVLMVTHDVDealLL--SDRVVMLTNGPAANIGQILEVpfprprdrleVVEDPSYYD-LRN 224
|
....
gi 1937891448 851 YAPD 854
Cdd:TIGR01184 225 EALY 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1285-1508 |
5.19e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 68.32 E-value: 5.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYRPGLELV---LKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDG----LNVAHIGLHD 1357
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEkkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1358 LRSQLTIIPQDP--ILFSGTLRMNLD--P--FGRYSDEdiwrtlelSHLSAFVSSQPTGLDFQCSEGGD-NLSVGQRQLV 1430
Cdd:PRK13641 83 LRKKVSLVFQFPeaQLFENTVLKDVEfgPknFGFSEDE--------AKEKALKWLKKVGLSEDLISKSPfELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1431 CLARALLRKSRVLVLDEATAAIDLET-DDLIQGTIRTQFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSPVNLIA 1508
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEYaDDVLVLEHGKLIKHASPKEIFS 234
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
643-838 |
5.43e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 67.69 E-value: 5.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSVAY----------VPQQAWIQNCTLQENVLFgQ 712
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkVADKNQLRLLRTRLTMVF-Q 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 713 PMNPKRYQQALETcALLADLDVLP-----------------GGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDD 775
Cdd:PRK10619 100 HFNLWSHMTVLEN-VMEAPIQVLGlskqeareravkylakvGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 776 PLSAVDSHVAKHIFD--QVIGPEgvlaGKTRVLVTHGISFLPQ-TDFIIVLADGQITEMGHYSELL 838
Cdd:PRK10619 179 PTSALDPELVGEVLRimQQLAEE----GKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
626-827 |
6.00e-12 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 64.78 E-value: 6.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWSKDlpPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSV--KGSVAYVPQqawiqnct 703
Cdd:cd03221 1 IELENLSKTYGGK--LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWgsTVKIGYFEQ-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 704 lqenvlfgqpmnpkryqqaletcalladldvlpggdqteigekginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSH 783
Cdd:cd03221 71 ----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1937891448 784 VAKHIFDQVIGPEGVLagktrVLVTHGISFLPQ-TDFIIVLADGQ 827
Cdd:cd03221 105 SIEALEEALKEYPGTV-----ILVSHDRYFLDQvATKIIELEDGK 144
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1285-1497 |
6.25e-12 |
|
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: 66.54 E-value: 6.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYRPglELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHD------- 1357
Cdd:cd03269 1 LEVENVTKRFGR--VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRigylpee 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1358 --LRSQLTIIPQdpILFSGTLR-MNLdpfgRYSDEDIWRTLELSHLSAFVSSQPtgldfqcseggDNLSVGQRQLVCLAR 1434
Cdd:cd03269 79 rgLYPKMKVIDQ--LVYLAQLKgLKK----EEARRRIDEWLERLELSEYANKRV-----------EELSKGNQQKVQFIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937891448 1435 ALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFED-CTVLTIAHRLNTIMDY-NRVLVLDKGVV 1497
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELcDRVLLLNKGRA 206
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
693-849 |
7.25e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.83 E-value: 7.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 693 VPQQAWIQNCTLQENVLFG-QPMNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIF 771
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGkEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKIL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 772 LLDDPLSAVDSHVAKHIFDQVIGPEGVlAGKTRVLVTHGISFLPQTDFIIVLADGQ-----ITEMGHYSELLQ-HDGSFA 845
Cdd:PTZ00265 1381 LLDEATSSLDSNSEKLIEKTIVDIKDK-ADKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLSvQDGVYK 1459
|
....
gi 1937891448 846 NFLR 849
Cdd:PTZ00265 1460 KYVK 1463
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
643-788 |
7.56e-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: 66.53 E-value: 7.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEK---LEGAVSVKG----------SVAYVPQQ-AWIQNCTLQENV 708
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGqprkpdqfqkCVAYVRQDdILLPGLTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 709 LFGQPM-----NPKRYQQALETCALLADLDVLPGGdqteiGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSH 783
Cdd:cd03234 103 TYTAILrlprkSSDAIRKKRVEDVLLRDLALTRIG-----GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
....*
gi 1937891448 784 VAKHI 788
Cdd:cd03234 178 TALNL 182
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1301-1499 |
8.91e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 67.08 E-value: 8.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1301 VLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLfRILEAAE------GEIFIDG---LNVA---------HIG-------L 1355
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI-NLLEQPEagtirvGDITIDTarsLSQQkglirqlrqHVGfvfqnfnL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1356 HDLRSQLTIIPQDPILFSGTLRMNLDPFGRysdediwRTLELSHLSAFVSSQPTgldfqcseggdNLSVGQRQLVCLARA 1435
Cdd:PRK11264 97 FPHRTVLENIIEGPVIVKGEPKEEATARAR-------ELLAKVGLAGKETSYPR-----------RLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 1436 LLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDC-TVLTIAHRLNTIMDY-NRVLVLDKGVVAE 1499
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDVaDRAIFMDQGRIVE 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
634-838 |
9.53e-12 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 68.60 E-value: 9.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 634 SWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-----------------SVAYVPQQ 696
Cdd:TIGR02142 4 RFSKRLGDFSLDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrkgiflppekrRIGYVFQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 697 AWI-QNCTLQENVLFGQ-----PMNPKRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANI 770
Cdd:TIGR02142 84 ARLfPHLSVRGNLRYGMkrarpSERRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 771 FLLDDPLSAVDSHVAkhifDQVIGPEGVLAGKTR---VLVTHGIS-FLPQTDFIIVLADGQITEMGHYSELL 838
Cdd:TIGR02142 153 LLMDEPLAALDDPRK----YEILPYLERLHAEFGipiLYVSHSLQeVLRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
647-839 |
9.61e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.53 E-value: 9.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 647 NIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGsvayvpqqawiQNCT------------LQENVLF---- 710
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG-----------QDHTttppsrrpvsmlFQENNLFshlt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 711 -----GQPMNP---------KRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDP 776
Cdd:PRK10771 88 vaqniGLGLNPglklnaaqrEKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 777 LSAVDSHVAKHIF---DQVIGPEGVlagkTRVLVTHGIS----FLPQTdfiIVLADGQITEMGHYSELLQ 839
Cdd:PRK10771 157 FSALDPALRQEMLtlvSQVCQERQL----TLLMVSHSLEdaarIAPRS---LVVADGRIAWDGPTDELLS 219
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1296-1495 |
9.64e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.26 E-value: 9.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1296 PGLElVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDlrSQ----------LTII 1365
Cdd:PRK10762 15 PGVK-ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKS--SQeagigiihqeLNLI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1366 PQDPI---LFSGtlRMNLDPFGR------YSDED-IWRTLELSHlsafVSSQPTGldfqcseggdNLSVGQRQLVCLARA 1435
Cdd:PRK10762 92 PQLTIaenIFLG--REFVNRFGRidwkkmYAEADkLLARLNLRF----SSDKLVG----------ELSIGEQQMVEIAKV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 1436 LLRKSRVLVLDEATAAI-DLETDDLIQgTIRT-QFEDCTVLTIAHRLNTIMDY-NRVLVLDKG 1495
Cdd:PRK10762 156 LSFESKVIIMDEPTDALtDTETESLFR-VIRElKSQGRGIVYISHRLKEIFEIcDDVTVFRDG 217
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
641-823 |
9.95e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.28 E-value: 9.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS-VAYVPQQAWIQN---CTlQENVLFGQPMN- 715
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdISTLKPEIYRQQvsyCA-QTPTLFGDTVYd 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 716 ----PkrYQ---QALETCALLADLDV--LPggdqTEIGEKGIN-LSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHvA 785
Cdd:PRK10247 100 nlifP--WQirnQQPDPAIFLDDLERfaLP----DTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDES-N 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 1937891448 786 KHIFDQVIgPEGVLAGKTRVL-VTHGISFLPQTDFIIVL 823
Cdd:PRK10247 173 KHNVNEII-HRYVREQNIAVLwVTHDKDEINHADKVITL 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1301-1499 |
1.02e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.35 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1301 VLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILeAAEGEIFIDGLNVAHIG---LHDLRSQLTIIPQDPilfSGTL- 1376
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDP---NSSLn 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1377 -RMNLdpfgrysDEDIWRTLELSH--LSA-------FVSSQPTGLDFQC-----SEggdnLSVGQRQLVCLARALLRKSR 1441
Cdd:PRK15134 377 pRLNV-------LQIIEEGLRVHQptLSAaqreqqvIAVMEEVGLDPETrhrypAE----FSGGQRQRIAIARALILKPS 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937891448 1442 VLVLDEATAAIDLETDDLIQGTIRT--QFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAE 1499
Cdd:PRK15134 446 LIILDEPTSSLDKTVQAQILALLKSlqQKHQLAYLFISHDLHVVRALcHQVIVLRQGEVVE 506
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
644-783 |
1.08e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 66.93 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 644 HSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGsvAYVPQQA----------WIQNCTLQENVLFGQP 713
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDG--EHIQHYAskevarriglLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937891448 714 MNPKRY-QQALETCALLADLDVLPGGDQ----TEIGEKGIN-LSGGQRQRVSLARAVYSDANIFLLDDPLSAVD-SH 783
Cdd:PRK10253 102 VARGRYpHQPLFTRWRKEDEEAVTKAMQatgiTHLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDiSH 178
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1295-1503 |
1.17e-11 |
|
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: 66.90 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1295 RPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIG---LHDLRSQ--------LT 1363
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKkismvfqsFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1364 IIPQDPILFSGTLRMNLDpfGRYSDEDIWR---TLELSHLSAFVSSQPtgldfqcseggDNLSVGQRQLVCLARALLRKS 1440
Cdd:cd03294 113 LLPHRTVLENVAFGLEVQ--GVPRAEREERaaeALELVGLEGWEHKYP-----------DELSGGMQQRVGLARALAVDP 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1441 RVLVLDEATAAIdletDDLIQGTIRTQFEDC------TVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSP 1503
Cdd:cd03294 180 DILLMDEAFSAL----DPLIRREMQDELLRLqaelqkTIVFITHDLDEALRLgDRIAIMKDGRLVQVGTP 245
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
626-840 |
1.19e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 67.08 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAV-------------SVKGSVAY 692
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddnfeKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 693 VPQQAWIQ--NCTLQENVLFGQPMNPKRYQQALETCA-LLADLDVLPGGDqteigEKGINLSGGQRQRVSLARAVYSDAN 769
Cdd:PRK13648 88 VFQNPDNQfvGSIVKYDVAFGLENHAVPYDEMHRRVSeALKQVDMLERAD-----YEPNALSGGQKQRVAIAGVLALNPS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 770 IFLLDDPLSAVDSHVAKHIFDQVigpEGVLAGK--TRVLVTHGISFLPQTDFIIVLADGQITEMGHYSELLQH 840
Cdd:PRK13648 163 VIILDEATSMLDPDARQNLLDLV---RKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1292-1492 |
1.24e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.89 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1292 VRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTIIPQDPIL 1371
Cdd:PRK10247 13 VGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1372 FSGTLRMNLD-PF---GRYSDEDIWRtlelSHLSAFvssqptGLDFQCSEGGDN-LSVGQRQLVCLARALLRKSRVLVLD 1446
Cdd:PRK10247 93 FGDTVYDNLIfPWqirNQQPDPAIFL----DDLERF------ALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1447 EATAAID----LETDDLIQGTIRTQfeDCTVLTIAHRLNTIMDYNRVLVL 1492
Cdd:PRK10247 163 EITSALDesnkHNVNEIIHRYVREQ--NIAVLWVTHDKDEINHADKVITL 210
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
1014-1179 |
1.30e-11 |
|
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: 67.05 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1014 LGILQGLLVMLSAFTMVVGAIQAARLLHTALLHNQIRAPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLFNSFYTS 1093
Cdd:cd18541 49 LALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1094 ISTIVV-IVASTPLFCVVVLPLAVFYGFVQRFyvatSRQL-KRLESVSRSpiFSHFS----ETVTGTSVIRAYGR----V 1163
Cdd:cd18541 129 VLVLVMmFTISPKLTLIALLPLPLLALLVYRL----GKKIhKRFRKVQEA--FSDLSdrvqESFSGIRVIKAFVQeeaeI 202
|
170
....*....|....*.
gi 1937891448 1164 QDFKVLSDAKVDSNQK 1179
Cdd:cd18541 203 ERFDKLNEEYVEKNLR 218
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
643-838 |
1.34e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 66.47 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSAL-----LGEMEKLEGAVSVKGS----------------VAYVPQQawIQN 701
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQdifkmdvielrrrvqmVFQIPNP--IPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 702 CTLQENVLFGQPMN---------PKRYQQALETCALLADLdvlpggdQTEIGEKGINLSGGQRQRVSLARAVYSDANIFL 772
Cdd:PRK14247 97 LSIFENVALGLKLNrlvkskkelQERVRWALEKAQLWDEV-------KDRLDAPAGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 773 LDDPLSAVDSHVAKHIFDQVIGPEGVLagkTRVLVTHgisFLPQ----TDFIIVLADGQITEMGHYSELL 838
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLELKKDM---TIVLVTH---FPQQaariSDYVAFLYKGQIVEWGPTREVF 233
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1293-1510 |
1.47e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.57 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1293 RYRPglELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDG--LNVAHIGLHDLRSQLTIIPQDP- 1369
Cdd:PRK13638 10 RYQD--EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDPe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1370 -----------ILFSgtLRmNL----DPFGRYSDEdiwrTLELSHLSAFvSSQPtgldFQCseggdnLSVGQRQLVCLAR 1434
Cdd:PRK13638 88 qqifytdidsdIAFS--LR-NLgvpeAEITRRVDE----ALTLVDAQHF-RHQP----IQC------LSHGQKKRVAIAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937891448 1435 ALLRKSRVLVLDEATAAIDLE-TDDLIQGTIRTQFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSPVNLIAAG 1510
Cdd:PRK13638 150 ALVLQARYLLLDEPTAGLDPAgRTQMIAIIRRIVAQGNHVIISSHDIDLIYEIsDAVYVLRQGQILTHGAPGEVFACT 227
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1291-1497 |
1.48e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.83 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1291 SVRYRPGlELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIglhdLRSQL-TIIPQD- 1368
Cdd:PRK15056 13 TVTWRNG-HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA----LQKNLvAYVPQSe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1369 ------PILFSGTLRMnldpfGRYSDEDiWRTLELSHLSAFVS---SQPTGLDFQCSEGGDnLSVGQRQLVCLARALLRK 1439
Cdd:PRK15056 88 evdwsfPVLVEDVVMM-----GRYGHMG-WLRRAKKRDRQIVTaalARVDMVEFRHRQIGE-LSGGQKKRVFLARAIAQQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1937891448 1440 SRVLVLDEATAAIDLETDDLIQGTIRT-QFEDCTVLTIAHRLNTIMDYNRVLVLDKGVV 1497
Cdd:PRK15056 161 GQVILLDEPFTGVDVKTEARIISLLRElRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTV 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
641-809 |
1.59e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 69.66 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG------------SVAYVPQQAWI-QNCTLQEN 707
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnldavrqSLGMCPQHNILfHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 708 VLFGQPMNPKRYQQA-LETCALLADLdvlpgGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAK 786
Cdd:TIGR01257 1024 ILFYAQLKGRSWEEAqLEMEAMLEDT-----GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180
....*....|....*....|...
gi 1937891448 787 HIFDQVIGPEgvlAGKTRVLVTH 809
Cdd:TIGR01257 1099 SIWDLLLKYR---SGRTIIMSTH 1118
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
643-832 |
1.61e-11 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 65.32 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLG--------------EMEKLEGAVSVKGSVAYVPqqAWIQNCTLQENV 708
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGlikpdsgeitfdgkSYQKNIEALRRIGALIEAP--GFYPNLTARENL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 709 LFGQPMNPKRYQQALETcalladLDVLpgGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDshvakhi 788
Cdd:cd03268 94 RLLARLLGIRKKRIDEV------LDVV--GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD------- 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 789 fdqvigPEGVLA-----------GKTRVLVTHGISFLPQT-DFIIVLADGQITEMG 832
Cdd:cd03268 159 ------PDGIKElrelilslrdqGITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1284-1495 |
1.74e-11 |
|
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: 64.38 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYRpglelvLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQ-L 1362
Cdd:cd03215 4 VLEVRGLSVKGA------VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1363 TIIPQDPilfsgtLRMNLDPfgrysDEDIWRTLELSHLsafvssqptgldfqcseggdnLSVGQRQLVCLARALLRKSRV 1442
Cdd:cd03215 78 AYVPEDR------KREGLVL-----DLSVAENIALSSL---------------------LSGGNQQKVVLARWLARDPRV 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1937891448 1443 LVLDEATAAIDLETDDLIQGTIRTQFED-CTVLTIAHRLNTIMDY-NRVLVLDKG 1495
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLGLcDRILVMYEG 180
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1302-1484 |
2.19e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.42 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1302 LKNLTLHVQGGEKVGIVGRTGAGKSSmtlcLFRILEAA------EGEIFIDG--LNVAHI------GLHDLRSQLTIIPQ 1367
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKST----LMKVLSGVyphgtyEGEIIFEGeeLQASNIrdteraGIAIIHQELALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1368 DPILFSGTLRMNLDPFGRYSDEDIWRTLE--LSHLSAFVS-SQPTGldfqcseggdNLSVGQRQLVCLARALLRKSRVLV 1444
Cdd:PRK13549 97 LSVLENIFLGNEITPGGIMDYDAMYLRAQklLAQLKLDINpATPVG----------NLGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1937891448 1445 LDEATAAI-DLETDDLIQGTIRTQFEDCTVLTIAHRLNTIM 1484
Cdd:PRK13549 167 LDEPTASLtESETAVLLDIIRDLKAHGIACIYISHKLNEVK 207
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
625-849 |
2.30e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 66.30 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 625 AITIHNGTFSWsKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSVAYVPQQAWIQN--- 701
Cdd:PRK13647 4 IIEVEDLHFRY-KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSkvg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 702 ------------CTLQENVLFGqPMN--------PKRYQQALETCALLADLDVLPggdqteigekgINLSGGQRQRVSLA 761
Cdd:PRK13647 83 lvfqdpddqvfsSTVWDDVAFG-PVNmgldkdevERRVEEALKAVRMWDFRDKPP-----------YHLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 762 RAVYSDANIFLLDDPLSAVDSHvakhifdqviGPEGVLA--------GKTRVLVTHGISFLPQ-TDFIIVLADGQITEMG 832
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPR----------GQETLMEildrlhnqGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEG 220
|
250
....*....|....*..
gi 1937891448 833 HYSELLQHDGSFANFLR 849
Cdd:PRK13647 221 DKSLLTDEDIVEQAGLR 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
643-776 |
2.69e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.17 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG--SVAYVPQQAWI-QNCTLQENVLFGqpmNPKRY 719
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLdDDLTVLDTVLDG---DAELR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 720 QQALETCALLADLDVlPGGDQTEIGEK-----------------------GI----------NLSGGQRQRVSLARAVYS 766
Cdd:COG0488 91 ALEAELEELEAKLAE-PDEDLERLAELqeefealggweaearaeeilsglGFpeedldrpvsELSGGWRRRVALARALLS 169
|
170
....*....|
gi 1937891448 767 DANIFLLDDP 776
Cdd:COG0488 170 EPDLLLLDEP 179
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
625-838 |
2.75e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 65.78 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 625 AITIHNGTFSWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG------SVAYVPQQAW 698
Cdd:PRK13632 7 MIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskeNLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 699 I--QN-------CTLQENVLFG---QPMNPKRYQQALETCALLADLDVLpggdqteIGEKGINLSGGQRQRVSLARAVYS 766
Cdd:PRK13632 87 IifQNpdnqfigATVEDDIAFGlenKKVPPKKMKDIIDDLAKKVGMEDY-------LDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 767 DANIFLLDDPLSAVDSHvAKHIFDQVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQITEMGHYSELL 838
Cdd:PRK13632 160 NPEIIIFDESTSMLDPK-GKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
653-783 |
3.42e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.12 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 653 GALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG----------SVAYV-PQQAWIQNCTLQENVLF-----GQpmNP 716
Cdd:PRK13539 28 GEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddpdvaeACHYLgHRNAMKPALTVAENLEFwaaflGG--EE 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937891448 717 KRYQQALETCALlADLDVLPGGdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSH 783
Cdd:PRK13539 106 LDIAAALEAVGL-APLAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1284-1501 |
4.07e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 65.53 E-value: 4.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYRPGLElVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLT 1363
Cdd:PRK13647 4 IIEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1364 IIPQDP--ILFSGT---------LRMNLDPfgrysDEDIWRT---LELSHLSAFVSSQPTgldfqcseggdNLSVGQRQL 1429
Cdd:PRK13647 83 LVFQDPddQVFSSTvwddvafgpVNMGLDK-----DEVERRVeeaLKAVRMWDFRDKPPY-----------HLSYGQKKR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937891448 1430 VCLARALLRKSRVLVLDEATAAIDLETDDLIQGTI-RTQFEDCTVLTIAHRLNTIMDY-NRVLVLDKG-VVAEFD 1501
Cdd:PRK13647 147 VAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILdRLHNQGKTVIVATHDVDLAAEWaDQVIVLKEGrVLAEGD 221
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
643-837 |
4.83e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 65.10 E-value: 4.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG--------SVAYVPQQAWI--QNC-------TLQ 705
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikydkkSLLEVRKTVGIvfQNPddqlfapTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 706 ENVLFGqPMN--------PKRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPL 777
Cdd:PRK13639 98 EDVAFG-PLNlglskeevEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937891448 778 SAVD----SHVAKHIFDqvIGPEGVlagkTRVLVTHGISFLP-QTDFIIVLADGQITEMGHYSEL 837
Cdd:PRK13639 166 SGLDpmgaSQIMKLLYD--LNKEGI----TIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEV 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1282-1502 |
4.97e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 67.24 E-value: 4.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1282 SGVVEFRNYSVRYrPGLeLVLKNLTLHVQGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAEGEIFIDGLNVAHIGLHD 1357
Cdd:PRK11288 2 SPYLSFDGIGKTF-PGV-KALDDISFDCRAGQVHALMGENGAGKST----LLKILsgnyQPDAGSILIDGQEMRFASTTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1358 -LRSQLTIIPQD----PILfsgTLRMNL------DPFG--RYSDEDIWRTLELSHLsafvssqptGLDFQCSEGGDNLSV 1424
Cdd:PRK11288 76 aLAAGVAIIYQElhlvPEM---TVAENLylgqlpHKGGivNRRLLNYEAREQLEHL---------GVDIDPDTPLKYLSI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1425 GQRQLVCLARALLRKSRVLVLDEATAAIDL-ETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDY-NRVLVLDKG-VVAEFD 1501
Cdd:PRK11288 144 GQRQMVEIAKALARNARVIAFDEPTSSLSArEIEQLFRVIRELRAEGRVILYVSHRMEEIFALcDAITVFKDGrYVATFD 223
|
.
gi 1937891448 1502 S 1502
Cdd:PRK11288 224 D 224
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
1016-1162 |
5.44e-11 |
|
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: 65.14 E-value: 5.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1016 ILQGLLVMLSAFTMVVGAIQAARLLHTALLHNQIRAPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLFNSFYTSIS 1095
Cdd:cd18552 50 LLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIG 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937891448 1096 TIVVIVASTP---LFCVVVLPLAVFygFVQRFyvatSRQLKRL-----ESVSRspIFSHFSETVTGTSVIRAYGR 1162
Cdd:cd18552 130 LLGVLFYLDWkltLIALVVLPLAAL--PIRRI----GKRLRKIsrrsqESMGD--LTSVLQETLSGIRVVKAFGA 196
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1284-1453 |
5.54e-11 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 64.67 E-value: 5.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSsmTL--CLFRILE-----AAEGEIFIDGLNV--AHIG 1354
Cdd:COG1117 11 KIEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKS--TLlrCLNRMNDlipgaRVEGEILLDGEDIydPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1355 LHDLRSQLTIIPQDPILFSGT--------LRMNldpfGRYS----DEDIWRTLELSHL----------SAFvssqptgld 1412
Cdd:COG1117 87 VVELRRRVGMVFQKPNPFPKSiydnvaygLRLH----GIKSkselDEIVEESLRKAALwdevkdrlkkSAL--------- 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1937891448 1413 fqcseggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAID 1453
Cdd:COG1117 154 --------GLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
643-840 |
5.75e-11 |
|
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: 64.10 E-value: 5.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG--------------SVAYVPQQAWI-QNCTLQEN 707
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklpmhkrarlGIGYLPQEASIfRKLTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 708 ---VLFGQPMNPKRYQQALEtcALLADLDVLPGGDQteigeKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD--- 781
Cdd:cd03218 96 ilaVLEIRGLSKKEREEKLE--ELLEEFHITHLRKS-----KASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDpia 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937891448 782 ----SHVAKHIFDQVIGpegvlagktrVLVT-HGIS-FLPQTDFIIVLADGQITEMGHYSELLQH 840
Cdd:cd03218 169 vqdiQKIIKILKDRGIG----------VLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
609-809 |
7.44e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 65.62 E-value: 7.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 609 ELDPQCVERKTISPGRAITIHNGTFS-WSKDL---------PPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEME 678
Cdd:PRK13536 13 RLELSPIERKHQGISEAKASIPGSMStVAIDLagvsksygdKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 679 KLEGAVSVKGsvAYVPQQAWI---------------QNCTLQENVL-FGQ--PMNPKRYQQALETcalLADLDVLPGGDQ 740
Cdd:PRK13536 93 PDAGKITVLG--VPVPARARLararigvvpqfdnldLEFTVRENLLvFGRyfGMSTREIEAVIPS---LLEFARLESKAD 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937891448 741 TEIGEkginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHvAKH-IFDQVigpEGVLA-GKTRVLVTH 809
Cdd:PRK13536 168 ARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-ARHlIWERL---RSLLArGKTILLTTH 230
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1233-1479 |
7.83e-11 |
|
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: 66.70 E-value: 7.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1233 TLSLNWMIRTLSDLESNIIAVERVKEYSKTETEApwvlesnRAPEGWPRSGVVEFRNYSVRYR------PGLELVLKNLT 1306
Cdd:TIGR00954 400 TARVDTLLQVLDDVKSGNFKRPRVEEIESGREGG-------RNSNLVPGRGIVEYQDNGIKFEniplvtPNGDVLIESLS 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1307 LHVQGGEKVGIVGRTGAGKSSmtlcLFRILeaaeGE---IFIDGLNVahiglhDLRSQLTIIPQDPILFSGTLR------ 1377
Cdd:TIGR00954 473 FEVPSGNNLLICGPNGCGKSS----LFRIL----GElwpVYGGRLTK------PAKGKLFYVPQRPYMTLGTLRdqiiyp 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1378 MNLDPFGR--YSDEDIWRTLELSHLSAFVSSQpTGLDFQCsEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLE 1455
Cdd:TIGR00954 539 DSSEDMKRrgLSDKDLEQILDNVQLTHILERE-GGWSAVQ-DWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVD 616
|
250 260
....*....|....*....|....*....
gi 1937891448 1456 TDDLIqgtirtqFEDC-----TVLTIAHR 1479
Cdd:TIGR00954 617 VEGYM-------YRLCrefgiTLFSVSHR 638
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1297-1466 |
8.08e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 63.35 E-value: 8.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1297 GLELVLKNLTLHVQGGEKVGIVGRTGAGKSSmtlcLFRI----LEAAEGEIFIDGLNvahIGLHDLRSQLTII-PQDPIL 1371
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTT----LLRLiaglLPPAAGTIKLDGGD---IDDPDVAEACHYLgHRNAMK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1372 FSGTLRMNLDPFGRY---SDEDIWRTLE---LSHLsafvssqpTGLDFQcseggdNLSVGQRQLVCLARALLRKSRVLVL 1445
Cdd:PRK13539 86 PALTVAENLEFWAAFlggEELDIAAALEavgLAPL--------AHLPFG------YLSAGQKRRVALARLLVSNRPIWIL 151
|
170 180
....*....|....*....|.
gi 1937891448 1446 DEATAAIDLETDDLIQGTIRT 1466
Cdd:PRK13539 152 DEPTAALDAAAVALFAELIRA 172
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
626-850 |
8.13e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.11 E-value: 8.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWSKDLP---PTLHSLNIQIPKGALVAVVGPVGCGKSSLV---SALL----GEME----------------- 678
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtelKALDNVSVEINQGEFIAIIGQTGSGKTTFIehlNALLlpdtGTIEwifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 679 -------------KLEGAVSVKGSVAYVPQQAWIQ--NCTLQENVLFGqPMN---PKryQQALEtcaLLADLDVLPGGDQ 740
Cdd:PRK13651 83 vleklviqktrfkKIKKIKEIRRRVGVVFQFAEYQlfEQTIEKDIIFG-PVSmgvSK--EEAKK---RAAKYIELVGLDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 741 TEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDqvIGPEGVLAGKTRVLVTHGI-SFLPQTDF 819
Cdd:PRK13651 157 SYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKQGKTIILVTHDLdNVLEWTKR 234
|
250 260 270
....*....|....*....|....*....|.
gi 1937891448 820 IIVLADGQITEMGHYSELLQHDgsfaNFLRN 850
Cdd:PRK13651 235 TIFFKDGKIIKDGDTYDILSDN----KFLIE 261
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
636-837 |
1.05e-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: 63.29 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 636 SKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG------------SVAYVPQqawiqnct 703
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGYCPQ-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 704 lqENVLFGQpMNPKryqQALETCALL-------ADLDVLPGGDQTEIGEKG----INLSGGQRQRVSLARAVYSDANIFL 772
Cdd:cd03263 83 --FDALFDE-LTVR---EHLRFYARLkglpkseIKEEVELLLRVLGLTDKAnkraRTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937891448 773 LDDPLSAVDsHVAKHIFDQVIgpEGVLAGKTRVLVTHG---ISFLpqTDFIIVLADGQITEMGHYSEL 837
Cdd:cd03263 157 LDEPTSGLD-PASRRAIWDLI--LEVRKGRSIILTTHSmdeAEAL--CDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1285-1453 |
1.07e-10 |
|
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: 63.04 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHD------- 1357
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDrdiamvf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1358 ----LRSQLTIIpqDPILFSGTLRmnldpfGRYSDE------DIWRTLELSHLsafvssqptgLDFQCSEggdnLSVGQR 1427
Cdd:cd03301 79 qnyaLYPHMTVY--DNIAFGLKLR------KVPKDEidervrEVAELLQIEHL----------LDRKPKQ----LSGGQR 136
|
170 180
....*....|....*....|....*.
gi 1937891448 1428 QLVCLARALLRKSRVLVLDEATAAID 1453
Cdd:cd03301 137 QRVALGRAIVREPKVFLMDEPLSNLD 162
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1282-1509 |
1.08e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 63.56 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1282 SGVVEFRNYSVRYRPGLE--------------------LVLKNLTLHVQGGEKVGIVGRTGAGKSsmTLC--LFRILEAA 1339
Cdd:COG1134 2 SSMIEVENVSKSYRLYHEpsrslkelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKS--TLLklIAGILEPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1340 EGEIFIDG-----LNVAHiGLHdlrSQLTIIpqDPILFSGTLrMNLdpfgrySDEDIWRTLElshlsaFVssqptgLDFq 1414
Cdd:COG1134 80 SGRVEVNGrvsalLELGA-GFH---PELTGR--ENIYLNGRL-LGL------SRKEIDEKFD------EI------VEF- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1415 cSEGGD-------NLSVGQRqlvclAR-----ALLRKSRVLVLDEATAAIDLE----TDDLIQGTIRtqfEDCTVLTIAH 1478
Cdd:COG1134 134 -AELGDfidqpvkTYSSGMR-----ARlafavATAVDPDILLVDEVLAVGDAAfqkkCLARIRELRE---SGRTVIFVSH 204
|
250 260 270
....*....|....*....|....*....|..
gi 1937891448 1479 RLNTIMDY-NRVLVLDKGVVAEFDSPVNLIAA 1509
Cdd:COG1134 205 SMGAVRRLcDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
626-844 |
1.16e-10 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 64.11 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLgEMEKLEGAVSVKG-------------SVAY 692
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwrkAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 693 VPQQAWIQNCTLQENV-LFGQPMNPKRYQQAlETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIF 771
Cdd:cd03289 82 IPQKVFIFSGTFRKNLdPYGKWSDEEIWKVA-EEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 772 LLDDP---LSAVDSHVAKHIFDQvigpegVLAGKTRVLVTHGISFLPQTDFIIVLADGQITEMGHYSELLQHDGSF 844
Cdd:cd03289 161 LLDEPsahLDPITYQVIRKTLKQ------AFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
626-832 |
1.16e-10 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 62.98 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWSKDLppTLHSLNIQIPKGaLVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS------------VAYV 693
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrrIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 694 PQQ-AWIQNCTLQENV-----LFGqpMNPKRYQQALetCALLADLDVLPGGDQtEIGEkginLSGGQRQRVSLARAVYSD 767
Cdd:cd03264 78 PQEfGVYPNFTVREFLdyiawLKG--IPSKEVKARV--DEVLELVNLGDRAKK-KIGS----LSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 768 ANIFLLDDPLSAVDShVAKHIFDQVIGpeGVLAGKTRVLVTHGISFLPQT-DFIIVLADGQITEMG 832
Cdd:cd03264 149 PSILIVDEPTAGLDP-EERIRFRNLLS--ELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1284-1495 |
1.18e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 62.97 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYRPGLElVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHD---LRS 1360
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQ-ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1361 QLTIIPQD-PILFSGTLRMNLD-PF--GRYSDEDIWRtlelsHLSAFVSSqpTGLDFQCSEGGDNLSVGQRQLVCLARAL 1436
Cdd:PRK10908 80 QIGMIFQDhHLLMDRTVYDNVAiPLiiAGASGDDIRR-----RVSAALDK--VGLLDKAKNFPIQLSGGEQQRVGIARAV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937891448 1437 LRKSRVLVLDEATAAIDletDDLIQGTIRTqFED-----CTVLTIAHRLNTIMDYN-RVLVLDKG 1495
Cdd:PRK10908 153 VNKPAVLLADEPTGNLD---DALSEGILRL-FEEfnrvgVTVLMATHDIGLISRRSyRMLTLSDG 213
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1297-1453 |
1.26e-10 |
|
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: 63.22 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1297 GLEL-VLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFID----GLNVAHIG---LHDLR-------SQ 1361
Cdd:COG4778 21 GKRLpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASpreILALRrrtigyvSQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1362 -LTIIPQ--------DPILFSGT-------------LRMNLdpfgrysDEDIWrtlelsHLSafvssqPTgldfqcsegg 1419
Cdd:COG4778 101 fLRVIPRvsaldvvaEPLLERGVdreearararellARLNL-------PERLW------DLP------PA---------- 151
|
170 180 190
....*....|....*....|....*....|....
gi 1937891448 1420 dNLSVGQRQLVCLARALLRKSRVLVLDEATAAID 1453
Cdd:COG4778 152 -TFSGGEQQRVNIARGFIADPPLLLLDEPTASLD 184
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1301-1503 |
1.33e-10 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 64.78 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1301 VLKNLTLHVQGGEKVGIVGRTGAGKSsMTLclfRI---LEAA-EGEIFIDGlNVAHIGLHDLRSQLTIIPQDPILFsgtl 1376
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKT-TLL---RIiagLETPdSGRIVLNG-RDLFTNLPPRERRVGFVFQHYALF---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1377 rmnldP---------FG----RYSDEDIWRT----LELSHLSAFVSSQPTgldfqcseggdNLSVGQRQLVCLARALLRK 1439
Cdd:COG1118 88 -----PhmtvaeniaFGlrvrPPSKAEIRARveelLELVQLEGLADRYPS-----------QLSGGQRQRVALARALAVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937891448 1440 SRVLVLDEATAAID------LET------DDLiqgtirtqfeDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSP 1503
Cdd:COG1118 152 PEVLLLDEPFGALDakvrkeLRRwlrrlhDEL----------GGTTVFVTHDQEEALELaDRVVVMNQGRIEQVGTP 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
643-838 |
1.44e-10 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 63.18 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEM------------EKLeGAVSV---KGSVAYV-P--QQAWIQNCTL 704
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpptygndvrlfgERR-GGEDVwelRKRIGLVsPalQLRFPRDETV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 705 QENVL---FGQPMNPKRY--QQALETCALLADLDVLPGGDQTeIGEkginLSGGQRQRVSLARAVYSDANIFLLDDPLSA 779
Cdd:COG1119 98 LDVVLsgfFDSIGLYREPtdEQRERARELLELLGLAHLADRP-FGT----LSQGEQRRVLIARALVKDPELLILDEPTAG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 780 VDSHvAKHIFDQVIgpeGVLAG---KTRVLVTHGISFLPQ-TDFIIVLADGQITEMGHYSELL 838
Cdd:COG1119 173 LDLG-ARELLLALL---DKLAAegaPTLVLVTHHVEEIPPgITHVLLLKDGRVVAAGPKEEVL 231
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1285-1506 |
1.80e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 64.36 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMtLCLFRILEA-AEGEIFIDGLNVAHIGLHdlRSQLT 1363
Cdd:PRK11432 7 VVLKNITKRF--GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTV-LRLVAGLEKpTEGQIFIDGEDVTHRSIQ--QRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1364 IIPQDPILFSGT---------LRMnldpFGRYSDEDIWR---TLELSHLSAF----VssqptgldfqcseggDNLSVGQR 1427
Cdd:PRK11432 82 MVFQSYALFPHMslgenvgygLKM----LGVPKEERKQRvkeALELVDLAGFedryV---------------DQISGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1428 QLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIR---TQFeDCTVLTIAH-RLNTIMDYNRVLVLDKGVVAEFDSP 1503
Cdd:PRK11432 143 QRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRelqQQF-NITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSP 221
|
...
gi 1937891448 1504 VNL 1506
Cdd:PRK11432 222 QEL 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
643-781 |
1.83e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 63.13 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSAL--LGEME---KLEGAVSVKG---------------SVAYVPQQAwiqN- 701
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIpgaRVEGEILLDGediydpdvdvvelrrRVGMVFQKP---Np 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 702 --CTLQENVLFG---QPMNPKRY-----QQALETCALLADL-DVLpggdqteiGEKGINLSGGQRQRVSLARAVYSDANI 770
Cdd:COG1117 104 fpKSIYDNVAYGlrlHGIKSKSEldeivEESLRKAALWDEVkDRL--------KKSALGLSGGQQQRLCIARALAVEPEV 175
|
170
....*....|.
gi 1937891448 771 FLLDDPLSAVD 781
Cdd:COG1117 176 LLMDEPTSALD 186
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
644-791 |
2.07e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.13 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 644 HSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG------------SVAYVPQQAWIQN-CTLQENVLF 710
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGepirrqrdeyhqDLLYLGHQPGIKTeLTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 711 GQPM----NPKRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSH-VA 785
Cdd:PRK13538 98 YQRLhgpgDDEALWEALAQVGLAGFEDVPVR-----------QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQgVA 166
|
....*...
gi 1937891448 786 --KHIFDQ 791
Cdd:PRK13538 167 rlEALLAQ 174
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1302-1498 |
2.11e-10 |
|
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: 62.31 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1302 LKNLTLHVQ---GGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGlnvahIGLHDLRSQLTIIPQD---PILFSG- 1374
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG-----TVLFDSRKKINLPPQQrkiGLVFQQy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1375 ------TLRMNLDpFG---------RYSDEDIWRTLELSHLSAFVSSQptgldfqcseggdnLSVGQRQLVCLARALLRK 1439
Cdd:cd03297 85 alfphlNVRENLA-FGlkrkrnredRISVDELLDLLGLDHLLNRYPAQ--------------LSGGEKQRVALARALAAQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 1440 SRVLVLDEATAAIDLETDDLIQGTIRTQFED--CTVLTIAHRLNTI-MDYNRVLVLDKGVVA 1498
Cdd:cd03297 150 PELLLLDEPFSALDRALRLQLLPELKQIKKNlnIPVIFVTHDLSEAeYLADRIVVMEDGRLQ 211
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1282-1484 |
2.74e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.44 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1282 SGVVEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIfidglnvahigLHDLRSQ 1361
Cdd:PRK09544 2 TSLVSLENVSVSF--GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1362 LTIIPQ----DPILFSGTLR-MNLDPFGRysDEDIWRTLELSHlSAFVSSQPTgldfqcseggDNLSVGQRQLVCLARAL 1436
Cdd:PRK09544 69 IGYVPQklylDTTLPLTVNRfLRLRPGTK--KEDILPALKRVQ-AGHLIDAPM----------QKLSGGETQRVLLARAL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 1437 LRKSRVLVLDEATAAID----LETDDLIQgTIRTQFeDCTVLTIAHRLNTIM 1484
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVDvngqVALYDLID-QLRREL-DCAVLMVSHDLHLVM 185
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1284-1499 |
3.11e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 62.24 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILE-----AAEGEIFIDGLNVAHIGLHDL 1358
Cdd:PRK14247 3 KIEIRDLKVSF--GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1359 RSQLTIIPQ--DPI----LFSGT---LRMN-LDPFGRYSDEDIWRTLELSHLSAFVSSQ---PTGldfqcseggdNLSVG 1425
Cdd:PRK14247 81 RRRVQMVFQipNPIpnlsIFENValgLKLNrLVKSKKELQERVRWALEKAQLWDEVKDRldaPAG----------KLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937891448 1426 QRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAH---RLNTIMDYnrVLVLDKGVVAE 1499
Cdd:PRK14247 151 QQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqQAARISDY--VAFLYKGQIVE 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1284-1508 |
3.21e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 64.44 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRY---RPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEI-------FID------- 1346
Cdd:TIGR03269 279 IIKVRNVSKRYisvDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDmtkpgpd 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1347 --GLNVAHIGLhdLRSQLTIIPQDPILFSGTLRMNLD-PFgrysdediwrtlELSHLSAFVSSQPTGLDFQCSEG----- 1418
Cdd:TIGR03269 359 grGRAKRYIGI--LHQEYDLYPHRTVLDNLTEAIGLElPD------------ELARMKAVITLKMVGFDEEKAEEildky 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1419 GDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTI---RTQFEDcTVLTIAHRLNTIMDY-NRVLVLDK 1494
Cdd:TIGR03269 425 PDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkaREEMEQ-TFIIVSHDMDFVLDVcDRAALMRD 503
|
250
....*....|....
gi 1937891448 1495 GVVAEFDSPVNLIA 1508
Cdd:TIGR03269 504 GKIVKIGDPEEIVE 517
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1301-1495 |
3.38e-10 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 61.96 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1301 VLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGL--------NVAHIGL-HDLRSQL--TIIPQDp 1369
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvpwkrrkkFLRRIGVvFGQKTQLwwDLPVID- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1370 ilfsgTLRMNLDPFgRYSDEDIWRTLElsHLSAFVSSQPTgLDFQCSeggdNLSVGQRQLVCLARALLRKSRVLVLDEAT 1449
Cdd:cd03267 115 -----SFYLLAAIY-DLPPARFKKRLD--ELSELLDLEEL-LDTPVR----QLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1937891448 1450 AAIDLETDDLIQGTIRTQFED--CTVLTIAHRLNTIMDY-NRVLVLDKG 1495
Cdd:cd03267 182 IGLDVVAQENIRNFLKEYNRErgTTVLLTSHYMKDIEALaRRVLVIDKG 230
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1297-1492 |
3.62e-10 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 61.35 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1297 GLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTL 1376
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1377 RMNLDPFGRY-SDEDIWRTLELSHLSAFvSSQPTGldfqcseggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLE 1455
Cdd:cd03231 91 LENLRFWHADhSDEQVEEALARVGLNGF-EDRPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 1937891448 1456 TDDLIQGTIRTQFED--CTVLTIAHRLNTIMDYNRVLVL 1492
Cdd:cd03231 160 GVARFAEAMAGHCARggMVVLTTHQDLGLSEAGARELDL 198
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
646-776 |
4.81e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 64.19 E-value: 4.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 646 LNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSV--AYVPQQ--AWIQNCTLQENVLFGQ--------P 713
Cdd:TIGR03719 341 LSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVklAYVDQSrdALDPNKTVWEEISGGLdiiklgkrE 420
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937891448 714 MNPKRYqqaletCALLAdldvLPGGDQTE-IGEkginLSGGQRQRVSLARAVYSDANIFLLDDP 776
Cdd:TIGR03719 421 IPSRAY------VGRFN----FKGSDQQKkVGQ----LSGGERNRVHLAKTLKSGGNVLLLDEP 470
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
643-841 |
4.86e-10 |
|
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: 61.54 E-value: 4.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS--------------VAYVPQQAWI-QNCTLQEN 707
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpphriarlgIGYVPEGRRIfPSLTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 708 VLFGQPMNPKRYQQAletcallADLD-------VL------PGGdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLD 774
Cdd:COG0410 99 LLLGAYARRDRAEVR-------ADLErvyelfpRLkerrrqRAG----------TLSGGEQQMLAIGRALMSRPKLLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 775 DP---LSAVdshVAKHIFDQV--IGPEGVlagkTRVLVTHGISF-LPQTDFIIVLADGQITEMGHYSELLQHD 841
Cdd:COG0410 162 EPslgLAPL---IVEEIFEIIrrLNREGV----TILLVEQNARFaLEIADRAYVLERGRIVLEGTAAELLADP 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
643-830 |
5.72e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 61.37 E-value: 5.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG---SVAYVPQQAWIQNCTLQ-------------- 705
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmSKLSSAAKAELRNQKLGfiyqfhhllpdfta 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 706 -ENV----LFGQpMNPKRYQQ-ALETCALLadldvlpgGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSA 779
Cdd:PRK11629 105 lENVamplLIGK-KKPAEINSrALEMLAAV--------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1937891448 780 VDSHVAKHIFdQVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQITE 830
Cdd:PRK11629 176 LDARNADSIF-QLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTA 225
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1285-1495 |
5.92e-10 |
|
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: 59.00 E-value: 5.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAEGEI-FIDGLNVAHIglhdlr 1359
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKST----LLKLIagelEPDEGIVtWGSTVKIGYF------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1360 SQLtiipqdpilfSGtlrmnldpfgrysdediwrtlelshlsafvssqptgldfqcseggdnlsvGQRQLVCLARALLRK 1439
Cdd:cd03221 69 EQL----------SG--------------------------------------------------GEKMRLALAKLLLEN 88
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1937891448 1440 SRVLVLDEATAAIDLETDDLIQGTIRTQfeDCTVLTIAH-R--LNTIMdyNRVLVLDKG 1495
Cdd:cd03221 89 PNLLLLDEPTNHLDLESIEALEEALKEY--PGTVILVSHdRyfLDQVA--TKIIELEDG 143
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
643-839 |
6.05e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 62.06 E-value: 6.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVK--------------------GSVAYVPQQAWIQNC 702
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGdivvsstskqkeikpvrkkvGVVFQFPESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 703 TLQEnVLFGqpmnPKRYQQALETCALLADLDVLPGGDQTEIGEKG-INLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD 781
Cdd:PRK13643 102 VLKD-VAFG----PQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSpFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 782 SHV---AKHIFDQVIGpegvlAGKTRVLVTHGISFLPQ-TDFIIVLADGQITEMGHYSELLQ 839
Cdd:PRK13643 177 PKArieMMQLFESIHQ-----SGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1284-1501 |
7.02e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.50 E-value: 7.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYRpglelvLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNV----------AHI 1353
Cdd:COG1129 256 VLEVEGLSVGGV------VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVrirsprdairAGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1354 GL--HDlRSQLTIIPQDPILFSGTLrMNLDPFGRYSdeDIWRTLELSHLSAFVSS---------QPTGldfqcseggdNL 1422
Cdd:COG1129 330 AYvpED-RKGEGLVLDLSIRENITL-ASLDRLSRGG--LLDRRRERALAEEYIKRlriktpspeQPVG----------NL 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1423 SVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFED-CTVLTIAHRLNTIMDY-NRVLVLDKG-VVAE 1499
Cdd:COG1129 396 SGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEgKAVIVISSELPELLGLsDRILVMREGrIVGE 475
|
..
gi 1937891448 1500 FD 1501
Cdd:COG1129 476 LD 477
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1302-1453 |
7.32e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 60.57 E-value: 7.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1302 LKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEA---AEGEIFIDGLNVAHIGLHdlRSQLTIIPQDPILFS----- 1373
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QRRIGILFQDDLLFPhlsvg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1374 GTLRMNLDP-FGRYSDED-IWRTLELSHLSAFVSSQPtgldfqcseggDNLSVGQRQLVCLARALLRKSRVLVLDEATAA 1451
Cdd:COG4136 95 ENLAFALPPtIGRAQRRArVEQALEEAGLAGFADRDP-----------ATLSGGQRARVALLRALLAEPRALLLDEPFSK 163
|
..
gi 1937891448 1452 ID 1453
Cdd:COG4136 164 LD 165
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
625-832 |
7.91e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 61.74 E-value: 7.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 625 AITIHNGTFSWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSS---LVSALLGEMEKLEGAVSVKGsVAYVPQQAW--- 698
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDG-ITLTAKTVWdir 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 699 ------IQN-------CTLQENVLFG-------QPMNPKRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRV 758
Cdd:PRK13640 84 ekvgivFQNpdnqfvgATVGDDVAFGlenravpRPEMIKIVRDVLADVGMLDYIDSEPA-----------NLSGGQKQRV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937891448 759 SLARAVYSDANIFLLDDPLSAVDSHVAKHIFDqVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQITEMG 832
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILK-LIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQG 225
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1284-1497 |
8.06e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 61.64 E-value: 8.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYRPGLE----LVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIG-LHDL 1358
Cdd:PRK13633 4 MIKCKNVSYKYESNEEstekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1359 RSQLTIIPQDP------------ILFsGTLRMNLDPfgrysdEDIwRT-----LELSHLSAFVSSQPtgldfqcseggDN 1421
Cdd:PRK13633 84 RNKAGMVFQNPdnqivativeedVAF-GPENLGIPP------EEI-RErvdesLKKVGMYEYRRHAP-----------HL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937891448 1422 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIR--TQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVV 1497
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKelNKKYGITIILITHYMEEAVEADRIIVMDSGKV 222
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
626-840 |
8.07e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 61.95 E-value: 8.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWSKDLPPTLHSLN---IQIPKGALVAVVGPVGCGKSSLV------------SALLGEMEKLEGAVSVK--- 687
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEFKALNntsLTFKKNKVTCVIGTTGSGKSTMIqltngliisetgQTIVGDYAIPANLKKIKevk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 688 ------GSVAYVPQQAWIQNcTLQENVLFGqPMN-PKRYQQALETCALLADLDVLPggdQTEIGEKGINLSGGQRQRVSL 760
Cdd:PRK13645 87 rlrkeiGLVFQFPEYQLFQE-TIEKDIAFG-PVNlGENKQEAYKKVPELLKLVQLP---EDYVKRSPFELSGGQKRRVAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 761 ARAVYSDANIFLLDDPLSAVDSHvAKHIFDQVIGPEGVLAGKTRVLVTHGI-SFLPQTDFIIVLADGQITEMGHYSELLQ 839
Cdd:PRK13645 162 AGIIAMDGNTLVLDEPTGGLDPK-GEEDFINLFERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
.
gi 1937891448 840 H 840
Cdd:PRK13645 241 N 241
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1301-1499 |
9.41e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 59.85 E-value: 9.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1301 VLKNLTLHVQGGEKVGIVGRTGAGKS--SMTLCLFRILEAAEGEIFIDGLNVAHIGLHDlRSQ--LTIIPQDPILFSGtl 1376
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKStlAKTIMGHPKYEVTEGEILFKGEDITDLPPEE-RARlgIFLAFQYPPEIPG-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1377 rMNLDPFGRYSDEdiwrtlelshlsafvssqptgldfqcseggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLET 1456
Cdd:cd03217 92 -VKNADFLRYVNE-------------------------------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1937891448 1457 DDLIQGTIRT-QFEDCTVLTIAHRLNtIMDY---NRVLVLDKGVVAE 1499
Cdd:cd03217 140 LRLVAEVINKlREEGKSVLIITHYQR-LLDYikpDRVHVLYDGRIVK 185
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
646-809 |
9.84e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 60.36 E-value: 9.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 646 LNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKgsvayVPQQAWIQNCTLQENVLFGQPMNPKRYqqALET 725
Cdd:COG2401 49 LNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----VPDNQFGREASLIDAIGRKGDFKDAVE--LLNA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 726 CALladldvlpgGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKhifdqvIGPEGVL-----A 800
Cdd:COG2401 122 VGL---------SDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK------RVARNLQklarrA 186
|
....*....
gi 1937891448 801 GKTRVLVTH 809
Cdd:COG2401 187 GITLVVATH 195
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
646-840 |
1.02e-09 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 60.53 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 646 LNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-SVAYVP-------------QQAWI-QNCTLQENVL- 709
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeDITGLPpheiarlgigrtfQIPRLfPELTVLENVMv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 710 ---------FGQPMNPKRYQQA-------LETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLL 773
Cdd:cd03219 99 aaqartgsgLLLARARREEREAreraeelLERVGLADLADRPAG-----------ELSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937891448 774 DDP---LSAVDSHVAKHIFDQVigpegVLAGKTRVLVTHGISFLPQ-TDFIIVLADGQITEMGHYSELLQH 840
Cdd:cd03219 168 DEPaagLNPEETEELAELIREL-----RERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNN 233
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
1010-1256 |
1.07e-09 |
|
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: 61.42 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1010 VYATLGILQGLLVMLSAFTMVVGAIQAARLLHTALLHNQIRAPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLFNS 1089
Cdd:cd18557 41 ILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1090 FYTSISTIVVIVAS----TPLFCVVVLPLAVFYGFVQRFYVATSRQLkrLESVSRSPifSHFSETVTGTSVIRAYGR--- 1162
Cdd:cd18557 121 ILQVIGGLIILFILswklTLVLLLVIPLLLIASKIYGRYIRKLSKEV--QDALAKAG--QVAEESLSNIRTVRSFSAeek 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1163 -VQDFKVLSDAKVDSNQKTTypyiasnRWLGVHvEFVGNCVVLFSaLFAV-------IGRNSLNPGLVGLSVSYALQVTL 1234
Cdd:cd18557 197 eIRRYSEALDRSYRLARKKA-------LANALF-QGITSLLIYLS-LLLVlwyggylVLSGQLTVGELTSFILYTIMVAS 267
|
250 260
....*....|....*....|..
gi 1937891448 1235 SLNWMIRTLSDLESNIIAVERV 1256
Cdd:cd18557 268 SVGGLSSLLADIMKALGASERV 289
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
643-828 |
1.10e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 63.20 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSaLLGEMEK-LEGAVSVKGS-VAYVPQQAWIQ-----------------NCT 703
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDKpTSGTYRVAGQdVATLDADALAQlrrehfgfifqryhllsHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 704 LQENV----LFGQPMNPKRYQQALEtcaLLADLdvlpgGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSA 779
Cdd:PRK10535 103 AAQNVevpaVYAGLERKQRLLRAQE---LLQRL-----GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 780 VDSH-------VAKHIFDQvigpegvlaGKTRVLVTHGISFLPQTDFIIVLADGQI 828
Cdd:PRK10535 175 LDSHsgeevmaILHQLRDR---------GHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
643-792 |
1.16e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 60.28 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG--------------SVAYVPQQAWI-QNCTLQEN 707
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkditdwqtakimreAVAIVPEGRRVfSRMTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 708 VLFGQPM-NPKRYQQALETCalladLDVLPGGDQTEIGEKGiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAK 786
Cdd:PRK11614 101 LAMGGFFaERDQFQERIKWV-----YELFPRLHERRIQRAG-TMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
....*.
gi 1937891448 787 HIFDQV 792
Cdd:PRK11614 175 QIFDTI 180
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1285-1483 |
1.19e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.82 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAaEGEIFIDG--------LNVAHIGLH 1356
Cdd:PRK14258 8 IKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGrveffnqnIYERRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1357 DLRSQLTIIPQDPILFSGTLRMNLdpfgRYSDEDI-WR-TLELSHLsafVSSQPTGLDF------QCSEGGDNLSVGQRQ 1428
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNV----AYGVKIVgWRpKLEIDDI---VESALKDADLwdeikhKIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1429 LVCLARALLRKSRVLVLDEATAAID----LETDDLIQG-TIRTQFedcTVLTIAHRLNTI 1483
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSlRLRSEL---TMVIVSHNLHQV 214
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
653-809 |
1.26e-09 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 59.43 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 653 GALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSVAYVPQQAWIQNC-------------TLQENVLFGQPMNPK-R 718
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLlylghapgikttlSVLENLRFWHADHSDeQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 719 YQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGPEGv 798
Cdd:cd03231 106 VEEALARVGLNGFEDRPVA-----------QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCA- 173
|
170
....*....|.
gi 1937891448 799 lAGKTRVLVTH 809
Cdd:cd03231 174 -RGGMVVLTTH 183
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
643-840 |
1.28e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.19 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVK--------------------GSVAYVPQQAWIQNc 702
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGervitagkknkklkplrkkvGIVFQFPEHQLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 703 TLQENVLFGqPMN---PKryQQALETCALLADLDVLPggdqTEIGEKG-INLSGGQRQRVSLARAVYSDANIFLLDDPLS 778
Cdd:PRK13634 102 TVEKDICFG-PMNfgvSE--EDAKQKAREMIELVGLP----EELLARSpFELSGGQMRRVAIAGVLAMEPEVLVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937891448 779 AVDSHVAKHIFDQV--IGPEGvlaGKTRVLVTHGISFLPQ-TDFIIVLADGQITEMGHYSELLQH 840
Cdd:PRK13634 175 GLDPKGRKEMMEMFykLHKEK---GLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFAD 236
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1301-1505 |
1.41e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 60.45 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1301 VLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGL------NVAHIGLHDLRSQLTIIPQDPILFS- 1373
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPh 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1374 ----GTLRMNLDPFGRYSDEDIWRTLELSHLSAFVSSQptgLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEAT 1449
Cdd:PRK14246 105 lsiyDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKE---VYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 1450 AAIDLETDDLIQGTIRTQFEDCTVLTIAH---RLNTIMDYnrVLVLDKGVVAE-------FDSPVN 1505
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHnpqQVARVADY--VAFLYNGELVEwgssneiFTSPKN 245
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1273-1450 |
1.50e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 62.30 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1273 NRAPEGWPRsgvVEFRNYSVRYR-PGLELVLKNLTLHvqGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVA 1351
Cdd:PRK10522 314 PQAFPDWQT---LELRNVTFAYQdNGFSVGPINLTIK--RGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1352 HIGLHDLRSQLTIIPQDPILFSGTlrmnLDPFGRYSDE---DIW-RTLELSHLSAFVSSQPTGLdfqcseggdNLSVGQR 1427
Cdd:PRK10522 389 AEQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPalvEKWlERLKMAHKLELEDGRISNL---------KLSKGQK 455
|
170 180
....*....|....*....|...
gi 1937891448 1428 QLVCLARALLRKSRVLVLDEATA 1450
Cdd:PRK10522 456 KRLALLLALAEERDILLLDEWAA 478
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1292-1508 |
1.59e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 60.37 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1292 VRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIglHDLRSQLTIIPQDPI- 1370
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLV--RDKDGQLKVADKNQLr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1371 LFSGTLRMNLDPFGRYSD--------EDIWRTLELSHLSAFVSS----QPTGLDfQCSEGG--DNLSVGQRQLVCLARAL 1436
Cdd:PRK10619 89 LLRTRLTMVFQHFNLWSHmtvlenvmEAPIQVLGLSKQEARERAvkylAKVGID-ERAQGKypVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937891448 1437 LRKSRVLVLDEATAAIDLE-TDDLIQGTIRTQFEDCTVLTIAHRlntiMDYNR-----VLVLDKGVVAEFDSPVNLIA 1508
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPElVGEVLRIMQQLAEEGKTMVVVTHE----MGFARhvsshVIFLHQGKIEEEGAPEQLFG 241
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1284-1453 |
2.04e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 61.50 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSmtlcLFRIL----EAAEGEIFIDGLNVAHIGLHD-- 1357
Cdd:PRK09452 14 LVELRGISKSF--DGKEVISNLDLTINNGEFLTLLGPSGCGKTT----VLRLIagfeTPDSGRIMLDGQDITHVPAENrh 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1358 ---------LRSQLTIIpqDPILFSgtLRMNLDPfgrySDEDIWRTLE---LSHLSAFVSSQPTgldfqcseggdNLSVG 1425
Cdd:PRK09452 88 vntvfqsyaLFPHMTVF--ENVAFG--LRMQKTP----AAEITPRVMEalrMVQLEEFAQRKPH-----------QLSGG 148
|
170 180
....*....|....*....|....*...
gi 1937891448 1426 QRQLVCLARALLRKSRVLVLDEATAAID 1453
Cdd:PRK09452 149 QQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
643-832 |
2.24e-09 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 59.30 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-SVAYVPQQA---------------WIqncTLQE 706
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEArrrlgfvsdstglydRL---TARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 707 NVLFGQPMnpkryqQALETCALLADLDVLpgGDQTEIGE----KGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDS 782
Cdd:cd03266 98 NLEYFAGL------YGLKGDELTARLEEL--ADRLGMEElldrRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1937891448 783 HVAKHIFDQVigPEGVLAGKTRVLVTHGISFLPQ-TDFIIVLADGQITEMG 832
Cdd:cd03266 170 MATRALREFI--RQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1284-1480 |
2.28e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 60.18 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILE-----AAEGEIFIDGLNV--AHIGLH 1356
Cdd:PRK14243 10 VLRTENLNVYY--GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1357 DLRSQLTIIPQDPILFSGTLRMNLDPFGRYS------DEDIWRTLELSHLSAFVSSQptgldfqCSEGGDNLSVGQRQLV 1430
Cdd:PRK14243 88 EVRRRIGMVFQKPNPFPKSIYDNIAYGARINgykgdmDELVERSLRQAALWDEVKDK-------LKQSGLSLSGGQQQRL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1431 CLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRL 1480
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
643-841 |
2.31e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.20 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS-------------VAYVPQQA--WIQNCTLQEN 707
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfVGLVFQNPddQIFSPTVEQD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 708 VLFGqPMN--------PKRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSA 779
Cdd:PRK13652 100 IAFG-PINlgldeetvAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 780 VDSHVAKHIFDqVIGPEGVLAGKTRVLVTHGISFLPQ-TDFIIVLADGQITEMGHYSELLQHD 841
Cdd:PRK13652 168 LDPQGVKELID-FLNDLPETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
653-839 |
2.48e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 61.99 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 653 GALVAVVGPVGCGKSSLVSALlgeMEKLEGAVSVKGSV----------------AYVPQQ-AWIQNCTLQENVLF----- 710
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNAL---AFRSPKGVKGSGSVllngmpidakemraisAYVQQDdLFIPTLTVREHLMFqahlr 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 711 -GQPMNPKRYQQALEtcALLADLDVLPGGDqTEIGEKGI--NLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKH 787
Cdd:TIGR00955 128 mPRRVTKKEKRERVD--EVLQALGLRKCAN-TRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYS 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 788 IFDQVIGpegvLA--GKTRVLVTHGIS--FLPQTDFIIVLADGQITEMGHYSELLQ 839
Cdd:TIGR00955 205 VVQVLKG----LAqkGKTIICTIHQPSseLFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
1017-1180 |
2.51e-09 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 60.09 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1017 LQGLLVMLSAFTMVVGAIQAARLLHTALLH-------NQIRA---------PQSFFDTTPSGRILNRFSKDIYVIDEVLA 1080
Cdd:cd18544 37 LQGLLLLALLYLGLLLLSFLLQYLQTYLLQklgqriiYDLRRdlfshiqrlPLSFFDRTPVGRLVTRVTNDTEALNELFT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1081 PTILMLFNSFYTSISTIVVIVASTP---LFCVVVLPLAVfygFVQRFYVATSRQLKRLESVSRSPIFSHFSETVTGTSVI 1157
Cdd:cd18544 117 SGLVTLIGDLLLLIGILIAMFLLNWrlaLISLLVLPLLL---LATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVI 193
|
170 180
....*....|....*....|....*..
gi 1937891448 1158 RAYGR----VQDFKVLSDAKVDSNQKT 1180
Cdd:cd18544 194 QLFNRekreFEEFDEINQEYRKANLKS 220
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
643-838 |
2.55e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 59.68 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSVAYVPQQAW-IQNCTLQENV--LFGQPmNPKRY 719
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFqIDAIKLRKEVgmVFQQP-NPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 720 QQALETCAL-LADLDVLPGGDQTEIGEKGI------------------NLSGGQRQRVSLARAVYSDANIFLLDDPLSAV 780
Cdd:PRK14246 105 LSIYDNIAYpLKSHGIKEKREIKKIVEECLrkvglwkevydrlnspasQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 781 DShVAKHIFDQVIGPegVLAGKTRVLVTHGisflPQ-----TDFIIVLADGQITEMGHYSELL 838
Cdd:PRK14246 185 DI-VNSQAIEKLITE--LKNEIAIVIVSHN----PQqvarvADYVAFLYNGELVEWGSSNEIF 240
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1284-1503 |
2.56e-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: 61.62 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYRPGLEL--VLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEA----AEGEIFIDGLNVAHIGLHD 1357
Cdd:COG4172 6 LLSVEDLSVAFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1358 LR----SQLTIIPQDPilfsgtlrMN-LDPF--------------GRYSDEDIW-RTLEL----------SHLSAFvssq 1407
Cdd:COG4172 86 LRrirgNRIAMIFQEP--------MTsLNPLhtigkqiaevlrlhRGLSGAAARaRALELlervgipdpeRRLDAY---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1408 PtgldFQcseggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLetddliqgTIRTQF----------EDCTVLTIA 1477
Cdd:COG4172 154 P----HQ-------LSGGQRQRVMIAMALANEPDLLIADEPTTALDV--------TVQAQIldllkdlqreLGMALLLIT 214
|
250 260 270
....*....|....*....|....*....|....
gi 1937891448 1478 HRLNTIMDY-NRVLVLDKGVVAE-------FDSP 1503
Cdd:COG4172 215 HDLGVVRRFaDRVAVMRQGEIVEqgptaelFAAP 248
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1284-1508 |
2.59e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 59.51 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHD-LRSQL 1362
Cdd:PRK11614 5 MLSFDKVSAHY--GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1363 TIIPQDPILFSG-TLRMNLDPFGRYSDED-----IWRTLELSHLSAFVSSQPTGldfqcseggdNLSVGQRQLVCLARAL 1436
Cdd:PRK11614 83 AIVPEGRRVFSRmTVEENLAMGGFFAERDqfqerIKWVYELFPRLHERRIQRAG----------TMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937891448 1437 LRKSRVLVLDEATAA----IDLETDDLIQgtiRTQFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSPVNLIA 1508
Cdd:PRK11614 153 MSQPRLLLLDEPSLGlapiIIQQIFDTIE---QLREQGMTIFLVEQNANQALKLaDRGYVLENGHVVLEDTGDALLA 226
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
618-841 |
2.84e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.80 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 618 KTISPGRAITIHNGTFSwskdLP--PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS------ 689
Cdd:PRK10575 4 YTNHSDTTFALRNVSFR----VPgrTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQplesws 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 690 -------VAYVPQQ-AWIQNCTLQENVLFGQ-PMNPK--RYQQA----LETCALLADLdvlpggdqTEIGEKGIN-LSGG 753
Cdd:PRK10575 80 skafarkVAYLPQQlPAAEGMTVRELVAIGRyPWHGAlgRFGAAdrekVEEAISLVGL--------KPLAHRLVDsLSGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 754 QRQRVSLARAVYSDANIFLLDDPLSAVDshvakhIFDQVigpeGVLA---------GKTRVLVTHGISFLPQ-TDFIIVL 823
Cdd:PRK10575 152 ERQRAWIAMLVAQDSRCLLLDEPTSALD------IAHQV----DVLAlvhrlsqerGLTVIAVLHDINMAARyCDYLVAL 221
|
250
....*....|....*...
gi 1937891448 824 ADGQITEMGHYSELLQHD 841
Cdd:PRK10575 222 RGGEMIAQGTPAELMRGE 239
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
643-839 |
2.91e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.84 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEK--LEGAVSVKGSV-------------------AYVPQQAwiQN 701
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGggAPRGARVTGDVtlngeplaaidaprlarlrAVLPQAA--QP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 702 C---TLQENVLFGQPMNPKR------YQQALETCAL-LADLDVLPGGDQTeigekgiNLSGGQRQRVSLARAV------- 764
Cdd:PRK13547 95 AfafSAREIVLLGRYPHARRagalthRDGEIAWQALaLAGATALVGRDVT-------TLSGGELARVQFARVLaqlwpph 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 765 --YSDANIFLLDDPLSAVDSHVAKHIFDQV--IGPE---GVLAgktrvlVTHGISFLPQ-TDFIIVLADGQITEMGHYSE 836
Cdd:PRK13547 168 daAQPPRYLLLDEPTAALDLAHQHRLLDTVrrLARDwnlGVLA------IVHDPNLAARhADRIAMLADGAIVAHGAPAD 241
|
...
gi 1937891448 837 LLQ 839
Cdd:PRK13547 242 VLT 244
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
636-837 |
3.02e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 61.19 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 636 SKDLPPT--LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS--------------VAYVPQQ-AW 698
Cdd:COG1129 11 SKSFGGVkaLDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvrfrsprdaqaagIAIIHQElNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 699 IQNCTLQENVLFGQP------MNPKR-YQQALETCALL-ADLDVlpggdQTEIGEkginLSGGQRQRVSLARAVYSDANI 770
Cdd:COG1129 91 VPNLSVAENIFLGREprrgglIDWRAmRRRARELLARLgLDIDP-----DTPVGD----LSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 771 FLLDDPLSAVDSHVAKHIFDQVigpeGVLA--GKTRVLVTHgisFLPQ----TDFIIVLADGQITEMGHYSEL 837
Cdd:COG1129 162 LILDEPTASLTEREVERLFRII----RRLKaqGVAIIYISH---RLDEvfeiADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
639-828 |
3.32e-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: 57.83 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 639 LPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS--------------VAYVP----QQAWIQ 700
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdairagIAYVPedrkREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 701 NCTLQENVLFGQPmnpkryqqaletcalladldvlpggdqteigekginLSGGQRQRVSLARAVYSDANIFLLDDPLSAV 780
Cdd:cd03215 92 DLSVAENIALSSL------------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 781 DSHVAKHIFDQVIgpEGVLAGKTRVLVThgiSFLPQ----TDFIIVLADGQI 828
Cdd:cd03215 136 DVGAKAEIYRLIR--ELADAGKAVLLIS---SELDEllglCDRILVMYEGRI 182
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
626-828 |
3.34e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 59.75 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWSKDLP-PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSvAYVPQQAW------ 698
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD-LLTEENVWdirhki 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 699 ---IQN-------CTLQENVLFG--------QPMNpKRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSL 760
Cdd:PRK13650 84 gmvFQNpdnqfvgATVEDDVAFGlenkgiphEEMK-ERVNEALELVGMQDFKEREPA-----------RLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 761 ARAVYSDANIFLLDDPLSAVDshvakhifdqvigPEGVLA------------GKTRVLVTHGISFLPQTDFIIVLADGQI 828
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLD-------------PEGRLEliktikgirddyQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1304-1495 |
3.39e-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: 61.38 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1304 NLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAA-EGEIFIDGLNVA-HIGLHDLRSQLTIIPQD-------PILFSG 1374
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDiRNPAQAIRAGIAMVPEDrkrhgivPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1375 ---TLRMnLDPFGRYSDED-------IWRTLELSHLSAFVSSQPTGldfqcseggdNLSVGQRQLVCLARALLRKSRVLV 1444
Cdd:TIGR02633 358 kniTLSV-LKSFCFKMRIDaaaelqiIGSAIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 1445 LDEATAAIDL----ETDDLIQGTIRtqfEDCTVLTIAHRLNTIMDY-NRVLVLDKG 1495
Cdd:TIGR02633 427 LDEPTRGVDVgakyEIYKLINQLAQ---EGVAIIVVSSELAEVLGLsDRVLVIGEG 479
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1284-1503 |
3.80e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 60.62 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYRPglELVLKNLTLHVQGGEKVGIVGRTGAGKSSmtlcLFRILEAAE----GEIFIDGLNVAHIGLHdlR 1359
Cdd:PRK11607 19 LLEIRNLTKSFDG--QHAVDDVSLTIYKGEIFALLGASGCGKST----LLRMLAGFEqptaGQIMLDGVDLSHVPPY--Q 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1360 SQLTIIPQDPILFSG-TLRMNLdPFGRYSDE--------DIWRTLELSHLSAFVSSQPtgldfqcseggDNLSVGQRQLV 1430
Cdd:PRK11607 91 RPINMMFQSYALFPHmTVEQNI-AFGLKQDKlpkaeiasRVNEMLGLVHMQEFAKRKP-----------HQLSGGQRQRV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 1431 CLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFE--DCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSP 1503
Cdd:PRK11607 159 ALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHDQEEAMTMaGRIAIMNRGKFVQIGEP 234
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
649-779 |
4.00e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.98 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 649 QIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSVAYVPQ----------QAWIQNCT--LQENVLFGQPMNP 716
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQyikpdydgtvEDLLRSITddLGSSYYKSEIIKP 440
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 717 KRYQQALEtcallADLDvlpggdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPlSA 779
Cdd:PRK13409 441 LQLERLLD-----KNVK---------------DLSGGELQRVAIAACLSRDADLYLLDEP-SA 482
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
626-828 |
4.69e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 59.23 E-value: 4.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWSkDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSL---VSALL--------------GEMEKLEGAVSVKG 688
Cdd:PRK13644 2 IRLENVSYSYP-DGTPALENINLVIKKGEYIGIIGKNGSGKSTLalhLNGLLrpqkgkvlvsgidtGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 689 SVAYVPQQAWIQNcTLQENVLFGqPMN--------PKRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSL 760
Cdd:PRK13644 81 IVFQNPETQFVGR-TVEEDLAFG-PENlclppieiRKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937891448 761 ARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGPEGvlAGKTRVLVTHGISFLPQTDFIIVLADGQI 828
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHE--KGKTIVYITHNLEELHDADRIIVMDRGKI 213
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
643-809 |
5.07e-09 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 58.06 E-value: 5.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS---------VAYVPQQAWI-QNCTLQENVL-FG 711
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaarnrIGYLPEERGLyPKMKVIDQLVyLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 712 QPMNPKRYQQALETCALLADLDVlpggdqTEIGEKGIN-LSGGQRQRVSLARAVYSDANIFLLDDPLSAVDShVAKHIFD 790
Cdd:cd03269 96 QLKGLKKEEARRRIDEWLERLEL------SEYANKRVEeLSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VNVELLK 168
|
170
....*....|....*....
gi 1937891448 791 QVIGpEGVLAGKTRVLVTH 809
Cdd:cd03269 169 DVIR-ELARAGKTVILSTH 186
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
650-788 |
5.16e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 58.57 E-value: 5.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 650 IPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-SVAYVPQQAWIQNCTLQENVLFGqpMNPKRYQQALETCAL 728
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYIKADYEGTVRDLLSS--ITKDFYTHPYFKTEI 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937891448 729 LADLDVLPGGDQtEIGEkginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDS----HVAKHI 788
Cdd:cd03237 100 AKPLQIEQILDR-EVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrlMASKVI 158
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1285-1510 |
6.21e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 59.02 E-value: 6.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYRPGLEL---VLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIG----LHD 1357
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1358 LRSQLTIIPQDP------------ILFS-GTLRMNLDPFGRYSDEDIwrtLELSHLSAFVSSQPtgldFQcseggdnLSV 1424
Cdd:PRK13646 83 VRKRIGMVFQFPesqlfedtvereIIFGpKNFKMNLDEVKNYAHRLL---MDLGFSRDVMSQSP----FQ-------MSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1425 GQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRT-QFEDC-TVLTIAHRLNTIMDY-NRVLVLDKGVVAEFD 1501
Cdd:PRK13646 149 GQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlQTDENkTIILVSHDMNEVARYaDEVIVMKEGSIVSQT 228
|
....*....
gi 1937891448 1502 SPVNLIAAG 1510
Cdd:PRK13646 229 SPKELFKDK 237
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
648-781 |
6.33e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 58.64 E-value: 6.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 648 IQIPKGALVAVVGPVGCGKSSLVSAL-----LGEMEKLEGAVSVKGSVAYVP---------------QQAWIQNCTLQEN 707
Cdd:PRK14243 31 LDIPKNQITAFIGPSGCGKSTILRCFnrlndLIPGFRVEGKVTFHGKNLYAPdvdpvevrrrigmvfQKPNPFPKSIYDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 708 VLFGQPMNPKR------YQQALETCALLADLdvlpggdQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD 781
Cdd:PRK14243 111 IAYGARINGYKgdmdelVERSLRQAALWDEV-------KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALD 183
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
643-832 |
6.63e-09 |
|
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: 57.93 E-value: 6.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSVAYVPQ-QAWIQ-NCTLQENVLF-----GqpMN 715
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGlGGGFNpELTGRENIYLngrllG--LS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 716 PKRYQQALETCAlladldvlpggDQTEIGE------KgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSH----VA 785
Cdd:cd03220 116 RKEIDEKIDEII-----------EFSELGDfidlpvK--TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfqekCQ 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1937891448 786 KHIFDQVIGpegvlaGKTRVLVTHGISFLPQT-DFIIVLADGQITEMG 832
Cdd:cd03220 183 RRLRELLKQ------GKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
647-781 |
7.66e-09 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 58.12 E-value: 7.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 647 NIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS--------------VAYVPQQAWI-QNCTLQEN---V 708
Cdd:COG1137 23 SLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmhkrarlgIGYLPQEASIfRKLTVEDNilaV 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 709 LFGQPMNPKRYQQALEtcALLADLDVLPGGDQteigeKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD 781
Cdd:COG1137 103 LELRKLSKKEREERLE--ELLEEFGITHLRKS-----KAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1302-1505 |
7.95e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 58.95 E-value: 7.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1302 LKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGL--------NVAHIGL---HdlRSQL--TIIPQD 1368
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYvpfkrrkeFARRIGVvfgQ--RSQLwwDLPAID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1369 pilfsgTLRMNLDPFgRYSDEDIWRTL----ELSHLSAFVSsQPTgldfqcseggDNLSVGQRQLVCLARALLRKSRVLV 1444
Cdd:COG4586 116 ------SFRLLKAIY-RIPDAEYKKRLdelvELLDLGELLD-TPV----------RQLSLGQRMRCELAAALLHRPKILF 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937891448 1445 LDEATaaIDLetDDLIQGTIRtQF-------EDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAeFDSPVN 1505
Cdd:COG4586 178 LDEPT--IGL--DVVSKEAIR-EFlkeynreRGTTILLTSHDMDDIEALcDRVIVIDHGRII-YDGSLE 240
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
640-839 |
8.71e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.17 E-value: 8.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 640 PPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEM----EKLEGAVSVKGsVAYVPQQA-WIQNCTLQENvlfgqP- 713
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDG-KPVAPCALrGRKIATIMQN-----Pr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 714 --MNPKR--YQQALETCA---LLADLDVLP--------GGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLS 778
Cdd:PRK10418 90 saFNPLHtmHTHARETCLalgKPADDATLTaaleavglENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937891448 779 AVDSHVAKHIFD------QVIGPeGVLagktrvLVTHGISFLPQ-TDFIIVLADGQITEMGHYSELLQ 839
Cdd:PRK10418 170 DLDVVAQARILDllesivQKRAL-GML------LVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFN 230
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1302-1497 |
9.23e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 58.10 E-value: 9.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1302 LKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRIL---EAAEGEIFIDGLNVAHIG-----LHDLRSQLTIIPQDPILFS 1373
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGrlardIRKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1374 GTLRMNLDPFGRYSDEDIWRTL-----ELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEA 1448
Cdd:PRK09984 100 RLSVLENVLIGALGSTPFWRTCfswftREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 1449 TAAIDLETDDLIQGTIR--TQFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVV 1497
Cdd:PRK09984 180 IASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDYALRYcERIVALRQGHV 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
639-829 |
9.43e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 59.65 E-value: 9.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 639 LPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS--------------VAYVP----QQAWIQ 700
Cdd:COG1129 264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAYVPedrkGEGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 701 NCTLQENVLF--------GQPMNPKRYQQALEtcALLADLDVLPGGDQTEIGekgiNLSGGQRQRVSLARAVYSDANIFL 772
Cdd:COG1129 344 DLSIRENITLasldrlsrGGLLDRRRERALAE--EYIKRLRIKTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLI 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937891448 773 LDDPLSAVDshV-AKH-IFDQVIGpegvLA--GKTRVLVThgiSFLPQ----TDFIIVLADGQIT 829
Cdd:COG1129 418 LDEPTRGID--VgAKAeIYRLIRE----LAaeGKAVIVIS---SELPEllglSDRILVMREGRIV 473
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
641-809 |
1.41e-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: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSVAYVPQQAWIQNCTlqenVLFGQ-------- 712
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIG----VVFGQktqlwwdl 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 713 -PMN------------PKRYQQALETCALLADLdvlpggdqTEIGEKGI-NLSGGQRQRVSLARAVYSDANIFLLDDPLS 778
Cdd:cd03267 111 pVIDsfyllaaiydlpPARFKKRLDELSELLDL--------EELLDTPVrQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190
....*....|....*....|....*....|.
gi 1937891448 779 AVDShVAKHIFDQVIGPEGVLAGKTRVLVTH 809
Cdd:cd03267 183 GLDV-VAQENIRNFLKEYNRERGTTVLLTSH 212
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1304-1519 |
1.46e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 58.20 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1304 NLTLHvqGGEKVGIVGRTGAGKSSMTLCLFRILeAAEGEI----FIDG---LNVAHIGLHDLRS-QLTIIPQDPIlfsgt 1375
Cdd:PRK09473 36 NFSLR--AGETLGIVGESGSGKSQTAFALMGLL-AANGRIggsaTFNGreiLNLPEKELNKLRAeQISMIFQDPM----- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1376 lrMNLDPFGRYSDEdIWRTLEL----SHLSAFVSSQPTgLD-FQCSEGGDNL-------SVGQRQLVCLARALLRKSRVL 1443
Cdd:PRK09473 108 --TSLNPYMRVGEQ-LMEVLMLhkgmSKAEAFEESVRM-LDaVKMPEARKRMkmyphefSGGMRQRVMIAMALLCRPKLL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937891448 1444 VLDEATAAIDLEtddlIQGTIRTQFEDctvltIAHRLNT--IMdynrvLVLDKGVVAEFDSPVNLIAAGGIF-YGMAKD 1519
Cdd:PRK09473 184 IADEPTTALDVT----VQAQIMTLLNE-----LKREFNTaiIM-----ITHDLGVVAGICDKVLVMYAGRTMeYGNARD 248
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
649-788 |
1.84e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.03 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 649 QIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSVAYVPQQAWIQNCTLQENVLFGqpMNPKRYQQALEtcal 728
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQYISPDYDGTVEEFLRS--ANTDDFGSSYY---- 435
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937891448 729 ladldvlpggdQTEIGEK-GI---------NLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDS----HVAKHI 788
Cdd:COG1245 436 -----------KTEIIKPlGLeklldknvkDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVAKAI 498
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
643-840 |
1.86e-08 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 58.17 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGemekLE----GAVSVKG----------------SVAYVPQQ-AWIQN 701
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL----LErptsGSVLVDGvdltalserelraarrKIGMIFQHfNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 702 CTLQENVLFgqPM------NPKRYQQALETCAL--LADL-DVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFL 772
Cdd:COG1135 97 RTVAENVAL--PLeiagvpKAEIRKRVAELLELvgLSDKaDAYPS-----------QLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 773 LDDPLSAVDshvakhifdqvigPE---GVLA---------GKTRVLVTHgisflpQTDFI--I-----VLADGQITEMGH 833
Cdd:COG1135 164 CDEATSALD-------------PEttrSILDllkdinrelGLTIVLITH------EMDVVrrIcdrvaVLENGRIVEQGP 224
|
....*..
gi 1937891448 834 YSELLQH 840
Cdd:COG1135 225 VLDVFAN 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1302-1483 |
1.93e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 58.68 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1302 LKNLTLHVQGGEKVGIVGRTGAGKSSmtlcLFRILEAA------EGEIFIDG--LNVAHI------GLHDLRSQLTIIPQ 1367
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKST----LMKILSGVyphgtwDGEIYWSGspLKASNIrdteraGIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1368 DPIL---FSG---TL---RMNLDPFGRYSdEDIWRTLELShlsAFVSSQPTGldfqcseggdNLSVGQRQLVCLARALLR 1438
Cdd:TIGR02633 93 LSVAeniFLGneiTLpggRMAYNAMYLRA-KNLLRELQLD---ADNVTRPVG----------DYGGGQQQLVEIAKALNK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1937891448 1439 KSRVLVLDEATAAI-DLETDDLIQGTIRTQFEDCTVLTIAHRLNTI 1483
Cdd:TIGR02633 159 QARLLILDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEV 204
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1288-1509 |
2.57e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.56 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1288 RNYSVRYRPGLEL--VLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAA-----EGEIFIDGLNVAHIGLHDLR- 1359
Cdd:PRK15134 9 ENLSVAFRQQQTVrtVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTLRg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1360 ---SQLTIIPQDPILfsgtlrmNLDPFG-------------RYSDEDIWRTLELSHLSAFVSSQPTGL--DFQcseggDN 1421
Cdd:PRK15134 89 vrgNKIAMIFQEPMV-------SLNPLHtlekqlyevlslhRGMRREAARGEILNCLDRVGIRQAAKRltDYP-----HQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1422 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIR--TQFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVA 1498
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKLaDRVAVMQNGRCV 236
|
250
....*....|.
gi 1937891448 1499 EFDSPVNLIAA 1509
Cdd:PRK15134 237 EQNRAATLFSA 247
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
653-810 |
2.88e-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: 55.44 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 653 GALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSVAYVPQQAWIQNC-------------TLQENVLFGQPMNpkRY 719
Cdd:TIGR01189 26 GEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENIlylghlpglkpelSALENLHFWAAIH--GG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 720 QQ-----ALETCALlADLDVLPGGdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD-SHVAK--HIFDQ 791
Cdd:TIGR01189 104 AQrtiedALAAVGL-TGFEDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPTTALDkAGVALlaGLLRA 172
|
170
....*....|....*....
gi 1937891448 792 VIGPEGVLagktrVLVTHG 810
Cdd:TIGR01189 173 HLARGGIV-----LLTTHQ 186
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
1008-1213 |
2.90e-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: 57.11 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1008 LGVYATLGILQGLLVMLSAFTMVVGAIQAARLLHTALL--------HNQiRAPQSFFDTTPSGRILNRFSKDIYVIDEVL 1079
Cdd:cd18546 35 LGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYdlrlrvfaHLQ-RLSLDFHERETSGRIMTRMTSDIDALSELL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1080 APTILMLFNSFYTSISTIVVIVASTP---LFCVVVLPLAVfygFVQRFYVATSRQLKRL--ESVSRspIFSHFSETVTGT 1154
Cdd:cd18546 114 QTGLVQLVVSLLTLVGIAVVLLVLDPrlaLVALAALPPLA---LATRWFRRRSSRAYRRarERIAA--VNADLQETLAGI 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 1155 SVIRAYGR----VQDFKVLSDAKVDSNQKTTYpYIAsnrWLGVHVEFVGNcvvLFSALFAVIG 1213
Cdd:cd18546 189 RVVQAFRRerrnAERFAELSDDYRDARLRAQR-LVA---IYFPGVELLGN---LATAAVLLVG 244
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1301-1453 |
2.93e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 56.44 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1301 VLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHD-LRSQLTIIPQDPILFS------ 1373
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFRrlsvyd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1374 ---GTLRMNLDPFGRYSDEDIWRTLELSHLSAFVSSQptgldfqcsegGDNLSVGQRQLVCLARALLRKSRVLVLDEATA 1450
Cdd:PRK10895 98 nlmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
...
gi 1937891448 1451 AID 1453
Cdd:PRK10895 167 GVD 169
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
646-809 |
3.74e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 56.74 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 646 LNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS------------VAYVPQQAWIQ-NCTLQENVL-FG 711
Cdd:PRK13537 26 LSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarharqrVGVVPQFDNLDpDFTVRENLLvFG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 712 qpmnpkRY-----QQALETCALLADLDVLPGGDQTEIGEkginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHvAK 786
Cdd:PRK13537 106 ------RYfglsaAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ-AR 174
|
170 180
....*....|....*....|....
gi 1937891448 787 HIFDQVIgpEGVLA-GKTRVLVTH 809
Cdd:PRK13537 175 HLMWERL--RSLLArGKTILLTTH 196
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1301-1503 |
4.14e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 57.02 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1301 VLKNLTLHVQGGEKVGIVGRTGAGKSSmtlcLFRILEAAE----GEIFIDGLNVAHIGLHD-----------LRSQLTII 1365
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTT----LLRIIAGLEhqtsGHIRFHGTDVSRLHARDrkvgfvfqhyaLFRHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1366 pqDPILFSGT-LRMNLDPFGRYSDEDIWRTLE---LSHLSAFVSSQptgldfqcseggdnLSVGQRQLVCLARALLRKSR 1441
Cdd:PRK10851 93 --DNIAFGLTvLPRRERPNAAAIKAKVTQLLEmvqLAHLADRYPAQ--------------LSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937891448 1442 VLVLDEATAAIDLETDDLIQGTIRTQFEDC--TVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSP 1503
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEAMEVaDRVVVMSQGNIEQAGTP 221
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1287-1509 |
4.52e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 55.95 E-value: 4.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1287 FRNYSVRYR-PGLELvLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTII 1365
Cdd:PRK10575 12 FALRNVSFRvPGRTL-LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1366 PQD-PILFSGTLR----MNLDPF----GRYSDEDIWRTLELSHLsafvssqpTGLDFQCSEGGDNLSVGQRQLVCLARAL 1436
Cdd:PRK10575 91 PQQlPAAEGMTVRelvaIGRYPWhgalGRFGAADREKVEEAISL--------VGLKPLAHRLVDSLSGGERQRAWIAMLV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937891448 1437 LRKSRVLVLDEATAAIDL----ETDDLIQGTirTQFEDCTVLTIAHRLNTIMDYNRVLVLDKG--VVAEfDSPVNLIAA 1509
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDIahqvDVLALVHRL--SQERGLTVIAVLHDINMAARYCDYLVALRGgeMIAQ-GTPAELMRG 238
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1301-1507 |
4.89e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.99 E-value: 4.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1301 VLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAA--------EGEIFIDGLNVAHIG---LHDLRSQLTIIPQDP 1369
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDaprLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1370 ILFSGTLRMNLdpfGRY-----------SDEDI-WRTLELSHLSAFVSSQPTgldfqcseggdNLSVGQRQLVCLARAL- 1436
Cdd:PRK13547 96 FAFSAREIVLL---GRYpharragalthRDGEIaWQALALAGATALVGRDVT-----------TLSGGELARVQFARVLa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1437 --------LRKSRVLVLDEATAAIDLETDDLIQGTIRTQFED--CTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSPVN 1505
Cdd:PRK13547 162 qlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwnLGVLAIVHDPNLAARHaDRIAMLADGAIVAHGAPAD 241
|
..
gi 1937891448 1506 LI 1507
Cdd:PRK13547 242 VL 243
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
643-828 |
5.46e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 55.86 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-SVAYVPQQ---AWI----QN-----C---TLQE 706
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkDVTKLPEYkraKYIgrvfQDpmmgtApsmTIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 707 NVL----------FGQPMNPKRYQQALEtcaLLADLDV-LPGGDQTEIGekgiNLSGGQRQRVSLARAVYSDANIFLLDD 775
Cdd:COG1101 102 NLAlayrrgkrrgLRRGLTKKRRELFRE---LLATLGLgLENRLDTKVG----LLSGGQRQALSLLMATLTKPKLLLLDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1937891448 776 PLSAVDSHVAKHIF---DQVIGPEGVlagkTRVLVTHGISF-LPQTDFIIVLADGQI 828
Cdd:COG1101 175 HTAALDPKTAALVLeltEKIVEENNL----TTLMVTHNMEQaLDYGNRLIMMHEGRI 227
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1009-1256 |
5.53e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 56.33 E-value: 5.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1009 GVYATLGILQGLLVMLsaFTMVVGAIQA--ARLLHTALLHNQIRAPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTIL-M 1085
Cdd:cd18540 46 LLYLGLILIQALSVFL--FIRLAGKIEMgvSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVdL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1086 LFNSFYTSISTIVVIVASTPLFCVVVL---PLAVFYGFVQRFYVATSRQLKRLESVsrspIFSHFSETVTGTSVIRAYGR 1162
Cdd:cd18540 124 VWGITYMIGILIVMLILNWKLALIVLAvvpVLAVVSIYFQKKILKAYRKVRKINSR----ITGAFNEGITGAKTTKTLVR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1163 VQdfKVLSDAKvdsnQKTTYPYIASNRwlgvhvefvgncVVLFSALF------------AVI----GRNSLNPGL-VG-L 1224
Cdd:cd18540 200 EE--KNLREFK----ELTEEMRRASVR------------AARLSALFlpivlflgsiatALVlwygGILVLAGAItIGtL 261
|
250 260 270
....*....|....*....|....*....|....
gi 1937891448 1225 SV--SYALQVTLSLNWMIRTLSDLESNIIAVERV 1256
Cdd:cd18540 262 VAfiSYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1288-1460 |
5.86e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 55.21 E-value: 5.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1288 RNYSVRYRPG--LELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDG--LN-VAHIGLHDLRSQ- 1361
Cdd:PRK11629 9 DNLCKRYQEGsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpMSkLSSAAKAELRNQk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1362 LTIIPQDPIL---FSG--TLRMNLDPFGRYSDEDIWRTLELshLSAfvssqpTGLDFQCSEGGDNLSVGQRQLVCLARAL 1436
Cdd:PRK11629 89 LGFIYQFHHLlpdFTAleNVAMPLLIGKKKPAEINSRALEM--LAA------VGLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180
....*....|....*....|....
gi 1937891448 1437 LRKSRVLVLDEATAAIDLETDDLI 1460
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSI 184
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
643-792 |
6.48e-08 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 53.70 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSAL-------LGEMEKLEGAvsvkgSVAYVPQQAWIQNCTLQENVLFgqpmn 715
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALaglwpwgSGRIGMPEGE-----DLLFLPQRPYLPLGTLREQLIY----- 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937891448 716 pkryqqaletcalladldvlPGGDqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQV 792
Cdd:cd03223 87 --------------------PWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL 134
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
647-851 |
6.73e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 56.58 E-value: 6.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 647 NIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-----------------SVAYVPQQ-AWIQNCTLQENV 708
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrkKIAMVFQSfALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 709 LFGQPMN----PKRYQQALETCALLAdLDVLPGGDQTEigekginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHV 784
Cdd:PRK10070 128 AFGMELAginaEERREKALDALRQVG-LENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937891448 785 AKHIFDQVIGPEGVlAGKTRVLVTHGI-SFLPQTDFIIVLADGQITEMGHYSELLQHDGSfaNFLRNY 851
Cdd:PRK10070 200 RTEMQDELVKLQAK-HQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAN--DYVRTF 264
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1302-1500 |
8.39e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.88 E-value: 8.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1302 LKNLTLHVQGGEKVGIVGRTGAGKSSmtlcLFRIL---------------------------EAAEGEIF---IDGlnVA 1351
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKST----LMKILngevllddgriiyeqdlivarlqqdppRNVEGTVYdfvAEG--IE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1352 HIG-----LHDLRSQLTIIPQDPILFS-GTLRMNLDPFGRYSDED-IWRTLELSHLSAfvssqptglDFQCSEggdnLSV 1424
Cdd:PRK11147 93 EQAeylkrYHDISHLVETDPSEKNLNElAKLQEQLDHHNLWQLENrINEVLAQLGLDP---------DAALSS----LSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1425 GQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTqFEDCTVLtIAH------RLNTimdynRVLVLDKGVVA 1498
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT-FQGSIIF-ISHdrsfirNMAT-----RIVDLDRGKLV 232
|
..
gi 1937891448 1499 EF 1500
Cdd:PRK11147 233 SY 234
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1298-1508 |
9.29e-08 |
|
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: 55.88 E-value: 9.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1298 LELVLKNLTLHVQ----GGEKVGIVGRTGAGKSSmtlcLFRI---LE-AAEGEIFIDG---------LNVA----HIGLh 1356
Cdd:COG4148 7 FRLRRGGFTLDVDftlpGRGVTALFGPSGSGKTT----LLRAiagLErPDSGRIRLGGevlqdsargIFLPphrrRIGY- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1357 dlrsqltiIPQDPILFSG-TLRMNLDpFG---------RYSDEDIWRTLELSHLsafVSSQPtgldfqcseggDNLSVGQ 1426
Cdd:COG4148 82 --------VFQEARLFPHlSVRGNLL-YGrkrapraerRISFDEVVELLGIGHL---LDRRP-----------ATLSGGE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1427 RQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQ---GTIRTQFeDCTVLTIAHRLNTIM---DynRVLVLDKGVVAEF 1500
Cdd:COG4148 139 RQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILpylERLRDEL-DIPILYVSHSLDEVArlaD--HVVLLEQGRVVAS 215
|
....*...
gi 1937891448 1501 DSPVNLIA 1508
Cdd:COG4148 216 GPLAEVLS 223
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
643-830 |
1.08e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 55.08 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG----------------SVAYVPQQAwIQNCTLQE 706
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGeplaklnraqrkafrrDIQMVFQDS-ISAVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 707 NV--LFGQPM----NPKRYQQALETCALL-------ADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLL 773
Cdd:PRK10419 107 TVreIIREPLrhllSLDKAERLARASEMLravdlddSVLDKRPP-----------QLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 774 DDPLSAVDSHVAKHIFDQVIGPEGVLaGKTRVLVTHGISFLPQtdF---IIVLADGQITE 830
Cdd:PRK10419 176 DEAVSNLDLVLQAGVIRLLKKLQQQF-GTACLFITHDLRLVER--FcqrVMVMDNGQIVE 232
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
646-776 |
1.17e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.28 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 646 LNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSV--AYVPQQ--AWIQNCTLQENVLFGQ--------P 713
Cdd:PRK11819 343 LSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVklAYVDQSrdALDPNKTVWEEISGGLdiikvgnrE 422
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937891448 714 MNPKRYqqaletCALLAdldvLPGGDQteigEKGI-NLSGGQRQRVSLARAVYSDANIFLLDDP 776
Cdd:PRK11819 423 IPSRAY------VGRFN----FKGGDQ----QKKVgVLSGGERNRLHLAKTLKQGGNVLLLDEP 472
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1302-1499 |
1.32e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.40 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1302 LKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGL-----NVAHIGLHDLR---------SQLTIIPQ 1367
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrSRQVIELSEQSaaqmrhvrgADMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1368 DPIlfsgTLRMNLDPFGRYSDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGD-------NLSVGQRQLVCLARALLRKS 1440
Cdd:PRK10261 112 EPM----TSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTilsryphQLSGGMRQRVMIAMALSCRP 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 1441 RVLVLDEATAAIDLETDDLIQGTIRTQFEDCT--VLTIAHRLNTIMDY-NRVLVLDKGVVAE 1499
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIaDRVLVMYQGEAVE 249
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
656-830 |
1.35e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.01 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 656 VAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-----------------SVAYVPQQ-AWIQNCTLQENV-----LFGQ 712
Cdd:PRK10584 39 IALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhqmdeearaklrakHVGFVFQSfMLIPTLNALENVelpalLRGE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 713 PMNPKRYQQA--LETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFD 790
Cdd:PRK10584 119 SSRQSRNGAKalLEQLGLGKRLDHLPA-----------QLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIAD 187
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1937891448 791 QVIGPEGVLAgKTRVLVTHGISFLPQTDFIIVLADGQITE 830
Cdd:PRK10584 188 LLFSLNREHG-TTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1285-1508 |
1.44e-07 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 55.96 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYRpGLElVLKNLTLHVQGGEKVGIVGRTGAGKSSMtLCLFRIL---EAAEGEIF----------------- 1344
Cdd:TIGR03269 1 IEVKNLTKKFD-GKE-VLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMdqyEPTSGRIIyhvalcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1345 ----------------IDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRM------NLDPFGRYSDEDIWRTLELSHLsa 1402
Cdd:TIGR03269 78 vgepcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTVldnvleALEEIGYEGKEAVGRAVDLIEM-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1403 fvssqpTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIR--TQFEDCTVLTIAHRL 1480
Cdd:TIGR03269 156 ------VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEeaVKASGISMVLTSHWP 229
|
250 260
....*....|....*....|....*....
gi 1937891448 1481 NTIMDY-NRVLVLDKGVVAEFDSPVNLIA 1508
Cdd:TIGR03269 230 EVIEDLsDKAIWLENGEIKEEGTPDEVVA 258
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
643-841 |
1.61e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 54.84 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-----------------SVAYV---PQQAWIQNc 702
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkKVSLVfqfPEAQLFEN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 703 TLQENVLFGqPMNPKRYQQALETCALLADLDVlpgGDQTEIGEKG-INLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD 781
Cdd:PRK13641 102 TVLKDVEFG-PKNFGFSEDEAKEKALKWLKKV---GLSEDLISKSpFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937891448 782 SHVAKHIFDqvIGPEGVLAGKTRVLVTHGISFLPQ-TDFIIVLadgqitEMGHyseLLQHD 841
Cdd:PRK13641 178 PEGRKEMMQ--LFKDYQKAGHTVILVTHNMDDVAEyADDVLVL------EHGK---LIKHA 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
643-837 |
1.73e-07 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 55.58 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLG--EMEKLEGAVSVKgsVAYVPQQAWI-------QNCTLQENVL---- 709
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYH--VALCEKCGYVerpskvgEPCPVCGGTLepee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 710 --FGQPMNPKRY----QQAL---ETCALLADLDVLPGGDQT--EIGEKGI------------------------NLSGGQ 754
Cdd:TIGR03269 94 vdFWNLSDKLRRrirkRIAImlqRTFALYGDDTVLDNVLEAleEIGYEGKeavgravdliemvqlshrithiarDLSGGE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 755 RQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIgpEGVLAGKTRVLVThgiSFLPQ-----TDFIIVLADGQIT 829
Cdd:TIGR03269 174 KQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALE--EAVKASGISMVLT---SHWPEviedlSDKAIWLENGEIK 248
|
....*...
gi 1937891448 830 EMGHYSEL 837
Cdd:TIGR03269 249 EEGTPDEV 256
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1284-1499 |
1.84e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 54.42 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYRPGLElVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLT 1363
Cdd:PRK13652 3 LIETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1364 IIPQDP--ILFSGTLRMNLdPFG-----------RYSDEDIWRTLELSHLSAFVSSqptgldfqcseggdNLSVGQRQLV 1430
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDI-AFGpinlgldeetvAHRVSSALHMLGLEELRDRVPH--------------HLSGGEKKRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937891448 1431 CLARALLRKSRVLVLDEATAAIDLE-TDDLIQGTIRTQFE-DCTVLTIAHRLNTI---MDYnrVLVLDKG-VVAE 1499
Cdd:PRK13652 147 AIAGVIAMEPQVLVLDEPTAGLDPQgVKELIDFLNDLPETyGMTVIFSTHQLDLVpemADY--IYVMDKGrIVAY 219
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
643-781 |
1.98e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.96 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAV--SVKGSVAYVPQQAWIqNCTLqenvlfgqPMNPKRYQ 720
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIkrNGKLRIGYVPQKLYL-DTTL--------PLTVNRFL 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937891448 721 QALETcalLADLDVLPGGDQTEIG-------EKginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD 781
Cdd:PRK09544 91 RLRPG---TKKEDILPALKRVQAGhlidapmQK---LSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1282-1453 |
2.03e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 55.89 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1282 SGVVEFRNYSVRYRPGLEL--VLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDL- 1358
Cdd:PRK10535 2 TALLELKDIRRSYPSGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1359 ---RSQLTIIPQDPILFSG-TLRMNLDPFGRYS----DEDIWRTLELSH---LSAFVSSQPTgldfqcseggdNLSVGQR 1427
Cdd:PRK10535 82 qlrREHFGFIFQRYHLLSHlTAAQNVEVPAVYAglerKQRLLRAQELLQrlgLEDRVEYQPS-----------QLSGGQQ 150
|
170 180
....*....|....*....|....*.
gi 1937891448 1428 QLVCLARALLRKSRVLVLDEATAAID 1453
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALD 176
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
979-1447 |
2.03e-07 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 55.57 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 979 AVAIGANVWLSAWTNDVEEHGQQNNTSVrLGVYAtlgilqgLLVMLSAFTMVVGAIQAARLLHTALLH------NQIR-A 1051
Cdd:COG4615 23 LLSGLANAGLIALINQALNATGAALARL-LLLFA-------GLLVLLLLSRLASQLLLTRLGQHAVARlrlrlsRRILaA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1052 PQSFFDTTPSGRILNRFSKDIYVIDE--VLAPTILmlfnsfytsISTIVVIVA-------STPLFCVVVLpLAVFYGFVQ 1122
Cdd:COG4615 95 PLERLERIGAARLLAALTEDVRTISQafVRLPELL---------QSVALVLGClaylawlSPPLFLLTLV-LLGLGVAGY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1123 RFYVATSRQLKRLESVSRSPIFSHFSETVTGTSVI------RAYGRVQDFKVLSDAKVDSNQKTTYPYIASNRWlgvhve 1196
Cdd:COG4615 165 RLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELklnrrrRRAFFDEDLQPTAERYRDLRIRADTIFALANNW------ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1197 fvGNCVVLF---SALFAVIGRNSLNPGLVGLSVSYALQVTLSLNWMIRTLSDLESNIIAVERVKEYSKTETEAPWVLESN 1273
Cdd:COG4615 239 --GNLLFFAligLILFLLPALGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKIEELELALAAAEPAAADA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1274 RAPEGWPRSGVVEFRNYSVRYRPGLE---LVLKNLTLHVQGGEKVGIVGRTGAGKS--SMTLC-LFRileAAEGEIFIDG 1347
Cdd:COG4615 317 AAPPAPADFQTLELRGVTYRYPGEDGdegFTLGPIDLTIRRGELVFIVGGNGSGKStlAKLLTgLYR---PESGEILLDG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1348 LNVAHIGLHDLRSQLTIIPQDPILFSGtlrmNLDPFGRYSDEDI--W-RTLELSHLSAFvssqptgldfqcsEGGD---- 1420
Cdd:COG4615 394 QPVTADNREAYRQLFSAVFSDFHLFDR----LLGLDGEADPARAreLlERLELDHKVSV-------------EDGRfstt 456
|
490 500
....*....|....*....|....*..
gi 1937891448 1421 NLSVGQRQLVCLARALLRKSRVLVLDE 1447
Cdd:COG4615 457 DLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1284-1456 |
2.32e-07 |
|
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: 53.59 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRY-RPGLEL-VLKNLTLHVQGGEKVGIVGRTGAGKSSmtlcLFRI---LEAA-EGEIFIDGLNVAHI---G 1354
Cdd:COG4181 8 IIELRGLTKTVgTGAGELtILKGISLEVEAGESVAIVGASGSGKST----LLGLlagLDRPtSGTVRLAGQDLFALdedA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1355 LHDLRSQLT-IIPQD-PILFSGT----------LRMNLDPFGRYSDEdiwrtLE---LSHLSAFVSSQptgldfqcsegg 1419
Cdd:COG4181 84 RARLRARHVgFVFQSfQLLPTLTalenvmlpleLAGRRDARARARAL-----LErvgLGHRLDHYPAQ------------ 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 1937891448 1420 dnLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLET 1456
Cdd:COG4181 147 --LSGGEQQRVALARAFATEPAILFADEPTGNLDAAT 181
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
624-838 |
2.32e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 53.94 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 624 RAITIHNGTFSWSKDLPPT-LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSvAYVPQQAW---- 698
Cdd:PRK13642 3 KILEVENLVFKYEKESDVNqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-LLTAENVWnlrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 699 -----IQN-------CTLQENVLFGQ-----PMNP--KRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVS 759
Cdd:PRK13642 82 kigmvFQNpdnqfvgATVEDDVAFGMenqgiPREEmiKRVDEALLAVNMLDFKTREPA-----------RLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937891448 760 LARAVYSDANIFLLDDPLSAVDSHVAKHIFdQVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQITEMGHYSELL 838
Cdd:PRK13642 151 VAGIIALRPEIIILDESTSMLDPTGRQEIM-RVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1302-1495 |
2.39e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.18 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1302 LKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGlHDLRSQL--TIIPQD-PILFSGTLRM 1378
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQLgiGIIYQElSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1379 NLdPFGRYSDEDI-------WRTLELShlsAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAA 1451
Cdd:PRK09700 100 NL-YIGRHLTKKVcgvniidWREMRVR---AAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1937891448 1452 I-DLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDY-NRVLVLDKG 1495
Cdd:PRK09700 176 LtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRIcDRYTVMKDG 221
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
626-847 |
2.41e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 54.02 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 626 ITIHNGTFSWSKDLP---PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVK--------------- 687
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDditithktkdkyirp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 688 -----GSVAYVPQQAWIQNcTLQENVLFGqpmnPKRYQQALETCA-----LLADLdvlpGGDQTEIGEKGINLSGGQRQR 757
Cdd:PRK13646 83 vrkriGMVFQFPESQLFED-TVEREIIFG----PKNFKMNLDEVKnyahrLLMDL----GFSRDVMSQSPFQMSGGQMRK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 758 VSLARAVYSDANIFLLDDPLSAVDSHvAKHIFDQVIGPEGVLAGKTRVLVTHGISFLPQ-TDFIIVLADGQITEMGHYSE 836
Cdd:PRK13646 154 IAIVSILAMNPDIIVLDEPTAGLDPQ-SKRQVMRLLKSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKE 232
|
250
....*....|.
gi 1937891448 837 LLQHDGSFANF 847
Cdd:PRK13646 233 LFKDKKKLADW 243
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1296-1483 |
2.88e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.12 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1296 PGLElVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVA-HIGLHDLRSQLTIIPQDPILFSG 1374
Cdd:PRK10982 9 PGVK-ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1375 TLRMNLDPFGRYSDEDIWrtleLSHLSAFVSSQPT----GLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATA 1450
Cdd:PRK10982 88 RSVMDNMWLGRYPTKGMF----VDQDKMYRDTKAIfdelDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190
....*....|....*....|....*....|....
gi 1937891448 1451 AI-DLETDDLIQGTIRTQFEDCTVLTIAHRLNTI 1483
Cdd:PRK10982 164 SLtEKEVNHLFTIIRKLKERGCGIVYISHKMEEI 197
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
650-856 |
3.08e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 52.19 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 650 IPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-SVAYVPQQawiqnctlqenvlfgqpmnpkryqqaletcal 728
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQY-------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 729 ladldvlpggdqteigekgINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDS----HVAKhifdqVIGPEGVLAGKTR 804
Cdd:cd03222 70 -------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrlNAAR-----AIRRLSEEGKKTA 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 805 VLVTHGISFLPQTDFIIVLADGQITEMGHYSELLQHDGSFANFLRNYAPDEN 856
Cdd:cd03222 126 LVVEHDLAVLDYLSDRIHVFEGEPGVYGIASQPKGTREGINRFLRGYLITFR 177
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
641-781 |
3.16e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 54.46 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGemekLE----GAVSVKGSV-----------AYVpqqawIQN---- 701
Cdd:PRK11650 18 QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAG----LEritsGEIWIGGRVvnelepadrdiAMV-----FQNyaly 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 702 --CTLQENVLFG---QPMnPK--RYQQALETCALLadldvlpggdqtEIGE----KGINLSGGQRQRVSLARAVYSDANI 770
Cdd:PRK11650 89 phMSVRENMAYGlkiRGM-PKaeIEERVAEAARIL------------ELEPlldrKPRELSGGQRQRVAMGRAIVREPAV 155
|
170
....*....|.
gi 1937891448 771 FLLDDPLSAVD 781
Cdd:PRK11650 156 FLFDEPLSNLD 166
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1306-1493 |
3.91e-07 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 53.18 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1306 TLHVQGG-----EKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHiglhdlRSQlTIIPQDP-----ILFSGT 1375
Cdd:cd03237 14 TLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY------KPQ-YIKADYEgtvrdLLSSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1376 LRMNLDPfgrYSDEDIWRTLELSHLsafvssqptgLDFQCSEggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLE 1455
Cdd:cd03237 87 KDFYTHP---YFKTEIAKPLQIEQI----------LDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1937891448 1456 TDDLIQGTIRTQFE--DCTVLTIAHrlNTIM-DY--NRVLVLD 1493
Cdd:cd03237 150 QRLMASKVIRRFAEnnEKTAFVVEH--DIIMiDYlaDRLIVFE 190
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
646-809 |
4.16e-07 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 52.37 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 646 LNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG------------SVAYVPQQAWIQN-CTLQENV---- 708
Cdd:cd03265 19 VSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDLSVDDeLTGWENLyiha 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 709 -LFGQPmNPKRYQQALEtcaLLADLDVLPGGDqteigEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKH 787
Cdd:cd03265 99 rLYGVP-GAERRERIDE---LLDFVGLLEAAD-----RLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAH 169
|
170 180
....*....|....*....|....
gi 1937891448 788 IFDQVigpEGVLA--GKTRVLVTH 809
Cdd:cd03265 170 VWEYI---EKLKEefGMTILLTTH 190
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1271-1454 |
4.22e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.48 E-value: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1271 ESNRAPEGWPrsgVVEFRNYSVRY--RPGL------EL-VLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEG 1341
Cdd:PRK10261 303 EQDTVVDGEP---ILQVRNLVTRFplRSGLlnrvtrEVhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGG 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1342 EIFIDGLNVAHIG---LHDLRSQLTIIPQDPIlfsgtlrMNLDPFGR--YSDEDIWRTLELSHLSAFVSS-----QPTGL 1411
Cdd:PRK10261 380 EIIFNGQRIDTLSpgkLQALRRDIQFIFQDPY-------ASLDPRQTvgDSIMEPLRVHGLLPGKAAAARvawllERVGL 452
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1937891448 1412 DFQCS-EGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDL 1454
Cdd:PRK10261 453 LPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1285-1478 |
4.42e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 52.92 E-value: 4.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILE-----AAEGEIFIDGLNVAHIGLH--D 1357
Cdd:PRK14267 5 IETVNLRVYY--GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDpiE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1358 LRSQLTIIPQDPILFS----------GTLRMNLDPFGRYSDEDIWRTLELSHLSAFVSSQptgldfqCSEGGDNLSVGQR 1427
Cdd:PRK14267 83 VRREVGMVFQYPNPFPhltiydnvaiGVKLNGLVKSKKELDERVEWALKKAALWDEVKDR-------LNDYPSNLSGGQR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1937891448 1428 QLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAH 1478
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
643-878 |
5.37e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.13 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSVAYVPQQAWIQN-CTLQENV-LFGQPMNPKRyQ 720
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGqLTGIENIeLKGLMMGLTK-E 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 721 QALETCALLADLdvlpggdqTEIGeKGIN-----LSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVigP 795
Cdd:PRK13545 119 KIKEIIPEIIEF--------ADIG-KFIYqpvktYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKM--N 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 796 EGVLAGKTRVLVTHGI----SFLPQTdfiIVLADGQITEMGHYSELLQHdgsFANFLRNYapdeNQEANEGVLQHANEEV 871
Cdd:PRK13545 188 EFKEQGKTIFFISHSLsqvkSFCTKA---LWLHYGQVKEYGDIKEVVDH---YDEFLKKY----NQMSVEERKDFREEQI 257
|
....*..
gi 1937891448 872 LLLEDTL 878
Cdd:PRK13545 258 SQFQHGL 264
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1284-1506 |
5.39e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 53.20 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYRPGLELV---LKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIG----LH 1356
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFAsraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1357 DLRSQLTIIPQDP--ILFSGTLRMNLdpfgRYSDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGD-NLSVGQRQLVCLA 1433
Cdd:PRK13643 81 PVRKKVGVVFQFPesQLFEETVLKDV----AFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPfELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937891448 1434 RALLRKSRVLVLDEATAAID----LETDDLIQGTIRTqfeDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAEFDSPVNL 1506
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDpkarIEMMQLFESIHQS---GQTVVLVTHLMDDVADYaDYVYLLEKGHIISCGTPSDV 231
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1286-1495 |
5.51e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 52.68 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1286 EFRNYSVRYrPGLeLVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHD-------- 1357
Cdd:PRK11300 7 SVSGLMMRF-GGL-LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiarmgvvr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1358 ------LRSQLTII-----PQDPILFSGTLR--MNLDPFGRYSDEDIWRT---LELSHLSAFvSSQPTGldfqcseggdN 1421
Cdd:PRK11300 85 tfqhvrLFREMTVIenllvAQHQQLKTGLFSglLKTPAFRRAESEALDRAatwLERVGLLEH-ANRQAG----------N 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937891448 1422 LSVGQRQLVCLARALLRKSRVLVLDEATAAID-LETDDLIQ--GTIRTQFeDCTVLTIAHRLNTIMDY-NRVLVLDKG 1495
Cdd:PRK11300 154 LAYGQQRRLEIARCMVTQPEILMLDEPAAGLNpKETKELDEliAELRNEH-NVTVLLIEHDMKLVMGIsDRIYVVNQG 230
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
625-840 |
5.75e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 52.82 E-value: 5.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 625 AITIHNGTFSWSKDLP---PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAV----------------- 684
Cdd:PRK13649 2 GINLQNVSYTYQAGTPfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVrvddtlitstsknkdik 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 685 SVKGSVAYVPQQAWIQ--NCTLQENVLFGqPMNPKRYQQALETCAL--LAdldvLPGGDQTEIGEKGINLSGGQRQRVSL 760
Cdd:PRK13649 82 QIRKKVGLVFQFPESQlfEETVLKDVAFG-PQNFGVSQEEAEALARekLA----LVGISESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 761 ARAVYSDANIFLLDDPLSAVDSHVAKHIFDqvIGPEGVLAGKTRVLVTHGISFLPQ-TDFIIVLADGQITEMGHYSELLQ 839
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMT--LFKKLHQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDIFQ 234
|
.
gi 1937891448 840 H 840
Cdd:PRK13649 235 D 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
641-776 |
5.81e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.88 E-value: 5.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS--------------VAYVPQ----QAWIQNC 702
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditglsprerrrlgVAYIPEdrlgRGLVPDM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 703 TLQENVLFGQPMNPK-------RYQQALETCA-LLADLDVLPGGDQTEIGekgiNLSGGQRQRVSLARAVYSDANIFLLD 774
Cdd:COG3845 352 SVAENLILGRYRRPPfsrggflDRKAIRAFAEeLIEEFDVRTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAA 427
|
..
gi 1937891448 775 DP 776
Cdd:COG3845 428 QP 429
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
646-781 |
5.93e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 53.34 E-value: 5.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 646 LNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSV-----------------AYVPQQAWI-QNCTLQEN 707
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgiclppekrriGYVFQDARLfPHYKVRGN 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937891448 708 VLFGqpMNPKRYQQALETCALLAD---LDVLPggdqteigekgINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD 781
Cdd:PRK11144 97 LRYG--MAKSMVAQFDKIVALLGIeplLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
641-828 |
6.96e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.90 E-value: 6.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS--------------VAYVPQQAWI-QNCTLQ 705
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQEPLLfPNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 706 ENVLFGQPMNPKRYQQALETCALLA---DLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDS 782
Cdd:PRK15439 105 ENILFGLPKRQASMQKMKQLLAALGcqlDLDSSAG-----------SLEVADRQIVEILRGLMRDSRILILDEPTASLTP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 783 HVAKHIFDQVigpegvlagktRVLVT--HGISF----LPQ----TDFIIVLADGQI 828
Cdd:PRK15439 174 AETERLFSRI-----------RELLAqgVGIVFishkLPEirqlADRISVMRDGTI 218
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
643-828 |
7.23e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.02 E-value: 7.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSV-KG-SVAYVPQQAwIQNCTLQENVLfgQPMN---PK 717
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGiKLGYFAQHQ-LEFLRADESPL--QHLArlaPQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 718 RYQQALEtcalladlDVLPG----GDQ-TEIGEKginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQV 792
Cdd:PRK10636 405 ELEQKLR--------DYLGGfgfqGDKvTEETRR---FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
170 180 190
....*....|....*....|....*....|....*..
gi 1937891448 793 IGPEGVLagktrVLVTHGISFL-PQTDFIIVLADGQI 828
Cdd:PRK10636 474 IDFEGAL-----VVVSHDRHLLrSTTDDLYLVHDGKV 505
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
643-841 |
7.53e-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: 53.53 E-value: 7.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGeMEKLEGAVSVKG-SVAYVPQQAW------IQnctlqenVLFGQP-- 713
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGqDLDGLSRRALrplrrrMQ-------VVFQDPfg 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 714 -MNP-------------------------KRYQQALETCALLAD-LDVLPggdqTEigekginLSGGQRQRVSLARAVYS 766
Cdd:COG4172 374 sLSPrmtvgqiiaeglrvhgpglsaaerrARVAEALEEVGLDPAaRHRYP----HE-------FSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 767 DANIFLLDDPLSAVDSHVAKHIFDqvigpegVLAGKTRvlvTHGISFLpqtdFI--------------IVLADGQITEMG 832
Cdd:COG4172 443 EPKLLVLDEPTSALDVSVQAQILD-------LLRDLQR---EHGLAYL----FIshdlavvralahrvMVMKDGKVVEQG 508
|
250
....*....|..
gi 1937891448 833 HYSELL---QHD 841
Cdd:COG4172 509 PTEQVFdapQHP 520
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1302-1484 |
7.74e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 53.64 E-value: 7.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1302 LKNLTLHVQGGEKVGIVGRTGAGKSSmtlcLFRILEAA------EGEIFIDGlNVAHigLHDLRS-----------QLTI 1364
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKST----LMKVLSGVyphgsyEGEILFDG-EVCR--FKDIRDsealgiviihqELAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1365 IPQDPI---LFSGTLRmnldpfGRYS----DEDIWRTLELShlsAFVssqptGLDFQCSEGGDNLSVGQRQLVCLARALL 1437
Cdd:NF040905 90 IPYLSIaenIFLGNER------AKRGvidwNETNRRARELL---AKV-----GLDESPDTLVTDIGVGKQQLVEIAKALS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 1438 RKSRVLVLDEATAAIDlETD-----DLIQGtIRTQfeDCTVLTIAHRLNTIM 1484
Cdd:NF040905 156 KDVKLLILDEPTAALN-EEDsaallDLLLE-LKAQ--GITSIIISHKLNEIR 203
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
636-789 |
9.53e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 9.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 636 SKDLP--PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS--------------VAYVPQQA-W 698
Cdd:PRK10982 5 SKSFPgvKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfksskealengISMVHQELnL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 699 IQNCTLQENVLFGQ-PM------NPKRYQqalETCALLADLDVlpggdQTEIGEKGINLSGGQRQRVSLARAVYSDANIF 771
Cdd:PRK10982 85 VLQRSVMDNMWLGRyPTkgmfvdQDKMYR---DTKAIFDELDI-----DIDPRAKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170
....*....|....*...
gi 1937891448 772 LLDDPLSAVDSHVAKHIF 789
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLF 174
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1422-1480 |
1.35e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 51.64 E-value: 1.35e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1937891448 1422 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRL 1480
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNL 222
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
749-840 |
1.42e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 52.11 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 749 NLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDqvigpegVLA------GKTRVLVTHGISFLPQT-DFII 821
Cdd:PRK11153 140 QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILE-------LLKdinrelGLTIVLITHEMDVVKRIcDRVA 212
|
90
....*....|....*....
gi 1937891448 822 VLADGQITEMGHYSELLQH 840
Cdd:PRK11153 213 VIDAGRLVEQGTVSEVFSH 231
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
643-828 |
1.46e-06 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 51.19 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-SVAYVPQQAwI---------QN------CTLQE 706
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGrDITGLPPHR-IarlgiartfQNprlfpeLTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 707 NVLFGQPMNPKRY----------------------QQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAV 764
Cdd:COG0411 99 NVLVAAHARLGRGllaallrlprarreereareraEELLERVGLADRADEPAG-----------NLSYGQQRRLEIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 765 YSDANIFLLDDP---LSAVDSHVAKHIFDQVIGPEGVlagkTRVLVTH------GISflpqtDFIIVLADGQI 828
Cdd:COG0411 168 ATEPKLLLLDEPaagLNPEETEELAELIRRLRDERGI----TILLIEHdmdlvmGLA-----DRIVVLDFGRV 231
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1306-1492 |
1.68e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.02 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1306 TLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDG---LNVAHIGLHDLRSQLTIIPQDPiLFSGTLRMNL-- 1380
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkdlLGMKDDEWRAVRSDIQMIFQDP-LASLNPRMTIge 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1381 ---DPFGRY----SDEDIWRtlELSHLSAFVSSQPTGLDFQCSEggdnLSVGQRQLVCLARALLRKSRVLVLDEATAAID 1453
Cdd:PRK15079 120 iiaEPLRTYhpklSRQEVKD--RVKAMMLKVGLLPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1937891448 1454 LEtddlIQGTI-----RTQFE-DCTVLTIAHRLNT---IMDynRVLVL 1492
Cdd:PRK15079 194 VS----IQAQVvnllqQLQREmGLSLIFIAHDLAVvkhISD--RVLVM 235
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
641-829 |
1.80e-06 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 50.34 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSAL---LGEMEKLEGAVSVKG------------SVAYVPQQAW-IQNCTL 704
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGipykefaekypgEIIYVSEEDVhFPTLTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 705 QENVLFgqpmnpkryqqALETCalladldvlpgGDQTEIGekginLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHV 784
Cdd:cd03233 101 RETLDF-----------ALRCK-----------GNEFVRG-----ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1937891448 785 AKHIFdQVIgpegvlagKTRVLVTHGISF--LPQT--------DFIIVLADGQIT 829
Cdd:cd03233 154 ALEIL-KCI--------RTMADVLKTTTFvsLYQAsdeiydlfDKVLVLYEGRQI 199
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
634-781 |
1.91e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 50.62 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 634 SWSKDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS----------VAYVPQ-QAWIQNC 702
Cdd:PRK13543 18 AFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrsrfMAYLGHlPGLKADL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 703 TLQENVLFGQPMNPKRYQQaletcalladldvLPGGDQTEIGEKGI------NLSGGQRQRVSLARAVYSDANIFLLDDP 776
Cdd:PRK13543 98 STLENLHFLCGLHGRRAKQ-------------MPGSALAIVGLAGYedtlvrQLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
....*
gi 1937891448 777 LSAVD 781
Cdd:PRK13543 165 YANLD 169
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
625-776 |
2.20e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.20 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 625 AITIHNGTFSWskDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAV--SVKGSVAYVPQ---QAWI 699
Cdd:PRK15064 319 ALEVENLTKGF--DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwSENANIGYYAQdhaYDFE 396
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937891448 700 QNCTLQEnvLFGQPMNPKRYQQALEtcALLADLdvLPGGDqtEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDP 776
Cdd:PRK15064 397 NDLTLFD--WMSQWRQEGDDEQAVR--GTLGRL--LFSQD--DIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
652-828 |
2.43e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 48.91 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 652 KGALVAVVGPVGCGKSSLVSALLGEMEKLEgavsvkGSVAYVpqqawiqNCTLQENVLFGQPMNpkryqqaletcallad 731
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPG------GGVIYI-------DGEDILEEVLDQLLL---------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 732 ldvlpggdqTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGPEGVLA---GKTRVLVT 808
Cdd:smart00382 52 ---------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLkseKNLTVILT 122
|
170 180
....*....|....*....|
gi 1937891448 809 HGISFLPQTDFIIVLADGQI 828
Cdd:smart00382 123 TNDEKDLGPALLRRRFDRRI 142
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1276-1456 |
2.62e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 51.86 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1276 PEGwPRSG--VVEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSmtlcLFRILEAAE----GEIFIdGLN 1349
Cdd:TIGR03719 313 PPG-PRLGdkVIEAENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKST----LFRMITGQEqpdsGTIEI-GET 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1350 VahiglhdlrsQLTIIPQDpilfsgtlRMNLDPfgrysDEDIWRTLE--LSHLS---------AFVSSqptgLDFQcseG 1418
Cdd:TIGR03719 385 V----------KLAYVDQS--------RDALDP-----NKTVWEEISggLDIIKlgkreipsrAYVGR----FNFK---G 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1937891448 1419 GD------NLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLET 1456
Cdd:TIGR03719 435 SDqqkkvgQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVET 478
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
643-827 |
2.65e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 49.24 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEmeklegavsvkgsvayvpqqawiQNCTLQENVLfgqPMNPKRYQQA 722
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA-----------------------SGKARLISFL---PKFSRNKLIF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 723 LETCALLAD--LDVLPggdqteIGEKGINLSGGQRQRVSLARAVYSDA--NIFLLDDPLSAVDSHVAKHIFDQV--IGPE 796
Cdd:cd03238 65 IDQLQFLIDvgLGYLT------LGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIkgLIDL 138
|
170 180 190
....*....|....*....|....*....|.
gi 1937891448 797 GVlagkTRVLVTHGISFLPQTDFIIVLADGQ 827
Cdd:cd03238 139 GN----TVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1309-1485 |
3.06e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.12 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1309 VQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVA---HIGLHDLRSQLTIIPQDPIlfsgtlrMNLDPfgR 1385
Cdd:PRK11308 38 LERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQKIQIVFQNPY-------GSLNP--R 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1386 YSDEDIW--------------RTLELSHLSAFVSSQPTGLD-----FqcseggdnlSVGQRQLVCLARALLRKSRVLVLD 1446
Cdd:PRK11308 109 KKVGQILeepllintslsaaeRREKALAMMAKVGLRPEHYDryphmF---------SGGQRQRIAIARALMLDPDVVVAD 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 1937891448 1447 EATAAIDLetddliqgTIRTQFedctvltiahrLNTIMD 1485
Cdd:PRK11308 180 EPVSALDV--------SVQAQV-----------LNLMMD 199
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1285-1503 |
3.07e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 50.79 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYRPGL---ELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIdGLNVAHIG-----LH 1356
Cdd:PRK13634 3 ITFQKVEHRYQYKTpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGkknkkLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1357 DLRSQLTIIPQDP--ILFSGTLR-------MNldpFGrYSDEDIWRT----LELSHLSAFVSSQ-PtgldFQcseggdnL 1422
Cdd:PRK13634 82 PLRKKVGIVFQFPehQLFEETVEkdicfgpMN---FG-VSEEDAKQKaremIELVGLPEELLARsP----FE-------L 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1423 SVGQRQLVCLARALLRKSRVLVLDEATAAID----LETDDLIQGTIRTQfeDCTVLTIAHRLNTIMDY-NRVLVLDKGVV 1497
Cdd:PRK13634 147 SGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDpkgrKEMMEMFYKLHKEK--GLTTVLVTHSMEDAARYaDQIVVMHKGTV 224
|
....*.
gi 1937891448 1498 AEFDSP 1503
Cdd:PRK13634 225 FLQGTP 230
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1284-1480 |
3.38e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 50.16 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1284 VVEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILE-----AAEGEIFIDGLNV--AHIGLH 1356
Cdd:PRK14239 5 ILQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysPRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1357 DLRSQLTIIPQDPILFSGT--------LRMNLDPFGRYSDEDIWRTLELSHLSAFVSSQptgldfqCSEGGDNLSVGQRQ 1428
Cdd:PRK14239 83 DLRKEIGMVFQQPNPFPMSiyenvvygLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDR-------LHDSALGLSGGQQQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 1429 LVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRL 1480
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
646-841 |
3.48e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.51 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 646 LNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS-VAYVPQQAWIQnctLQENV-----LFGQPMNPKry 719
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKpVTAEQPEDYRK---LFSAVftdfhLFDQLLGPE-- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 720 QQALETCALLADLDVLPGGDQTEIGE---KGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKhIFDQVIGPE 796
Cdd:PRK10522 417 GKPANPALVEKWLERLKMAHKLELEDgriSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRR-EFYQVLLPL 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1937891448 797 GVLAGKTRVLVTHGISFLPQTDFIIVLADGQITEM-GHYSELLQHD 841
Cdd:PRK10522 496 LQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSELtGEERDAASRD 541
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
640-781 |
4.03e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 50.73 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 640 PPTLHSLN---IQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSVAYVPQQAWIQNCTLQENVLFGQP--- 713
Cdd:PRK11308 25 ERLVKALDgvsFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNPygs 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 714 MNP-KRYQQAL-ETCALLADLDvlpggdQTEIGEKGINL------------------SGGQRQRVSLARAVYSDANIFLL 773
Cdd:PRK11308 105 LNPrKKVGQILeEPLLINTSLS------AAERREKALAMmakvglrpehydryphmfSGGQRQRIAIARALMLDPDVVVA 178
|
....*...
gi 1937891448 774 DDPLSAVD 781
Cdd:PRK11308 179 DEPVSALD 186
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1299-1453 |
4.19e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.18 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1299 ELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHiGLHDLRSQLTIIPQ----DPILfsg 1374
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHrsgiNPYL--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1375 TLRMNL-----DPFGRYSDEDIWRTLELSHLsafvssqptgLDFQCSEggdnLSVGQRQLVCLARALLRKSRVLVLDEAT 1449
Cdd:PRK13540 90 TLRENClydihFSPGAVGITELCRLFSLEHL----------IDYPCGL----LSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
....
gi 1937891448 1450 AAID 1453
Cdd:PRK13540 156 VALD 159
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
310-552 |
4.42e-06 |
|
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: 50.10 E-value: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 310 LLMGACFKLIQDLLSFINPQLLSILIRFISDPTAPTWWGFLLAGLMFVSSTMQTLILHQHYHCIFVMALRIRTAIIGVIY 389
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 390 RKALTITNSVKREYTVGEMVNLMS--VDAQRFMdVSPFINLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNGA 467
Cdd:cd18541 81 AHLLTLSPSFYQKNRTGDLMARATndLNAVRMA-LGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 468 VSMKM-KTYQVQQMKFKDsriklMS----EILNGIKVLKLYAWEPT----FLEQVEGIRQSELQLLRKGAYLQAISTFIw 538
Cdd:cd18541 160 LGKKIhKRFRKVQEAFSD-----LSdrvqESFSGIRVIKAFVQEEAeierFDKLNEEYVEKNLRLARVDALFFPLIGLL- 233
|
250
....*....|....
gi 1937891448 539 vctPFMVTLITLGV 552
Cdd:cd18541 234 ---IGLSFLIVLWY 244
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
646-781 |
4.77e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 49.51 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 646 LNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSV--------------KGSVAYVPQQAWI-QNCTLQENVLF 710
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedisllplharaRRGIGYLPQEASIfRRLSVYDNLMA 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 711 GQPM--NPKRYQQALETCALLADLDVLPGGDQTeigekGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD 781
Cdd:PRK10895 102 VLQIrdDLSAEQREDRANELMEEFHIEHLRDSM-----GQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
1049-1182 |
5.67e-06 |
|
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: 50.14 E-value: 5.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1049 IRAPQSFFDTTPSGRILNRFSkDIYVIDEVLAPTILMLF-NSFYTSISTIVVIVASTPLFCVVVLPLAVfYGFVQRFYVA 1127
Cdd:cd18570 86 LKLPLSFFETRKTGEIISRFN-DANKIREAISSTTISLFlDLLMVIISGIILFFYNWKLFLITLLIIPL-YILIILLFNK 163
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1937891448 1128 TSRQLKRLESVSRSPIFSHFSETVTGTSVIRAYGRVQDFKVLSDAKVDSNQKTTY 1182
Cdd:cd18570 164 PFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSF 218
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1301-1455 |
6.22e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 49.24 E-value: 6.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1301 VLKNLTLHVQGGEKVGIVGRTGAGKSSmtlcLFRILEAAE----GEIFIDGLNV---AHIG---LHDLRSQLTIIPQD-- 1368
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSS----LLRVLNLLEmprsGTLNIAGNHFdfsKTPSdkaIRELRRNVGMVFQQyn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1369 --PILfsgTLRMNL--DP---FGRYSDEDIWRTLELS---HLSAFVSSQPTgldfqcseggdNLSVGQRQLVCLARALLR 1438
Cdd:PRK11124 93 lwPHL---TVQQNLieAPcrvLGLSKDQALARAEKLLerlRLKPYADRFPL-----------HLSGGQQQRVAIARALMM 158
|
170
....*....|....*..
gi 1937891448 1439 KSRVLVLDEATAAIDLE 1455
Cdd:PRK11124 159 EPQVLLFDEPTAALDPE 175
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
653-808 |
7.47e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 50.65 E-value: 7.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 653 GALVAVVGPVGCGKSSLVSALLGEMEK--LEGAVSVKGS---------VAYVPQQAWI-QNCTLQENVLFGQ----PMNP 716
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGnnFTGTILANNRkptkqilkrTGFVTQDDILyPHLTVRETLVFCSllrlPKSL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 717 KRYQQALETCALLADLDvLPGGDQTEIGEKGIN-LSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGp 795
Cdd:PLN03211 174 TKQEKILVAESVISELG-LTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGS- 251
|
170
....*....|...
gi 1937891448 796 egvLAGKTRVLVT 808
Cdd:PLN03211 252 ---LAQKGKTIVT 261
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
1014-1162 |
8.04e-06 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 49.40 E-value: 8.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1014 LGILQGLLVMLSAFTMVVGAIQAARLLHTALLHNQIRAPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLFNSFYTS 1093
Cdd:cd18543 48 LGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGNLLTLV 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 1094 ISTIVVIVASTPLFCVVVLPLAVFYGFVQRF---YVATSRQLK-RLESVSrspifSHFSETVTGTSVIRAYGR 1162
Cdd:cd18543 128 VGLVVMLVLSPPLALVALASLPPLVLVARRFrrrYFPASRRAQdQAGDLA-----TVVEESVTGIRVVKAFGR 195
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1269-1501 |
1.04e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.03 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1269 VLESNRAPegwPRSG--VVEFRNYSVRYRPGLElVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFID 1346
Cdd:COG3845 243 LLRVEKAP---AEPGevVLEVENLSVRDDRGVP-ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLD 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1347 GLNVAHIGLHDLRSQ-LTIIPQDP-----ILfSGTLRMNLDpFGRYSDEDIWR--TLELSHLSAFVSS-------QPTGL 1411
Cdd:COG3845 319 GEDITGLSPRERRRLgVAYIPEDRlgrglVP-DMSVAENLI-LGRYRRPPFSRggFLDRKAIRAFAEElieefdvRTPGP 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1412 DFQCSeggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFED-CTVLTIAHRLNTIMDY-NRV 1489
Cdd:COG3845 397 DTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAgAAVLLISEDLDEILALsDRI 472
|
250
....*....|...
gi 1937891448 1490 LVLDKG-VVAEFD 1501
Cdd:COG3845 473 AVMYEGrIVGEVP 485
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
979-1256 |
1.08e-05 |
|
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: 48.97 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 979 AVAIGANV---WLSAWT-NDVEEHGQQNNTSVRLGVYATLGILQGLLVMLSAFTMVVGAIQAARLLHTALLHNQIRAPQS 1054
Cdd:cd18542 9 LLATALNLlipLLIRRIiDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1055 FFDTTPSGRILNRFSKDIYVIDEVLAPTILMLFNSFYTSISTIVVIVASTP---LFCVVVLPLAVFYGF-----VQRFYV 1126
Cdd:cd18542 89 FHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWkltLISLAIIPFIALFSYvffkkVRPAFE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1127 ATSRQLKRLESVsrspifshFSETVTGTSVIRAYGR----VQDFKVLSDAKVDSNQKTT------YPYIasnrwlgvhvE 1196
Cdd:cd18542 169 EIREQEGELNTV--------LQENLTGVRVVKAFARedyeIEKFDKENEEYRDLNIKLAkllakyWPLM----------D 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 1197 FVGNC----VVLFSALFAVigRNSLNPGlvglsvsyALQVTLSLNWMI--------RTLSDLESNIIAVERV 1256
Cdd:cd18542 231 FLSGLqivlVLWVGGYLVI--NGEITLG--------ELVAFISYLWMLiwpvrqlgRLINDMSRASASAERI 292
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
1050-1177 |
1.12e-05 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 49.00 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1050 RAPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLFNSFYTSISTIVVIVASTP---LFCVVVLP-LAVFYGFVQRFy 1125
Cdd:cd18545 85 KLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVrlaLVTLAVLPlLVLVVFLLRRR- 163
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 1126 vatSRQLKRLESVSRSPIFSHFSETVTGTSVIRAYGR----VQDFKVLSDAKVDSN 1177
Cdd:cd18545 164 ---ARKAWQRVRKKISNLNAYLHESISGIRVIQSFARedenEEIFDELNRENRKAN 216
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
641-829 |
1.18e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.62 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 641 PTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS--VAYVPQQ------AWI------------- 699
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHevVTRSPQDglangiVYIsedrkrdglvlgm 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 700 ---QN---CTLQENVLFGQPMNPKRYQQALETCALLADLDVlPGGDQTeIGekgiNLSGGQRQRVSLARAVYSDANIFLL 773
Cdd:PRK10762 346 svkENmslTALRYFSRAGGSLKHADEQQAVSDFIRLFNIKT-PSMEQA-IG----LLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 774 DDPLSAVDSHVAKHIFdQVIG---PEGVlagkTRVLVThgiSFLPQ----TDFIIVLADGQIT 829
Cdd:PRK10762 420 DEPTRGVDVGAKKEIY-QLINqfkAEGL----SIILVS---SEMPEvlgmSDRILVMHEGRIS 474
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
650-781 |
1.34e-05 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 48.96 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 650 IPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG-SVAYVPQQAW------IQnctlqenVLFGQPM---NP-KR 718
Cdd:COG4608 41 IRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGqDITGLSGRELrplrrrMQ-------MVFQDPYaslNPrMT 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937891448 719 YQQALEtcALLADLDVLPGGDQTEIGEK-----GIN----------LSGGQRQRVSLARAVYSDANIFLLDDPLSAVD 781
Cdd:COG4608 114 VGDIIA--EPLRIHGLASKAERRERVAEllelvGLRpehadrypheFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1012-1256 |
1.70e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 48.66 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1012 ATLGI--LQGLLVMLSAFTMVVGAIQAARLLHTALLHNQIRAPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLFNS 1089
Cdd:cd18564 59 ALVGIalLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1090 FYTSISTIVVIVASTPLFCVVVL-PLAVFYGFVQRFYvatsrqlKRLESVSR------SPIFSHFSETVTGTSVIRAYGR 1162
Cdd:cd18564 139 LLTLVGMLGVMFWLDWQLALIALaVAPLLLLAARRFS-------RRIKEASReqrrreGALASVAQESLSAIRVVQAFGR 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1163 ----VQDFKVLSDAKVDSNQKTTypYIASNRWLGVHV-EFVGNCVVLFSALFAVIgRNSLNPGLVGLSVSYalqvtlsLN 1237
Cdd:cd18564 212 eeheERRFARENRKSLRAGLRAA--RLQALLSPVVDVlVAVGTALVLWFGAWLVL-AGRLTPGDLLVFLAY-------LK 281
|
250 260
....*....|....*....|....*.
gi 1937891448 1238 WM---IRTLSDLESNI----IAVERV 1256
Cdd:cd18564 282 NLykpVRDLAKLTGRIakasASAERV 307
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
646-781 |
1.87e-05 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 48.51 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 646 LNIQIPKGALVAVVGPVGCGKSSLVSALLG---EMEKLEGAVSVKGS-----------------VAYVPQ---------- 695
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEdllklsekelrkirgreIQMIFQdpmtslnpvm 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 696 ----QawiqnctLQENVLFGQPMNPK-RYQQALEtcaLLADLdvlpggdqteigekGIN------------LSGGQRQRV 758
Cdd:COG0444 104 tvgdQ-------IAEPLRIHGGLSKAeARERAIE---LLERV--------------GLPdperrldrypheLSGGMRQRV 159
|
170 180
....*....|....*....|...
gi 1937891448 759 SLARAVYSDANIFLLDDPLSAVD 781
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALD 182
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
643-832 |
1.87e-05 |
|
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: 47.14 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEM--EKLEGAVSVKGSVayvpqqawIQNCTLQENVLFGQPM---NPK 717
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGED--------ITDLPPEERARLGIFLafqYPP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 718 RYqQALETCALLADLDVlpggdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD----SHVAKHIfDQVI 793
Cdd:cd03217 88 EI-PGVKNADFLRYVNE--------------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDidalRLVAEVI-NKLR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1937891448 794 GPegvlaGKTRVLVTH--GISFLPQTDFIIVLADGQITEMG 832
Cdd:cd03217 152 EE-----GKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
649-776 |
2.37e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.79 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 649 QIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSV--KGSVAYV--------PQQAWIQNCT--LQENVLFGQPMNP 716
Cdd:PRK11147 341 QVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCgtKLEVAYFdqhraeldPEKTVMDNLAegKQEVMVNGRPRHV 420
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937891448 717 KRYQQaletcalladlDVL--PGGDQTEIGEkginLSGGQRQRVSLARAVYSDANIFLLDDP 776
Cdd:PRK11147 421 LGYLQ-----------DFLfhPKRAMTPVKA----LSGGERNRLLLARLFLKPSNLLILDEP 467
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
636-826 |
2.48e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.63 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 636 SKDLPPT--LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKG----------------SVAYvPQQA 697
Cdd:PRK09700 12 GKSFGPVhaLKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldhklaaqlgiGIIY-QELS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 698 WIQNCTLQENVLFGQPMNPK--------------RYQQALETCALLADLDvlpggdqteigEKGINLSGGQRQRVSLARA 763
Cdd:PRK09700 91 VIDELTVLENLYIGRHLTKKvcgvniidwremrvRAAMMLLRVGLKVDLD-----------EKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937891448 764 VYSDANIFLLDDPLSAVDSHVAKHIF---DQVIGpegvlAGKTRVLVTHGISFLPQT-DFIIVLADG 826
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFlimNQLRK-----EGTAIVYISHKLAEIRRIcDRYTVMKDG 221
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
748-836 |
4.20e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 46.41 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 748 INLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDqvIGPEGVLAGKTRVLVTHGISFLPQTDF-IIVLADG 826
Cdd:PRK10908 136 IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILR--LFEEFNRVGVTVLMATHDIGLISRRSYrMLTLSDG 213
|
90
....*....|
gi 1937891448 827 QITEmGHYSE 836
Cdd:PRK10908 214 HLHG-GVGGE 222
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1011-1161 |
4.26e-05 |
|
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: 47.08 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1011 YATLGILQGLLVMLSAFT-MVVGAIQAARLlHTALLHNQIRAPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLFNS 1089
Cdd:cd18577 53 FVYLGIGSFVLSYIQTACwTITGERQARRI-RKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1090 FYTSISTIV-----------VIVASTPLfcvVVLPLAVFYGFVQRFyvaTSRQLKRLESVSrspifSHFSETVTGTSVIR 1158
Cdd:cd18577 132 LSTFIAGFIiafiyswkltlVLLATLPL---IAIVGGIMGKLLSKY---TKKEQEAYAKAG-----SIAEEALSSIRTVK 200
|
...
gi 1937891448 1159 AYG 1161
Cdd:cd18577 201 AFG 203
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1272-1453 |
4.61e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.86 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1272 SNRAPEGWPRSG--VVEFRNYSVrYRPGLE--LVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLF------RIleaaEG 1341
Cdd:NF040905 243 EDRYPERTPKIGevVFEVKNWTV-YHPLHPerKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgrsygrNI----SG 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1342 EIFIDGLNVahiglhDLRSqltiiPQDPILfSG---------TLRMNLdpfgrysDEDIWRTLELSHLSAfVSS------ 1406
Cdd:NF040905 318 TVFKDGKEV------DVST-----VSDAID-AGlayvtedrkGYGLNL-------IDDIKRNITLANLGK-VSRrgvide 377
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937891448 1407 ----------------------QPTGldfqcseggdNLSVGQRQLVCLARALLRKSRVLVLDEATAAID 1453
Cdd:NF040905 378 neeikvaeeyrkkmniktpsvfQKVG----------NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
750-841 |
5.16e-05 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 46.75 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 750 LSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFD------QVIGPEGVLAGKTRVLVTHgISflpqtDFIIVL 823
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINlmlelqEKLGISYIYVSQHLGIVKH-IS-----DKVLVM 223
|
90 100
....*....|....*....|.
gi 1937891448 824 ADGQITEMGHYSELL---QHD 841
Cdd:COG4167 224 HQGEVVEYGKTAEVFanpQHE 244
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
640-838 |
6.50e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 46.08 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 640 PPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGeMEKLEGAVSVKGSV-------------AYVPQQawiQNCTLQE 706
Cdd:PRK03695 9 STRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPleawsaaelarhrAYLSQQ---QTPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 707 NV-----LFGQPMNPKRYQQAL--ETCALLADLDVLPGGDQTeigekginLSGGQRQRVSLA-------RAVYSDANIFL 772
Cdd:PRK03695 85 PVfqyltLHQPDKTRTEAVASAlnEVAEALGLDDKLGRSVNQ--------LSGGEWQRVRLAavvlqvwPDINPAGQLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937891448 773 LDDPLSAVDshVA-KHIFDQVIGpEGVLAGKTRVLVTHGISF-LPQTDFIIVLADGQITEMGHYSELL 838
Cdd:PRK03695 157 LDEPMNSLD--VAqQAALDRLLS-ELCQQGIAVVMSSHDLNHtLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1281-1473 |
7.18e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.25 E-value: 7.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1281 RSGVVEFR----NYSVryrPGLELVlKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIdG--LNVAHIG 1354
Cdd:PRK11147 314 RSGKIVFEmenvNYQI---DGKQLV-KDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GtkLEVAYFD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1355 LHdlrsqltiipqdpilfsgtlRMNLDPfgrysdEdiwRTLE-------------------LSHLSAFVSS-----QPTg 1410
Cdd:PRK11147 389 QH--------------------RAELDP------E---KTVMdnlaegkqevmvngrprhvLGYLQDFLFHpkramTPV- 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 1411 ldfqcseggDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLI-------QGTI------RtQFEDCTV 1473
Cdd:PRK11147 439 ---------KALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLeelldsyQGTVllvshdR-QFVDNTV 504
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1295-1453 |
1.06e-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: 47.32 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1295 RPGLELVlkNLTLHVQggEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVaHIGLHDLRSQLTIIPQDPILFSg 1374
Cdd:TIGR01257 943 RPAVDRL--NITFYEN--QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFH- 1016
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937891448 1375 tlRMNLDPFGRYSDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAID 1453
Cdd:TIGR01257 1017 --HLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
643-838 |
1.39e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 45.47 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEG-------------------AVSVKGSVAYVPQQAWIQNCT 703
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgdvllggrsifnyrdVLEFRRRVGMLFQRPNPFPMS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 704 LQENVLFG---QPMNPKRYQQALETcALLADLDvLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAV 780
Cdd:PRK14271 117 IMDNVLAGvraHKLVPRKEFRGVAQ-ARLTEVG-LWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSAL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 781 DSHVAKHIFDQVIGpegvLAGK-TRVLVTHGISFLPQ-TDFIIVLADGQITEMGHYSELL 838
Cdd:PRK14271 195 DPTTTEKIEEFIRS----LADRlTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLF 250
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
652-832 |
1.62e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 45.61 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 652 KGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVK----------GSVAYVPQQAWIQNC------------------- 702
Cdd:PRK13631 51 KNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkknnHELITNPYSKKIKNFkelrrrvsmvfqfpeyqlf 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 703 --TLQENVLFGqPMNPKryQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAV 780
Cdd:PRK13631 131 kdTIEKDIMFG-PVALG--VKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGL 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1937891448 781 DSHVAKHIFDQVIgpEGVLAGKTRVLVTHGI-SFLPQTDFIIVLADGQITEMG 832
Cdd:PRK13631 208 DPKGEHEMMQLIL--DAKANNKTVFVITHTMeHVLEVADEVIVMDKGKILKTG 258
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1014-1165 |
1.71e-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: 45.17 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1014 LGILQGLLVMLSAFTMVVGAIQ---AARL-------LHTALLHNQIRAPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTI 1083
Cdd:cd18550 38 LVLLALGMVAVAVASALLGVVQtylSARIgqgvmydLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1084 LMLFNSFYTSISTIVVIVASTP---LFCVVVLPLAVFYG--FVQRFYVATSRQLKRLESVSrspifSHFSET--VTGTSV 1156
Cdd:cd18550 118 TSVVSNVVTLVATLVAMLALDWrlaLLSLVLLPLFVLPTrrVGRRRRKLTREQQEKLAELN-----SIMQETlsVSGALL 192
|
....*....
gi 1937891448 1157 IRAYGRVQD 1165
Cdd:cd18550 193 VKLFGREDD 201
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1305-1497 |
2.09e-04 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 44.54 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1305 LTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEaAEGEIFIDGLNVAHIGLHDL---RSQLTiiPQDPILFSgtlrMnld 1381
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELarhRAYLS--QQQTPPFA----M--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1382 pfgrysdeDIWRTLELshlsafvsSQPTGLDFQCSEG-----------GD-------NLSVGQRQLVCLARALLR----- 1438
Cdd:PRK03695 85 --------PVFQYLTL--------HQPDKTRTEAVASalnevaealglDDklgrsvnQLSGGEWQRVRLAAVVLQvwpdi 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937891448 1439 --KSRVLVLDEATAAIDLETDDLIQGTIRtqfEDC----TVLTIAHRLNTIMDY-NRVLVLDKGVV 1497
Cdd:PRK03695 149 npAGQLLLLDEPMNSLDVAQQAALDRLLS---ELCqqgiAVVMSSHDLNHTLRHaDRVWLLKQGKL 211
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
1012-1115 |
2.18e-04 |
|
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: 45.12 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1012 ATLGILQGLLVMLSAFTMVVGAIQAARLLHTALLHNQIRAPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLFNSFY 1091
Cdd:cd18551 43 VALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVL 122
|
90 100 110
....*....|....*....|....*....|....*
gi 1937891448 1092 TSISTIV-----------VIVASTPLFCVVVLPLA 1115
Cdd:cd18551 123 TVVGAVVlmflldwvltlVTLAVVPLAFLIILPLG 157
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1312-1485 |
2.83e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 42.75 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1312 GEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTIIpqdpilfsgtlrmnldpfgrysdedi 1391
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVG-------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1392 wrtlelshlsafvssqptgldfqcsEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQF--- 1468
Cdd:smart00382 56 -------------------------GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLlll 110
|
170 180
....*....|....*....|.
gi 1937891448 1469 ----EDCTVLTIAHRLNTIMD 1485
Cdd:smart00382 111 lkseKNLTVILTTNDEKDLGP 131
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
656-841 |
3.75e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 44.01 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 656 VAVVGPVGCGKSSLVSALLGEMEKLEGAVSVK------GSVAYVPQQAwiqnctlqeNVLFGQP---MNPK-RYQQALET 725
Cdd:PRK15112 42 LAIIGENGSGKSTLAKMLAGMIEPTSGELLIDdhplhfGDYSYRSQRI---------RMIFQDPstsLNPRqRISQILDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 726 CALL-ADLDvlpggdqTEIGEKGIN-------------------LSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVA 785
Cdd:PRK15112 113 PLRLnTDLE-------PEQREKQIIetlrqvgllpdhasyyphmLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937891448 786 KHIFDQVIgpegvlagktRVLVTHGISFLPQT----------DFIIVLADGQITEMGHYSELL---QHD 841
Cdd:PRK15112 186 SQLINLML----------ELQEKQGISYIYVTqhlgmmkhisDQVLVMHQGEVVERGSTADVLaspLHE 244
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
643-779 |
4.48e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.53 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLG-------------EMEKLEgAVSVKGS----VAYVPQQ-AWIQNCTL 704
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgtyegeiifEGEELQ-ASNIRDTeragIAIIHQElALVKELSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 705 QENVLFGQPMNP-------KRYQQALEtcaLLAD--LDVLPGgdqTEIGekgiNLSGGQRQRVSLARAVYSDANIFLLDD 775
Cdd:PRK13549 100 LENIFLGNEITPggimdydAMYLRAQK---LLAQlkLDINPA---TPVG----NLGLGQQQLVEIAKALNKQARLLILDE 169
|
....
gi 1937891448 776 PLSA 779
Cdd:PRK13549 170 PTAS 173
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
751-866 |
4.88e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 751 SGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVakhifdqVIGPEGVLAG--KTRVLVTHGISFLPQTDFIIVLADGQi 828
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA-------VLWLETYLLKwpKTFIVVSHAREFLNTVVTDILHLHGQ- 417
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1937891448 829 temghysELLQHDGSFANFLRNYAPD-ENQ----EANEGVLQH 866
Cdd:PLN03073 418 -------KLVTYKGDYDTFERTREEQlKNQqkafESNERSRSH 453
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1049-1162 |
6.04e-04 |
|
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: 43.63 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1049 IRAPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTI-------LMLFNS----FYTSISTIVVIVASTPLfcvVVLPLAVF 1117
Cdd:cd18575 80 LRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLsialrnlLLLIGGlvmlFITSPKLTLLVLLVIPL---VVLPIILF 156
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1937891448 1118 YGFVQRFyvatSRQ-LKRLESVSrspifSHFSETVTGTSVIRAYGR 1162
Cdd:cd18575 157 GRRVRRL----SRAsQDRLADLS-----AFAEETLSAIKTVQAFTR 193
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1422-1503 |
6.59e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 43.69 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1422 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETD-DLIQGTIRTQFEDCTVLTIAHRLNTIMDY-NRVLVLDKGVVAE 1499
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEhEMMQLILDAKANNKTVFVITHTMEHVLEVaDEVIVMDKGKILK 256
|
....
gi 1937891448 1500 FDSP 1503
Cdd:PRK13631 257 TGTP 260
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1009-1180 |
8.79e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 43.27 E-value: 8.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1009 GVYATLGILQGLLVMLSAFTMVVGAIQA---ARL-------LHTALLHNQIRAPQSFFDTTPSGRILNRFSKDIYVIDEV 1078
Cdd:cd18563 37 GNTSLLLLLVLGLAGAYVLSALLGILRGrllARLgeritadLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1079 LAPTILMLFNSFYTSISTIVVIVASTP---LFCVVVLPLAVF--YGFVQRFYVATSRQLKRLESVSrspifSHFSETVTG 1153
Cdd:cd18563 117 LSDGLPDFLTNILMIIGIGVVLFSLNWklaLLVLIPVPLVVWgsYFFWKKIRRLFHRQWRRWSRLN-----SVLNDTLPG 191
|
170 180 190
....*....|....*....|....*....|.
gi 1937891448 1154 TSVIRAYGR----VQDFKVLSDAKVDSNQKT 1180
Cdd:cd18563 192 IRVVKAFGQekreIKRFDEANQELLDANIRA 222
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1285-1495 |
1.00e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 43.15 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1285 VEFRNYSVRYRPGLELVLK---NLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEI---FIDGLNVAHIGLH-- 1356
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1357 -------------------DLRSQLTIIPQ--DPILFSGTLRMNLdPFGRYS-----DEDIWRTLELSHLsafvssqpTG 1410
Cdd:PRK13651 83 vleklviqktrfkkikkikEIRRRVGVVFQfaEYQLFEQTIEKDI-IFGPVSmgvskEEAKKRAAKYIEL--------VG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1411 LDFQCSEGGD-NLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLE-TDDLIQGTIRTQFEDCTVLTIAHRLNTIMDY-N 1487
Cdd:PRK13651 154 LDESYLQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEILEIFDNLNKQGKTIILVTHDLDNVLEWtK 233
|
....*...
gi 1937891448 1488 RVLVLDKG 1495
Cdd:PRK13651 234 RTIFFKDG 241
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1299-1343 |
1.38e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.96 E-value: 1.38e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1937891448 1299 ELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEI 1343
Cdd:PRK15064 332 GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
751-788 |
1.75e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.77 E-value: 1.75e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1937891448 751 SGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHI 788
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQI 464
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
652-859 |
1.93e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.59 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 652 KGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS--------------VAYVP----QQAWIQNCTLQENV----- 708
Cdd:PRK11288 278 AGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpidirsprdairagIMLCPedrkAEGIIPVHSVADNInisar 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 709 ----LFGQPMNPKRYQQALETcaLLADLDV-LPGGDQteigeKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDsh 783
Cdd:PRK11288 358 rhhlRAGCLINNRWEAENADR--FIRSLNIkTPSREQ-----LIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID-- 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 784 V-AKHIFDQVIGPegvLA--GKTRVLVThgiSFLPQ----TDFIIVLADGQITemghySELLQHDGSFANFLRNYAPDEN 856
Cdd:PRK11288 429 VgAKHEIYNVIYE---LAaqGVAVLFVS---SDLPEvlgvADRIVVMREGRIA-----GELAREQATERQALSLALPRTS 497
|
...
gi 1937891448 857 QEA 859
Cdd:PRK11288 498 AAV 500
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
709-781 |
1.97e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.80 E-value: 1.97e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937891448 709 LFGQPMN--PKRYQQALETCALLADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVD 781
Cdd:NF033858 366 LFHLPAAeiAARVAEMLERFDLADVADALPD-----------SLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
718-837 |
2.12e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.04 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 718 RYQQALETCALL------ADLDVLPGgdqteigekgiNLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQ 791
Cdd:PRK11022 127 RRQRAIDLLNQVgipdpaSRLDVYPH-----------QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIEL 195
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1937891448 792 VIGpegvLAGKTR---VLVTHGISFLPQT-DFIIVLADGQITEMGHYSEL 837
Cdd:PRK11022 196 LLE----LQQKENmalVLITHDLALVAEAaHKIIVMYAGQVVETGKAHDI 241
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
650-789 |
2.16e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.59 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 650 IPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGS--------------VA-------YVPQQawiqncTLQENV 708
Cdd:PRK11288 27 CRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasttaalaagVAiiyqelhLVPEM------TVAENL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 709 LFGQPmnPKR---------YQQALETCALLAdLDVLPggdQTEIGEkginLSGGQRQRVSLARAVYSDANIFLLDDPLSA 779
Cdd:PRK11288 101 YLGQL--PHKggivnrrllNYEAREQLEHLG-VDIDP---DTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170
....*....|
gi 1937891448 780 VDSHVAKHIF 789
Cdd:PRK11288 171 LSAREIEQLF 180
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1252-1460 |
2.23e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1252 AVERVKEYSKTETEAPWVLE-----SNRAPEGWPrSGVVEFRNYSVRYrpGLELVLKNLTLHVQGGEKVGIVGRTGAGKS 1326
Cdd:PRK10636 276 AQSRIKMLERMELIAPAHVDnpfhfSFRAPESLP-NPLLKMEKVSAGY--GDRIILDSIKLNLVPGSRIGLLGRNGAGKS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1327 SMTLCLFRILEAAEGEI-FIDGLNVAHIGLHDL------RSQLT----IIPQDPilfSGTLRMNLDPFGRYSDediwrtl 1395
Cdd:PRK10636 353 TLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLeflradESPLQhlarLAPQEL---EQKLRDYLGGFGFQGD------- 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1396 elshlsafvssqptgldfQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLE-----TDDLI 1460
Cdd:PRK10636 423 ------------------KVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDmrqalTEALI 474
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
1011-1159 |
2.73e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 41.42 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1011 YATLGILQGLLVMLSAFTMVVGAIQAARLLHTA----------LLHNQIRAPQSFFDTTPSGRILNRFSkDIYVIDEVLA 1080
Cdd:cd18782 38 LATLYVIGVVMLVAALLEAVLTALRTYLFTDTAnridlelggtIIDHLLRLPLGFFDKRPVGELSTRIS-ELDTIRGFLT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1081 PTILMLFNSFYTSISTIVVIVASTPLFCVVVL---PL-AVFYGFVQRFyvaTSRQLKRLESvSRSPIFSHFSETVTGTSV 1156
Cdd:cd18782 117 GTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLatvPLqLLLTFLFGPI---LRRQIRRRAE-ASAKTQSYLVESLTGIQT 192
|
...
gi 1937891448 1157 IRA 1159
Cdd:cd18782 193 VKA 195
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1301-1492 |
3.99e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 40.78 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1301 VLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCL-----FRILeaaEGEIFIDGLNVAHIGlHDLRSQLTIIP--QDPILFS 1373
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaghpaYKIL---EGDILFKGESILDLE-PEERAHLGIFLafQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 1374 GTlrMNLDpFGR--YSDEDIWRTL-ELSHLSAF---------VSSQPTGLDFQCSEGgdnLSVGQRQLVCLARALLRKSR 1441
Cdd:CHL00131 98 GV--SNAD-FLRlaYNSKRKFQGLpELDPLEFLeiineklklVGMDPSFLSRNVNEG---FSGGEKKRNEILQMALLDSE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1937891448 1442 VLVLDEATAAIDLetdDLIQgtirtqfedctvlTIAHRLNTIMDYNRVLVL 1492
Cdd:CHL00131 172 LAILDETDSGLDI---DALK-------------IIAEGINKLMTSENSIIL 206
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
648-676 |
4.82e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 4.82e-03
10 20 30
....*....|....*....|....*....|..
gi 1937891448 648 IQIPKGaLVAVVGPVGCGKSSLVSAL---LGE 676
Cdd:TIGR02168 19 INFDKG-ITGIVGPNGCGKSNIVDAIrwvLGE 49
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
643-780 |
7.65e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 40.58 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 643 LHSLNIQIPKGALVAVVGPVGCGKSSLVSALLG-------------EMEKLEGA----VSVKGSVAYVPQQAWIQNCTLQ 705
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwdgeiywSGSPLKASnirdTERAGIVIIHQELTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937891448 706 ENVLFGQPMNPK----RYQQALETC-ALLADLDVLPGGDQTEIGEKGinlsGGQRQRVSLARAVYSDANIFLLDDPLSAV 780
Cdd:TIGR02633 97 ENIFLGNEITLPggrmAYNAMYLRAkNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1422-1461 |
7.89e-03 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 40.07 E-value: 7.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1937891448 1422 LSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQ 1461
Cdd:PRK11248 129 LSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQ 168
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
648-676 |
9.11e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 38.99 E-value: 9.11e-03
10 20 30
....*....|....*....|....*....|..
gi 1937891448 648 IQIPKGaLVAVVGPVGCGKSSLVSAL---LGE 676
Cdd:cd03278 18 IPFPPG-LTAIVGPNGSGKSNIIDAIrwvLGE 48
|
|
| |
