|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
222-1533 |
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: 886.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 222 LLSKATYWWMNTLIISAHKKPIDLKAIGKLPIAMRAVTNYVCLKDAYEEQKKKVADHP---------------------- 279
Cdd:TIGR00957 209 FLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKECKKTRKQPvsavygkkdpskpkgssqldan 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 280 -------------NRTPSIWLAMYRAFGRPILLSSTFRYLADLLGFAGPLCISGIVQRVNETQNGTnnttgisetlsske 346
Cdd:TIGR00957 289 eevealivksphkPRKPSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPD-------------- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 347 flENAYVLAVLLFLALILQRTFLQASYYVTIETGINLRGALLAMIYNKILRLStsNLSMGEMTLGQINNLVAIETNQLMW 426
Cdd:TIGR00957 355 --WQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVIT--NSARKSSTVGEIVNLMSVDAQRFMD 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 427 FLFLCPNLWAMPVQIIMGVILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLK 506
Cdd:TIGR00957 431 LATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLK 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 507 LYAWEHIFCKSVEETRMKELSSLKTFALYTSLSIFMNAAIPIAAVLATFVTHAYASGNNLKPAE-AFASLSLFHILVTPL 585
Cdd:TIGR00957 511 LYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENNILDAEkAFVSLALFNILRFPL 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 586 FLLSTVVRFAVKAIISVQKLNEFLLSDEIgddswrtgesslpfesckkhtgvQPKTINRkqpgryhldsyeqstRRLRPA 665
Cdd:TIGR00957 591 NILPMVISSIVQASVSLKRLRIFLSHEEL-----------------------EPDSIER---------------RTIKPG 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 666 ETEDIAIKvtNGYFSWGSGLA-TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNrnrySVAYAAQ 744
Cdd:TIGR00957 633 EGNSITVH--NATFTWARDLPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG----SVAYVPQ 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 745 KPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDD 824
Cdd:TIGR00957 707 QAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDD 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 825 PFSALDIHLSDHLMQ-----EGILKflqddKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEHWKT 899
Cdd:TIGR00957 787 PLSAVDAHVGKHIFEhvigpEGVLK-----NKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRT 861
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 900 LMNRQDQElekDMEADQTTL------ERKTLRRAMY-----SREAKAQMEDEDEEEEEEEDEDDNMSTVMRLRTKMP-WK 967
Cdd:TIGR00957 862 YAPDEQQG---HLEDSWTALvsgegkEAKLIENGMLvtdvvGKQLQRQLSASSSDSGDQSRHHGSSAELQKAEAKEEtWK 938
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 968 TC---------------WRYLTSGGFFLLILMIFSKLLKHSVIVAIDYWLATWTSEYSINNTgKADQTYYV---AGFSIL 1029
Cdd:TIGR00957 939 LMeadkaqtgqvelsvyWDYMKAIGLFITFLSIFLFVCNHVSALASNYWLSLWTDDPMVNGT-QNNTSLRLsvyGALGIL 1017
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1030 CGAGIFLclvTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCL 1109
Cdd:TIGR00957 1018 QGFAVFG---YSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVI 1094
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1110 SAIGMISYATPVFLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELT 1189
Cdd:TIGR00957 1095 GALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKV 1174
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1190 DTNNIAYLFLSAANRWLEVRTDYLGACIVL--TASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVK 1267
Cdd:TIGR00957 1175 DENQKAYYPSIVANRWLAVRLECVGNCIVLfaALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVE 1254
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1268 KVNSFLTMESENyEGTMDPSQVPEHWPQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFF 1347
Cdd:TIGR00957 1255 RLKEYSETEKEA-PWQIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLF 1333
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1348 RMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDA 1427
Cdd:TIGR00957 1334 RINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDH 1413
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1428 VVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMK 1507
Cdd:TIGR00957 1414 ECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLD 1493
|
1370 1380
....*....|....*....|....*.
gi 530398972 1508 RGNILEYDTPESLLAQEnGVFASFVR 1533
Cdd:TIGR00957 1494 KGEVAEFGAPSNLLQQR-GIFYSMAK 1518
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
220-1534 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 769.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 220 VNLLSKATYWWMNTLIISAHKKPIDLKAIGKLPIAMRAVTNYVCLKDAYEEQKKKvadhpnrtPSIWL--AMYRAFGRPI 297
Cdd:PLN03130 232 ANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKK--------PKPWLlrALNNSLGGRF 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 298 LLSSTFRYLADLLGFAGPLCISGIVQRVnetQNGTNNTTGISETLSskeflenayvlavllflalilqrTFLQASYYVTI 377
Cdd:PLN03130 304 WLGGFFKIGNDLSQFVGPLLLNLLLESM---QNGEPAWIGYIYAFS-----------------------IFVGVVLGVLC 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 378 E---------TGINLRGALLAMIYNKILRLStsNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILL 448
Cdd:PLN03130 358 EaqyfqnvmrVGFRLRSTLVAAVFRKSLRLT--HEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 449 YNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSS 528
Cdd:PLN03130 436 YQQLGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSW 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 529 LKTFALYTSLSIFMNAAIPIAAVLATFVTHAYASGNnLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKLNEF 608
Cdd:PLN03130 516 FRKAQLLSAFNSFILNSIPVLVTVVSFGVFTLLGGD-LTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEEL 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 609 LLSDEigddswRTGESSLPFESCkkhtgvqpktinrkQPgryhldsyeqstrrlrpaetediAIKVTNGYFSWGSGL--A 686
Cdd:PLN03130 595 LLAEE------RVLLPNPPLEPG--------------LP-----------------------AISIKNGYFSWDSKAerP 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 687 TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKvhwSNRNRYSVAYAAQKPWLLNATVEENITFGSPFNKQ 766
Cdd:PLN03130 632 TLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDA---SVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 767 RYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFL 846
Cdd:PLN03130 709 RYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDEL 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 847 QddKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIqTKDVELYehwKTLMNR---------------QDQELEKD 911
Cdd:PLN03130 789 R--GKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEEL-SNNGPLF---QKLMENagkmeeyveengeeeDDQTSSKP 862
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 912 MEADQTTLERKTLRRAMYSREAKAQMededeeeeeeededdnMSTVMRLRTKMPWKTCWRYLTS-GGFFLLILMIFSKLL 990
Cdd:PLN03130 863 VANGNANNLKKDSSSKKKSKEGKSVL----------------IKQEERETGVVSWKVLERYKNAlGGAWVVMILFLCYVL 926
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 991 KHSVIVAIDYWLATWTSEYSINNTGKAdqtYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRF 1070
Cdd:PLN03130 927 TEVFRVSSSTWLSEWTDQGTPKTHGPL---FYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSF 1003
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1071 FDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQKYFRVASKDLQEL 1150
Cdd:PLN03130 1004 FHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVKRL 1083
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1151 DDSTQLPLLCHFSETAEGLTTIRAFRHetrfKQRMLELTDT---NNIAYLFLS-AANRWLEVRTDYLGACIV-LTASIA- 1224
Cdd:PLN03130 1084 DSITRSPVYAQFGEALNGLSTIRAYKA----YDRMAEINGRsmdNNIRFTLVNmSSNRWLAIRLETLGGLMIwLTASFAv 1159
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1225 -----SISGSSNSGLVGLGLLYALTITNYLNWVVRnLADL-EVQMGAVKKVNSFLTMESENyEGTMDPSQVPEHWPQEGE 1298
Cdd:PLN03130 1160 mqngrAENQAAFASTMGLLLSYALNITSLLTAVLR-LASLaENSLNAVERVGTYIDLPSEA-PLVIENNRPPPGWPSSGS 1237
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1378
Cdd:PLN03130 1238 IKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGI 1317
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1379 ILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILI 1458
Cdd:PLN03130 1318 IPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILV 1397
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530398972 1459 MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQENGVFASFVRA 1534
Cdd:PLN03130 1398 LDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQS 1473
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
221-1534 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 736.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 221 NLLSKATYWWMNTLIISAHKKPIDLKAIGKLPIAMRAVTNYVCLKDAYEEQkkkvadhpNRTPSIWL--AMYRAFGRPIL 298
Cdd:PLN03232 233 SIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEE--------SRRPKPWLlrALNNSLGGRFW 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 299 LSSTFRYLADLLGFAGPLCISGIVQRVNEtqngtNNTTGISETLSSKEFLENAYVlavllflalilqrTFLQASYYVTI- 377
Cdd:PLN03232 305 LGGIFKIGHDLSQFVGPVILSHLLQSMQE-----GDPAWVGYVYAFLIFFGVTFG-------------VLCESQYFQNVg 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 378 ETGINLRGALLAMIYNKILRLStsNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSAL 457
Cdd:PLN03232 367 RVGFRLRSTLVAAIFHKSLRLT--HEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 458 VGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTS 537
Cdd:PLN03232 445 FGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSA 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 538 LSIFMNAAIPIAAVLATFVTHAYASGNnLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKLNEFLLSDEigdd 617
Cdd:PLN03232 525 FNSFILNSIPVVVTLVSFGVFVLLGGD-LTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEE---- 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 618 swRTGESSLPFesckkhtgvqpktinrkQPGRyhldsyeqstrrlrPAetediaIKVTNGYFSWGSGLA--TLSNIDIRI 695
Cdd:PLN03232 600 --RILAQNPPL-----------------QPGA--------------PA------ISIKNGYFSWDSKTSkpTLSDINLEI 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 696 PTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKvhwSNRNRYSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDAC 775
Cdd:PLN03232 641 PVGSLVAIVGGTGEGKTSLISAMLGELSHAETS---SVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVT 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 776 SLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDdkRTLVL 855
Cdd:PLN03232 718 ALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKG--KTRVL 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 856 VTHKLQYLTHADWIIAMKDGSVLREGTLKDIqTKDVELYehwKTLM------------NRQDQELEKDMEADQTTLERKT 923
Cdd:PLN03232 796 VTNQLHFLPLMDRIILVSEGMIKEEGTFAEL-SKSGSLF---KKLMenagkmdatqevNTNDENILKLGPTVTIDVSERN 871
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 924 LRRAMYSREAKAQMEDEDEeeeeeededdnmstvmRLRTKMPWKTCWRYLTS-GGFFLLILMIFSKLLKHSVIVAIDYWL 1002
Cdd:PLN03232 872 LGSTKQGKRGRSVLVKQEE----------------RETGIISWNVLMRYNKAvGGLWVVMILLVCYLTTEVLRVSSSTWL 935
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1003 ATWTSEYSINNTGKAdqtYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNR 1082
Cdd:PLN03232 936 SIWTDQSTPKSYSPG---FYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINR 1012
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1083 FSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHF 1162
Cdd:PLN03232 1013 FSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQF 1092
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1163 SETAEGLTTIRAFRHETRFKQRMLELTDtNNIAY-LFLSAANRWLEVRTDYLGACIV-LTASIASISGSSNSGLVG---- 1236
Cdd:PLN03232 1093 GEALNGLSSIRAYKAYDRMAKINGKSMD-NNIRFtLANTSSNRWLTIRLETLGGVMIwLTATFAVLRNGNAENQAGfast 1171
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1237 LGLL--YALTITNYLNWVVRNLADLEVQMGAVKKVNSFLTMESENyEGTMDPSQVPEHWPQEGEIKIHDLCVRYENNLKP 1314
Cdd:PLN03232 1172 MGLLlsYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEA-TAIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPP 1250
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1315 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 1394
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI 1330
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1395 DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENIL 1474
Cdd:PLN03232 1331 DPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLI 1410
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1475 QKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQENGVFASFVRA 1534
Cdd:PLN03232 1411 QRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHS 1470
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
365-1534 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 672.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 365 QRTFLQASYYVTIETGINLRGALLAMIYNKILRLSTSNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMG 444
Cdd:PTZ00243 298 QSVCLHRFYYISIRCGLQYRSALNALIFEKCFTISSKSLAQPDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLS 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 445 VILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMK 524
Cdd:PTZ00243 378 ILLLSRLVGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRAR 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 525 ELSSLKTFALYTSLSIFMNAAIPIAAVLATFVTHaYASGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQK 604
Cdd:PTZ00243 458 ELRYLRDVQLARVATSFVNNATPTLMIAVVFTVY-YLLGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKR 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 605 LNEFLLSDE-----IGD--DSWRTGESS----------------------LPF------------------ESCKKHTGV 637
Cdd:PTZ00243 537 ISTFLECDNatcstVQDmeEYWREQREHstacqlaavlenvdvtafvpvkLPRapkvktsllsralrmlccEQCRPTKRH 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 638 QPKTI---------------NRKQPGRYHLDSyEQSTrrlrPAETEDIAIKVTNGYFSWGSGLaTLSNIDIRIPTGQLTM 702
Cdd:PTZ00243 617 PSPSVvvedtdygspssasrHIVEGGTGGGHE-ATPT----SERSAKTPKMKTDDFFELEPKV-LLRDVSVSVPRGKLTV 690
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 703 IVGQVGCGKSSLLLAILGEMQTLEGKVhWSNRnrySVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDID 782
Cdd:PTZ00243 691 VLGATGSGKSTLLQSLLSQFEISEGRV-WAER---SIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLA 766
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 783 LLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDdkRTLVLVTHKLQY 862
Cdd:PTZ00243 767 QLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAG--KTRVLATHQVHV 844
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 863 LTHADWIIAMKDGSVLREGTLKD-IQTkdvELYEHWKT-LMNRQDQElEKDMEADQTTLER-KTLRRAMYSREAKAQMED 939
Cdd:PTZ00243 845 VPRADYVVALGDGRVEFSGSSADfMRT---SLYATLAAeLKENKDSK-EGDADAEVAEVDAaPGGAVDHEPPVAKQEGNA 920
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 940 EDEEEEEEEDEDDNMSTVMRLRTKM-PWKTCWRYLTS-GGFFLLILMIFSKLLKHSVIVAIDYWLATWTSeysiNNTGKA 1017
Cdd:PTZ00243 921 EGGDGAALDAAAGRLMTREEKASGSvPWSTYVAYLRFcGGLHAAGFVLATFAVTELVTVSSGVWLSMWST----RSFKLS 996
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1018 DQTY-YV-AGFSILCGAGIFLCLVTSLTVEWMGltaAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIP 1095
Cdd:PTZ00243 997 AATYlYVyLGIVLLGTFSVPLRFFLSYEAMRRG---SRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLP 1073
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1096 PTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAF 1175
Cdd:PTZ00243 1074 MSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAY 1153
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1176 RHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACIVLT------ASIASISGSSNSGLVGLGLLYALTITNYL 1249
Cdd:PTZ00243 1154 GKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVialigvIGTMLRATSQEIGLVSLSLTMAMQTTATL 1233
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1250 NWVVRNLADLEVQMGAVKKVNSF--------------LTMESENYEGT---------MDPSQVPEHWP---QEGEIKIHD 1303
Cdd:PTZ00243 1234 NWLVRQVATVEADMNSVERLLYYtdevphedmpeldeEVDALERRTGMaadvtgtvvIEPASPTSAAPhpvQAGSLVFEG 1313
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1304 LCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDP 1383
Cdd:PTZ00243 1314 VQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDP 1393
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1384 ILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILI-MDEA 1462
Cdd:PTZ00243 1394 VLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFIlMDEA 1473
|
1210 1220 1230 1240 1250 1260 1270
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398972 1463 TASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQENGVFASFVRA 1534
Cdd:PTZ00243 1474 TANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVEA 1545
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1297-1536 |
2.45e-172 |
|
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: 516.38 E-value: 2.45e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1297 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1376
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1377 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 1456
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1457 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQENGVFASFVRADM 1536
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVRTDK 257
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
672-876 |
7.24e-149 |
|
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: 452.56 E-value: 7.24e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN-------------RNRYS 738
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNknesepsfeatrsRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 739 VAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTN 818
Cdd:cd03290 81 VAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 530398972 819 IVFLDDPFSALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGS 876
Cdd:cd03290 161 IVFLDDPFSALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
221-1523 |
5.18e-141 |
|
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: 471.70 E-value: 5.18e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 221 NLLSKATYWWMNTLIISAHKKPIDLKAIGKLPIAMRAVTnyvcLKDAYEEQKKKVADHPNRTPSIWLAMYRAFGRPILLS 300
Cdd:TIGR01271 10 NFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADN----LSERLEREWDRELASAKKNPKLLNALRRCFFWRFVFY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 301 STFRYLADLLGFAGPLCISGIVQRVNEtqngtnnttgisetlSSKEFLENAYVLAVLLFLALILQRTFLQASYYVTIETG 380
Cdd:TIGR01271 86 GILLYFGEATKAVQPLLLGRIIASYDP---------------FNAPEREIAYYLALGLCLLFIVRTLLLHPAIFGLHHLG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 381 INLRGALLAMIYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSALVGA 460
Cdd:TIGR01271 151 MQMRIALFSLIYKKTLKLSSRVLD--KISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 461 AVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFAlytSLSI 540
Cdd:TIGR01271 229 GFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIA---YLRY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 541 FMNAAIPIAAVLATF---VTHAYASGNNLKpaEAFASLSLFHIL-VTPLFLLSTVVRFAVKAIISVQKLNEFLLSDEigd 616
Cdd:TIGR01271 306 FYSSAFFFSGFFVVFlsvVPYALIKGIILR--RIFTTISYCIVLrMTVTRQFPGAIQTWYDSLGAITKIQDFLCKEE--- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 617 dsWRTGESSLpfesckkhTGVQPKTINRKQpgryhldSYEQSTRRL-RPAETEDIAIKVTNG----YFSWGSGLAT--LS 689
Cdd:TIGR01271 381 --YKTLEYNL--------TTTEVEMVNVTA-------SWDEGIGELfEKIKQNNKARKQPNGddglFFSNFSLYVTpvLK 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 690 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRnrysVAYAAQKPWLLNATVEENITFGSPFNKQRYK 769
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR----ISFSPQTSWIMPGTIKDNIIFGLSYDEYRYT 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 770 AVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDd 849
Cdd:TIGR01271 520 SVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSN- 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 850 kRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKD---------VELYEHWK----------TLM--------- 901
Cdd:TIGR01271 599 -KTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRpdfsslllgLEAFDNFSaerrnsilteTLRrvsidgdst 677
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 902 ----------------------------------NRQDQELEKDMEADQTT---------LERK------------TLRR 926
Cdd:TIGR01271 678 vfsgpetikqsfkqpppefaekrkqsiilnpiasARKFSFVQMGPQKAQATtiedavrepSERKfslvpedeqgeeSLPR 757
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 927 A-MYSREAKAQMEDEDEEEEEEEDEDDNMSTVMRLRT---KM-------------------------------------- 964
Cdd:TIGR01271 758 GnQYHHGLQHQAQRRQSVLQLMTHSNRGENRREQLQTsfrKKssitqqnelaseldiysrrlskdsvyeiseeineedlk 837
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 965 --------------PWKTCWRYLTSGG--FFLLI--LMIFSKLLKHSVIVaidYWLATWTSEYSINNTGK-ADQTYYVAG 1025
Cdd:TIGR01271 838 ecfaderenvfettTWNTYLRYITTNRnlVFVLIfcLVIFLAEVAASLLG---LWLITDNPSAPNYVDQQhANASSPDVQ 914
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1026 FSILCGAG-----IFLCLVTSLTVEWMG-----------LTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNI 1089
Cdd:TIGR01271 915 KPVIITPTsayyiFYIYVGTADSVLALGffrglplvhtlLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAI 994
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1090 IDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGL 1169
Cdd:TIGR01271 995 IDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGL 1074
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1170 TTIRAFRHETRFK---QRMLELTDTNNIAYLflsAANRWLEVRTDYLGACIVLTASIASISGSSNSG-LVGLGLLYALTI 1245
Cdd:TIGR01271 1075 WTIRAFGRQSYFEtlfHKALNLHTANWFLYL---STLRWFQMRIDIIFVFFFIAVTFIAIGTNQDGEgEVGIILTLAMNI 1151
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1246 TNYLNWVVRNLADLEVQMGAVKKVNSFLTMESENYEGT-------------MDPSQVPEHWPQEGEIKIHDLCVRYENNL 1312
Cdd:TIGR01271 1152 LSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRPSggggkyqlstvlvIENPHAQKCWPSGGQMDVQGLTAKYTEAG 1231
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1313 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRF 1392
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRK 1310
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1393 NLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEN 1472
Cdd:TIGR01271 1311 NLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQ 1390
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|.
gi 530398972 1473 ILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1523
Cdd:TIGR01271 1391 IIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNE 1441
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
299-605 |
1.37e-137 |
|
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: 426.27 E-value: 1.37e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 299 LSSTFRYLADLLGFAGPLCISGIVQRVNETQNGTNNTTGISET--LSSKEFLENAYVLAVLLFLALILQRTFLQASYYVT 376
Cdd:cd18591 1 LGGILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNSTDKLSVsyVTVEEFFSNGYVLAVILFLALLLQATFSQASYHIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 377 IETGINLRGALLAMIYNKILRLSTSNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSA 456
Cdd:cd18591 81 IREGIRLKTALQAMIYEKALRLSSWNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 457 LVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYT 536
Cdd:cd18591 161 LIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYW 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398972 537 SLSIFMNAAIPIAAVLATFVTHAYASGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 605
Cdd:cd18591 241 SLMTFLTQASPILVTLVTFGLYPYLEGEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1297-1517 |
4.43e-129 |
|
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: 399.56 E-value: 4.43e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1297 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1376
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1377 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 1456
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398972 1457 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTP 1517
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
982-1273 |
1.58e-123 |
|
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: 388.11 E-value: 1.58e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 982 ILMIFSKLLKHSVIVAIDYWLATWTSE----------YSINNTGKADQTYYVAGFSILCGAGIFLCLVTSLTVEWMGLTA 1051
Cdd:cd18602 2 ALVLALALLKQGLRVATDFWLADWTEAnhdvasvvfnITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGELAGLRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1052 AKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGV 1131
Cdd:cd18602 82 ARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIII 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1132 AFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTD 1211
Cdd:cd18602 162 VYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRLD 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530398972 1212 YLGACIVL----TASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFL 1273
Cdd:cd18602 242 YLGAVIVFlaalSSLTAALAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
672-876 |
4.56e-106 |
|
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: 335.59 E-value: 4.56e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWGSGLA----TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNrnrySVAYAAQKPW 747
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG----SIAYVSQEPW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 748 LLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 827
Cdd:cd03250 77 IQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 530398972 828 ALDIHLSDHLMQEGILKFLQDDKrTLVLVTHKLQYLTHADWIIAMKDGS 876
Cdd:cd03250 157 AVDAHVGRHIFENCILGLLLNNK-TRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
958-1534 |
5.43e-102 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 339.06 E-value: 5.43e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 958 MRLRTKMPWKTCWRYLtSGGFFLLILMIFSKLLKHSVIVAIDYWLATWTSEYSinNTGKADQTYYVAGFSILCGAGIFLC 1037
Cdd:COG1132 1 MSKSPRKLLRRLLRYL-RPYRGLLILALLLLLLSALLELLLPLLLGRIIDALL--AGGDLSALLLLLLLLLGLALLRALL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1038 -LVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMIS 1116
Cdd:COG1132 78 sYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1117 YATP----VFLVALLPLGVAFYFIQKYFRVASKDLQE-LDDSTQlpllcHFSETAEGLTTIRAFRHETRFKQRMLELTDT 1191
Cdd:COG1132 158 VIDWrlalIVLLVLPLLLLVLRLFGRRLRKLFRRVQEaLAELNG-----RLQESLSGIRVVKAFGREERELERFREANEE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1192 NNIAYLFLSAANRWLEVRTDYLGACIVLTasiasisgssnsgLVGLG-----------------LLYALTITNYLNWVVR 1254
Cdd:COG1132 233 LRRANLRAARLSALFFPLMELLGNLGLAL-------------VLLVGgllvlsgsltvgdlvafILYLLRLFGPLRQLAN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1255 NLADLEVQMGAVKKVNSFLTMESENYEGTmDPSQVPehwPQEGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGR 1334
Cdd:COG1132 300 VLNQLQRALASAERIFELLDEPPEIPDPP-GAVPLP---PVRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1335 TGSGKSSL-SLaFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPECkcTDDRLWEALE 1410
Cdd:COG1132 375 SGSGKSTLvNL-LLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRPDA--TDEEVEEAAK 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1411 IAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTI 1490
Cdd:COG1132 452 AAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVI 531
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 530398972 1491 AHRVHTILTADLVIVMKRGNILEYDTPESLLAQeNGVFASFVRA 1534
Cdd:COG1132 532 AHRLSTIRNADRILVLDDGRIVEQGTHEELLAR-GGLYARLYRL 574
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1293-1517 |
4.53e-90 |
|
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: 290.85 E-value: 4.53e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1293 WPQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTL 1372
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1373 RSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEiaqlknmvkslpggldavVTEGGENFSVGQRQLFCLARAFVR 1452
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398972 1453 KSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTP 1517
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
977-1272 |
8.55e-82 |
|
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: 270.91 E-value: 8.55e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 977 GFFLLILMIFSKLLKHSVIVAIDYWLATWTSEYSINNTgkadqTYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLH 1056
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSG-----YYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1057 HNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFI 1136
Cdd:cd18580 76 DKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1137 QKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGAC 1216
Cdd:cd18580 156 QRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGAL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 530398972 1217 IV--LTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSF 1272
Cdd:cd18580 236 LAlvVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEY 293
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1023-1533 |
5.68e-81 |
|
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: 282.88 E-value: 5.68e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1023 VAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSaDTNIIDQHIP-PTLESL 1101
Cdd:COG2274 199 AIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTgSLLTAL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1102 TRSTLLCLSAIGMISYATPVFLVALLPLGVAF---YFIQKYFRVASKDLQELDDSTQLpllcHFSETAEGLTTIRAFRHE 1178
Cdd:COG2274 278 LDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVllgLLFQPRLRRLSREESEASAKRQS----LLVETLRGIETIKALGAE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1179 TRFKQRMLELTdtnnIAYLFLSAANRWLEVRTDYLGACIvltasiasisgssnSGLVGLGLLYA---------LTI---- 1245
Cdd:COG2274 354 SRFRRRWENLL----AKYLNARFKLRRLSNLLSTLSGLL--------------QQLATVALLWLgaylvidgqLTLgqli 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1246 -TNYLNWV----VRNLADL--EVQM--GAVKKVNSFLTMESENYEGTmDPSQVPEhwpQEGEIKIHDLCVRYENNLKPVL 1316
Cdd:COG2274 416 aFNILSGRflapVAQLIGLlqRFQDakIALERLDDILDLPPEREEGR-SKLSLPR---LKGDIELENVSFRYPGDSPPVL 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1317 KHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL-- 1394
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItl 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1395 -DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENI 1473
Cdd:COG2274 572 gDPDA--TDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAI 649
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1474 LQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQeNGVFASFVR 1533
Cdd:COG2274 650 ILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR-KGLYAELVQ 708
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
979-1260 |
1.48e-77 |
|
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: 258.95 E-value: 1.48e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 979 FLLILMIFskLLKHSVIVAIDYWLATWTSEYSINNTGKADQT-YYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHH 1057
Cdd:cd18603 1 SLLILLLY--LLSQAFSVGSNIWLSEWSDDPALNGTQDTEQRdYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1058 NLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQ 1137
Cdd:cd18603 79 KLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1138 KYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACI 1217
Cdd:cd18603 159 RFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLI 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 530398972 1218 VLTASIASISGSSNSG--LVGLGLLYALTITNYLNWVVRNLADLE 1260
Cdd:cd18603 239 VLFAALFAVLSRDSLSpgLVGLSISYALQITQTLNWLVRMTSELE 283
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
982-1273 |
3.60e-72 |
|
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: 243.53 E-value: 3.60e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 982 ILMIFSKLLKHSVIVAIDYWLATWTSEYSINNTGKADQ---TYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHN 1058
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEvsvLYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1059 LLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQK 1138
Cdd:cd18604 82 LLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1139 YFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACIV 1218
Cdd:cd18604 162 LYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFS 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 530398972 1219 L-TASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFL 1273
Cdd:cd18604 242 FaTAALLVYGPGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1297-1523 |
5.25e-72 |
|
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: 240.21 E-value: 5.25e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1297 GEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1376
Cdd:cd03254 1 GEIEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1377 SIILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 1453
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIrlgRPNA--TDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1454 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1523
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1105-1524 |
1.99e-69 |
|
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: 244.67 E-value: 1.99e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1105 TLLCLSAIGMISYATPVFLVALLPLGVAF-YFIQKYFRVASKD----LQELDDstqlpllcHFSETAEGLTTIRAFRHET 1179
Cdd:COG4988 146 PLLILVAVFPLDWLSGLILLVTAPLIPLFmILVGKGAAKASRRqwraLARLSG--------HFLDRLRGLTTLKLFGRAK 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1180 RFKQRMLELTDTNNIAYL------FLSAANrwLEVRTdYLGACIVLtasiasisgssnsGLVGLGLLYA-LTITN----- 1247
Cdd:COG4988 218 AEAERIAEASEDFRKRTMkvlrvaFLSSAV--LEFFA-SLSIALVA-------------VYIGFRLLGGsLTLFAalfvl 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1248 ------YLNwvVRNLAdleVQ-------MGAVKKVNSFLTMESEnyegTMDPSQVPEHWPQEGEIKIHDLCVRYENNlKP 1314
Cdd:COG4988 282 llapefFLP--LRDLG---SFyharangIAAAEKIFALLDAPEP----AAPAGTAPLPAAGPPSIELEDVSFSYPGG-RP 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1315 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 1394
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENL 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1395 ---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 1471
Cdd:COG4988 432 rlgRPDA--SDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETE 509
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 530398972 1472 NILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQE 1524
Cdd:COG4988 510 AEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
299-605 |
1.14e-68 |
|
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: 233.15 E-value: 1.14e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 299 LSSTFRYLADLLGFAGPLCISGIVQRVNETQNgtnnttgisetlsskEFLENAYVLAVLLFLALILQRTFLQASYYVTIE 378
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPD---------------EPLSEGYLLALALFLVSLLQSLLLHQYFFLSFR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 379 TGINLRGALLAMIYNKILRLSTSnlSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSALV 458
Cdd:cd18579 66 LGMRVRSALSSLIYRKALRLSSS--ARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 459 GAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTSL 538
Cdd:cd18579 144 GLGVLLLLIPLQAFLAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRAL 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398972 539 SIFMNAAIPIAAVLATFVTHAYaSGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 605
Cdd:cd18579 224 NSFLFFSTPVLVSLATFATYVL-LGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
978-1273 |
2.28e-66 |
|
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: 227.03 E-value: 2.28e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 978 FFLLILMIFSKllkhsviVAIDYWLATWTSEYSIN--NTGKADQTYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNL 1055
Cdd:cd18605 5 LLSLILMQASR-------NLIDFWLSYWVSHSNNSffNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1056 HHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYF 1135
Cdd:cd18605 78 HNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1136 IQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGA 1215
Cdd:cd18605 158 IQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGV 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398972 1216 CIV-----LTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFL 1273
Cdd:cd18605 238 LIVtfvalTAVVQHFFGLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1299-1509 |
6.90e-63 |
|
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: 211.86 E-value: 6.90e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1378
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1379 ILQDPILFSGSIRFNLdpeckctddrlwealeiaqlknmvkslpggldavvteggenFSVGQRQLFCLARAFVRKSSILI 1458
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 530398972 1459 MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRG 1509
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
978-1266 |
7.46e-63 |
|
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: 216.19 E-value: 7.46e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 978 FFLLILMIFSKllkhsviVAIDYWLATWTSeysinNTGKADQTYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHH 1057
Cdd:cd18606 5 LLLLILSQFAQ-------VFTNLWLSFWTE-----DFFGLSQGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1058 NLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQ 1137
Cdd:cd18606 73 KALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1138 KYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACI 1217
Cdd:cd18606 153 NYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 530398972 1218 VL--TASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAV 1266
Cdd:cd18606 233 VLivALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSV 283
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
365-605 |
5.60e-61 |
|
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: 210.79 E-value: 5.60e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 365 QRTFLQASYYVTIETGINLRGALLAMIYNKILRLStsNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMG 444
Cdd:cd18595 51 QSLLLHQYFHRCFRLGMRIRTALTSAIYRKALRLS--NSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 445 VILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMK 524
Cdd:cd18595 129 LYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 525 ELSSLKTFALYTSLSIFMNAAIPIAAVLATFVTHAYASGNN-LKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQ 603
Cdd:cd18595 209 ELKLLKKAAYLNAVSSFLWTCAPFLVSLATFATYVLSDPDNvLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLK 288
|
..
gi 530398972 604 KL 605
Cdd:cd18595 289 RL 290
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
977-1273 |
1.28e-60 |
|
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: 210.88 E-value: 1.28e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 977 GFFLLILMIFSKLLKHSVIVAIDYWLATW--------------TSEYSINNTGKADQTYYVAGFSILCGAGIFLCLVTSL 1042
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWlkqgsgnttnnvdnSTVDSGNISDNPDLNFYQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1043 TVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVF 1122
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1123 LVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAA 1202
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398972 1203 NRWLEVRTDYLGACIVLTASIASISGSSNS--GLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFL 1273
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLKGSIspAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1299-1530 |
3.47e-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: 200.92 E-value: 3.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1378
Cdd:cd03253 1 IEFENVTFAYDPG-RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1379 ILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 1455
Cdd:cd03253 80 VPQDTVLFNDTIGYNIrygRPDA--TDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398972 1456 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAqENGVFAS 1530
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLA-KGGLYAE 231
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1299-1529 |
1.19e-57 |
|
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: 199.38 E-value: 1.19e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1378
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1379 ILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 1455
Cdd:cd03251 81 VSQDVFLFNDTVAENIaygRPGA--TREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398972 1456 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQeNGVFA 1529
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ-GGVYA 231
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1023-1530 |
1.47e-57 |
|
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: 209.96 E-value: 1.47e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1023 VAGFSILCGAGIFlclVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLT 1102
Cdd:TIGR02203 60 VIGLAVLRGICSF---VSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1103 RSTLLCLSAIGMI---SYATPVFLVALLPL-GVAFYFIQKYFRVASKDLQELD-DSTQLpllchFSETAEGLTTIRAFRH 1177
Cdd:TIGR02203 137 RETLTVIGLFIVLlyySWQLTLIVVVMLPVlSILMRRVSKRLRRISKEIQNSMgQVTTV-----AEETLQGYRVVKLFGG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1178 ETRFKQRmleltdtnniaYLFLSAANRWLEVRTDYLGACI-----VLTASIASISGSSNSGLVGLGLLYALTITNYLNWV 1252
Cdd:TIGR02203 212 QAYETRR-----------FDAVSNRNRRLAMKMTSAGSISspitqLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAM 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1253 ------VRNLADLEVQM----GAVKKVNSFLTMESENYEGTMDPSQVpehwpqEGEIKIHDLCVRYENNLKPVLKHVKAY 1322
Cdd:TIGR02203 281 ialirpLKSLTNVNAPMqrglAAAESLFTLLDSPPEKDTGTRAIERA------RGDVEFRNVTFRYPGRDRPALDSISLV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1323 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPEcK 1399
Cdd:TIGR02203 355 IEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRTE-Q 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1400 CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVM 1479
Cdd:TIGR02203 434 ADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALE 513
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 530398972 1480 TAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQeNGVFAS 1530
Cdd:TIGR02203 514 RLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLAR-NGLYAQ 563
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
371-882 |
1.93e-55 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 203.86 E-value: 1.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 371 ASYYVTIETGINLRGALLAMIYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFL-FLCPNLWAMPVQIIMGVILLY 449
Cdd:COG1132 80 LQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFD--RRRTGDLLSRLTNDVDAVEQFLaHGLPQLVRSVVTLIGALVVLF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 450 NLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWE----HIFCKSVEETRMKE 525
Cdd:COG1132 158 VIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREerelERFREANEELRRAN 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 526 LSSLKTFALYTSLSIFMNAAIpIAAVLAtFVTHAYASGNnLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 605
Cdd:COG1132 238 LRAARLSALFFPLMELLGNLG-LALVLL-VGGLLVLSGS-LTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERI 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 606 NEFL-LSDEIGDdswrtGESSLPFesckkhtgvqpktinrkqpgryhldsyeqstrrlrPAETEDIAIK-VTngyFSWGS 683
Cdd:COG1132 315 FELLdEPPEIPD-----PPGAVPL-----------------------------------PPVRGEIEFEnVS---FSYPG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN---------RYSVAYAAQKPWLLNATVE 754
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDirdltleslRRQIGVVPQDTFLFSGTIR 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 755 ENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHl 833
Cdd:COG1132 432 ENIRYGRPdATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTE- 510
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 530398972 834 SDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 882
Cdd:COG1132 511 TEALIQEALERLMKG--RTTIVIAHRLSTIRNADRILVLDDGRIVEQGT 557
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
368-605 |
2.62e-55 |
|
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: 194.59 E-value: 2.62e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 368 FLQASYYVTIETGINLRGALLAMIYNKILRLSTSnlSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVIL 447
Cdd:cd18597 59 LLNHFFYRSMLTGAQVRAALTKAIYRKSLRLSGK--SRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIAL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 448 LYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELS 527
Cdd:cd18597 137 LIVNLGPSALVGIGVLILSIPLQGFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELK 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530398972 528 SLKTFALYTSLSIFMNAAIPIAAVLATFVThAYASGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 605
Cdd:cd18597 217 YVRKLQILRSILTAVAFSLPVLASMLSFIT-YYATGHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1314-1534 |
5.58e-55 |
|
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: 191.60 E-value: 5.58e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1314 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFN 1393
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1394 L---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT 1470
Cdd:cd03249 97 IrygKPDA--TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398972 1471 ENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQEnGVFASFVRA 1534
Cdd:cd03249 175 EKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQK-GVYAKLVKA 237
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
367-898 |
7.87e-54 |
|
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: 201.99 E-value: 7.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 367 TFLQASYYVTIETGINLRgaLLAMIYNKILRLSTSNL---SMGEMtLGQINNLVAIE---TNQLMWFLFLCPNLWampvq 440
Cdd:COG2274 213 RLLRSYLLLRLGQRIDLR--LSSRFFRHLLRLPLSFFesrSVGDL-ASRFRDVESIReflTGSLLTALLDLLFVL----- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 441 IIMGVILLYNllGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYA--------WEH 512
Cdd:COG2274 285 IFLIVLFFYS--PPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGaesrfrrrWEN 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 513 IFCKSVEetrmKELSSLKTFALYTSLSIFMNAAIPIAAVL--ATFVTHayasgNNLKPAEAFASLSLFHILVTPLF-LLS 589
Cdd:COG2274 363 LLAKYLN----ARFKLRRLSNLLSTLSGLLQQLATVALLWlgAYLVID-----GQLTLGQLIAFNILSGRFLAPVAqLIG 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 590 TVVRFAvKAIISVQKLNEFLlsdeigddswrtgesSLPFEsckkhtgvqpktinrkqpgryhldsyEQSTRRLRPAETED 669
Cdd:COG2274 434 LLQRFQ-DAKIALERLDDIL---------------DLPPE--------------------------REEGRSKLSLPRLK 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 670 IAIKVTNGYFSW-GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN---------RYSV 739
Cdd:COG2274 472 GDIELENVSFRYpGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDlrqidpaslRRQI 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 740 AYAAQKPWLLNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTN 818
Cdd:COG2274 552 GVVLQDVFLFSGTIRENITLGDPdATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPR 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 819 IVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEHWK 898
Cdd:COG2274 632 ILILDEATSALDAE-TEAIILENLRRLLKG--RTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
367-603 |
4.76e-52 |
|
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: 185.78 E-value: 4.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 367 TFLQASYYVTIETGINLRGALLAMIYNKILRL-----------------STSNLSMGEMTLGQINNLVAIETN---QLMW 426
Cdd:cd18596 54 LLDQQYLWIGRRLSVRLRAILTQLIFEKALRRrdksgssksseskkkdkEEDEDEKSSASVGKINNLMSVDANrisEFAA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 427 FLFLcpnLWAMPVQIIMGVILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLK 506
Cdd:cd18596 134 FLHL---LVSAPLQIVIAIVFLYRLLGWSALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIK 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 507 LYAWEHIFCKSVEETRMKELSSLKTFALYTSLSIFMNAAIPIAAVLATFVTHAYASGNNLKPAEAFASLSLFHILVTPLF 586
Cdd:cd18596 211 FFAWERKWEERILEAREEELKWLRKRFLLDLLLSLLWFLIPILVTVVTFATYTLVMGQELTASVAFTSLALFNMLRGPLN 290
|
250
....*....|....*..
gi 530398972 587 LLSTVVRFAVKAIISVQ 603
Cdd:cd18596 291 VLPELITQLLQAKVSLD 307
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
977-1269 |
7.16e-52 |
|
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: 185.60 E-value: 7.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 977 GFFLLILMIFSKLLKHSVIVAIDYWLATWTSEY---------------SINNTGKADQTYYVAGFSILCGAGIFLCLVTS 1041
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLEeklndttdrvqgensTNVDIEDLDRDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1042 LTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPV 1121
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1122 FLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAY-LFLs 1200
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWfLFL- 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398972 1201 AANRWLEVRTDYLGA--CIVLTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKV 1269
Cdd:cd18601 240 ATSRWLAVRLDALCAlfVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERV 310
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
970-1532 |
1.05e-51 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 195.71 E-value: 1.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 970 WRYLTSGGFFLLILMIFSKLLKHSVIVAIDYWLATWTSEYSINNTGKADQTYYVAGFSILCGAGIFLCLvtsltvewMGL 1049
Cdd:TIGR00958 160 WPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNYT--------MAR 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1050 TAAKnLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRS--TLLCLSAIgMIS---YATPVFLV 1124
Cdd:TIGR00958 232 INLR-IREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNlvMLLGLLGF-MLWlspRLTMVTLI 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1125 ALLPLGVAFYFIQKYFRVASKDLQE-LDDSTQLPLlchfsETAEGLTTIRAFRHE----TRFKQ---RMLELTDTNNIAY 1196
Cdd:TIGR00958 310 NLPLVFLAEKVFGKRYQLLSEELQEaVAKANQVAE-----EALSGMRTVRSFAAEegeaSRFKEaleETLQLNKRKALAY 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1197 LFLSAANRWLE----VRTDYLGACIVLTASIASISgssnsgLVGLgLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSF 1272
Cdd:TIGR00958 385 AGYLWTTSVLGmliqVLVLYYGGQLVLTGKVSSGN------LVSF-LLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEY 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1273 L--TMESENyEGTMDPSQVpehwpqEGEIKIHDLCVRYENNL-KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRM 1349
Cdd:TIGR00958 458 LdrKPNIPL-TGTLAPLNL------EGLIEFQDVSFSYPNRPdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNL 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1350 VDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAV 1428
Cdd:TIGR00958 531 YQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLtDTPDEEIMAAAKAANAHDFIMEFPNGYDTE 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1429 VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKvvMTAFADRTVVTIAHRVHTILTADLVIVMKR 1508
Cdd:TIGR00958 611 VGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKK 688
|
570 580
....*....|....*....|....
gi 530398972 1509 GNILEYDTPESLLAQEnGVFASFV 1532
Cdd:TIGR00958 689 GSVVEMGTHKQLMEDQ-GCYKHLV 711
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1297-1525 |
1.35e-51 |
|
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: 183.52 E-value: 1.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1297 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDGKIVIDGIDISKLPLHTLRSRL 1376
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1377 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 1456
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398972 1457 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQEN 1525
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKS 228
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1036-1524 |
2.87e-51 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 191.86 E-value: 2.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1036 LCLVTSLTVEWMGLTA-AKNLHHN---LLNKIILG----------------PIRFFDTTPLGLILNRFSADTNIIDQHIP 1095
Cdd:PRK10790 61 LGLVAGLAAAYVGLQLlAAGLHYAqslLFNRAAVGvvqqlrtdvmdaalrqPLSAFDTQPVGQLISRVTNDTEVIRDLYV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1096 PTLESLTRSTLLcLSA--IGMISYATPVFLVALL--PLGVAFYFIQKYF------RVASKdLQELDDStqlpllchFSET 1165
Cdd:PRK10790 141 TVVATVLRSAAL-IGAmlVAMFSLDWRMALVAIMifPAVLVVMVIYQRYstpivrRVRAY-LADINDG--------FNEV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1166 AEGLTTIRAFRHETRFKQRMLELTDTNNIAylflsaanRWLEVRTD--------YLGACIVLTASIASISGSSNSGlVGL 1237
Cdd:PRK10790 211 INGMSVIQQFRQQARFGERMGEASRSHYMA--------RMQTLRLDgfllrpllSLFSALILCGLLMLFGFSASGT-IEV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1238 GLLYALTitNYLNWVVRNLADLE-----VQMGAVKKVNSFLTMESENYEGTMDPSQVpehwpQEGEIKIHDLCVRYENNl 1312
Cdd:PRK10790 282 GVLYAFI--SYLGRLNEPLIELTtqqsmLQQAVVAGERVFELMDGPRQQYGNDDRPL-----QSGRIDIDNVSFAYRDD- 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1313 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRF 1392
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLA 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1393 NLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEN 1472
Cdd:PRK10790 434 NVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQ 513
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 530398972 1473 ILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQE 1524
Cdd:PRK10790 514 AIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQ 565
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
667-890 |
9.08e-50 |
|
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: 186.89 E-value: 9.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 667 TEDIAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN---------RY 737
Cdd:COG4988 332 AGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDlsdldpaswRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 738 SVAYAAQKPWLLNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQN 816
Cdd:COG4988 412 QIAWVPQNPYLFAGTIRENLRLGRPdASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRD 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398972 817 TNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKD 890
Cdd:COG4988 492 APLLLLDEPTAHLDAE-TEAEILQALRRLAKG--RTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1297-1511 |
2.87e-49 |
|
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: 174.70 E-value: 2.87e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1297 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1376
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1377 SIILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 1453
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNItlgAPLA--DDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 530398972 1454 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNI 1511
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1247-1530 |
1.10e-48 |
|
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: 184.64 E-value: 1.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1247 NYLNWVVR----NLADLEvQMGAVkkvnsfLTMESEnyegTMDPSQVPEHWPQEGEIKIHDLCVRYENNlKPVLKHVKAY 1322
Cdd:COG5265 313 NFLGFVYReirqALADME-RMFDL------LDQPPE----VADAPDAPPLVVGGGEVRFENVSFGYDPE-RPILKGVSFE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1323 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPECk 1399
Cdd:COG5265 381 VPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIaygRPDA- 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1400 cTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVM 1479
Cdd:COG5265 460 -SEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALR 538
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 530398972 1480 TAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQeNGVFAS 1530
Cdd:COG5265 539 EVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQ-GGLYAQ 588
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1273-1536 |
2.45e-48 |
|
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: 185.16 E-value: 2.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1273 LTMESENYEGTMDPSQVpehwpqEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDI 1352
Cdd:TIGR03797 432 LEALPEVDEAKTDPGKL------SGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTL----LRLLLG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1353 FD----GKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAV 1428
Cdd:TIGR03797 502 FEtpesGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTV 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1429 VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDmateNILQKVVMTAFA--DRTVVTIAHRVHTILTADLVIVM 1506
Cdd:TIGR03797 582 ISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALD----NRTQAIVSESLErlKVTRIVIAHRLSTIRNADRIYVL 657
|
250 260 270
....*....|....*....|....*....|
gi 530398972 1507 KRGNILEYDTPESLLAQEnGVFASFVRADM 1536
Cdd:TIGR03797 658 DAGRVVQQGTYDELMARE-GLFAQLARRQL 686
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
303-605 |
3.18e-47 |
|
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: 171.20 E-value: 3.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 303 FRYLADLLGFAGPLCISGIVQRVNETQNGTNNTTGISETLSSKEFLenayvlavllflalilqRTFLQASY-YVTIETGI 381
Cdd:cd18598 5 LKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLL-----------------GALLSSHYnFQMNKVSL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 382 NLRGALLAMIYNKILRLSTSnlSMGEMTLGQINNLVAIETNQLMWFlflCPNL---WAMPVQIIMGVILLYNLLGSSALV 458
Cdd:cd18598 68 KVRAALVTAVYRKALRVRSS--SLSKFSTGEIVNLMSTDADRIVNF---CPSFhdlWSLPLQIIVALYLLYQQVGVAFLA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 459 GAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTSL 538
Cdd:cd18598 143 GLVFALVLIPINKWIAKRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDAL 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398972 539 SIFMNAAIPIAAVLATFVTHAYaSGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 605
Cdd:cd18598 223 CVYFWATTPVLISILTFATYVL-MGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1307-1532 |
5.70e-47 |
|
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: 168.82 E-value: 5.70e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1307 RYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILF 1386
Cdd:cd03252 9 RYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1387 SGSIRFNL---DPECKCtdDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEAT 1463
Cdd:cd03252 89 NRSIRDNIalaDPGMSM--ERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398972 1464 ASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAqENGVFASFV 1532
Cdd:cd03252 167 SALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLA-ENGLYAYLY 234
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
1281-1533 |
1.81e-46 |
|
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: 179.75 E-value: 1.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1281 EGTMDPSQVPEHWPQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSlaffRMV----DIFDGK 1356
Cdd:TIGR03796 460 EPEGSAATSEPPRRLSGYVELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIA----KLVaglyQPWSGE 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1357 IVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPecKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGG 1433
Cdd:TIGR03796 536 ILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLtlwDP--TIPDADLVRACKDAAIHDVITSRPGGYDAELAEGG 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1434 ENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEnilqKVVMTAFADR--TVVTIAHRVHTILTADLVIVMKRGNI 1511
Cdd:TIGR03796 614 ANLSGGQRQRLEIARALVRNPSILILDEATSALDPETE----KIIDDNLRRRgcTCIIVAHRLSTIRDCDEIIVLERGKV 689
|
250 260
....*....|....*....|..
gi 530398972 1512 LEYDTPESLLAQEnGVFASFVR 1533
Cdd:TIGR03796 690 VQRGTHEELWAVG-GAYARLIR 710
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
688-926 |
1.66e-45 |
|
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: 166.19 E-value: 1.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRnrysVAYAAQKPWLLNATVEENITFGSPFNKQR 767
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR----ISFSSQFSWIMPGTIKENIIFGVSYDEYR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 768 YKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQ 847
Cdd:cd03291 129 YKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 848 DdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEHwktLMNRQdqelekdmEADQTTLERK----- 922
Cdd:cd03291 209 N--KTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSK---LMGYD--------TFDQFSAERRnsilt 275
|
....*
gi 530398972 923 -TLRR 926
Cdd:cd03291 276 eTLRR 280
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
368-605 |
1.31e-44 |
|
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: 163.50 E-value: 1.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 368 FLQASYYVTIETGINLRGALLAMIYNKILRLStsnlSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVIL 447
Cdd:cd18592 55 FFSLTWAISYRTGIRLRGAVLGLLYKKILRLR----SLGDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 448 LYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELS 527
Cdd:cd18592 131 STYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERK 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530398972 528 SLKTFALYTSLSIFMNAAIPIAAVLATFVTHaYASGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 605
Cdd:cd18592 211 ILEKAGYLQSISISLAPIVPVIASVVTFLAH-VALGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1263-1529 |
1.88e-44 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 171.36 E-value: 1.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1263 MGAVKKVNSFLTMESENYEGTMDPSQVpehwpqEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSL 1342
Cdd:PRK11176 312 MAACQTLFAILDLEQEKDEGKRVIERA------KGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTI 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1343 SLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPEC--KCTDDRLWEALEIAQLKNMVKS 1420
Cdd:PRK11176 386 ANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARteQYSREQIEEAARMAYAMDFINK 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1421 LPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTA 1500
Cdd:PRK11176 466 MDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKA 545
|
250 260
....*....|....*....|....*....
gi 530398972 1501 DLVIVMKRGNILEYDTPESLLAQeNGVFA 1529
Cdd:PRK11176 546 DEILVVEDGEIVERGTHAELLAQ-NGVYA 573
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1268-1534 |
9.64e-44 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 169.37 E-value: 9.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1268 KVNSFLTME-----SENYEGTMDPSQVpehwpqEGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSL 1342
Cdd:PRK13657 305 KLEEFFEVEdavpdVRDPPGAIDLGRV------KGAVEFDDVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1343 SLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVK 1419
Cdd:PRK13657 378 INLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIrvgRPDA--TDEEMRAAAERAQAHDFIE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1420 SLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILT 1499
Cdd:PRK13657 456 RKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRN 535
|
250 260 270
....*....|....*....|....*....|....*
gi 530398972 1500 ADLVIVMKRGNILEYDTPESLLAQeNGVFASFVRA 1534
Cdd:PRK13657 536 ADRILVFDNGRVVESGSFDELVAR-GGRFAALLRA 569
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
672-875 |
1.34e-42 |
|
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: 153.69 E-value: 1.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWGSGLA-TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN---------RYSVAY 741
Cdd:cd03228 1 IEFKNVSFSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDlrdldleslRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 742 AAQKPWLLNATVEENItfgspfnkqrykavtdacslqpdidllpfgdqteigerginLSGGQRQRICVARALYQNTNIVF 821
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 530398972 822 LDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDG 875
Cdd:cd03228 120 LDEATSALDPE-TEALILEALRALAKG--KTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1105-1506 |
9.26e-42 |
|
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: 162.07 E-value: 9.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1105 TLLCLSAIGMISYATPVFLVALLPLgVAFYFIQKYFRVASKDLQELDDSTQLPllCHFSETAEGLTTIRAFRHETRFKQR 1184
Cdd:TIGR02857 132 PLAILAAVFPQDWISGLILLLTAPL-IPIFMILIGWAAQAAARKQWAALSRLS--GHFLDRLRGLPTLKLFGRAKAQAAA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1185 MLELTD--------TNNIAylFLSAANrwLEVRTDyLGACIVLTAsiasisgssnsglVGLGLLY-------ALTI---- 1245
Cdd:TIGR02857 209 IRRSSEeyrertmrVLRIA--FLSSAV--LELFAT-LSVALVAVY-------------IGFRLLAgdldlatGLFVllla 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1246 -TNYLNwvVRNL-ADLEVQMGAVKKVNSFLTMESENyeGTMDPSQVPEHWPQEGEIKIHDLCVRYENNlKPVLKHVKAYI 1323
Cdd:TIGR02857 271 pEFYLP--LRQLgAQYHARADGVAAAEALFAVLDAA--PRPLAGKAPVTAAPASSLEFSGVSVAYPGR-RPALRPVSFTV 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1324 KPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPECkc 1400
Cdd:TIGR02857 346 PPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaRPDA-- 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1401 TDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMT 1480
Cdd:TIGR02857 424 SDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRA 503
|
410 420
....*....|....*....|....*.
gi 530398972 1481 AFADRTVVTIAHRVHTILTADLVIVM 1506
Cdd:TIGR02857 504 LAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
651-882 |
3.25e-41 |
|
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: 161.47 E-value: 3.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 651 HLDSYEQSTRRL------RPAETE---------DIAIKVTNGYFSW-GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSL 714
Cdd:COG4987 298 HLGRVRAAARRLnelldaPPAVTEpaepapapgGPSLELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 715 LLAILGEMQTLEGKVHWSNRN---------RYSVAYAAQKPWLLNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLL 784
Cdd:COG4987 378 LALLLRFLDPQSGSITLGGVDlrdldeddlRRRIAVVPQRPHLFDTTLRENLRLARPdATDEELWAALERVGLGDWLAAL 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 785 PFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDdkRTLVLVTHKLQYLT 864
Cdd:COG4987 458 PDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLAD-LLEALAG--RTVLLITHRLAGLE 534
|
250
....*....|....*...
gi 530398972 865 HADWIIAMKDGSVLREGT 882
Cdd:COG4987 535 RMDRILVLEDGRIVEQGT 552
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
368-606 |
1.99e-40 |
|
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: 151.63 E-value: 1.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 368 FLQASYYVTIETGINLRGALLAMIYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVIL 447
Cdd:cd18594 55 LHHPYFFGLHRYGMQLRIALSSLIYKKTLKLSSSALS--KITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 448 LYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELS 527
Cdd:cd18594 133 LWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 528 SLKTFALYTSLSIFMNAAIPIAAVLATFVTHAYaSGNNLKPAEAFASLSLFHILVTPL-FLLSTVVRFAVKAIISVQKLN 606
Cdd:cd18594 213 LIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVL-TGNTLTARKVFTVISLLNALRMTItRFFPESIQTLSESRVSLKRIQ 291
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
672-898 |
1.14e-39 |
|
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: 147.76 E-value: 1.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN---------RYSVAYA 742
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDirevtldslRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 743 AQKPWLLNATVEENITFGSP--FNKQRYKAVTDACsLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIV 820
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPdaTDEEVIEAAKAAQ-IHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530398972 821 FLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEHWK 898
Cdd:cd03253 160 LLDEATSALDTH-TEREIQAALRDVSKG--RTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWK 234
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1055-1534 |
6.77e-39 |
|
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: 156.44 E-value: 6.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1055 LHHNLLNKIILG--------PIRFFDTTPLGLILNRFSADTNIIDqhippTLESLTRSTLLCLSAIGMISYA-----TPV 1121
Cdd:TIGR01193 223 LGQRLSIDIILSyikhlfelPMSFFSTRRTGEIVSRFTDASSIID-----ALASTILSLFLDMWILVIVGLFlvrqnMLL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1122 FLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLpLLCHFSETAEGLTTIRAFRHE-TRFKQ----------RMLELTD 1190
Cdd:TIGR01193 298 FLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAV-LNSSIIEDLNGIETIKSLTSEaERYSKidsefgdylnKSFKYQK 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1191 TNNIAYLFLSAANRWLEVRTDYLGACIVLTASIAsisgssnsglVGLGLLYALTITNYLNwVVRNLADLEVQMGAVK--- 1267
Cdd:TIGR01193 377 ADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLT----------LGQLITFNALLSYFLT-PLENIINLQPKLQAARvan 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1268 -KVNSFLTMESE-NYEGTMDPSQVPEhwpqeGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLA 1345
Cdd:TIGR01193 446 nRLNEVYLVDSEfINKKKRTELNNLN-----GDIVINDVSYSYGYG-SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKL 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1346 FFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL--DPECKCTDDRLWEALEIAQLKNMVKSLPG 1423
Cdd:TIGR01193 520 LVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLllGAKENVSQDEIWAACEIAEIKDDIENMPL 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1424 GLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEnilQKVV--MTAFADRTVVTIAHRVHTILTAD 1501
Cdd:TIGR01193 600 GYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE---KKIVnnLLNLQDKTIIFVAHRLSVAKQSD 676
|
490 500 510
....*....|....*....|....*....|...
gi 530398972 1502 LVIVMKRGNILEYDTPESLLAQeNGVFASFVRA 1534
Cdd:TIGR01193 677 KIIVLDHGKIIEQGSHDELLDR-NGFYASLIHN 708
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1294-1493 |
2.70e-38 |
|
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: 151.74 E-value: 2.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1294 PQEGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLR 1373
Cdd:TIGR02868 330 LGKPTLELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1374 SRLSIILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAF 1450
Cdd:TIGR02868 409 RRVSVCAQDAHLFDTTVRENLrlaRPDA--TDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARAL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 530398972 1451 VRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR 1493
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
672-882 |
3.34e-38 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 143.13 E-value: 3.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN---------RYSVAYA 742
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDirdisrkslRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 743 AQKPWLLNATVEENITFGSPFNKQ-RYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVF 821
Cdd:cd03254 83 LQDTFLFSGTIMENIRLGRPNATDeEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398972 822 LDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 882
Cdd:cd03254 163 LDEATSNIDTE-TEKLIQEALEKLMKG--RTSIIIAHRLSTIKNADKILVLDDGKIIEEGT 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
686-881 |
8.90e-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: 138.88 E-value: 8.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 686 ATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN---------RYSVAYAAQKPWLLNATVEEN 756
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDirqldpadlRRNIGYVPQDVTLFYGTLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 757 ITFGSPF-NKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD 835
Cdd:cd03245 98 ITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 530398972 836 HLMQEgiLKFLQDDKrTLVLVTHKLQYLTHADWIIAMKDGSVLREG 881
Cdd:cd03245 178 RLKER--LRQLLGDK-TLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1264-1534 |
9.99e-37 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 148.07 E-value: 9.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1264 GAVKKVNSFLTMESEnyegTMDPSQVPEHWPQEGEIKIHDLCVrYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLS 1343
Cdd:PRK11174 319 GAAESLVTFLETPLA----HPQQGEKELASNDPVTIEAEDLEI-LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1344 ---LAFFRmvdiFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNM 1417
Cdd:PRK11174 394 nalLGFLP----YQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVllgNPDA--SDEQLQQALENAWVSEF 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1418 VKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTI 1497
Cdd:PRK11174 468 LPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDL 547
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 530398972 1498 LTADLVIVMKRGNILE---YDTpeslLAQENGVFASFVRA 1534
Cdd:PRK11174 548 AQWDQIWVMQDGQIVQqgdYAE----LSQAGGLFATLLAH 583
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
682-882 |
4.45e-36 |
|
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: 137.36 E-value: 4.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 682 GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN---------RYSVAYAAQKPWLLNAT 752
Cdd:cd03251 12 GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDvrdytlaslRRQIGLVSQDVFLFNDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 753 VEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 831
Cdd:cd03251 92 VAENIAYGRPgATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 530398972 832 HlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 882
Cdd:cd03251 172 E-SERLVQAALERLMKN--RTTFVIAHRLSTIENADRIVVLEDGKIVERGT 219
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1294-1529 |
1.59e-35 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 144.20 E-value: 1.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1294 PQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLR 1373
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1374 SRLSIILQDPILFSGSIRFNL---DPEckCTDDRLWEALEIAQLKNMVKSlPGGLDAVVTEGGENFSVGQRQLFCLARAF 1450
Cdd:PRK11160 414 QAISVVSQRVHLFSATLRDNLllaAPN--ASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARAL 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1451 VRKSSILIMDEATASIDMATEN-ILQkVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQENGVFA 1529
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERqILE-LLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQ 569
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
667-896 |
1.41e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 133.29 E-value: 1.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 667 TEDIAIKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN----RYSVAYA 742
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPV-LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPprraRRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 743 AQK---PWLLNATVEE--------NITFGSPFNKQRYKAVTDACSLqpdIDLLPFGDQTeIGErginLSGGQRQRICVAR 811
Cdd:COG1121 81 PQRaevDWDFPITVRDvvlmgrygRRGLFRRPSRADREAVDEALER---VGLEDLADRP-IGE----LSGGQQQRVLLAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 812 ALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYL-THADWIIAMKDGsVLREGTLKDIQTKD 890
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYE--LLRELRREGKTILVVTHDLGAVrEYFDRVLLLNRG-LVAHGPPEEVLTPE 229
|
....*...
gi 530398972 891 V--ELYEH 896
Cdd:COG1121 230 NlsRAYGG 237
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
688-882 |
1.82e-34 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 132.66 E-value: 1.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN---------RYSVAYAAQKPWLLNATVEENIT 758
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDirdlnlrwlRSQIGLVSQEPVLFDGTIAENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 759 FGSPFNKQryKAVTDACSL---QPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSD 835
Cdd:cd03249 99 YGKPDATD--EEVEEAAKKaniHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE-SE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 530398972 836 HLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 882
Cdd:cd03249 176 KLVQEALDRAMKG--RTTIVIAHRLSTIRNADLIAVLQNGQVVEQGT 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
652-872 |
3.33e-34 |
|
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: 139.34 E-value: 3.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 652 LDSYEQSTRRLRPA-ETEDIAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV- 729
Cdd:TIGR02857 301 LDAAPRPLAGKAPVtAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIa 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 730 ------------HWsnrnRYSVAYAAQKPWLLNATVEENITFGSPFNKQ-RYKAVTDACSLQPDIDLLPFGDQTEIGERG 796
Cdd:TIGR02857 381 vngvpladadadSW----RDQIAWVPQHPFLFAGTIAENIRLARPDASDaEIREALERAGLDEFVAALPQGLDTPIGEGG 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530398972 797 INLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAM 872
Cdd:TIGR02857 457 AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAE-TEAEVLEALRALAQG--RTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1287-1511 |
5.04e-34 |
|
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: 131.05 E-value: 5.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1287 SQVPEHWpqEGEIKIHDLCVRYENNL-KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIS 1365
Cdd:cd03248 2 SLAPDHL--KGIVKFQNVTFAYPTRPdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1366 KLPLHTLRSRLSIILQDPILFSGSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLF 1444
Cdd:cd03248 80 QYEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQsCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398972 1445 CLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNI 1511
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1299-1511 |
1.19e-33 |
|
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: 128.10 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAffrMVDIF---DGKIVIDGIDISKLPLHTLRSR 1375
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARL---ILGLLrptSGRVRLDGADISQWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1376 LSIILQDPILFSGSIRFNLdpeckctddrlwealeiaqlknmvkslpggldavvteggenFSVGQRQLFCLARAFVRKSS 1455
Cdd:cd03246 78 VGYLPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 530398972 1456 ILIMDEATASIDMATEN-ILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNI 1511
Cdd:cd03246 117 ILVLDEPNSHLDVEGERaLNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
372-579 |
1.26e-33 |
|
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: 131.96 E-value: 1.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 372 SYYVTIETGINLRGALLAMIYNKILRLSTSnlSMGEMTLGQINNLVAIETNQL-MWFLFLcPNLWAMPVQIIMGVILLYN 450
Cdd:cd18593 60 YFFGMQRIGMRLRVACSSLIYRKALRLSQA--ALGKTTVGQIVNLLSNDVNRFdQAVLFL-HYLWVAPLQLIAVIYILWF 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 451 LLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLK 530
Cdd:cd18593 137 EIGWSCLAGLAVLLILIPLQSFFGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVR 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 530398972 531 TFALYTSlsifMNAAIPIAA----VLATFVTHAYaSGNNLKPAEAFASLSLFH 579
Cdd:cd18593 217 RTSFLRA----LNMGLFFVSskliLFLTFLAYIL-LGNILTAERVFVTMALYN 264
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1299-1523 |
3.25e-33 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 137.15 E-value: 3.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCvrYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1378
Cdd:PRK10789 316 VNIRQFT--YPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1379 ILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSIL 1457
Cdd:PRK10789 394 VSQTPFLFSDTVANNIALGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398972 1458 IMDEATASIDMATE-NILQKVVMTAfADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1523
Cdd:PRK10789 474 ILDDALSAVDGRTEhQILHNLRQWG-EGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQ 539
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
688-894 |
4.55e-33 |
|
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: 129.01 E-value: 4.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN--RYS-------VAYAAQK---PWLLnaTVEE 755
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDlaSLSrrelarrIAYVPQEppaPFGL--TVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 756 NITFG--------SPFNKQRYKAVTDACslqpdidllpfgDQTEIG---ERGIN-LSGGQRQRICVARALYQNTNIVFLD 823
Cdd:COG1120 95 LVALGryphlglfGRPSAEDREAVEEAL------------ERTGLEhlaDRPVDeLSGGERQRVLIARALAQEPPLLLLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530398972 824 DPFSALDIHlsdHlmQEGILKFLQD----DKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREGTLKDIQTKDV--ELY 894
Cdd:COG1120 163 EPTSHLDLA---H--QLEVLELLRRlareRGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEVLTPELleEVY 235
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
673-875 |
1.84e-32 |
|
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: 126.04 E-value: 1.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 673 KVTNGYFSWGSGL-ATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRNRYS---------VAYA 742
Cdd:cd03225 1 ELKNLSFSYPDGArPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKlslkelrrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 743 AQKP--WLLNATVEENITFGsPFN--------KQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARA 812
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFG-LENlglpeeeiEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398972 813 LYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYL-THADWIIAMKDG 875
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLE--LLKKLKAEGKTIIIVTHDLDLLlELADRVIVLEDG 210
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1299-1513 |
1.79e-31 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 122.04 E-value: 1.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPlHTLRSRLSI 1378
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1379 ILQDPILFSGSIRFNLdpeckctddrlwealeiaqlknmvkslpggldavvtegGENFSVGQRQLFCLARAFVRKSSILI 1458
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 530398972 1459 MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILE 1513
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
688-907 |
6.02e-31 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 130.35 E-value: 6.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG-------------EMQTLEgKVHWsnrnRYSVAYAAQKPWLLNATVE 754
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGflpyqgslkingiELRELD-PESW----RKHLSWVGQNPQLPHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 755 ENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHl 833
Cdd:PRK11174 441 DNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH- 519
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398972 834 SDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEhwktlMNRQDQE 907
Cdd:PRK11174 520 SEQLVMQALNAASRR--QTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFAT-----LLAHRQE 586
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
682-890 |
7.90e-31 |
|
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: 129.84 E-value: 7.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 682 GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV--------HWSNRN-RYSVAYAAQKPWLLNAT 752
Cdd:TIGR02203 342 GRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQIlldghdlaDYTLASlRRQVALVSQDVVLFNDT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 753 VEENITFGSP--FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD 830
Cdd:TIGR02203 422 IANNIAYGRTeqADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALD 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 831 IHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKD 890
Cdd:TIGR02203 502 NE-SERLVQAALERLMQG--RTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARN 558
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
672-895 |
1.02e-30 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 122.50 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI--LGEMQtlEGKVHWSNRN--RYSVAYAAQKPW 747
Cdd:COG4604 2 IEIKNVSKRYG-GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMIsrLLPPD--SGEVLVDGLDvaTTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 748 LL---NA-----TVEENITFGS-PFNKQR-----YKAVTDAcslqpdIDLLpfgDQTEIGERGIN-LSGGQRQRICVARA 812
Cdd:COG4604 79 ILrqeNHinsrlTVRELVAFGRfPYSKGRltaedREIIDEA------IAYL---DLEDLADRYLDeLSGGQRQRAFIAMV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 813 LYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDK-RTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQTKD 890
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDMKHSVQMMK--LLRRLADELgKTVVIVLHDINFASCyADHIVAMKDGRVVAQGTPEEIITPE 227
|
....*..
gi 530398972 891 V--ELYE 895
Cdd:COG4604 228 VlsDIYD 234
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
672-886 |
1.20e-30 |
|
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: 121.29 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN---------RYSVAYA 742
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDitkknlrelRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 743 AQKPW--LLNATVEENITFGsPFN--------KQRYKAVTDACSLQpdiDLL---PFgdqteigergiNLSGGQRQRICV 809
Cdd:COG1122 81 FQNPDdqLFAPTVEEDVAFG-PENlglpreeiRERVEEALELVGLE---HLAdrpPH-----------ELSGGQKQRVAI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530398972 810 ARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDI 886
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLE--LLKRLNKEGKTVIIVTHDLDLVAeLADRVIVLDDGRIVADGTPREV 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1299-1524 |
1.47e-30 |
|
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: 121.29 E-value: 1.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1378
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1379 ILQDPI--LFSGSIR---------FNLDPECkcTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLA 1447
Cdd:COG1122 80 VFQNPDdqLFAPTVEedvafgpenLGLPREE--IRERVEEALELVGLEHLADRPPHEL-----------SGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398972 1448 RAFVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLAQE 1524
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDpRGRRELLELLKRLNKEGKTVIIVTHDLDLVAeLADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
687-889 |
1.78e-30 |
|
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: 128.23 E-value: 1.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 687 TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV--------HWsNRNRY--SVAYAAQKPWLLNATVEEN 756
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVrldgadlkQW-DRETFgkHIGYLPQDVELFPGTVAEN 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 757 IT-FGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD 835
Cdd:TIGR01842 412 IArFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQ 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 530398972 836 HLMQEgiLKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTK 889
Cdd:TIGR01842 492 ALANA--IKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
682-877 |
1.87e-30 |
|
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: 128.71 E-value: 1.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 682 GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV--------HWsNRNRY--SVAYAAQKPWLLNA 751
Cdd:COG4618 342 GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsQW-DREELgrHIGYLPQDVELFDG 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 752 TVEENIT-FGSPfNKQrykAVTDACSLQpD----IDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 826
Cdd:COG4618 421 TIAENIArFGDA-DPE---KVVAAAKLA-GvhemILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPN 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 530398972 827 SALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSV 877
Cdd:COG4618 496 SNLDDEGEAALAA--AIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1300-1509 |
2.51e-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: 118.12 E-value: 2.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1300 KIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSII 1379
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1380 LQdpilfsgsirfnldpeckctddrlwealeiaqlknmvkslpggldavvteggenFSVGQRQLFCLARAFVRKSSILIM 1459
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 530398972 1460 DEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTILTA-DLVIVMKRG 1509
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
981-1219 |
2.55e-30 |
|
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: 121.98 E-value: 2.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 981 LILMIFSKLLKHSVIVAIDYWLATWTSEYS-INNTGKADQTYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNL 1059
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLpDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1060 LNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQKY 1139
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1140 FRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACIVL 1219
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
672-886 |
3.18e-30 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 120.67 E-value: 3.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWGS-GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHW---------SNRNRYSVAY 741
Cdd:cd03252 1 ITFEHVRFRYKPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVdghdlaladPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 742 AAQKPWLLNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIV 820
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPgMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530398972 821 FLDDPFSALDIHlSDHLMQEGILKFLqdDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDI 886
Cdd:cd03252 161 IFDEATSALDYE-SEHAIMRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1299-1509 |
4.47e-30 |
|
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: 118.73 E-value: 4.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENN---LKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIvidgidisklplhTLRSR 1375
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1376 LSIILQDPILFSGSIRFN------LDPEckctddRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARA 1449
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENilfgkpFDEE------RYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398972 1450 FVRKSSILIMDEATASIDMATEN-ILQKVVMTAFAD-RTVVTIAHRVHTILTADLVIVMKRG 1509
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRhIFENCILGLLLNnKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
672-882 |
5.56e-30 |
|
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: 119.14 E-value: 5.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWGSGLAT-LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN---------RYSVAY 741
Cdd:cd03244 3 IEFKNVSLRYRPNLPPvLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDiskiglhdlRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 742 AAQKPWLLNATVEENItfgSPFNK----QRYKAVtDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 817
Cdd:cd03244 83 IPQDPVLFSGTIRSNL---DPFGEysdeELWQAL-ERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398972 818 NIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 882
Cdd:cd03244 159 KILVLDEATASVDPE-TDALIQKTIREAFKD--CTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
667-886 |
8.10e-30 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 119.81 E-value: 8.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 667 TEDIAIKVTN---GYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN----RYSV 739
Cdd:COG1116 3 AAAPALELRGvskRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPvtgpGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 740 AYAAQK----PWLlnaTVEENITFGSPFN----KQRYKAVTDACSLqpdIDLLPFGD----QteigerginLSGGQRQRI 807
Cdd:COG1116 83 GVVFQEpallPWL---TVLDNVALGLELRgvpkAERRERARELLEL---VGLAGFEDayphQ---------LSGGMRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 808 CVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQ---YLthADWIIAMKDgsvlREGTLK 884
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDALTRERLQDE-LLRLWQETGKTVLFVTHDVDeavFL--ADRVVVLSA----RPGRIV 220
|
..
gi 530398972 885 DI 886
Cdd:COG1116 221 EE 222
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
688-882 |
2.02e-29 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 125.60 E-value: 2.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN---------RYSVAYAAQKPWLLNATVEENIT 758
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPltklqldswRSRLAVVSQTPFLFSDTVANNIA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 759 FGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHl 837
Cdd:PRK10789 411 LGRPdATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGR-TEH- 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 530398972 838 mqeGILKFLQD--DKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 882
Cdd:PRK10789 489 ---QILHNLRQwgEGRTVIISAHRLSALTEASEILVMQHGHIAQRGN 532
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
481-1533 |
4.27e-29 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 127.07 E-value: 4.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 481 QKSTLDYSTERLKKTNEILKGIKLLKLYAWEHifcksveeTRMKELS-SLKTFALYTSLSIFMNAaIPIAaVLATFVTHA 559
Cdd:PTZ00265 225 KKTSLLYNNNTMSIIEEALVGIRTVVSYCGEK--------TILKKFNlSEKLYSKYILKANFMES-LHIG-MINGFILAS 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 560 YASG------------NNLKPAEAFASLSLFHILV---TPLFLLSTV---VRFAVKAIISVQKLNEFLLSDEIGDDSwRT 621
Cdd:PTZ00265 295 YAFGfwygtriiisdlSNQQPNNDFHGGSVISILLgvlISMFMLTIIlpnITEYMKSLEATNSLYEIINRKPLVENN-DD 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 622 GESslpFESCKKhtgVQPKTInrkqpgRYHLDsyeqsTRRlrpaeteDIAIkvtngyfswgsglatLSNIDIRIPTGQLT 701
Cdd:PTZ00265 374 GKK---LKDIKK---IQFKNV------RFHYD-----TRK-------DVEI---------------YKDLNFTLTEGKTY 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 702 MIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN----------RYSVAYAAQKPWLLNATVEENITFG----------- 760
Cdd:PTZ00265 415 AFVGESGCGKSTILKLIERLYDPTEGDIIINDSHnlkdinlkwwRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdleals 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 761 -----SPFNKQRYKAVTDACSLQPDIDL------------------------------------------LPFGDQTEIG 793
Cdd:PTZ00265 495 nyyneDGNDSQENKNKRNSCRAKCAGDLndmsnttdsneliemrknyqtikdsevvdvskkvlihdfvsaLPDKYETLVG 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 794 ERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAMK 873
Cdd:PTZ00265 575 SNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLS 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 874 --------DGSVLREGTLKDIQTKD--------------------------VELYEH----------WKTLMNRQ----- 904
Cdd:PTZ00265 654 nrergstvDVDIIGEDPTKDNKENNnknnkddnnnnnnnnnnkinnagsyiIEQGTHdalmknkngiYYTMINNQkvssk 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 905 -----DQELEKDM------------EADQTTLERKTLRRAMySREAKAQMEDEDEEEEEEEDEDDNMSTVMRLRTKMP-- 965
Cdd:PTZ00265 734 kssnnDNDKDSDMkssaykdsergyDPDEMNGNSKHENESA-SNKKSCKMSDENASENNAGGKLPFLRNLFKRKPKAPnn 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 966 ----WKTCWRY-----------LTSGGFFLLILMIFSKLlkhsVIVAIDYW-LATWTSEYSInntgkadqtyyvagFSIL 1029
Cdd:PTZ00265 813 lrivYREIFSYkkdvtiialsiLVAGGLYPVFALLYAKY----VSTLFDFAnLEANSNKYSL--------------YILV 874
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1030 CGAGIFLC-LVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDT---TPlGLILNRFSADTNIIDQHIPPTLESLTRST 1105
Cdd:PTZ00265 875 IAIAMFISeTLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHINRDVHLLKTGLVNNIVIFTHFI 953
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1106 LLCLSAIGMISYATPVflVALLPLGVAFYFIqKYFRV-----ASKDLQELDDSTQLPLLCHFS-------------ETAE 1167
Cdd:PTZ00265 954 VLFLVSMVMSFYFCPI--VAAVLTGTYFIFM-RVFAIrarltANKDVEKKEINQPGTVFAYNSddeifkdpsfliqEAFY 1030
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1168 GLTTIRAFRHETRFKQRMLELTDTNN------------------IAYLFLSAANRW----------LEVrTDYLGAciVL 1219
Cdd:PTZ00265 1031 NMNTVIIYGLEDYFCNLIEKAIDYSNkgqkrktlvnsmlwgfsqSAQLFINSFAYWfgsflirrgtILV-DDFMKS--LF 1107
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1220 TASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNlADLEVQ-MGAVKKVNSFLTmesenyegtmdpsqvpehwpqEGE 1298
Cdd:PTZ00265 1108 TFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRK-SNIDVRdNGGIRIKNKNDI---------------------KGK 1165
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFD----------------------- 1354
Cdd:PTZ00265 1166 IEIMDVNFRYISRPNvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtndmtneqdyqgd 1245
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1355 -------------------------------GKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLD-PECKCTD 1402
Cdd:PTZ00265 1246 eeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKfGKEDATR 1325
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1403 DRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVV--MT 1480
Cdd:PTZ00265 1326 EDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdIK 1405
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*...
gi 530398972 1481 AFADRTVVTIAHRVHTILTADLVIVM----KRGNILE-YDTPESLLAQENGVFASFVR 1533
Cdd:PTZ00265 1406 DKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaHGTHEELLSVQDGVYKKYVK 1463
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
679-873 |
5.31e-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: 116.09 E-value: 5.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 679 FSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH----WSNRNRYSVAYAAQK---PWLLNA 751
Cdd:cd03235 7 VSYGGHPV-LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkPLEKERKRIGYVPQRrsiDRDFPI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 752 TVEE--------NITFGSPFNKQRYKAVTDAcslqpdidlLPFGDQTEIGERGI-NLSGGQRQRICVARALYQNTNIVFL 822
Cdd:cd03235 86 SVRDvvlmglygHKGLFRRLSKADKAKVDEA---------LERVGLSELADRQIgELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 530398972 823 DDPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMK 873
Cdd:cd03235 157 DEPFAGVDPKTQEDIY--ELLRELRREGMTILVVTHDLGLVLeYFDRVLLLN 206
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
303-605 |
9.39e-29 |
|
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: 117.70 E-value: 9.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 303 FRYLADLLGFAGPLCISGIVQRVNETQngtnnttgisetlsskEFLENAYVLAVLLFLALILQRTFLQASYYVTIETGIN 382
Cdd:cd18559 5 IKLVLCNHVFSGPSNLWLLLWFDDPVN----------------GPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 383 LRGALLAMIYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSALVGAAV 462
Cdd:cd18559 69 ASRAVHLDLYHKALRSPISFFE--RTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 463 IVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTSLSIFM 542
Cdd:cd18559 147 GLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRL 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398972 543 NAAIPIAAVLATFVTHAYASGNN-LKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 605
Cdd:cd18559 227 WCVGPCIVLFASFFAYVSRHSLAgLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
674-880 |
3.84e-28 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 113.72 E-value: 3.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 674 VTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS----NRNRYSVAYAAQK---- 745
Cdd:cd03293 6 VSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDgepvTGPGPDRGYVFQQdall 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 746 PWLlnaTVEENITFGSPFN----KQRYKAVTDACSLqpdIDLLPFGDQTeIGErginLSGGQRQRICVARALYQNTNIVF 821
Cdd:cd03293 86 PWL---TVLDNVALGLELQgvpkAEARERAEELLEL---VGLSGFENAY-PHQ----LSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398972 822 LDDPFSALDiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQ---YLthADWIIAM--KDGSVLRE 880
Cdd:cd03293 155 LDEPFSALD-ALTREQLQEELLDIWRETGKTVLLVTHDIDeavFL--ADRVVVLsaRPGRIVAE 215
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
385-860 |
8.87e-28 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 119.77 E-value: 8.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 385 GALLAMIYNKILRLS---TSNLSMGEMtlgqINNLVA-IETNQLMWFLFLCPNLWAMPVQII--MGVILLYNLLGSSALV 458
Cdd:TIGR02868 86 GALRVRVYERLARQAlagRRRLRRGDL----LGRLGAdVDALQDLYVRVIVPAGVALVVGAAavAAIAVLSVPAALILAA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 459 GAAVIVLLAPiqyFIATKLAEAQKSTLDYS-TERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTS 537
Cdd:TIGR02868 162 GLLLAGFVAP---LVSLRAARAAEQALARLrGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 538 LSIFMNAAIPIAAVLATFVTHAYASGNNLKPAEAFASLSLFHILVT-PLFLLSTVVRFAVKAIISVQKLNEFLlsdeigD 616
Cdd:TIGR02868 239 LGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFeAFAALPAAAQQLTRVRAAAERIVEVL------D 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 617 DSWRTGESSLPfesckkhtgvQPKTINRKQPGRyhldsyeqstrrlrpaETEDIAikvtngyFSWGSGLATLSNIDIRIP 696
Cdd:TIGR02868 313 AAGPVAEGSAP----------AAGAVGLGKPTL----------------ELRDLS-------AGYPGAPPVLDGVSLDLP 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 697 TGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV---------HWSNRNRYSVAYAAQKPWLLNATVEENITFGSP-FNKQ 766
Cdd:TIGR02868 360 PGERVAILGPSGSGKSTLLATLAGLLDPLQGEVtldgvpvssLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPdATDE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 767 RYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMqEGILKfl 846
Cdd:TIGR02868 440 ELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELL-EDLLA-- 516
|
490
....*....|....
gi 530398972 847 QDDKRTLVLVTHKL 860
Cdd:TIGR02868 517 ALSGRTVVLITHHL 530
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
673-881 |
1.17e-27 |
|
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: 110.99 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 673 KVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN--RYSVAYAAQKpwlln 750
Cdd:cd03214 1 EVENLSVGYGGRTV-LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDlaSLSPKELARK----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 751 atveenITFgspfnkqrykaVTDACSLqpdIDLLPFGDqteigeRGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSAL 829
Cdd:cd03214 75 ------IAY-----------VPQALEL---LGLAHLAD------RPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 530398972 830 DIHLSDHLMQegILKFLQDDK-RTLVLVTHKL-QYLTHADWIIAMKDGSVLREG 881
Cdd:cd03214 129 DIAHQIELLE--LLRRLARERgKTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1299-1523 |
1.39e-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: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI---FDGKIVIDGIDISKLPLHTLRSR 1375
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1376 LSIILQDPI--LFSGSIRFNLD--PECKCTD-----DRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCL 1446
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGDQIAeaLENLGLSraearARVLELLEAVGLERRLDRYPHQL-----------SGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1447 ARAFVRKSSILIMDEATASIDMATenilQKVVMTAFAD------RTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPES 1519
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTT----QAEILDLLRElqrergTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEE 229
|
....
gi 530398972 1520 LLAQ 1523
Cdd:COG1123 230 ILAA 233
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1300-1509 |
1.92e-27 |
|
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: 111.40 E-value: 1.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1300 KIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSII 1379
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1380 LQDP--ILFSGSIR----FNLDPECKCTDD---RLWEALEIAQLKNMVKSLPggldavvteggENFSVGQRQLFCLARAF 1450
Cdd:cd03225 81 FQNPddQFFGPTVEeevaFGLENLGLPEEEieeRVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398972 1451 VRKSSILIMDEATASIDMATENILQKVVmTAFADR--TVVTIAHRVHTILT-ADLVIVMKRG 1509
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELL-KKLKAEgkTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1299-1514 |
2.21e-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: 111.83 E-value: 2.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTL---R 1373
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1374 SRLSIILQDPILfsgsirfNLDP------------ECKCTDDRLWEALEIAQLKNMVKSLPGG-LDAVVTEggenFSVGQ 1440
Cdd:cd03257 82 KEIQMVFQDPMS-------SLNPrmtigeqiaeplRIHGKLSKKEARKEAVLLLLVGVGLPEEvLNRYPHE----LSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398972 1441 RQLFCLARAFVRKSSILIMDEATASIDMATE-NILQkvVMTAFADR---TVVTIAHRVHTIL-TADLVIVMKRGNILEY 1514
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQaQILD--LLKKLQEElglTLLFITHDLGVVAkIADRVAVMYAGKIVEE 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
680-881 |
3.32e-27 |
|
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: 111.07 E-value: 3.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 680 SWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN-------RYSVAYAAQK----PWL 748
Cdd:cd03259 9 TYGSVRA-LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDvtgvppeRRNIGMVFQDyalfPHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 749 lnaTVEENITFGSPFNKQRYKAVTDACSLqpdidLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFS 827
Cdd:cd03259 88 ---TVAENIAFGLKLRGVPKAEIRARVRE-----LLELVGLEGLLNRYPHeLSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 530398972 828 ALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQ-YLTHADWIIAMKDGSVLREG 881
Cdd:cd03259 160 ALDAKLREELREE-LKELQRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
666-875 |
7.28e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 109.91 E-value: 7.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 666 ETEDIAIKVTNGYFswgsglatLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN---------R 736
Cdd:COG4619 2 ELEGLSFRVGGKPI--------LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsampppewR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 737 YSVAYAAQKPWLLNATVEENITFGSPFNKQRYkavtdacSLQPDIDLLP-FGDQTEIGERGI-NLSGGQRQRICVARALY 814
Cdd:COG4619 74 RQVAYVPQEPALWGGTVRDNLPFPFQLRERKF-------DRERALELLErLGLPPDILDKPVeRLSGGERQRLALIRALL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398972 815 QNTNIVFLDDPFSALDIHLSDHLmQEGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDG 875
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRV-EELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAG 207
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1296-1523 |
9.93e-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: 9.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1296 EGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAffrMVDIFD---GKIVIDGIDISKLPlhtl 1372
Cdd:COG4618 328 KGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARL---LVGVWPptaGSVRLDGADLSQWD---- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1373 RSRLSIIL----QDPILFSGSI-----RFNlDPeckcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQL 1443
Cdd:COG4618 401 REELGRHIgylpQDVELFDGTIaeniaRFG-DA----DPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1444 FCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLA 1522
Cdd:COG4618 476 IGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
.
gi 530398972 1523 Q 1523
Cdd:COG4618 556 R 556
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
673-875 |
1.00e-26 |
|
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: 107.72 E-value: 1.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 673 KVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSnrnrysvayaaqkpwllnat 752
Cdd:cd00267 1 EIENLSFRYGGRTA-LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID-------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 753 veenitfGSPFNKQRYKAVTDACSLQPDidllpfgdqteigerginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 832
Cdd:cd00267 60 -------GKDIAKLPLEELRRRIGYVPQ------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 530398972 833 LSDHLMQegILKFLQDDKRTLVLVTHKLQYLTHA-DWIIAMKDG 875
Cdd:cd00267 115 SRERLLE--LLRELAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
672-875 |
1.66e-26 |
|
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: 109.12 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWGSG---LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTL-EGKV--------HWSNRN---- 735
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLL-NILGGLDRPtSGEVrvdgtdisKLSEKElaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 736 -RYSVAYAAQKPWLLNA-TVEENITFGSPFNKQRYKAVTDACslqpdIDLLpfgDQTEIGERgIN-----LSGGQRQRIC 808
Cdd:cd03255 80 rRRHIGFVFQSFNLLPDlTALENVELPLLLAGVPKKERRERA-----EELL---ERVGLGDR-LNhypseLSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398972 809 VARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDG 875
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMEL-LRELNKEAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
688-900 |
1.74e-26 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 116.34 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN---------RYSVAYAAQKPWLLNATVEENIT 758
Cdd:TIGR02204 356 LDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDlrqldpaelRARMALVPQDPVLFAASVMENIR 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 759 FGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhLSDHL 837
Cdd:TIGR02204 436 YGRPdATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDA-ESEQL 514
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398972 838 MQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDvELYEHWKTL 900
Cdd:TIGR02204 515 VQQALETLMKG--RTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKG-GLYARLARL 574
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
688-877 |
1.92e-26 |
|
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: 107.30 E-value: 1.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV----------HWSNRnRYSVAYAAQKPWLLNATVEENI 757
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrldgadisqwDPNEL-GDHVGYLPQDDELFSGSIAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 758 tfgspfnkqrykavtdacslqpdidllpfgdqteigerginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHL 837
Cdd:cd03246 97 -----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERAL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 530398972 838 MQegILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSV 877
Cdd:cd03246 136 NQ--AIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1299-1520 |
2.60e-26 |
|
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: 108.81 E-value: 2.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIF-----DGKIVIDGIDISKLPLH--T 1371
Cdd:cd03260 1 IELRDLNVYYGD--KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDVDvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1372 LRSRLSIILQDPILFSGSIRFNLD--------PECKCTDDRLWEALEIAQLKNMVKSLPGGLDavvteggenFSVGQRQL 1443
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAyglrlhgiKLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398972 1444 FCLARAFVRKSSILIMDEATASID-MATENIlQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESL 1520
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDpISTAKI-EELIAELKKEYTIVIVTHNMQQAArVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
371-585 |
3.78e-26 |
|
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: 109.65 E-value: 3.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 371 ASYYVTIETGINLRGALLAMIYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYN 450
Cdd:pfam00664 60 LQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMF 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 451 LLG-SSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSL 529
Cdd:pfam00664 138 YYGwKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAG 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 530398972 530 KTFALYTSLSI-FMNAAIPIAAVLATFVTHAYASGNNLKPAEAFASLSLFHILVTPL 585
Cdd:pfam00664 218 IKKAVANGLSFgITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
688-827 |
3.95e-26 |
|
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: 105.81 E-value: 3.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN---------RYSVAYAAQKPWLLNA-TVEENI 757
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDltdderkslRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398972 758 TFGSPFnkQRYKAVTDACSLQPDIDLLPFGDQ--TEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 827
Cdd:pfam00005 81 RLGLLL--KGLSKREKDARAEEALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
1000-1267 |
4.58e-26 |
|
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: 110.00 E-value: 4.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1000 YWLATWTSEysiNNTGKADQTY-YVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGL 1078
Cdd:cd18559 20 LWLLLWFDD---PVNGPQEHGQvYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1079 ILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVAlLPLGVAFYFIQKYFRVASKDLQELDDSTQLPL 1158
Cdd:cd18559 97 LVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVG-IPLGLLYVPVNRVYAASSRQLKRLESVSKDPR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1159 LCHFSETAEGLTTIRAFRHETRFKQRMLELTDtNNIAYLFLSAANRWLEVRTDYLGACIV-LTASIASISGSSNSGLVGL 1237
Cdd:cd18559 176 YKLFNETLLGISVIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVRLWCVGPCIVlFASFFAYVSRHSLAGLVAL 254
|
250 260 270
....*....|....*....|....*....|
gi 530398972 1238 GLLYALTITNYLNWVVRNLADLEVQMGAVK 1267
Cdd:cd18559 255 KVFYSLALTTYLNWPLNMSPEVITNIVAAE 284
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
688-877 |
2.03e-25 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 106.40 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSL--LLAILGEMQ----TLEGKVHWSNRNRY---SVAYAAQKPWLLNATVEENIT 758
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVvaLLENFYQPQggqvLLDGKPISQYEHKYlhsKVSLVGQEPVLFARSLQDNIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 759 FG---SPFnkQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSD 835
Cdd:cd03248 110 YGlqsCSF--ECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE-SE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 530398972 836 HLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSV 877
Cdd:cd03248 187 QQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
669-880 |
4.21e-25 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 105.13 E-value: 4.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 669 DIAIKVTNGYFSWGSGLAT---LSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTL-EGKVHWSNRN--------- 735
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEvtaLRGVSLSIEAGEFVAIVGPSGSGKSTLL-NILGGLDRPtSGEVLIDGQDisslserel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 736 ----RYSVAYAAQKPWLL-NATVEENITF-----GSPFNKQRYKAvtdacslqpdIDLLpfgDQTEIGERgIN-----LS 800
Cdd:COG1136 81 arlrRRHIGFVFQFFNLLpELTALENVALplllaGVSRKERRERA----------RELL---ERVGLGDR-LDhrpsqLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 801 GGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFL-QDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLR 879
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLE--LLRELnRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
.
gi 530398972 880 E 880
Cdd:COG1136 225 D 225
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
966-1273 |
4.84e-25 |
|
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: 107.97 E-value: 4.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 966 WKTCWRYLTSGGFFLLILmIFSKLLKHSVIVAIDYWLATWTSEYSINNTGKAD---QTY---------------YVAGFS 1027
Cdd:cd18600 3 WNTYLRYITSHKSLIFVL-ILCLVIFAIEVAASLVGLWLLRSQADRVNTTRPEsssNTYavivtftssyyvfyiYVGVAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1028 ILCGAGIF--LCLVTSLtvewmgLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRST 1105
Cdd:cd18600 82 SLLAMGFFrgLPLVHTL------ITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1106 LLCLSAIGMISYATPVFLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRM 1185
Cdd:cd18600 156 LIVIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1186 LELTDTNNIAYLFLSAANRWLEVRTDYLGAC-IVLTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMG 1264
Cdd:cd18600 236 HKALNLHTANWFLYLSTLRWFQMRIEMIFVIfFTAVTFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMR 315
|
....*....
gi 530398972 1265 AVKKVNSFL 1273
Cdd:cd18600 316 SVSRIFKFI 324
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1316-1464 |
5.99e-25 |
|
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: 102.34 E-value: 5.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1316 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSG-SIRFNL 1394
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398972 1395 DPECKCT-------DDRLWEALEiaQLknmvkSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA 1464
Cdd:pfam00005 81 RLGLLLKglskrekDARAEEALE--KL-----GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
650-886 |
9.70e-25 |
|
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: 111.76 E-value: 9.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 650 YHLDSYEQSTRRLRPAETEDIAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV 729
Cdd:TIGR01193 452 YLVDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEI 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 730 HWSNRN---------RYSVAYAAQKPWLLNATVEENITFGSPFN--KQRYKAVTDACSLQPDIDLLPFGDQTEIGERGIN 798
Cdd:TIGR01193 532 LLNGFSlkdidrhtlRQFINYLPQEPYIFSGSILENLLLGAKENvsQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSS 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 799 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIhLSDHLMQEGILkFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVL 878
Cdd:TIGR01193 612 ISGGQKQRIALARALLTDSKVLILDESTSNLDT-ITEKKIVNNLL-NLQD--KTIIFVAHRLSVAKQSDKIIVLDHGKII 687
|
....*...
gi 530398972 879 REGTLKDI 886
Cdd:TIGR01193 688 EQGSHDEL 695
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
688-886 |
1.01e-24 |
|
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: 111.76 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLE-GKV------------HWSNRNrysVAYAAQKPWLLNATVE 754
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLT-KLLQRLYTPQhGQVlvdgvdlaiadpAWLRRQ---MGVVLQENVLFSRSIR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 755 ENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHl 833
Cdd:TIGR01846 549 DNIALCNPgAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYE- 627
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 530398972 834 SDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDI 886
Cdd:TIGR01846 628 SEALIMRNMREICRG--RTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1299-1525 |
1.19e-24 |
|
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: 104.55 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHtLRSRLSI 1378
Cdd:COG4555 2 IEVENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1379 ILQDPILFSG-SIRFNLDPECKCTDDRLWEALEIAQlkNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSIL 1457
Cdd:COG4555 79 LPDERGLYDRlTVRENIRYFAELYGLFDEELKKRIE--ELIELL--GLEEFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1458 IMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLAQEN 1525
Cdd:COG4555 155 LLDEPTNGLDvMARRLLREILRALKKEGKTVLFSSHIMQEVEaLCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1299-1523 |
4.12e-24 |
|
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: 108.45 E-value: 4.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNLK---PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTL 1372
Cdd:COG1123 261 LEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1373 RSRLSIILQDPilfSGSirfnLDPECKCTDDrLWEALEI------AQLKNMVKSLpggLDAVvteG----------GEnF 1436
Cdd:COG1123 341 RRRVQMVFQDP---YSS----LNPRMTVGDI-IAEPLRLhgllsrAERRERVAEL---LERV---GlppdladrypHE-L 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1437 SVGQRQLFCLARAFVRKSSILIMDEATASIDMATenilQKVVMTAFAD------RTVVTIAHRVHTILT-ADLVIVMKRG 1509
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALDVSV----QAQILNLLRDlqrelgLTYLFISHDLAVVRYiADRVAVMYDG 481
|
250
....*....|....
gi 530398972 1510 NILEYDTPESLLAQ 1523
Cdd:COG1123 482 RIVEDGPTEEVFAN 495
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1299-1522 |
4.15e-24 |
|
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: 102.96 E-value: 4.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYE--NNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1376
Cdd:COG1124 2 LEVRNLSVSYGqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1377 SIILQDPIlfsGSI--RFNLDpeckctdDRLWEALEIAQLKNMVKSLPGGLDAVvteG-GENF--------SVGQRQLFC 1445
Cdd:COG1124 82 QMVFQDPY---ASLhpRHTVD-------RILAEPLRIHGLPDREERIAELLEQV---GlPPSFldryphqlSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1446 LARAFVRKSSILIMDEATASIDMATE----NILQKvvMTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESL 1520
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQaeilNLLKD--LREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADL 226
|
..
gi 530398972 1521 LA 1522
Cdd:COG1124 227 LA 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
668-877 |
4.16e-24 |
|
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: 101.72 E-value: 4.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 668 EDIAIKVTNGYFSWGSGLA-TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN---------RY 737
Cdd:cd03369 3 EHGEIEVENLSVRYAPDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDistipledlRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 738 SVAYAAQKPWLLNATVEENItfgSPFNKQRYKAVTDACSlqpdidllpfgdqteIGERGINLSGGQRQRICVARALYQNT 817
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGALR---------------VSEGGLNLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 818 NIVFLDDPFSALDIHlSDHLMQEGILKFLQDDkrTLVLVTHKLQYLTHADWIIAMKDGSV 877
Cdd:cd03369 145 RVLVLDEATASIDYA-TDALIQKTIREEFTNS--TILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
377-904 |
4.62e-24 |
|
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: 109.66 E-value: 4.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 377 IETGINlrGALLAMIYNKILRL--------STSNLSMGEMTLGQINNLVAIET-NQLMWFLFLCPNLWAMpvqiimgviL 447
Cdd:TIGR03797 203 LETRMD--ASLQAAVWDRLLRLpvsffrqySTGDLASRAMGISQIRRILSGSTlTTLLSGIFALLNLGLM---------F 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 448 LYNLlgSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLK--------LYAWEHIFCKSVE 519
Cdd:TIGR03797 272 YYSW--KLALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRvagaenraFARWAKLFSRQRK 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 520 ---ETRMKE--LSSLKT-FALYTSLSIFMNAAIPIAAV---LATFVTHAYASGNNLKPAEAFASlSLFHIL-VTPLFlls 589
Cdd:TIGR03797 350 lelSAQRIEnlLTVFNAvLPVLTSAALFAAAISLLGGAglsLGSFLAFNTAFGSFSGAVTQLSN-TLISILaVIPLW--- 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 590 tvvrfavkaiisvqklnefllsdeigddswrtgESSLP-FESckkhtgvQPKT-INRKQPGRYHLdsyeqstrrlrpaet 667
Cdd:TIGR03797 426 ---------------------------------ERAKPiLEA-------LPEVdEAKTDPGKLSG--------------- 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 668 ediAIKVTNGYFSWG-SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRNRYSVAYAA--- 743
Cdd:TIGR03797 451 ---AIEVDRVTFRYRpDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAvrr 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 744 ------QKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 817
Cdd:TIGR03797 528 qlgvvlQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKP 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 818 NIVFLDDPFSALdihlsDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEhw 897
Cdd:TIGR03797 608 RILLFDEATSAL-----DNRTQAIVSESLERLKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQ-- 680
|
....*..
gi 530398972 898 ktLMNRQ 904
Cdd:TIGR03797 681 --LARRQ 685
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
684-867 |
4.78e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 101.16 E-value: 4.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRNRysVAYAAQK---PWLLNATVEENITFG 760
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGAR--VAYVPQRsevPDSLPLTVRDLVAMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 761 --------SPFNKQRYKAVTDACSlqpDIDLLPFGDQtEIGErginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 832
Cdd:NF040873 82 rwarrglwRRLTRDDRAAVDDALE---RVGLADLAGR-QLGE----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
|
170 180 190
....*....|....*....|....*....|....*
gi 530398972 833 LSDHLmqEGILKFLQDDKRTLVLVTHKLQYLTHAD 867
Cdd:NF040873 154 SRERI--IALLAEEHARGATVVVVTHDLELVRRAD 186
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
672-886 |
6.78e-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: 102.38 E-value: 6.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN---------RYSVAYA 742
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDireqdpvelRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 743 AQKPWLL-NATVEENITFGSPFNK-QRYKAVTDACSLQPDIDLLPfgdqTEIGER-GINLSGGQRQRICVARALYQNTNI 819
Cdd:cd03295 81 IQQIGLFpHMTVEENIALVPKLLKwPKEKIRERADELLALVGLDP----AEFADRyPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530398972 820 VFLDDPFSALDIHLSDHLmQEGILKFLQDDKRTLVLVTHKLQ-YLTHADWIIAMKDGSVLREGTLKDI 886
Cdd:cd03295 157 LLMDEPFGALDPITRDQL-QEEFKRLQQELGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
672-890 |
1.01e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 107.80 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSW-GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSL--LLAILGEMQtlEGKVHWSNRN---------RYSV 739
Cdd:PRK11176 342 IEFRNVTFTYpGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIanLLTRFYDID--EGEILLDGHDlrdytlaslRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 740 AYAAQKPWLLNATVEENITFGSpfnKQRY------KAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRICVARAL 813
Cdd:PRK11176 420 ALVSQNVHLFNDTIANNIAYAR---TEQYsreqieEAARMAYAMD-FINKMDNGLDTVIGENGVLLSGGQRQRIAIARAL 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398972 814 YQNTNIVFLDDPFSALDIHlSDHLMQEGiLKFLQDDKRTLVlVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKD 890
Cdd:PRK11176 496 LRDSPILILDEATSALDTE-SERAIQAA-LDELQKNRTSLV-IAHRLSTIEKADEILVVEDGEIVERGTHAELLAQN 569
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1299-1525 |
1.25e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 102.38 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1378
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1379 ILQDPI-LFSGS-----IRFNLdpECKCTD-----DRLWEALEIAQLKNMVKSLPggldavvteggENFSVGQRQLFCLA 1447
Cdd:PRK13632 88 IFQNPDnQFIGAtveddIAFGL--ENKKVPpkkmkDIIDDLAKKVGMEDYLDKEP-----------QNLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1448 RAFVRKSSILIMDEATASID-MATENILQKVV-MTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQEN 1525
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDpKGKREIKKIMVdLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
671-886 |
2.49e-23 |
|
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: 100.65 E-value: 2.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 671 AIKVTN---GYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN---------RYS 738
Cdd:COG1124 1 MLEVRNlsvSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPvtrrrrkafRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 739 VAYAAQKPWL-LNA--TVEENIT-----FGSPFNKQRYKAVTDACSLQPDI-DLLPfgDQteigerginLSGGQRQRICV 809
Cdd:COG1124 81 VQMVFQDPYAsLHPrhTVDRILAeplriHGLPDREERIAELLEQVGLPPSFlDRYP--HQ---------LSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 810 ARALYQNTNIVFLDDPFSALDIHlsdhlMQEGILKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLK 884
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVS-----VQAEILNLLKDLREerglTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVA 224
|
..
gi 530398972 885 DI 886
Cdd:COG1124 225 DL 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
672-892 |
2.96e-23 |
|
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: 100.32 E-value: 2.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN--------RYSVAYAA 743
Cdd:COG4555 2 IEVENLSKKYGKVPA-LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDvrkepreaRRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 744 QKPWL-LNATVEENITFGSPFN---KQRYKAVTDacSLQPDIDLLPFGDQTeIGErginLSGGQRQRICVARALYQNTNI 819
Cdd:COG4555 81 DERGLyDRLTVRENIRYFAELYglfDEELKKRIE--ELIELLGLEEFLDRR-VGE----LSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398972 820 VFLDDPFSALDIhLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQTKDVE 892
Cdd:COG4555 154 LLLDEPTNGLDV-MARRLLRE-ILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
672-893 |
3.51e-23 |
|
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: 99.88 E-value: 3.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN------------RYSV 739
Cdd:cd03261 1 IELRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisglseaelyrlRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 740 AYAAQKPWLLNA-TVEENITFG----SPFNKQRYKAVT----DACSLQPDIDLLPfgdqteigergINLSGGQRQRICVA 810
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVAFPlrehTRLSEEEIREIVleklEAVGLRGAEDLYP-----------AELSGGMKKRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 811 RALYQNTNIVFLDDPFSALDIHLSDhLMQEGILKfLQDDKR-TLVLVTHKLQ-YLTHADWIIAMKDGSVLREGTLKDIQT 888
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASG-VIDDLIRS-LKKELGlTSIMVTHDLDtAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
....*
gi 530398972 889 KDVEL 893
Cdd:cd03261 227 SDDPL 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
657-894 |
4.26e-23 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 105.37 E-value: 4.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 657 QSTRRLRPAETEDIAIKVTN---GYFSWGSGLAT-LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS 732
Cdd:COG1123 246 ARGRAAPAAAAAEPLLEVRNlskRYPVRGKGGVRaVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 733 NRN------------RYSVAYAAQKPWL-LNA--TVEENITFG-------SPfnKQRYKAVT---DACSLQPD-IDLLPF 786
Cdd:COG1123 326 GKDltklsrrslrelRRRVQMVFQDPYSsLNPrmTVGDIIAEPlrlhgllSR--AERRERVAellERVGLPPDlADRYPH 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 787 GdqteigerginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKR----TLVLVTHKL-- 860
Cdd:COG1123 404 E-----------LSGGQRQRVAIARALALEPKLLILDEPTSALDVSV-----QAQILNLLRDLQRelglTYLFISHDLav 467
|
250 260 270
....*....|....*....|....*....|....*
gi 530398972 861 -QYLthADWIIAMKDGSVLREGTLKDIQTKDVELY 894
Cdd:COG1123 468 vRYI--ADRVAVMYDGRIVEDGPTEEVFANPQHPY 500
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1299-1525 |
6.03e-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: 99.73 E-value: 6.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAffRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1376
Cdd:COG1120 2 LEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLlrALA--GLLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1377 SIILQDPIL-FSGSIR--------------FNLDPEckctDDRL-WEALE---IAQLKN-MVKSLPGGldavvteggenf 1436
Cdd:COG1120 78 AYVPQEPPApFGLTVRelvalgryphlglfGRPSAE----DREAvEEALErtgLEHLADrPVDELSGG------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1437 svgQRQLFCLARAFVRKSSILIMDEATASIDMA----TENILQKvvMTAFADRTVVTIAHRV-HTILTADLVIVMKRGNI 1511
Cdd:COG1120 142 ---ERQRVLIARALAQEPPLLLLDEPTSHLDLAhqleVLELLRR--LARERGRTVVMVLHDLnLAARYADRLVLLKDGRI 216
|
250
....*....|....
gi 530398972 1512 LEYDTPESLLAQEN 1525
Cdd:COG1120 217 VAQGPPEEVLTPEL 230
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
688-881 |
6.84e-23 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 97.38 E-value: 6.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN--------RYSVAYAAQKPWLLNATVEENItf 759
Cdd:cd03247 18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPvsdlekalSSLISVLNQRPYLFDTTLRNNL-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 760 gspfnkqrykavtdacslqpdidllpfgdqteigerGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMq 839
Cdd:cd03247 96 ------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLL- 138
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 530398972 840 EGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREG 881
Cdd:cd03247 139 SLIFEVLKD--KTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
688-886 |
7.68e-23 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 98.98 E-value: 7.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH------WSNRNRY--SVAYAAQKPWL-LNATVEENIT 758
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvARDPAEVrrRIGYVPQEPALyPDLTVRENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 759 F-------GSPFNKQRYKAVTDACSLQPDIDllpfgdqteigERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 831
Cdd:COG1131 96 FfarlyglPRKEARERIDELLELFGLTDAAD-----------RKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 530398972 832 HLSDHLMQegILKFLQDDKRTLVLVTHklqYLTHA----DWIIAMKDGSVLREGTLKDI 886
Cdd:COG1131 165 EARRELWE--LLRELAAEGKTVLLSTH---YLEEAerlcDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
672-894 |
7.82e-23 |
|
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: 99.18 E-value: 7.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS------------NRNRYSV 739
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgtdinklkgkalRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 740 AYAAQKPWLLN-ATVEENITFG------------SPFNKQRYKAvtdACSLQPDIDLLPFGDQteigeRGINLSGGQRQR 806
Cdd:cd03256 81 GMIFQQFNLIErLSVLENVLSGrlgrrstwrslfGLFPKEEKQR---ALAALERVGLLDKAYQ-----RADQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 807 ICVARALYQNTNIVFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQY-LTHADWIIAMKDGSVLREGTLKD 885
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVM-DLLKRINREEGITVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAE 231
|
250
....*....|
gi 530398972 886 IQTKDV-ELY 894
Cdd:cd03256 232 LTDEVLdEIY 241
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
672-886 |
9.80e-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: 98.41 E-value: 9.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLL-----LAILGEMQTLEGKVHWSNRNRYS-------- 738
Cdd:cd03260 1 IELRDLNVYYGDKHA-LKDISLDIPKGEITALIGPSGCGKSTLLrllnrLNDLIPGAPDEGEVLLDGKDIYDldvdvlel 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 739 ---VAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDAC---SLQpDIDLLP-FGDQTEIGErginLSGGQRQRICVAR 811
Cdd:cd03260 80 rrrVGMVFQKPNPFPGSIYDNVAYGLRLHGIKLKEELDERveeALR-KAALWDeVKDRLHALG----LSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530398972 812 ALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFlqDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 886
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPI-STAKIEELIAEL--KKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
688-896 |
1.58e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 104.80 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV------------HWSNRNrysVAYAAQKPWLLNATVEE 755
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVlldgvplvqydhHYLHRQ---VALVGQEPVLFSGSVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 756 NITFGSPF-NKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlS 834
Cdd:TIGR00958 574 NIAYGLTDtPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE-C 652
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398972 835 DHLMQEgiLKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTkDVELYEH 896
Cdd:TIGR00958 653 EQLLQE--SRSRAS--RTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLME-DQGCYKH 709
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
688-886 |
2.40e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 100.22 E-value: 2.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGemqtLE----GKVHWSNRNRYS--------VAYAAQKPWLL-NATVE 754
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAG----LEtpdsGRIVLNGRDLFTnlpprerrVGFVFQHYALFpHMTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 755 ENITFG---SPFNKQRYKA-VTDACSLqpdIDLLPFGD----QteigerginLSGGQRQRICVARALYQNTNIVFLDDPF 826
Cdd:COG1118 94 ENIAFGlrvRPPSKAEIRArVEELLEL---VQLEGLADrypsQ---------LSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398972 827 SALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQ-YLTHADWIIAMKDGSVLREGTLKDI 886
Cdd:COG1118 162 GALDAKVRKELRRW-LRRLHDELGGTTVFVTHDQEeALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
672-875 |
3.77e-22 |
|
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: 95.33 E-value: 3.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN-----------RYSVA 740
Cdd:cd03229 1 LELKNVSKRYGQKTV-LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDltdledelpplRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 741 YAAQKPWLL-NATVEENITFGspfnkqrykavtdacslqpdidllpfgdqteigerginLSGGQRQRICVARALYQNTNI 819
Cdd:cd03229 80 MVFQDFALFpHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398972 820 VFLDDPFSALDIhlsdhLMQEGILKFLQD----DKRTLVLVTHKLQYLTH-ADWIIAMKDG 875
Cdd:cd03229 122 LLLDEPTSALDP-----ITRREVRALLKSlqaqLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
688-888 |
1.31e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 95.85 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNR--NRYSVAYAAQKPWLL--------NATVEENI 757
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpiSMLSSRQLARRLALLpqhhltpeGITVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 758 TFG-SPFNK------QRYKAVTDACSLQPDIDllpfgdqtEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFSAL 829
Cdd:PRK11231 98 AYGrSPWLSlwgrlsAEDNARVNQAMEQTRIN--------HLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 830 DIHLSDHLMqeGILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREGTLKDIQT 888
Cdd:PRK11231 170 DINHQVELM--RLMRELNTQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
671-896 |
4.33e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 96.68 E-value: 4.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 671 AIKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG-EMQTlEGKVHW----------SNRNrysV 739
Cdd:COG3839 3 SLELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGlEDPT-SGEILIggrdvtdlppKDRN---I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 740 AYAAQKPWLL-NATVEENITFG------SPfnKQRYKAVTDACSLqpdIDLLPFGDQteigeRGINLSGGQRQRICVARA 812
Cdd:COG3839 78 AMVFQSYALYpHMTVYENIAFPlklrkvPK--AEIDRRVREAAEL---LGLEDLLDR-----KPKQLSGGQRQRVALGRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 813 LYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKdiqtkdv 891
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDAKLRVEMRAE-IKRLHRRLGTTTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPE------- 219
|
....*
gi 530398972 892 ELYEH 896
Cdd:COG3839 220 ELYDR 224
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
688-882 |
4.33e-21 |
|
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: 100.02 E-value: 4.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRNR---------YSVAYAAQKPWLLNATVEENIT 758
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPReeiprevlaNSVAMVDQDIFLFEGTVRDNLT 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 759 FGSPF--NKQRYKAVTDACsLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD----IH 832
Cdd:TIGR03796 575 LWDPTipDADLVRACKDAA-IHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDpeteKI 653
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 530398972 833 LSDHLMQEGIlkflqddkrTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 882
Cdd:TIGR03796 654 IDDNLRRRGC---------TCIIVAHRLSTIRDCDEIIVLERGKVVQRGT 694
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
688-881 |
5.79e-21 |
|
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: 93.34 E-value: 5.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN------------RYSVAYAAQKPWL-LNA--T 752
Cdd:cd03257 21 LDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDllklsrrlrkirRKEIQMVFQDPMSsLNPrmT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 753 VEENIT-----FGSPFNKQRYKAVT--DACSLQPDIDLL---PFGdqteigerginLSGGQRQRICVARALYQNTNIVFL 822
Cdd:cd03257 101 IGEQIAeplriHGKLSKKEARKEAVllLLVGVGLPEEVLnryPHE-----------LSGGQRQRVAIARALALNPKLLIA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398972 823 DDPFSALDIHLSDHLMQegILKFLQDDK-RTLVLVTHKL---QYLthADWIIAMKDGSVLREG 881
Cdd:cd03257 170 DEPTSALDVSVQAQILD--LLKKLQEELgLTLLFITHDLgvvAKI--ADRVAVMYAGKIVEEG 228
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
666-895 |
1.17e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 93.66 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 666 ETEDIAIKVTNGYFSWGSGLA-TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN--------- 735
Cdd:PRK13648 2 EDKNSIIVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAitddnfekl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 736 RYSVAYAAQKP--WLLNATVEENITFG-----SPFNKQRYKaVTDACSlqpDIDLLPFGDQTEigergINLSGGQRQRIC 808
Cdd:PRK13648 82 RKHIGIVFQNPdnQFVGSIVKYDVAFGlenhaVPYDEMHRR-VSEALK---QVDMLERADYEP-----NALSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 809 VARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKR-TLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQ 887
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLLD--LVRKVKSEHNiTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIF 230
|
....*...
gi 530398972 888 TKDVELYE 895
Cdd:PRK13648 231 DHAEELTR 238
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1299-1515 |
1.25e-20 |
|
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: 91.81 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHtlRS 1374
Cdd:cd03259 1 LELKGLSKTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTL----LRLIAGLErpdsGEILIDGRDVTGVPPE--RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1375 RLSIILQDPILFS-----GSIRFNLDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCL 1446
Cdd:cd03259 73 NIGMVFQDYALFPhltvaENIAFGLKLRGVPKAEiraRVRELLELVGLEGLLNRYPHEL-----------SGGQQQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398972 1447 ARAFVRKSSILIMDEATASIDMAT-ENILQKVV-MTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYD 1515
Cdd:cd03259 142 ARALAREPSLLLLDEPLSALDAKLrEELREELKeLQRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
667-893 |
1.29e-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: 92.74 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 667 TEDIAIKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRNRYSVAYAAQKP 746
Cdd:COG1127 1 MSEPMIEVRNLTKSFG-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 747 W------------LLNA-TVEENITFG-------SPfnKQRYKAVT---DACSLQPDIDLLPfgdqteiGErginLSGGQ 803
Cdd:COG1127 80 LrrrigmlfqggaLFDSlTVFENVAFPlrehtdlSE--AEIRELVLeklELVGLPGAADKMP-------SE----LSGGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 804 RQRICVARALYQNTNIVFLDDPFSALDIHLS---DHLMQEgilkfLQDD-KRTLVLVTHKLQYL-THADWIIAMKDGSVL 878
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDPITSaviDELIRE-----LRDElGLTSVVVTHDLDSAfAIADRVAVLADGKII 221
|
250
....*....|....*
gi 530398972 879 REGTLKDIQTKDVEL 893
Cdd:COG1127 222 AEGTPEELLASDDPW 236
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1300-1512 |
2.21e-20 |
|
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: 90.19 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1300 KIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSII 1379
Cdd:cd03214 1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1380 LQdpILfsgsirfnldpeckctddrlwEALEIAQLKN-MVKSLPGGldavvteggenfsvgQRQLFCLARAFVRKSSILI 1458
Cdd:cd03214 79 PQ--AL---------------------ELLGLAHLADrPFNELSGG---------------ERQRVLLARALAQEPPILL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 530398972 1459 MDEATASIDMATE-NILQKVV-MTAFADRTVVTIAHRV-HTILTADLVIVMKRGNIL 1512
Cdd:cd03214 121 LDEPTSHLDIAHQiELLELLRrLARERGKTVVMVLHDLnLAARYADRVILLKDGRIV 177
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
672-877 |
2.67e-20 |
|
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: 89.76 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN--------RYSVAYAA 743
Cdd:cd03230 1 IEVRNLSKRYGKKTA-LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDikkepeevKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 744 QKPWLL-NATVEENItfgspfnkqrykavtdacslqpdidllpfgdqteigergiNLSGGQRQRICVARALYQNTNIVFL 822
Cdd:cd03230 80 EEPSLYeNLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 530398972 823 DDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYL-THADWIIAMKDGSV 877
Cdd:cd03230 120 DEPTSGLDPESRREFWE--LLRELKKEGKTILLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
688-882 |
3.70e-20 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 94.01 E-value: 3.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG-EMQTlEGKVHWSNR-------NRYSVAYAAQK----PWLlnaTVEE 755
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGfETPD-SGRILLDGRdvtglppEKRNVGMVFQDyalfPHL---TVAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 756 NITFG------SPfnKQRYKAVTDACSLqpdIDLLPFGDqteigeRGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSA 828
Cdd:COG3842 97 NVAFGlrmrgvPK--AEIRARVAELLEL---VGLEGLAD------RYPHqLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 530398972 829 LDIHLSDHLMQEgiLKFLQDD-KRTLVLVTHKlQY--LTHADWIIAMKDGSVLREGT 882
Cdd:COG3842 166 LDAKLREEMREE--LRRLQRElGITFIYVTHD-QEeaLALADRIAVMNDGRIEQVGT 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
688-858 |
6.62e-20 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 89.46 E-value: 6.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN--------RYSVAYAAQKPWLLNA-TVEENIT 758
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPirdaredyRRRLAYLGHADGLKPElTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 759 F-----GSPFNKQRYKAVTDACSLQPDIDLlPFGdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDI-- 831
Cdd:COG4133 98 FwaalyGLRADREAIDEALEAVGLAGLADL-PVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAag 166
|
170 180 190
....*....|....*....|....*....|...
gi 530398972 832 ------HLSDHLMQEGIlkflqddkrtLVLVTH 858
Cdd:COG4133 167 vallaeLIAAHLARGGA----------VLLTTH 189
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
690-881 |
7.37e-20 |
|
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: 89.66 E-value: 7.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 690 NIDIRIPtGQLTMIVGQVGCGKSSLLLAILGeMQTLEG---------------KVHWSNRNRySVAYAAQKPWLL-NATV 753
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAG-LEKPDGgtivlngtvlfdsrkKINLPPQQR-KIGLVFQQYALFpHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 754 EENITFGSPFN-----KQRYKAVTDACSLQPdidllpfgdqteIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFS 827
Cdd:cd03297 93 RENLAFGLKRKrnredRISVDELLDLLGLDH------------LLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 530398972 828 ALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKL---QYLthADWIIAMKDGSVLREG 881
Cdd:cd03297 161 ALDRALRLQLLPE-LKQIKKNLNIPVIFVTHDLseaEYL--ADRIVVMEDGRLQYIG 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1236-1523 |
7.55e-20 |
|
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: 95.14 E-value: 7.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1236 GLGLLYaltITNYLNwVVRNLAD----LE----VQMGAVKKVnsFLTM---------ESEnyegtmdPSQVPEHWPQEGE 1298
Cdd:COG4172 207 GMALLL---ITHDLG-VVRRFADrvavMRqgeiVEQGPTAEL--FAAPqhpytrkllAAE-------PRGDPRPVPPDAP 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 --IKIHDLCVRYENN---LKPVLKHVKAY------IKPGQKVGICGRTGSGKSSLSLAFFRMVDiFDGKIVIDGIDISKL 1367
Cdd:COG4172 274 plLEARDLKVWFPIKrglFRRTVGHVKAVdgvsltLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGL 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1368 P---LHTLRSRLSIILQDPilFsGSirfnLDPeckctddRL------WEALEI-------AQLKNMVKSLPG--GLDAVV 1429
Cdd:COG4172 353 SrraLRPLRRRMQVVFQDP--F-GS----LSP-------RMtvgqiiAEGLRVhgpglsaAERRARVAEALEevGLDPAA 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1430 -----TEggenFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATenilQKVVMTAFA---------------DRTVV- 1488
Cdd:COG4172 419 rhrypHE----FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV----QAQILDLLRdlqrehglaylfishDLAVVr 490
|
330 340 350
....*....|....*....|....*....|....*
gi 530398972 1489 TIAHRvhtiltadlVIVMKRGNILEYDTPESLLAQ 1523
Cdd:COG4172 491 ALAHR---------VMVMKDGKVVEQGPTEQVFDA 516
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
682-891 |
7.59e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 91.20 E-value: 7.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 682 GSGLATLS-NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN--RYSVAYAAQKPWLL--NATVEEN 756
Cdd:PRK10253 16 GYGKYTVAeNLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHiqHYASKEVARRIGLLaqNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 757 ITFGSPFNKQRYKAvtdacslQP--------DIDLLPFGDQ----TEIGERGIN-LSGGQRQRICVARALYQNTNIVFLD 823
Cdd:PRK10253 96 ITVQELVARGRYPH-------QPlftrwrkeDEEAVTKAMQatgiTHLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530398972 824 DPFSALDIhlsDHlmQEGILKFLQDDKR----TLVLVTHKL----QYLTHadwIIAMKDGSVLREGTLKDIQTKDV 891
Cdd:PRK10253 169 EPTTWLDI---SH--QIDLLELLSELNRekgyTLAAVLHDLnqacRYASH---LIALREGKIVAQGAPKEIVTAEL 236
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
663-882 |
8.73e-20 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 95.56 E-value: 8.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 663 RPAETEDIAIKvtNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN------- 735
Cdd:PRK10790 334 RPLQSGRIDID--NVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPlsslshs 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 736 --RYSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARAL 813
Cdd:PRK10790 412 vlRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398972 814 YQNTNIVFLDDPFSALDIHlsdhlMQEGILKFLQ--DDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 882
Cdd:PRK10790 492 VQTPQILILDEATANIDSG-----TEQAIQQALAavREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGT 557
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
703-900 |
9.62e-20 |
|
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: 92.17 E-value: 9.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 703 IVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN-------RYSVAYAAQKPWLL-NATVEENITFGSPFNK----QRYKA 770
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDvtnvpphLRHINMVFQSYALFpHMTVEENVAFGLKMRKvpraEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 771 VTDACSLqpdIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDD- 849
Cdd:TIGR01187 81 VLEALRL---VQLEEFADR-----KPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLE--LKTIQEQl 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 530398972 850 KRTLVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKdiqtkdvELYEHWKTL 900
Cdd:TIGR01187 151 GITFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPE-------EIYEEPANL 195
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
690-886 |
1.57e-19 |
|
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: 90.40 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 690 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN-------------RYSVAYAAQKPWLL-NATVEE 755
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDiaamsrkelrelrRKKISMVFQSFALLpHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 756 NITFGSPFN----KQRYKAVTDACSLqpdIDLLPFGDQtEIGErginLSGGQRQRICVARALYQNTNIVFLDDPFSALD- 830
Cdd:cd03294 122 NVAFGLEVQgvprAEREERAAEALEL---VGLEGWEHK-YPDE----LSGGMQQRVGLARALAVDPDILLMDEAFSALDp 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 530398972 831 -IHLSdhlMQEGILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREGTLKDI 886
Cdd:cd03294 194 lIRRE---MQDELLRLQAELQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
664-882 |
1.62e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 94.51 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 664 PAETEDIAIKVTNGYFSW-GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN------- 735
Cdd:PRK11160 331 TAAADQVSLTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPiadysea 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 736 --RYSVAYAAQKPWLLNATVEENITFGSP-FNKQRYKAVTDACSLQpdiDLLPfGDQ---TEIGERGINLSGGQRQRICV 809
Cdd:PRK11160 411 alRQAISVVSQRVHLFSATLRDNLLLAAPnASDEALIEVLQQVGLE---KLLE-DDKglnAWLGEGGRQLSGGEQRRLGI 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398972 810 ARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 882
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILEL-LAEHAQN--KTVLMITHRLTGLEQFDRICVMDNGQIIEQGT 556
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
671-864 |
2.62e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 89.33 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 671 AIKVTNGYFSWGSGlATLSNIDIRIPTGQLTMIVGQVGCGKSSLL--LAILGEMQT---LEGKVHWSNRN---------- 735
Cdd:PRK14258 7 AIKVNNLSFYYDTQ-KILEGVSMEIYQSKVTAIIGPSGCGKSTFLkcLNRMNELESevrVEGRVEFFNQNiyerrvnlnr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 736 -RYSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDAC--SLQPDIDLLpfgDQTE--IGERGINLSGGQRQRICVA 810
Cdd:PRK14258 86 lRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIveSALKDADLW---DEIKhkIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 530398972 811 RALYQNTNIVFLDDPFSALDIHLS---DHLMQEGILKflqdDKRTLVLVTHKLQYLT 864
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASmkvESLIQSLRLR----SELTMVIVSHNLHQVS 215
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
690-890 |
2.74e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 88.66 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 690 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRNrYSVAYAAQKP-----------WLLnaTVEENIT 758
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD-LTALPPAERPvsmlfqennlfPHL--TVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 759 FG-------SPFNKQRYKAVTDACSLQPDIDLLPfgDQteigerginLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 831
Cdd:COG3840 94 LGlrpglklTAEQRAQVEQALERVGLAGLLDRLP--GQ---------LSGGQRQRVALARCLVRKRPILLLDEPFSALDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398972 832 HLSDHLMQegILKFLQDD-KRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQTKD 890
Cdd:COG3840 163 ALRQEMLD--LVDELCRErGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGE 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
672-900 |
2.94e-19 |
|
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: 88.45 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNR-------NRYSVAYAAQ 744
Cdd:cd03300 1 IELENVSKFYGGFVA-LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKditnlppHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 745 KPWLL-NATVEENITFG---SPFNKQRYKA-VTDACSLqpdIDLLPFGDqteigeRGIN-LSGGQRQRICVARALYQNTN 818
Cdd:cd03300 80 NYALFpHLTVFENIAFGlrlKKLPKAEIKErVAEALDL---VQLEGYAN------RKPSqLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 819 IVFLDDPFSALDIHLSDHLMQEgiLKFLQDD-KRTLVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKDIqtkdvelYEH 896
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLE--LKRLQKElGITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEI-------YEE 221
|
....
gi 530398972 897 WKTL 900
Cdd:cd03300 222 PANR 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1299-1511 |
4.42e-19 |
|
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: 87.55 E-value: 4.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYEN--NLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHTL 1372
Cdd:cd03255 1 IELKNLSKTYGGggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTL----LNILGGLDrptsGEVRVDGTDISKLSEKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1373 ----RSRLSIILQD---------------PILFSGSIRfnldPECKctdDRLWEALEIAQLKNMVKSLPGGLdavvtegg 1433
Cdd:cd03255 77 aafrRRHIGFVFQSfnllpdltalenvelPLLLAGVPK----KERR---ERAEELLERVGLGDRLNHYPSEL-------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1434 enfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE----NILQKvvMTAFADRTVVTIAHRVHTILTADLVIVMKRG 1509
Cdd:cd03255 142 ---SGGQQQRVAIARALANDPKIILADEPTGNLDSETGkevmELLRE--LNKEAGTTIVVVTHDPELAEYADRIIELRDG 216
|
..
gi 530398972 1510 NI 1511
Cdd:cd03255 217 KI 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1299-1523 |
4.44e-19 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 88.02 E-value: 4.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNLK--PVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLP---L 1369
Cdd:cd03258 2 IELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTL----IRCINGLErptsGSVLVDGTDLTLLSgkeL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1370 HTLRSRLSIILQDPILFS-----GSIRFNLD---PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQR 1441
Cdd:cd03258 78 RKARRRIGMIFQHFNLLSsrtvfENVALPLEiagVPKAEIEERVLELLELVGLEDKADAYPAQL-----------SGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1442 QLFCLARAFVRKSSILIMDEATASIDMA-TENILQ--KVVMTAFaDRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTP 1517
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPEtTQSILAllRDINREL-GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTV 225
|
....*.
gi 530398972 1518 ESLLAQ 1523
Cdd:cd03258 226 EEVFAN 231
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
678-858 |
4.57e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 88.77 E-value: 4.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 678 YFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNR-------NRYSVAyaaQK----P 746
Cdd:COG4525 13 YPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVpvtgpgaDRGVVF---QKdallP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 747 WLlnaTVEENITFGSPFNK----QRYKAVTDACSLqpdIDLLPFGDQtEIGErginLSGGQRQRICVARALYQNTNIVFL 822
Cdd:COG4525 90 WL---NVLDNVAFGLRLRGvpkaERRARAEELLAL---VGLADFARR-RIWQ----LSGGMRQRVGIARALAADPRFLLM 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 530398972 823 DDPFSALDIhLSDHLMQEGILKFLQDDKRTLVLVTH 858
Cdd:COG4525 159 DEPFGALDA-LTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
663-861 |
1.24e-18 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 87.40 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 663 RPAETEDIAIKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI-----LGEMQTLEGKVHWSNRNRY 737
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDKQA-LKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndLIPGARVEGEILLDGEDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 738 S-----------VAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDacslqpdidllpfgdqtEIGER----------- 795
Cdd:COG1117 82 DpdvdvvelrrrVGMVFQKPNPFPKSIYDNVAYGLRLHGIKSKSELD-----------------EIVEEslrkaalwdev 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530398972 796 -------GINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDH---LMQEgiLKflqdDKRTLVLVTHKLQ 861
Cdd:COG1117 145 kdrlkksALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKieeLILE--LK----KDYTIVIVTHNMQ 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
671-886 |
1.40e-18 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 91.12 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 671 AIKVTNGYFSWGSG-LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG---EMQTLEGKVHWSNRN---------RY 737
Cdd:COG1123 4 LLEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDllelsealrGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 738 SVAYAAQKPW--LLNATVEENITFGSpfnkqRYKAVTDACSLQPDIDLLPFGDQTEIGERGIN-LSGGQRQRICVARALY 814
Cdd:COG1123 84 RIGMVFQDPMtqLNPVTVGDQIAEAL-----ENLGLSRAEARARVLELLEAVGLERRLDRYPHqLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398972 815 QNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDK-RTLVLVTHKLQY-LTHADWIIAMKDGSVLREGTLKDI 886
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILD--LLRELQRERgTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
672-877 |
1.52e-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: 85.77 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNR-------NRYSVAYAAQ 744
Cdd:cd03301 1 VELENVTKRFGNVTA-LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlppKDRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 745 KPWLL-NATVEENITFGSPFNKQRY----KAVTDACSLQpDIDLLpfgdqteIGERGINLSGGQRQRICVARALYQNTNI 819
Cdd:cd03301 80 NYALYpHMTVYDNIAFGLKLRKVPKdeidERVREVAELL-QIEHL-------LDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 530398972 820 VFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTH-KLQYLTHADWIIAMKDGSV 877
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAE-LKRLQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1314-1522 |
1.93e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 87.35 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1314 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGI---DISKLPlhTLRSRLSIILQDP-ILFSG- 1388
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgDFSKLQ--GIRKLVGIVFQNPeTQFVGr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1389 SIRFNL--DPECKCTddrlwEALEIAQLKNMVKSlPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASI 1466
Cdd:PRK13644 94 TVEEDLafGPENLCL-----PPIEIRKRVDRALA-EIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 530398972 1467 DMAT-ENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLA 1522
Cdd:PRK13644 168 DPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
664-861 |
1.93e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 87.14 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 664 PAETEDIAIKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLL-----LAILGEMQTLEGKVHWSNRNRYS 738
Cdd:PRK14243 3 TLNGTETVLRTENLNVYYGSFLA-VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrLNDLIPGFRVEGKVTFHGKNLYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 739 -----------VAYAAQKPWLLNATVEENITFGSPFNKqrYKavtdacslqpdidllpfGDQTEIGER------------ 795
Cdd:PRK14243 82 pdvdpvevrrrIGMVFQKPNPFPKSIYDNIAYGARING--YK-----------------GDMDELVERslrqaalwdevk 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398972 796 ------GINLSGGQRQRICVARALYQNTNIVFLDDPFSALDiHLSDhLMQEGILKFLQDDkRTLVLVTHKLQ 861
Cdd:PRK14243 143 dklkqsGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALD-PIST-LRIEELMHELKEQ-YTIIIVTHNMQ 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1299-1509 |
2.44e-18 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 84.16 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYenNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHT--L 1372
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTL----LRCIAGLEepdsGSILIDGEDLTDLEDELppL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1373 RSRLSIILQDPILFSGsirfnldpeckctddrlweaLEIAQlkNMVKSLPGGldavvteggenfsvgQRQLFCLARAFVR 1452
Cdd:cd03229 75 RRRIGMVFQDFALFPH--------------------LTVLE--NIALGLSGG---------------QQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1453 KSSILIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTILT-ADLVIVMKRG 1509
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1299-1513 |
2.63e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.12 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIF-----DGKIVIDGIDISKLPLHTLR 1373
Cdd:PRK14247 4 IEIRDLKVSFGQ--VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1374 SRLSIILQ--DPI----LFSG---SIRFN-LDPECKCTDDRLWEALEIAQLKNMVKSLpggLDAVVTEggenFSVGQRQL 1443
Cdd:PRK14247 82 RRVQMVFQipNPIpnlsIFENvalGLKLNrLVKSKKELQERVRWALEKAQLWDEVKDR---LDAPAGK----LSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530398972 1444 FCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAH------RVhtiltADLVIVMKRGNILE 1513
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVE 225
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
688-882 |
3.07e-18 |
|
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: 90.65 E-value: 3.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSL--LL---------AILGEMQTLegkvhwsnRN------RYSVAYAAQKPWLLN 750
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLarLLfrfydvtsgRILIDGQDI--------RDvtqaslRAAIGIVPQDTVLFN 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 751 ATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 829
Cdd:COG5265 446 DTIAYNIAYGRPdASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSAL 525
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 530398972 830 DIHlSDHLMQEGiLKFLQDDKRTLVlVTHKLQYLTHADWIIAMKDGSVLREGT 882
Cdd:COG5265 526 DSR-TERAIQAA-LREVARGRTTLV-IAHRLSTIVDADEILVLEAGRIVERGT 575
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
687-909 |
3.44e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 85.98 E-value: 3.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 687 TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI--LGEMQ---TLEGKVHWSNRNRYS-----------VAYAAQKPWLLN 750
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNpevTITGSIVYNGHNIYSprtdtvdlrkeIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 751 ATVEENITFGSPFNKQRYKAVTDAcSLQPDIDLLPFGDQTE--IGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 828
Cdd:PRK14239 100 MSIYENVVYGLRLKGIKDKQVLDE-AVEKSLKGASIWDEVKdrLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 829 LDiHLSDHLMQEGILKFlqDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIqtkdvelyehwktLMNRQDQE 907
Cdd:PRK14239 179 LD-PISAGKIEETLLGL--KDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQM-------------FMNPKHKE 242
|
..
gi 530398972 908 LE 909
Cdd:PRK14239 243 TE 244
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
672-877 |
4.67e-18 |
|
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: 82.86 E-value: 4.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSnrnrysvayaaqkpwllna 751
Cdd:cd03216 1 LELRGITKRFGGVKA-LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 752 tvEENITFGSPFNKQRykavtdacslqpdidllpfgdqteigeRGIN----LSGGQRQRICVARALYQNTNIVFLDDPFS 827
Cdd:cd03216 61 --GKEVSFASPRDARR---------------------------AGIAmvyqLSVGERQMVEIARALARNARLLILDEPTA 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 530398972 828 ALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQY-LTHADWIIAMKDGSV 877
Cdd:cd03216 112 ALTPAEVERLFK--VIRRLRAQGVAVIFISHRLDEvFEIADRVTVLRDGRV 160
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1314-1509 |
5.42e-18 |
|
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: 84.69 E-value: 5.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1314 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR----LSIILQDPILFSGS 1389
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1390 IRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDM- 1468
Cdd:cd03290 95 VEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIh 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 530398972 1469 ATENILQKVVMTAFAD--RTVVTIAHRVHTILTADLVIVMKRG 1509
Cdd:cd03290 175 LSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
690-914 |
6.33e-18 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 89.56 E-value: 6.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 690 NIDIRIPTGQLTMIVGQVGCGKSSLLLAI-------LGEMQTLEGKVHWSNRN--RYSVAYAAQKPWLLNATVEENITFG 760
Cdd:TIGR01192 353 DVSFEAKAGQTVAIVGPTGAGKTTLINLLqrvydptVGQILIDGIDINTVTREslRKSIATVFQDAGLFNRSIRENIRLG 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 761 --SPFNKQRYKAvTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLM 838
Cdd:TIGR01192 433 reGATDEEVYEA-AKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVE-TEARV 510
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530398972 839 QEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEHWKTLMNRQDQELEKDMEA 914
Cdd:TIGR01192 511 KNAIDALRKN--RTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRRSGLLTNQPATKPLRK 584
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1299-1525 |
8.11e-18 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 84.76 E-value: 8.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidiskLPLHTLRSRLSI 1378
Cdd:COG1121 7 IELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG-----KPPRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1379 ILQD-------PIL--------FSGSIRF--NLDPECKctdDRLWEALE---IAQLKN-MVKSLpggldavvteggenfS 1437
Cdd:COG1121 80 VPQRaevdwdfPITvrdvvlmgRYGRRGLfrRPSRADR---EAVDEALErvgLEDLADrPIGEL---------------S 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1438 VGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMT-AFADRTVVTIAHRVHTILT-ADLVIVMKRGnILEYD 1515
Cdd:COG1121 142 GGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRG-LVAHG 220
|
250
....*....|
gi 530398972 1516 TPESLLAQEN 1525
Cdd:COG1121 221 PPEEVLTPEN 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
671-886 |
9.82e-18 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 84.31 E-value: 9.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 671 AIKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRNRYSVA---------- 740
Cdd:cd03296 2 SIEVRNVSKRFGDFVA-LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPvqernvgfvf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 741 --YAAQKpwllNATVEENITFGSPFNKQRYKAVTDACSLQPDiDLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNT 817
Cdd:cd03296 81 qhYALFR----HMTVFDNVAFGLRVKPRSERPPEAEIRAKVH-ELLKLVQLDWLADRYPAqLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398972 818 NIVFLDDPFSALDIHLSDHLmqEGILKFLQDDKR-TLVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKDI 886
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKEL--RRWLRRLHDELHvTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
688-886 |
1.24e-17 |
|
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: 83.78 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG-EMQTlEGKVHWSNRN------------RYSVAYAAQKPWLLNA-TV 753
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGlERPT-SGSVLVDGTDltllsgkelrkaRRRIGMIFQHFNLLSSrTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 754 EENITF-----GSPfNKQRYKAVTDacslqpdidLLPFGDQTEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFS 827
Cdd:cd03258 100 FENVALpleiaGVP-KAEIEERVLE---------LLELVGLEDKADAYPaQLSGGQKQRVGIARALANNPKVLLCDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398972 828 ALDIHLSDhlmqeGILKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 886
Cdd:cd03258 170 ALDPETTQ-----SILALLRDINRelglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
667-886 |
1.25e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 84.66 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 667 TEDIAIKVTNGYFSWGSG-LATLSNIDIRIPTGQLTMIVGQVGCGKSS---LLLAIL----GEMQtLEGKVhWSNRN--- 735
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTiskILTGLLkpqsGEIK-IDGIT-ISKENlke 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 736 -RYSVAYAAQKP--WLLNATVEENITFG---SPFNKQRYKAVTDACSLQPDI-DLLPFGDQteigergiNLSGGQRQRIC 808
Cdd:PRK13632 81 iRKKIGIIFQNPdnQFIGATVEDDIAFGlenKKVPPKKMKDIIDDLAKKVGMeDYLDKEPQ--------NLSGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398972 809 VARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDD-KRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDI 886
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKK--IMVDLRKTrKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1294-1493 |
1.51e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 88.33 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1294 PQEGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVI-DGIDISKLP 1368
Cdd:COG4178 358 SEDGALALEDLTLRTPDG-RPLLEDLSLSLKPGERLLITGPSGSGKSTL----LRAIaglwPYGSGRIARpAGARVLFLP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1369 lhtlrsrlsiilQDPILFSGSIRFNL---DPECKCTDDRLWEALEIAQLKNmvksLPGGLDaVVTEGGENFSVGQRQLFC 1445
Cdd:COG4178 433 ------------QRPYLPLGTLREALlypATAEAFSDAELREALEAVGLGH----LAERLD-EEADWDQVLSLGEQQRLA 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 530398972 1446 LARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR 1493
Cdd:COG4178 496 FARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1299-1513 |
2.12e-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: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYE--NNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAffrMVDIFD-GKIVIDGIDISKLP---LH 1370
Cdd:COG1136 5 LELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLlnILG---GLDRPTsGEVLIDGQDISSLSereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1371 TLRSR-LSIILQDpilfsgsirFNLDPE-----------------CKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteg 1432
Cdd:COG1136 82 RLRRRhIGFVFQF---------FNLLPEltalenvalplllagvsRKERRERARELLERVGLGDRLDHRPSQL------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1433 genfSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT-ENILQkvVMTAFAD---RTVVTIAHRVHTILTADLVIVMKR 1508
Cdd:COG1136 146 ----SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgEEVLE--LLRELNRelgTTIVMVTHDPELAARADRVIRLRD 219
|
....*
gi 530398972 1509 GNILE 1513
Cdd:COG1136 220 GRIVS 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1299-1511 |
2.42e-17 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 81.29 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRM----VDIFDGKIVIDGIDISKLPlHTLRS 1374
Cdd:cd03230 1 IEVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTTL----IKIilglLKPDSGEIKVLGKDIKKEP-EEVKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1375 RLSIILQDPILFSG-SIRFNLDpeckctddrlwealeiaqlknmvkslpggldavvteggenFSVGQRQLFCLARAFVRK 1453
Cdd:cd03230 74 RIGYLPEEPSLYENlTVRENLK----------------------------------------LSGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1454 SSILIMDEATASIDMATENILQKVVMT-AFADRTVVTIAHRVHTILT-ADLVIVMKRGNI 1511
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
681-859 |
2.57e-17 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 82.70 E-value: 2.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 681 WGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ---TLEGKVHWSNRNR------YSVAYAAQKPWLL-N 750
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRkpdqfqKCVAYVRQDDILLpG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 751 ATVEENITFGSPF-----NKQRYKAVTDACSLQPDIDLLPFGdqteiGERGINLSGGQRQRICVARALYQNTNIVFLDDP 825
Cdd:cd03234 96 LTVRETLTYTAILrlprkSSDAIRKKRVEDVLLRDLALTRIG-----GNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190
....*....|....*....|....*....|....
gi 530398972 826 FSALDIHLSDHLMQegILKFLQDDKRTLVLVTHK 859
Cdd:cd03234 171 TSGLDSFTALNLVS--TLSQLARRNRIVILTIHQ 202
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1299-1525 |
2.92e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 82.50 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYEN-----NLKpvlkhvkayIKPGQKVGICGRTGSGKSSLS--LAFFRMVDifDGKIVIDGIDISKLPLHT 1371
Cdd:COG3840 2 LRLDDLTYRYGDfplrfDLT---------IAAGERVAILGPSGAGKSTLLnlIAGFLPPD--SGRILWNGQDLTALPPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1372 lrsR-LSIILQDPILFSG-SIRFN----LDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQ 1442
Cdd:COG3840 71 ---RpVSMLFQENNLFPHlTVAQNiglgLRPGLKLTAEqraQVEQALERVGLAGLLDRLPGQL-----------SGGQRQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1443 LFCLARAFVRKSSILIMDEATASIDMA-TENILQKVV-MTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPES 1519
Cdd:COG3840 137 RVALARCLVRKRPILLLDEPFSALDPAlRQEMLDLVDeLCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAA 216
|
....*.
gi 530398972 1520 LLAQEN 1525
Cdd:COG3840 217 LLDGEP 222
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
688-886 |
2.94e-17 |
|
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: 82.77 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS----------NRNrysVAYAAQKPWLL-NATVEEN 756
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkditnlppeKRD---ISYVPQNYALFpHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 757 ITFGspFNKQRYKAVTDACSLQpdidllpfgdqtEIGER-GIN---------LSGGQRQRICVARALYQNTNIVFLDDPF 826
Cdd:cd03299 92 IAYG--LKKRKVDKKEIERKVL------------EIAEMlGIDhllnrkpetLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398972 827 SALDIHLSDHLMQEgiLKFLQDDKRTLVL-VTHKL-QYLTHADWIIAMKDGSVLREGTLKDI 886
Cdd:cd03299 158 SALDVRTKEKLREE--LKKIRKEFGVTVLhVTHDFeEAWALADKVAIMLNGKLIQVGKPEEV 217
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
688-906 |
3.49e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 83.14 E-value: 3.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLL----------------LAILGEMQTLEGKVHWSNR-NRYSVAYAAQKPWLLN 750
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsglitgdksagshIELLGRTVQREGRLARDIRkSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 751 A-TVEENITFG---------------SPFNKQR-YKAVTDacslqpdIDLLPFGDQteigeRGINLSGGQRQRICVARAL 813
Cdd:PRK09984 100 RlSVLENVLIGalgstpfwrtcfswfTREQKQRaLQALTR-------VGMVHFAHQ-----RVSTLSGGQQQRVAIARAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 814 YQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDDKRTLVLVTHKLQY-LTHADWIIAMKDGSVLREGTlkdIQTKDVE 892
Cdd:PRK09984 168 MQQAKVILADEPIASLDPE-SARIVMDTLRDINQNDGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGS---SQQFDNE 243
|
250
....*....|....
gi 530398972 893 LYEHWKTLMNRQDQ 906
Cdd:PRK09984 244 RFDHLYRSINRVEE 257
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
688-872 |
3.59e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 82.45 E-value: 3.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN---------RNRYSVAYAAQKPWLLNATVEENIT 758
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGedistlkpeIYRQQVSYCAQTPTLFGDTVYDNLI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 759 FGSPFNKQRykavtdacsLQPDI---DLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlS 834
Cdd:PRK10247 103 FPWQIRNQQ---------PDPAIfldDLERFALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDES-N 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 530398972 835 DHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAM 872
Cdd:PRK10247 173 KHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
691-896 |
4.01e-17 |
|
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: 84.78 E-value: 4.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 691 IDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNR-------------NRYSVAYAAQKPWLL-NATVEEN 756
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrkgiflppEKRRIGYVFQEARLFpHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 757 ITFG-----SPFNKQRYKAVTDACSLQPDIDLLPfGDqteigerginLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 831
Cdd:TIGR02142 96 LRYGmkrarPSERRISFERVIELLGIGHLLGRLP-GR----------LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398972 832 HLSDHlmqegILKFLQDDKRTL----VLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQ-TKDVELYEH 896
Cdd:TIGR02142 165 PRKYE-----ILPYLERLHAEFgipiLYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWaSPDLPWLAR 230
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1299-1520 |
4.02e-17 |
|
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: 82.62 E-value: 4.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSR 1375
Cdd:cd03256 1 IEVENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1376 LSIILQDpilfsgsirFNLDPECKCTDDRLWEALeiAQlKNMVKSLPG-----------------GLDAVVTEGGENFSV 1438
Cdd:cd03256 80 IGMIFQQ---------FNLIERLSVLENVLSGRL--GR-RSTWRSLFGlfpkeekqralaalervGLLDKAYQRADQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1439 GQRQLFCLARAFVRKSSILIMDEATASIDMATENIlqkvVMTAFAD------RTVVTIAHRVHTILT-ADLVIVMKRGNI 1511
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQ----VMDLLKRinreegITVIVSLHQVDLAREyADRIVGLKDGRI 223
|
....*....
gi 530398972 1512 LEYDTPESL 1520
Cdd:cd03256 224 VFDGPPAEL 232
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
684-861 |
5.11e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.44 E-value: 5.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNR-------NRYSV-AYAAQKPWLlnaTVEE 755
Cdd:PRK11248 13 GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKpvegpgaERGVVfQNEGLLPWR---NVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 756 NITFGspfnkQRYKAVTDACSLQPDIDLLPFGDQTEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 834
Cdd:PRK11248 90 NVAFG-----LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTR 164
|
170 180
....*....|....*....|....*..
gi 530398972 835 DHlMQEGILKFLQDDKRTLVLVTHKLQ 861
Cdd:PRK11248 165 EQ-MQTLLLKLWQETGKQVLLITHDIE 190
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
688-896 |
6.40e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 83.15 E-value: 6.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN-------------RYSVAYAAQKP--WLLNAT 752
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVitagkknkklkplRKKVGIVFQFPehQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 753 VEENITFGsPFN--------KQRYKAVTDACSLQPDI-DLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLD 823
Cdd:PRK13634 103 VEKDICFG-PMNfgvseedaKQKAREMIELVGLPEELlARSPF-----------ELSGGQMRRVAIAGVLAMEPEVLVLD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398972 824 DPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQTKDVELYEH 896
Cdd:PRK13634 171 EPTAGLDPKGRKEMM-EMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFADPDELEAI 243
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
692-881 |
6.86e-17 |
|
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: 81.00 E-value: 6.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 692 DIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWsNRNRYSVAYAAQKP---------WLLNATVEENITFG-S 761
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLI-NGVDVTAAPPADRPvsmlfqennLFAHLTVEQNVGLGlS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 762 P---FNKQRYKAVTDAcslqpdidLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHlM 838
Cdd:cd03298 97 PglkLTAEDRQAIEVA--------LARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE-M 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 530398972 839 QEGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREG 881
Cdd:cd03298 168 LDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
688-882 |
9.87e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 81.74 E-value: 9.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRnrysvAYAAQKPWLLNA---------------T 752
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGR-----PLADWSPAELARrravlpqhsslsfpfT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 753 VEENITFG-SPF--NKQRYKAVTDACSLQpdIDLLPFGD---QTeigerginLSGGQRQRICVARALYQNTN------IV 820
Cdd:PRK13548 93 VEEVVAMGrAPHglSRAEDDALVAAALAQ--VDLAHLAGrdyPQ--------LSGGEQQRVQLARVLAQLWEpdgpprWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398972 821 FLDDPFSALDIHLSDHLMQegILK-FLQDDKRTLVLVTHKL----QYlthADWIIAMKDGSVLREGT 882
Cdd:PRK13548 163 LLDEPTSALDLAHQHHVLR--LARqLAHERGLAVIVVLHDLnlaaRY---ADRIVLLHQGRLVADGT 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1299-1525 |
1.01e-16 |
|
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: 81.01 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFR-MVDIF---DGKIVIDGIDISKL---PLHT 1371
Cdd:cd03261 1 IELRGLTKSFGG--RTVLKGVDLDVRRGEILAIIGPSGSGKSTL----LRlIVGLLrpdSGEVLIDGEDISGLseaELYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1372 LRSRLSIILQDPILFSG-----SIRFNLDPECKCTDdrlWEALEIAQLK-NMVkSLPGGLDAVVTEggenFSVGQRQLFC 1445
Cdd:cd03261 75 LRRRMGMLFQSGALFDSltvfeNVAFPLREHTRLSE---EEIREIVLEKlEAV-GLRGAEDLYPAE----LSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1446 LARAFVRKSSILIMDEATASID-MATENI------LQKVVmtafaDRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTP 1517
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDpIASGVIddlirsLKKEL-----GLTSIMVTHDLDTAFaIADRIAVLYDGKIVAEGTP 221
|
....*...
gi 530398972 1518 ESLLAQEN 1525
Cdd:cd03261 222 EELRASDD 229
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1299-1508 |
1.09e-16 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 80.59 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENN--LKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGidiskLPLHTL 1372
Cdd:cd03293 1 LEVRNVSKTYGGGggAVTALEDISLSVEEGEFVALVGPSGCGKSTL----LRIIAGLErptsGEVLVDG-----EPVTGP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1373 RSRLSIILQDPILFS-GSIRFN--LDPECKCTDDRLW-----EALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1444
Cdd:cd03293 72 GPDRGYVFQQDALLPwLTVLDNvaLGLELQGVPKAEAreraeELLELVGLSGFENAYPHQL-----------SGGMRQRV 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398972 1445 CLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVH-TILTADLVIVMKR 1508
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDeAVFLADRVVVLSA 207
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
688-886 |
1.33e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 83.46 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRNRYSVAyAAQKPwlLNA-----------TVEEN 756
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP-AENRH--VNTvfqsyalfphmTVFEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 757 ITFG-----SPfNKQRYKAVTDACSLqpdIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 831
Cdd:PRK09452 107 VAFGlrmqkTP-AAEITPRVMEALRM---VQLEEFAQR-----KPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDY 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 832 HLSDHLMQEgiLKFLQddkRTL----VLVTH-KLQYLTHADWIIAMKDGSVLREGTLKDI 886
Cdd:PRK09452 178 KLRKQMQNE--LKALQ---RKLgitfVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1299-1535 |
1.52e-16 |
|
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: 80.81 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYeNNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1378
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1379 ILQDPILFSG-SIRFNLD--------PECKcTDDRLWEALEIAQL--KNMVKSLPGGLdavvteggenfSVGQRQLFCLA 1447
Cdd:cd03295 80 VIQQIGLFPHmTVEENIAlvpkllkwPKEK-IRERADELLALVGLdpAEFADRYPHEL-----------SGGQQQRVGVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1448 RAFVRKSSILIMDEATASIDMATENILQKvvmtAFAD------RTVVTIAHRV-HTILTADLVIVMKRGNILEYDTPESL 1520
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQE----EFKRlqqelgKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
250
....*....|....*.
gi 530398972 1521 LA-QENGVFASFVRAD 1535
Cdd:cd03295 224 LRsPANDFVAEFVGAD 239
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
690-888 |
1.85e-16 |
|
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: 82.84 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 690 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH-----WSNRNRY--------SVAYAAQK----PWLlnaT 752
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevLQDSARGiflpphrrRIGYVFQEarlfPHL---S 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 753 VEENITFGSPFNKQRYKAVtdacslQPD--IDLLpfgdqtEIG---ERGI-NLSGGQRQRICVARALYQNTNIVFLDDPF 826
Cdd:COG4148 94 VRGNLLYGRKRAPRAERRI------SFDevVELL------GIGhllDRRPaTLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398972 827 SALDIHLSDHLMQegILKFLQDDKRTLVL-VTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQT 888
Cdd:COG4148 162 AALDLARKAEILP--YLERLRDELDIPILyVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLS 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1295-1523 |
1.87e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 81.60 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1295 QEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS 1374
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1375 RLSIILQDPI-LFSGS-----IRFNLDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 1445
Cdd:PRK13635 82 QVGMVFQNPDnQFVGAtvqddVAFGLENIGVPREEmveRVDQALRQVGMEDFLNREPHRL-----------SGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1446 LARAFVRKSSILIMDEATASID-MATENILQKV-VMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1523
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDpRGRREVLETVrQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1316-1533 |
1.99e-16 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 81.15 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1316 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRS-RLSIILQDPILFS---- 1387
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRkKISMVFQSFALLPhrtv 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1388 -GSIRFNLDPECKCTDDRL---WEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEAT 1463
Cdd:cd03294 120 lENVAFGLEVQGVPRAEREeraAEALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398972 1464 ASIDMATENILQKVVMTAFAD--RTVVTIAHRV-HTILTADLVIVMKRGNILEYDTPESLLAQ-ENGVFASFVR 1533
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAElqKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILTNpANDYVREFFR 262
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
686-895 |
2.03e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 81.38 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 686 ATLSNIDIRIPTGQLTMIVGQVGCGKSS-------LLL---------AILGemQTLEGKVHWSNRNRYSVAYAAQKPWLL 749
Cdd:PRK13640 21 PALNDISFSIPRGSWTALIGHNGSGKSTisklingLLLpddnpnskiTVDG--ITLTAKTVWDIREKVGIVFQNPDNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 750 NATVEENITFGSPfNKQ--RYKAVTDACSLQPDIDLLPFGDQTEIgergiNLSGGQRQRICVARALYQNTNIVFLDDPFS 827
Cdd:PRK13640 99 GATVGDDVAFGLE-NRAvpRPEMIKIVRDVLADVGMLDYIDSEPA-----NLSGGQKQRVAIAGILAVEPKIIILDESTS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398972 828 ALDIHLSDHLMQegILKFLQDDKR-TLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYE 895
Cdd:PRK13640 173 MLDPAGKEQILK--LIRKLKKKNNlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVEMLKE 239
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
679-882 |
2.08e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 84.63 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 679 FSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQT-LEGKVHWSNRN---------RYSVAYAAQKPWL 748
Cdd:PRK13657 342 FSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI-NLLQRVFDpQSGRILIDGTDirtvtraslRRNIAVVFQDAGL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 749 LNATVEENITFGSP--FNKQRYKAVTDACSLqpD-IDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 825
Cdd:PRK13657 421 FNRSIEDNIRVGRPdaTDEEMRAAAERAQAH--DfIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEA 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 530398972 826 FSALDIHLSDHLmQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 882
Cdd:PRK13657 499 TSALDVETEAKV-KAALDELMKG--RTTFIIAHRLSTVRNADRILVFDNGRVVESGS 552
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1299-1522 |
2.17e-16 |
|
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: 79.79 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTlRSRLSI 1378
Cdd:cd03224 1 LEVENLNAGYGKS--QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-RARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1379 IL--QDPILFSG-SIRFNLD-PECKCTDDRLWEALEIA-----QLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARA 1449
Cdd:cd03224 78 GYvpEGRRIFPElTVEENLLlGAYARRRAKRKARLERVyelfpRLKERRKQLAGTL-----------SGGEQQMLAIARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398972 1450 FVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLA 1522
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLApKIVEEIFEAIRELRDEGVTILLVEQNARFALeIADRAYVLERGRVVLEGTAAELLA 221
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
684-842 |
2.94e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.15 E-value: 2.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN------RYSVAYA----AQKPWLlnaTV 753
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDiddpdvAEACHYLghrnAMKPAL---TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 754 EENITFGSPFNKQRYKAVTDACS---LQPDIDLlPFGdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALD 830
Cdd:PRK13539 91 AENLEFWAAFLGGEELDIAAALEavgLAPLAHL-PFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180
....*....|....*....|
gi 530398972 831 IH--------LSDHLMQEGI 842
Cdd:PRK13539 160 AAavalfaelIRAHLAQGGI 179
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
671-881 |
3.74e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 80.31 E-value: 3.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 671 AIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHW----SNR--NRYSVAYAAQ 744
Cdd:PRK15056 6 GIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISIlgqpTRQalQKNLVAYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 745 KP---WLLNATVEENITFGS---------PFNKQRyKAVTDACSlqpDIDLLPFgDQTEIGErginLSGGQRQRICVARA 812
Cdd:PRK15056 86 SEevdWSFPVLVEDVVMMGRyghmgwlrrAKKRDR-QIVTAALA---RVDMVEF-RHRQIGE----LSGGQKKRVFLARA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 813 LYQNTNIVFLDDPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKdGSVLREG 881
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARII--SLLRELRDEGKTMLVSTHNLGSVTEfCDYTVMVK-GTVLASG 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1326-1511 |
4.49e-16 |
|
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: 78.69 E-value: 4.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1326 GQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPlhTLRSRLSIILQDPILFS-----GSIRFNLDP 1396
Cdd:cd03298 24 GEITAIVGPSGSGKSTL----LNLIAGFEtpqsGRVLINGVDVTAAP--PADRPVSMLFQENNLFAhltveQNVGLGLSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1397 ECKCT-DDRlwEALEIAQ----LKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 1471
Cdd:cd03298 98 GLKLTaEDR--QAIEVALarvgLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 530398972 1472 NILQKVVMTAFADR--TVVTIAHRVHTILT-ADLVIVMKRGNI 1511
Cdd:cd03298 165 AEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
688-886 |
4.99e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 81.67 E-value: 4.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG-EMQT-----LEGK----VHWSNRNrysVAYAAQKPWLL-NATVEEN 756
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGlEHQTsghirFHGTdvsrLHARDRK---VGFVFQHYALFrHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 757 ITFGS---PFNKQRYKAVTDACSLQpdidLLPFGDQTEIGER-GINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 832
Cdd:PRK10851 95 IAFGLtvlPRRERPNAAAIKAKVTQ----LLEMVQLAHLADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 530398972 833 LSDHLmQEGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 886
Cdd:PRK10851 171 VRKEL-RRWLRQLHEELKFTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1299-1532 |
5.60e-16 |
|
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: 78.92 E-value: 5.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNlkpVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDifDGKIVIDGIDISKLPlhTLRSRL 1376
Cdd:cd03299 1 LKVENLSKDWKEF---KLKNVSLEVERGDYFVILGPTGSGKSVLleTIAGFIKPD--SGKILLNGKDITNLP--PEKRDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1377 SIILQDPILFSG-SIRFNLDPECKctdDRLWEALEI-AQLKNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKS 1454
Cdd:cd03299 74 SYVPQNYALFPHmTVYKNIAYGLK---KRKVDKKEIeRKVLEIAEML--GIDHLLNRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1455 SILIMDEATASIDMATENILQKVVMTAF--ADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQ-ENGVFAS 1530
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRkeFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKpKNEFVAE 228
|
..
gi 530398972 1531 FV 1532
Cdd:cd03299 229 FL 230
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1300-1511 |
5.67e-16 |
|
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: 78.34 E-value: 5.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1300 KIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidiskLPLHTLRSRL--- 1376
Cdd:cd03235 1 EVEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIgyv 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1377 ---SIILQD-PILFSGSIRFNLDPEC------KCTD-DRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 1445
Cdd:cd03235 74 pqrRSIDRDfPISVRDVVLMGLYGHKglfrrlSKADkAKVDEALERVGLSELADRQIGEL-----------SGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530398972 1446 LARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTILT-ADLVIVMKRGNI 1511
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEyFDRVLLLNRTVV 210
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
688-877 |
6.47e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 79.34 E-value: 6.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV--------HWSNRNRYSVAYAAQKPWllnATVEENITF 759
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELlagtaplaEAREDTRLMFQDARLLPW---KKVIDNVGL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 760 GSPFN-KQRYKAVTDACSLQPdidllpfgdqtEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhLSDHLM 838
Cdd:PRK11247 105 GLKGQwRDAALQALAAVGLAD-----------RANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA-LTRIEM 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 530398972 839 QEGILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMKDGSV 877
Cdd:PRK11247 173 QDLIESLWQQHGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
672-890 |
7.29e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.81 E-value: 7.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRNRYS---------VAYA 742
Cdd:PRK09536 4 IDVSDLSVEFG-DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAlsaraasrrVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 743 AQKPWL-LNATVEENITFGSPFNKQRYKAVTDACSLQPDiDLLPFGDQTEIGERGI-NLSGGQRQRICVARALYQNTNIV 820
Cdd:PRK09536 83 PQDTSLsFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVE-RAMERTGVAQFADRPVtSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398972 821 FLDDPFSALDIHlsdHLMQE-GILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDIQTKD 890
Cdd:PRK09536 162 LLDEPTASLDIN---HQVRTlELVRRLVDDGKTAVAAIHDLDLAArYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
692-877 |
8.18e-16 |
|
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: 77.98 E-value: 8.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 692 DIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhWSNRNRYSVAYAAQKPWLL---------NATVEENITFG-S 761
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSI-KVNDQSHTGLAPYQRPVSMlfqennlfaHLTVRQNIGLGlH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 762 PFNK----QRYKAVTDACSLQPD--IDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD 835
Cdd:TIGR01277 97 PGLKlnaeQQEKVVDAAQQVGIAdyLDRLPE-----------QLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 530398972 836 HlMQEGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSV 877
Cdd:TIGR01277 166 E-MLALVKQLCSERQRTLLMVTHHLSDARAiASQIAVVSQGKI 207
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
1331-1532 |
9.43e-16 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 80.23 E-value: 9.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1331 ICGRTGSGKSSL--SLAFFRMVDifDGKIVIDGIDISKLPLHtLRSrLSIILQDPILF-----SGSIRFNL--DPECKCT 1401
Cdd:TIGR01187 1 LLGPSGCGKTTLlrLLAGFEQPD--SGSIMLDGEDVTNVPPH-LRH-INMVFQSYALFphmtvEENVAFGLkmRKVPRAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1402 -DDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASID------MATE--N 1472
Cdd:TIGR01187 77 iKPRVLEALRLVQLEEFADRKPHQL-----------SGGQQQRVALARALVFKPKILLLDEPLSALDkklrdqMQLElkT 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398972 1473 ILQKVVMtafadrTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQENGVF-ASFV 1532
Cdd:TIGR01187 146 IQEQLGI------TFVFVTHDQEEAMTmSDRIAIMRKGKIAQIGTPEEIYEEPANLFvARFI 201
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1299-1512 |
9.95e-16 |
|
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: 77.79 E-value: 9.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIF----DGKIVIDGIDISKLPLHTl 1372
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTT----LRMLAGLlepdAGFATVDGFDVVKEPAEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1373 RSRLSIilqdpilFSGSIRFNldpeckctdDRL--WEALEI---------AQLKNMVKSLPGGLD--AVVTEGGENFSVG 1439
Cdd:cd03266 77 RRRLGF-------VSDSTGLY---------DRLtaRENLEYfaglyglkgDELTARLEELADRLGmeELLDRRVGGFSTG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398972 1440 QRQLFCLARAFVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNIL 1512
Cdd:cd03266 141 MRQKVAIARALVHDPPVLLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1299-1523 |
1.10e-15 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 80.10 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNLKPVlkhvKA------YIKPGQKVGICGRTGSGKSSLSLAFFRMVD---IFDGKIVIDGIDISKLPL 1369
Cdd:COG0444 2 LEVRNLKVYFPTRRGVV----KAvdgvsfDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1370 HTLRS----RLSIILQDPIlfsGSirfnLDPeCKCTDDRLWEALEI------AQLKNMVKSLpggLDAV-VTEGGE---- 1434
Cdd:COG0444 78 KELRKirgrEIQMIFQDPM---TS----LNP-VMTVGDQIAEPLRIhgglskAEARERAIEL---LERVgLPDPERrldr 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1435 ---NFSVGQRQLFCLARAFVRKSSILIMDEATASIDmATeniLQKVVMTAFADR------TVVTIAHRVHTIL-TADLVI 1504
Cdd:COG0444 147 yphELSGGMRQRVMIARALALEPKLLIADEPTTALD-VT---IQAQILNLLKDLqrelglAILFITHDLGVVAeIADRVA 222
|
250
....*....|....*....
gi 530398972 1505 VMKRGNILEYDTPESLLAQ 1523
Cdd:COG0444 223 VMYAGRIVEEGPVEELFEN 241
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
672-886 |
1.11e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 78.97 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV-------HWSNRN----RYSVA 740
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVlikgepiKYDKKSllevRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 741 YAAQKP--WLLNATVEENITFGsPFN-----KQRYKAVTDACSlqpdidllpfgdqtEIGERGI------NLSGGQRQRI 807
Cdd:PRK13639 82 IVFQNPddQLFAPTVEEDVAFG-PLNlglskEEVEKRVKEALK--------------AVGMEGFenkpphHLSGGQKKRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 808 CVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYL-THADWIIAMKDGSVLREGTLKDI 886
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLDPMGASQIMK--LLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
688-858 |
1.47e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 77.14 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ---TLEGKVhWSNRNRYS--------VAYAAQKPWLL-NATVEE 755
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEV-LLNGRRLTalpaeqrrIGILFQDDLLFpHLSVGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 756 NITFGSP--FNK-QRYKAVTDAcsLQpDIDLLPFGDQTeIGErginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 832
Cdd:COG4136 96 NLAFALPptIGRaQRRARVEQA--LE-EAGLAGFADRD-PAT----LSGGQRARVALLRALLAEPRALLLDEPFSKLDAA 167
|
170 180
....*....|....*....|....*...
gi 530398972 833 LSDHLMQegiLKFLQDDKRTL--VLVTH 858
Cdd:COG4136 168 LRAQFRE---FVFEQIRQRGIpaLLVTH 192
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
688-870 |
1.53e-15 |
|
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: 75.65 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRNRysVAYAAQKPWLLNATVEENITFgspfnkqr 767
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGED--LLFLPQRPYLPLGTLREQLIY-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 768 ykavtdacslqpdidllPFGDqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegilkFLQ 847
Cdd:cd03223 87 -----------------PWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQ-----LLK 135
|
170 180
....*....|....*....|...
gi 530398972 848 DDKRTLVLVTHKLQYLTHADWII 870
Cdd:cd03223 136 ELGITVISVGHRPSLWKFHDRVL 158
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
669-881 |
1.54e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 78.62 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 669 DIAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN---------RYSV 739
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREvnaenekwvRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 740 AYAAQKP--WLLNATVEENITFGsPFN--------KQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICV 809
Cdd:PRK13647 82 GLVFQDPddQVFSSTVWDDVAFG-PVNmgldkdevERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398972 810 ARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQY-LTHADWIIAMKDGSVLREG 881
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLME--ILDRLHNQGKTVIVATHDVDLaAEWADQVIVLKEGRVLAEG 220
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1299-1497 |
1.78e-15 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 77.06 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNLkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSR 1375
Cdd:cd03292 1 IEFINVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1376 LSIILQDPILFSG-----SIRFNLdpECKCTDDRLW-----EALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 1445
Cdd:cd03292 80 IGVVFQDFRLLPDrnvyeNVAFAL--EVTGVPPREIrkrvpAALELVGLSHKHRALPAEL-----------SGGEQQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398972 1446 LARAFVRKSSILIMDEATASIDMATE----NILQK-------VVMTAFADRTVVTIAHRVHTI 1497
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTweimNLLKKinkagttVVVATHAKELVDTTRHRVIAL 209
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
668-881 |
1.89e-15 |
|
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: 76.44 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 668 EDIAIKVTNGyfSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG--EMQTLEGKVHWSNRN------RYSV 739
Cdd:cd03213 7 RNLTVTVKSS--PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPldkrsfRKII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 740 AYAAQKPWLL-NATVEENITFgspfnkqrykavtdACSLQpdidllpfgdqteigergiNLSGGQRQRICVARALYQNTN 818
Cdd:cd03213 85 GYVPQDDILHpTLTVRETLMF--------------AAKLR-------------------GLSGGERKRVSIALELVSNPS 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398972 819 IVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTHA--DWIIAMKDGSVLREG 881
Cdd:cd03213 132 LLFLDEPTSGLDSSSALQVMS--LLRRLADTGRTIICSIHQPSSEIFElfDKLLLLSQGRVIYFG 194
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1299-1467 |
2.33e-15 |
|
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: 76.36 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIDGIDISKLPLHtLRS 1374
Cdd:COG4133 3 LEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTTL----LRILagllPPSAGEVLWNGEPIRDARED-YRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1375 RLSIILQDPILFSG-SIRFNLD-----PECKCTDDRLWEALEIAqlknmvkslpgGLDAVVTEGGENFSVGQRQLFCLAR 1448
Cdd:COG4133 76 RLAYLGHADGLKPElTVRENLRfwaalYGLRADREAIDEALEAV-----------GLAGLADLPVRQLSAGQKRRVALAR 144
|
170
....*....|....*....
gi 530398972 1449 AFVRKSSILIMDEATASID 1467
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALD 163
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
672-875 |
2.49e-15 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 74.41 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWGSGLaTLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRNRysVAYAAQkpwllna 751
Cdd:cd03221 1 IELENLSKTYGGKL-LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK--IGYFEQ------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 752 tveenitfgspfnkqrykavtdacslqpdidllpfgdqteigerginLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 831
Cdd:cd03221 71 -----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDL 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 530398972 832 HLSDHLMQegilkFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDG 875
Cdd:cd03221 104 ESIEALEE-----ALKEYPGTVILVSHDRYFLDQvATKIIELEDG 143
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
672-877 |
2.61e-15 |
|
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: 76.68 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYfswGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN-----RYSVAYAAQK- 745
Cdd:cd03292 4 INVTKTY---PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdlrGRAIPYLRRKi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 746 -------PWLLNATVEENITF-----GSPFN--KQRYKAVTDACSLQPDIDLLPFGdqteigerginLSGGQRQRICVAR 811
Cdd:cd03292 81 gvvfqdfRLLPDRNVYENVAFalevtGVPPReiRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398972 812 ALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTH-KLQYLTHADWIIAMKDGSV 877
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMN--LLKKINKAGTTVVVATHaKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
688-886 |
2.72e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 78.28 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN---------------RNRYSVAYAAQKPWLLNAT 752
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvRKRIGMVFQFPESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 753 VEENITFGSP-FNKQRYKAVTDACSLqpdidLLPFGDQTEIGERG-INLSGGQRQRICVARALYQNTNIVFLDDPFSALD 830
Cdd:PRK13646 103 VEREIIFGPKnFKMNLDEVKNYAHRL-----LMDLGFSRDVMSQSpFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 530398972 831 IHLSDHLMQegILKFLQ-DDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDI 886
Cdd:PRK13646 178 PQSKRQVMR--LLKSLQtDENKTIILVSHDMNEVArYADEVIVMKEGSIVSQTSPKEL 233
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
688-886 |
2.77e-15 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 76.70 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN----------RNRYSVAYAAQKPWLL-NATVEEN 756
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGrditglppheRARAGIGYVPEGRRIFpELTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 757 ITFG-SPFNKQRYKAVTDACslqpdIDLLPfgdqtEIGER----GINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 831
Cdd:cd03224 96 LLLGaYARRRAKRKARLERV-----YELFP-----RLKERrkqlAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 530398972 832 HLSDHLMQegILKFLQDDKRTLVLVTHKLQY-LTHADWIIAMKDGSVLREGTLKDI 886
Cdd:cd03224 166 KIVEEIFE--AIRELRDEGVTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAEL 219
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
680-879 |
2.85e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 81.31 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 680 SWGSG---LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILG---------------EMQTLEGKVHWSNRnRYSVAY 741
Cdd:PRK10535 13 SYPSGeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLM-NILGcldkptsgtyrvagqDVATLDADALAQLR-REHFGF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 742 AAQKPWLL-NATVEENITF-----GSPFNKQRYKAvtdacslqpdIDLLP-FGDQTEIGERGINLSGGQRQRICVARALY 814
Cdd:PRK10535 91 IFQRYHLLsHLTAAQNVEVpavyaGLERKQRLLRA----------QELLQrLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398972 815 QNTNIVFLDDPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLR 879
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVM--AILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
672-881 |
2.95e-15 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 76.63 E-value: 2.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN-----RYSVAYAAQK- 745
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrlkRREIPYLRRRi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 746 ------PWLL-NATVEENITF-----GSPfNKQRYKAVTDACS---LQPDIDLLPfgdqteigergINLSGGQRQRICVA 810
Cdd:COG2884 82 gvvfqdFRLLpDRTVYENVALplrvtGKS-RKEIRRRVREVLDlvgLSDKAKALP-----------HELSGGEQQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398972 811 RALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTHADW-IIAMKDGSVLREG 881
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIME--LLEEINRRGTTVLIATHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1299-1513 |
3.31e-15 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 76.24 E-value: 3.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSR 1375
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1376 LSIILQD-PILFSGSIRFNL----------DPECKctdDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1444
Cdd:COG2884 81 IGVVFQDfRLLPDRTVYENValplrvtgksRKEIR---RRVREVLDLVGLSDKAKALPHEL-----------SGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398972 1445 CLARAFVRKSSILIMDEATASIDMAT-ENILQkvVMTAFADR--TVVtIA-HRVHTILTADL-VIVMKRGNILE 1513
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETsWEIME--LLEEINRRgtTVL-IAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
684-896 |
4.04e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 79.11 E-value: 4.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRNRYSVAyAAQKPWLL---------NATVE 754
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-PYQRPINMmfqsyalfpHMTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 755 ENITFGSPFNKQRYKAVTDACSlqpdiDLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 833
Cdd:PRK11607 110 QNIAFGLKQDKLPKAEIASRVN-----EMLGLVHMQEFAKRKPHqLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKL 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398972 834 SDHlMQEGILKFLQDDKRTLVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKdiqtkdvELYEH 896
Cdd:PRK11607 185 RDR-MQLEVVDILERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPE-------EIYEH 240
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1313-1512 |
4.10e-15 |
|
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: 75.28 E-value: 4.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1313 KPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDIFDGKIVIDGIDISKlplHTLRSRLSIILQDPILFSgsi 1390
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLlnALAGRRTGLGVSGEVLINGRPLDK---RSFRKIIGYVPQDDILHP--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1391 rfnldpeckctDDRLWEALEI-AQLknmvKSLPGgldavvteggenfsvGQRQLFCLARAFVRKSSILIMDEATASIDMA 1469
Cdd:cd03213 96 -----------TLTVRETLMFaAKL----RGLSG---------------GERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 530398972 1470 TENILQKVVMtAFAD--RTVVTIAHRVHTILTA--DLVIVMKRGNIL 1512
Cdd:cd03213 146 SALQVMSLLR-RLADtgRTIICSIHQPSSEIFElfDKLLLLSQGRVI 191
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
734-900 |
4.13e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 81.23 E-value: 4.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 734 RNRYSVAyaAQKPWLLNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARA 812
Cdd:PTZ00265 1295 RNLFSIV--SQEPMLFNMSIYENIKFGKEdATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARA 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 813 LYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAM----KDGS-VLREGTLKDIQ 887
Cdd:PTZ00265 1373 LLREPKILLLDEATSSLDSN-SEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSfVQAHGTHEELL 1451
|
170
....*....|...
gi 530398972 888 TKDVELYEHWKTL 900
Cdd:PTZ00265 1452 SVQDGVYKKYVKL 1464
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
677-880 |
4.44e-15 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 77.15 E-value: 4.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 677 GYFSWGSG-LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRNRYSVAYAAQK---------- 745
Cdd:TIGR02769 15 GGLFGAKQrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRafrrdvqlvf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 746 ---PWLLNA--TVEENItfGSPF----------NKQRYKAVTDACSLQPDI-DLLPfgdqteigergINLSGGQRQRICV 809
Cdd:TIGR02769 95 qdsPSAVNPrmTVRQII--GEPLrhltsldeseQKARIAELLDMVGLRSEDaDKLP-----------RQLSGGQLQRINI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530398972 810 ARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAMKDGSVLRE 880
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVL-----QAVILELLRKLQQafgtAYLFITHDLRLVQSfCQRVAVMDKGQIVEE 232
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
641-876 |
5.92e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 79.85 E-value: 5.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 641 TINRkqpgryhLDSYEQSTRRLRPAETEDIAIKVTNGyfswgSGLAT-------------LSNIDIRIPTGQLTMIVGQV 707
Cdd:COG4178 331 TVDR-------LAGFEEALEAADALPEAASRIETSED-----GALALedltlrtpdgrplLEDLSLSLKPGERLLITGPS 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 708 GCGKSSLLLAILGemqtL----EGKVHWSNRNRysVAYAAQKPWLLNATVEENITFGSP---FNKQRYKAVTDACSLQPD 780
Cdd:COG4178 399 GSGKSTLLRAIAG----LwpygSGRIARPAGAR--VLFLPQRPYLPLGTLREALLYPATaeaFSDAELREALEAVGLGHL 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 781 IDLLpfgDQTEIGERGinLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDdkRTLVLVTHKL 860
Cdd:COG4178 473 AERL---DEEADWDQV--LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-LREELPG--TTVISVGHRS 544
|
250
....*....|....*.
gi 530398972 861 QYLTHADWIIAMKDGS 876
Cdd:COG4178 545 TLAAFHDRVLELTGDG 560
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
688-878 |
6.28e-15 |
|
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: 76.49 E-value: 6.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV------------HwSNRNRYSVAYaaQKPWLLNATVEE 755
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIvidgidisklplH-TLRSRLSIIL--QDPILFSGSIRF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 756 NITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhLSD 835
Cdd:cd03288 114 NLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDM-ATE 192
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 530398972 836 HLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVL 878
Cdd:cd03288 193 NILQKVVMTAFAD--RTVVTIAHRVSTILDADLVLVLSRGILV 233
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1299-1525 |
8.57e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 76.69 E-value: 8.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNL-KPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIF----DGKIVIDGIDISKLPLHTLR 1373
Cdd:PRK13650 5 IEVKNLTFKYKEDQeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTT----VRLIDGLleaeSGQIIIDGDLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1374 SRLSIILQDPI-LFSGS-----IRFNLDP---ECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1444
Cdd:PRK13650 81 HKIGMVFQNPDnQFVGAtveddVAFGLENkgiPHEEMKERVNEALELVGMQDFKEREPARL-----------SGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1445 CLARAFVRKSSILIMDEATASID--------MATENILQKVVMTafadrtVVTIAHRVHTILTADLVIVMKRGNILEYDT 1516
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDpegrleliKTIKGIRDDYQMT------VISITHDLDEVALSDRVLVMKNGQVESTST 223
|
....*....
gi 530398972 1517 PESLLAQEN 1525
Cdd:PRK13650 224 PRELFSRGN 232
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
672-875 |
9.33e-15 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 74.87 E-value: 9.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI--LGEMQ----TLEGKVHWSNRN-----RYSVA 740
Cdd:cd03262 1 IEIKNLHKSFG-DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCInlLEEPDsgtiIIDGLKLTDDKKninelRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 741 YAAQKPWLL-NATVEENITFGsP---FNKQRYKAVTDACSLQPDIDLLPFGDQteigeRGINLSGGQRQRICVARALYQN 816
Cdd:cd03262 80 MVFQQFNLFpHLTVLENITLA-PikvKGMSKAEAEERALELLEKVGLADKADA-----YPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 817 TNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDG 875
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLD--VMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDG 211
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1299-1523 |
1.87e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.51 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENN----LKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP-LHTLR 1373
Cdd:PRK13633 5 IKCKNVSYKYESNeestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1374 SRLSIILQDP------ILFSGSIRF---NLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1444
Cdd:PRK13633 85 NKAGMVFQNPdnqivaTIVEEDVAFgpeNLGIPPEEIRERVDESLKKVGMYEYRRHAPHLL-----------SGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1445 CLARAFVRKSSILIMDEATASIDmateNILQKVVMTAFADR------TVVTIAHRVHTILTADLVIVMKRGNILEYDTPE 1518
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLD----PSGRREVVNTIKELnkkygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPK 229
|
....*
gi 530398972 1519 SLLAQ 1523
Cdd:PRK13633 230 EIFKE 234
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1299-1524 |
1.96e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 75.65 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG--IDISKLPLHTLRSRL 1376
Cdd:PRK13636 6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1377 SIILQDP--ILFSGSIR-------FNLDPECKCTDDRLWEALE---IAQLKNmvkslpggldavvtEGGENFSVGQRQLF 1444
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYqdvsfgaVNLKLPEDEVRKRVDNALKrtgIEHLKD--------------KPTHCLSFGQKKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1445 CLARAFVRKSSILIMDEATASID-MATENILQKVVMTAFA-DRTVVTIAHRVHTI-LTADLVIVMKRGNILEYDTPESLL 1521
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDpMGVSEIMKLLVEMQKElGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVF 230
|
...
gi 530398972 1522 AQE 1524
Cdd:PRK13636 231 AEK 233
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
688-882 |
2.17e-14 |
|
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: 74.08 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN--------RYSVAYAAQK---PWLLnaTVEEN 756
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSirtdrkaaRQSLGYCPQFdalFDEL--TVREH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 757 ITF-----GSPFNKQRY--KAVTDACSLQPDIDllpfgdqTEIGergiNLSGGQRQRICVARALYQNTNIVFLDDPFSAL 829
Cdd:cd03263 96 LRFyarlkGLPKSEIKEevELLLRVLGLTDKAN-------KRAR----TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 530398972 830 dihlsDHLMQEGILKFLQDDK--RTLVLVTHKLQ---YLthADWIIAMKDGSVLREGT 882
Cdd:cd03263 165 -----DPASRRAIWDLILEVRkgRSIILTTHSMDeaeAL--CDRIAIMSDGKLRCIGS 215
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1316-1521 |
2.61e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 77.00 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1316 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS----RLSIILQDpilfsgsir 1391
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQS--------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1392 FNLDPECKCTDDRLWeALEIAQLKNMVKSlPGGLDAVVTEGGENF--------SVGQRQLFCLARAFVRKSSILIMDEAT 1463
Cdd:PRK10070 115 FALMPHMTVLDNTAF-GMELAGINAEERR-EKALDALRQVGLENYahsypdelSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398972 1464 ASID--MATENILQKVVMTAFADRTVVTIAHRV-HTILTADLVIVMKRGNILEYDTPESLL 1521
Cdd:PRK10070 193 SALDplIRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1314-1523 |
2.76e-14 |
|
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: 75.28 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1314 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLSIILQDPILFSGSIRFN 1393
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1394 LDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEN- 1472
Cdd:cd03291 118 IIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKe 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 530398972 1473 ILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1523
Cdd:cd03291 198 IFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSL 248
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1299-1527 |
2.80e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 74.79 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1378
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1379 ILQDPI-LFSGSI-----RFNLDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARA 1449
Cdd:PRK13648 88 VFQNPDnQFVGSIvkydvAFGLENHAVPYDEmhrRVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1450 FVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQENGV 1527
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
684-888 |
3.35e-14 |
|
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: 73.63 E-value: 3.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHW----------SNRNRYSVAYAAQKPWLL-NAT 752
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFdgeditglppHEIARLGIGRTFQIPRLFpELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 753 VEENITFGSPFNKQRYKAVTDACSLQPDI-----DLLpfgDQTEIGERG----INLSGGQRQRICVARALYQNTNIVFLD 823
Cdd:cd03219 92 VLENVMVAAQARTGSGLLLARARREEREAreraeELL---ERVGLADLAdrpaGELSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530398972 824 DPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDIQT 888
Cdd:cd03219 169 EPAAGLNPEETEELAE--LIRELRERGITVLLVEHDMDVVMsLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1299-1524 |
3.36e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 74.84 E-value: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSlaffRMV-------DIFDGKIVIDGIDISKLPLHT 1371
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTIS----KLInglllpdDNPNSKITVDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1372 LRSRLSIILQDPI-LFSGS-----IRFNLDpeckctdDRLWEALEIAQLKNMVKSLPGGLDAVVTEGgENFSVGQRQLFC 1445
Cdd:PRK13640 82 IREKVGIVFQNPDnQFVGAtvgddVAFGLE-------NRAVPRPEMIKIVRDVLADVGMLDYIDSEP-ANLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1446 LARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1523
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
.
gi 530398972 1524 E 1524
Cdd:PRK13640 234 V 234
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
668-886 |
3.55e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 74.88 E-value: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 668 EDIAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN-----------R 736
Cdd:PRK13636 2 EDYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPidysrkglmklR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 737 YSVAYAAQKP--WLLNATVEENITFGsPFNKQrykavtdacslqpdidlLPfgdQTEIGER--------GIN-------- 798
Cdd:PRK13636 82 ESVGMVFQDPdnQLFSASVYQDVSFG-AVNLK-----------------LP---EDEVRKRvdnalkrtGIEhlkdkpth 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 799 -LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDGS 876
Cdd:PRK13636 141 cLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIM-KLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGR 219
|
250
....*....|
gi 530398972 877 VLREGTLKDI 886
Cdd:PRK13636 220 VILQGNPKEV 229
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
672-893 |
3.90e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 74.64 E-value: 3.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN----------RYSVAY 741
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDtgdfsklqgiRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 742 AAQKP--WLLNATVEENITFGsPFNkqrykavtdACslQPDIDLLPFGDQTeIGERGI---------NLSGGQRQRICVA 810
Cdd:PRK13644 82 VFQNPetQFVGRTVEEDLAFG-PEN---------LC--LPPIEIRKRVDRA-LAEIGLekyrhrspkTLSGGQGQCVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 811 RALYQNTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT----LKDI 886
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLER--IKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEpenvLSDV 226
|
....*..
gi 530398972 887 QTKDVEL 893
Cdd:PRK13644 227 SLQTLGL 233
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1294-1509 |
3.98e-14 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 73.97 E-value: 3.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1294 PQEGEIKIHDLCVRY--ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIDGidiskL 1367
Cdd:COG1116 3 AAAPALELRGVSKRFptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTL----LRLIagleKPTSGEVLVDG-----K 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1368 PLHTLRSRLSIILQDPILF-----SGSIRFNLD------PECKctdDRLWEALEIAQLKNMVKSLPGGLdavvteggenf 1436
Cdd:COG1116 74 PVTGPGPDRGVVFQEPALLpwltvLDNVALGLElrgvpkAERR---ERARELLELVGLAGFEDAYPHQL----------- 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530398972 1437 SVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVH-TILTADLVIVMKRG 1509
Cdd:COG1116 140 SGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETgkTVLFVTHDVDeAVFLADRVVVLSAR 215
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
688-912 |
4.53e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 74.66 E-value: 4.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLL-----LAILGEMQTLEG---------KVHWSNRNRYSVAYAAQKP--WLLNA 751
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIqltngLIISETGQTIVGdyaipanlkKIKEVKRLRKEIGLVFQFPeyQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 752 TVEENITFGsPFN-----KQRYKAVTDACSLQPdidlLPfgdqTEIGERG-INLSGGQRQRICVARALYQNTNIVFLDDP 825
Cdd:PRK13645 107 TIEKDIAFG-PVNlgenkQEAYKKVPELLKLVQ----LP----EDYVKRSpFELSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 826 FSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREGT----------LKDIQTKDVELY 894
Cdd:PRK13645 178 TGGLDPKGEEDFINL-FERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSpfeifsnqelLTKIEIDPPKLY 256
|
250
....*....|....*...
gi 530398972 895 EHWKTLMNRQDQELEKDM 912
Cdd:PRK13645 257 QLMYKLKNKGIDLLNKNI 274
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
684-884 |
5.04e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 73.63 E-value: 5.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI------------LGEMqTLEGKVHWSNRN------RYSVAYAAQK 745
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirVGDI-TIDTARSLSQQKglirqlRQHVGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 746 PWLL-NATVEENITFGSPFNKQ--RYKAVTDACSLQPDIDLLpfGDQTEIGERginLSGGQRQRICVARALYQNTNIVFL 822
Cdd:PRK11264 94 FNLFpHRTVLENIIEGPVIVKGepKEEATARARELLAKVGLA--GKETSYPRR---LSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398972 823 DDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLK 884
Cdd:PRK11264 169 DEPTSALDPELVGEVLN--TIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAK 229
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1299-1519 |
6.02e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 74.31 E-value: 6.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNL---KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIS--KLPLHTLR 1373
Cdd:PRK13637 3 IKIENLTHIYMEGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1374 SRLSIILQDP------------ILFsGSIRFNL-DPECKctdDRLWEALEIAqlknmvkslpgGLDAVVTEGGENF--SV 1438
Cdd:PRK13637 83 KKVGLVFQYPeyqlfeetiekdIAF-GPINLGLsEEEIE---NRVKRAMNIV-----------GLDYEDYKDKSPFelSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1439 GQRQLFCLARAFVRKSSILIMDEATASID-MATENILQKV-VMTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYD 1515
Cdd:PRK13637 148 GQKRRVAIAGVVAMEPKILILDEPTAGLDpKGRDEILNKIkELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQG 227
|
....
gi 530398972 1516 TPES 1519
Cdd:PRK13637 228 TPRE 231
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1299-1524 |
6.39e-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: 72.96 E-value: 6.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslaFFRMVDIF---DGKIVIDGIDISKLPLHTlRSR 1375
Cdd:cd03218 1 LRAENLSKRYGK--RKVVNGVSLSVKQGEIVGLLGPNGAGKTTT---FYMIVGLVkpdSGKILLDGQDITKLPMHK-RAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1376 LSIIL--QDPILFSG-SIRFNL--------DPEcKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1444
Cdd:cd03218 75 LGIGYlpQEASIFRKlTVEENIlavleirgLSK-KEREEKLEELLEEFHITHLRKSKASSL-----------SGGERRRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1445 CLARAFVRKSSILIMDEATASID-MATENIlQKVVMTaFADRTV-VTIA-HRVHTIL-TADLVIVMKRGNILEYDTPESL 1520
Cdd:cd03218 143 EIARALATNPKFLLLDEPFAGVDpIAVQDI-QKIIKI-LKDRGIgVLITdHNVRETLsITDRAYIIYEGKVLAEGTPEEI 220
|
....
gi 530398972 1521 LAQE 1524
Cdd:cd03218 221 AANE 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1299-1511 |
8.22e-14 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 72.18 E-value: 8.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDI--SKLPLHTLRSRL 1376
Cdd:cd03262 1 IEIKNLHKSFGDF--HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1377 SIILQDpilfsgsirFNLDPECK----CTDDRLW-------EALEIA-------QLKNMVKSLPGGLdavvteggenfSV 1438
Cdd:cd03262 79 GMVFQQ---------FNLFPHLTvlenITLAPIKvkgmskaEAEERAlellekvGLADKADAYPAQL-----------SG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530398972 1439 GQRQLFCLARAFVRKSSILIMDEATASID--MATEnILQkvVMTAFADR--TVVTIAHRVHTIL-TADLVIVMKRGNI 1511
Cdd:cd03262 139 GQQQRVAIARALAMNPKVMLFDEPTSALDpeLVGE-VLD--VMKDLAEEgmTMVVVTHEMGFAReVADRVIFMDDGRI 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
690-886 |
1.11e-13 |
|
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: 75.49 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 690 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGeMQTLEGKVHWSNRNRYSVAYAAQKPWL-------------LNA--TVE 754
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGLSRRALRPLRrrmqvvfqdpfgsLSPrmTVG 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 755 ENITFG--------SPfnKQRYKAVTDAcsLQpDIDLLPfgdqtEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDP 825
Cdd:COG4172 383 QIIAEGlrvhgpglSA--AERRARVAEA--LE-EVGLDP-----AARHRYPHeFSGGQRQRIAIARALILEPKLLVLDEP 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530398972 826 FSALDIHLsdhlmQEGILKFLQD--DKRTL--VLVTHKLQ---YLTHadWIIAMKDGSVLREGTLKDI 886
Cdd:COG4172 453 TSALDVSV-----QAQILDLLRDlqREHGLayLFISHDLAvvrALAH--RVMVMKDGKVVEQGPTEQV 513
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1297-1532 |
1.28e-13 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 73.95 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1297 GEIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLsLaffRMV----DIFDGKIVIDGIDISKLPlhTL 1372
Cdd:COG3839 2 ASLELENVSKSYGG--VEALKDIDLDIEDGEFLVLLGPSGCGKSTL-L---RMIagleDPTSGEILIGGRDVTDLP--PK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1373 RSRLSIILQDPILF-SGSIRFNL----------DPEckcTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQR 1441
Cdd:COG3839 74 DRNIAMVFQSYALYpHMTVYENIafplklrkvpKAE---IDRRVREAAELLGLEDLLDRKPKQL-----------SGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1442 QLFCLARAFVRKSSILIMDEATASID------MATE--NILQKVVMTafadrTV-VTiaHRVHTILT-ADLVIVMKRGNI 1511
Cdd:COG3839 140 QRVALGRALVREPKVFLLDEPLSNLDaklrveMRAEikRLHRRLGTT-----TIyVT--HDQVEAMTlADRIAVMNDGRI 212
|
250 260
....*....|....*....|..
gi 530398972 1512 LEYDTPESLLAQENGVF-ASFV 1532
Cdd:COG3839 213 QQVGTPEELYDRPANLFvAGFI 234
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
672-895 |
1.95e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 72.77 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSW--GSGLAT--LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN-----------R 736
Cdd:PRK13637 3 IKIENLTHIYmeGTPFEKkaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitdkkvklsdiR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 737 YSVAYAAQKP--WLLNATVEENITFGsPFN--------KQRYKAVTDACSLQPDI--DLLPFgdqteigergiNLSGGQR 804
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAFG-PINlglseeeiENRVKRAMNIVGLDYEDykDKSPF-----------ELSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 805 QRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDD-KRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGT 882
Cdd:PRK13637 151 RRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNK--IKELHKEyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
250
....*....|...
gi 530398972 883 LKDIqTKDVELYE 895
Cdd:PRK13637 229 PREV-FKEVETLE 240
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1299-1532 |
2.13e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 73.59 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDifDGKIVIDGIDISKLPLHtlRSRL 1376
Cdd:COG3842 6 LELENVSKRYGDV--TALDDVSLSIEPGEFVALLGPSGCGKTTLlrMIAGFETPD--SGRILLDGRDVTGLPPE--KRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1377 SIILQDPILF-----SGSIRFNLD------PECKctdDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 1445
Cdd:COG3842 80 GMVFQDYALFphltvAENVAFGLRmrgvpkAEIR---ARVAELLELVGLEGLADRYPHQL-----------SGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1446 LARAFVRKSSILIMDEATASID------MATE--NILQKVVMTAFadrtVVTiaHRVHTILT-ADLVIVMKRGNILEYDT 1516
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDaklreeMREElrRLQRELGITFI----YVT--HDQEEALAlADRIAVMNDGRIEQVGT 219
|
250
....*....|....*..
gi 530398972 1517 PESLLAQENGVF-ASFV 1532
Cdd:COG3842 220 PEEIYERPATRFvADFI 236
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
671-899 |
2.23e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 71.80 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 671 AIKVTNGYFSWGSGlATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI-----LGEMQTLEGKVHWSNRNRYS------- 738
Cdd:PRK14267 4 AIETVNLRVYYGSN-HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSpdvdpie 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 739 ----VAYAAQKP-WLLNATVEENITFGSPFNK---------QRYKAVTDACSLQPDIdllpfgdQTEIGERGINLSGGQR 804
Cdd:PRK14267 83 vrreVGMVFQYPnPFPHLTIYDNVAIGVKLNGlvkskkeldERVEWALKKAALWDEV-------KDRLNDYPSNLSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 805 QRICVARALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDdkRTLVLVTHK-LQYLTHADWIIAMKDGSVLREG-T 882
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANID-PVGTAKIEELLFELKKE--YTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGpT 232
|
250
....*....|....*..
gi 530398972 883 LKDIQTKDVELYEHWKT 899
Cdd:PRK14267 233 RKVFENPEHELTEKYVT 249
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1314-1524 |
2.34e-13 |
|
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: 75.72 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1314 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLSIILQDPILFSGSIRFN 1393
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1394 LDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE-N 1472
Cdd:TIGR01271 507 IIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEkE 586
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 530398972 1473 ILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQE 1524
Cdd:TIGR01271 587 IFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
683-891 |
2.36e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.70 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 683 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEG--KVHWSNRNRYSVAYA--------AQKPWLL-NA 751
Cdd:PRK15439 22 SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGtlEIGGNPCARLTPAKAhqlgiylvPQEPLLFpNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 752 TVEENITFGSPFNKQRYKAVTD-----ACSLQPDID--LLPFGDQteigerginlsggqrQRICVARALYQNTNIVFLDD 824
Cdd:PRK15439 102 SVKENILFGLPKRQASMQKMKQllaalGCQLDLDSSagSLEVADR---------------QIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530398972 825 PFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQTKDV 891
Cdd:PRK15439 167 PTASLTPAETERLFSR--IRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLSTDDI 232
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1299-1512 |
2.39e-13 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 70.68 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENnlKPVLKHVKAYIKPGQkVGICGRTGSGKSSL--SLA-FFRMVDifdGKIVIDGIDISKLPlHTLRSR 1375
Cdd:cd03264 1 LQLENLTKRYGK--KRALDGVSLTLGPGM-YGLLGPNGAGKTTLmrILAtLTPPSS---GTIRIDGQDVLKQP-QKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1376 LSIILQDpilFSGSIRFnldpeckctddRLWEALE-IAQLKNMVKS-----LPGGLDAVVTEGGEN-----FSVGQRQLF 1444
Cdd:cd03264 74 IGYLPQE---FGVYPNF-----------TVREFLDyIAWLKGIPSKevkarVDEVLELVNLGDRAKkkigsLSGGMRRRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398972 1445 CLARAFVRKSSILIMDEATASID----MATENILQKVVmtafADRTVVTIAHRVHTI-LTADLVIVMKRGNIL 1512
Cdd:cd03264 140 GIAQALVGDPSILIVDEPTAGLDpeerIRFRNLLSELG----EDRIVILSTHIVEDVeSLCNQVAVLNKGKLV 208
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1311-1521 |
2.46e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 71.62 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1311 NLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGI------DISKLPLHTLRSRLSIILQDPI 1384
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1385 LFSG-SIRFNLDPECKCTDDRlwEALEIAQLKNMVKSLPGGLDAV---VTEGGENFSVGQRQLFCLARAFVRKSSILIMD 1460
Cdd:PRK14246 101 PFPHlSIYDNIAYPLKSHGIK--EKREIKKIVEECLRKVGLWKEVydrLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398972 1461 EATASIDMATENILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLL 1521
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVArVADYVAFLYNGELVEWGSSNEIF 240
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
676-894 |
3.05e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.14 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 676 NGYFSWGSGLATlSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRNRYSVAYA-----------AQ 744
Cdd:PRK11000 8 NVTKAYGDVVIS-KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAergvgmvfqsyAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 745 KPWLlnaTVEENITFGSPFNK-------QRYKAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARALYQNT 817
Cdd:PRK11000 87 YPHL---SVAENMSFGLKLAGakkeeinQRVNQVAEVLQLAHLLDRKP-----------KALSGGQRQRVAIGRTLVAEP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530398972 818 NIVFLDDPFSALDIHLSDHlMQEGILKFLQDDKRTLVLVTH-KLQYLTHADWIIAMKDGSVLREGtlkdiqtKDVELY 894
Cdd:PRK11000 153 SVFLLDEPLSNLDAALRVQ-MRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG-------KPLELY 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1299-1509 |
3.17e-13 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 68.99 E-value: 3.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL-PLHTLRSRLS 1377
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAsPRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1378 IILQdpilfsgsirfnldpeckctddrlwealeiaqlknmvkslpggldavvteggenFSVGQRQLFCLARAFVRKSSIL 1457
Cdd:cd03216 79 MVYQ------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 530398972 1458 IMDEATASIDMA-TENILQkvVMTAFADR--TVVTIAHRVHTIL-TADLVIVMKRG 1509
Cdd:cd03216 105 ILDEPTAALTPAeVERLFK--VIRRLRAQgvAVIFISHRLDEVFeIADRVTVLRDG 158
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
684-858 |
4.14e-13 |
|
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: 69.83 E-value: 4.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRNRY--------SVAYAAQKPWLLNA-TVE 754
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDfqrdsiarGLLYLGHAPGIKTTlSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 755 ENITFGSPFNKQryKAVTDACSlqpDIDLLPFGDqteigeRGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDI-- 831
Cdd:cd03231 92 ENLRFWHADHSD--EQVEEALA---RVGLNGFED------RPVAqLSAGQQRRVALARLLLSGRPLWILDEPTTALDKag 160
|
170 180 190
....*....|....*....|....*....|...
gi 530398972 832 ------HLSDHLMQEGIlkflqddkrtLVLVTH 858
Cdd:cd03231 161 varfaeAMAGHCARGGM----------VVLTTH 183
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1299-1493 |
5.84e-13 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 68.33 E-value: 5.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIdgidisklplhTLRS 1374
Cdd:cd03223 1 IELENLSLATPDG-RVLLKDLSFEIKPGDRLLITGPSGTGKSSL----FRALaglwPWGSGRIGM-----------PEGE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1375 RLSIILQDPILFSGSIRfnldpeckctddrlwealeiaqlknmvkslpgglDAVVTEGGENFSVGQRQLFCLARAFVRKS 1454
Cdd:cd03223 65 DLLFLPQRPYLPLGTLR----------------------------------EQLIYPWDDVLSGGEQQRLAFARLLLHKP 110
|
170 180 190
....*....|....*....|....*....|....*....
gi 530398972 1455 SILIMDEATASIDMATENILQKVVMTAFAdrTVVTIAHR 1493
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
688-886 |
6.15e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 71.30 E-value: 6.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN---------------RNRYSVAYAAQKPWLLNAT 752
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsstskqkeikpvRKKVGVVFQFPESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 753 VEENITFGsPFNKQRYKAVTDACSLQpdiDLLPFGDQTEIGERG-INLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 831
Cdd:PRK13643 102 VLKDVAFG-PQNFGIPKEKAEKIAAE---KLEMVGLADEFWEKSpFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 530398972 832 HLSDHLMQegILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDI 886
Cdd:PRK13643 178 KARIEMMQ--LFESIHQSGQTVVLVTHLMDDVAdYADYVYLLEKGHIISCGTPSDV 231
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
692-860 |
6.84e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 70.00 E-value: 6.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 692 DIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhWSNRNRYSVAYAAQKPWLL---------NATVEENITFG-- 760
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSL-TLNGQDHTTTPPSRRPVSMlfqennlfsHLTVAQNIGLGln 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 761 -----SPFNKQRYKAVTDACSLQPDIDLLPfgdqteiGErginLSGGQRQRICVARALYQNTNIVFLDDPFSALDihlsD 835
Cdd:PRK10771 98 pglklNAAQREKLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCLVREQPILLLDEPFSALD----P 162
|
170 180
....*....|....*....|....*....
gi 530398972 836 HLMQEgILKFLQD--DKR--TLVLVTHKL 860
Cdd:PRK10771 163 ALRQE-MLTLVSQvcQERqlTLLMVSHSL 190
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1236-1513 |
8.52e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.82 E-value: 8.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1236 GLGLLYaltITNYLNwVVRNLADLEVQMGAVKKV--NSFLTMESE----------NYEGTMDPSQVPEHWPQEgeIKIHD 1303
Cdd:PRK15134 207 NMGLLF---ITHNLS-IVRKLADRVAVMQNGRCVeqNRAATLFSApthpytqkllNSEPSGDPVPLPEPASPL--LDVEQ 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1304 LCVRYE---------NNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDGKIVIDGidiskLPLHTL-- 1372
Cdd:PRK15134 281 LQVAFPirkgilkrtVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIWFDG-----QPLHNLnr 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1373 ------RSRLSIILQDPilfSGSIRFNLDPEckctdDRLWEALEI-------AQLKNMVKSLPG--GLDAVV-----TEg 1432
Cdd:PRK15134 355 rqllpvRHRIQVVFQDP---NSSLNPRLNVL-----QIIEEGLRVhqptlsaAQREQQVIAVMEevGLDPETrhrypAE- 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1433 genFSVGQRQLFCLARAFVRKSSILIMDEATASID-------MATENILQKVVMTAFadrtvVTIAHRVHTILT-ADLVI 1504
Cdd:PRK15134 426 ---FSGGQRQRIAIARALILKPSLIILDEPTSSLDktvqaqiLALLKSLQQKHQLAY-----LFISHDLHVVRAlCHQVI 497
|
....*....
gi 530398972 1505 VMKRGNILE 1513
Cdd:PRK15134 498 VLRQGEVVE 506
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
688-899 |
1.82e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 69.17 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLL-----LAILGEMQTLEGKVHWSN-----------RNRYSVAYAAQKPwLLNA 751
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLrvfnrLIELYPEARVSGEVYLDGqdifkmdvielRRRVQMVFQIPNP-IPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 752 TVEENITFGSPFNK---------QRYKAVTDACSLQPDIdllpfgdQTEIGERGINLSGGQRQRICVARALYQNTNIVFL 822
Cdd:PRK14247 98 SIFENVALGLKLNRlvkskkelqERVRWALEKAQLWDEV-------KDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398972 823 DDPFSALDIHLSDHLmqEGILKFLQDDKrTLVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKDIQTKDV-ELYEHWKT 899
Cdd:PRK14247 171 DEPTANLDPENTAKI--ESLFLELKKDM-TIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRhELTEKYVT 246
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
690-886 |
2.66e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 70.13 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 690 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV--------HWSNRNRySVAYAAQKPWLL-NATVEENITFG 760
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfidgedvtHRSIQQR-DICMVFQSYALFpHMSLGENVGYG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 761 -------SPFNKQRykaVTDACSLqpdIDLLPFGDqteigeRGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 832
Cdd:PRK11432 103 lkmlgvpKEERKQR---VKEALEL---VDLAGFED------RYVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 530398972 833 LSDHlMQEGILKFLQDDKRTLVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKDI 886
Cdd:PRK11432 171 LRRS-MREKIRELQQQFNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1299-1534 |
2.72e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.99 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1378
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1379 ILQDP--ILFSGSIR-------FNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARA 1449
Cdd:PRK13647 84 VFQDPddQVFSSTVWddvafgpVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1450 FVRKSSILIMDEATASIDMATenilQKVVMTAFAD-----RTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPeSLLAQ 1523
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRG----QETLMEILDRlhnqgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDK-SLLTD 227
|
250
....*....|.
gi 530398972 1524 ENGVFASFVRA 1534
Cdd:PRK13647 228 EDIVEQAGLRL 238
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
688-886 |
2.75e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.20 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLlAIL--------GEMqTLEGK-VHWSNRNrysvayAAQK------------- 745
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLM-KILsgvyqpdsGEI-LLDGEpVRFRSPR------DAQAagiaiihqelnlv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 746 PWLlnaTVEENITFGSPFNK----------QRYKAVTDacSLQPDIDLlpfgdQTEIGErginLSGGQRQRICVARALYQ 815
Cdd:COG1129 92 PNL---SVAENIFLGREPRRgglidwramrRRARELLA--RLGLDIDP-----DTPVGD----LSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398972 816 NTNIVFLDDPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREGTLKDI 886
Cdd:COG1129 158 DARVLILDEPTASLTEREVERLF--RIIRRLKAQGVAIIYISHRLdEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1299-1524 |
2.83e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.07 E-value: 2.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENnlkpvLK-HVKAYIKPGQKVGICGRTGSGKSSL-SL-AFFRMVDifDGKIVIDGIDisklplHTL--- 1372
Cdd:PRK10771 2 LKLTDITWLYHH-----LPmRFDLTVERGERVAILGPSGAGKSTLlNLiAGFLTPA--SGSLTLNGQD------HTTtpp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1373 -RSRLSIILQDPILFSG-SIRFN----LDPECKCTDDRLWEALEIAQ---LKNMVKSLPGGLdavvteggenfSVGQRQL 1443
Cdd:PRK10771 69 sRRPVSMLFQENNLFSHlTVAQNiglgLNPGLKLNAAQREKLHAIARqmgIEDLLARLPGQL-----------SGGQRQR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1444 FCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRV---HTILTADLVIVmkRGNILeYDTP- 1517
Cdd:PRK10771 138 VALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLedaARIAPRSLVVA--DGRIA-WDGPt 214
|
....*..
gi 530398972 1518 ESLLAQE 1524
Cdd:PRK10771 215 DELLSGK 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1299-1524 |
4.25e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 69.34 E-value: 4.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLSlaffRMVDIFD----GKIVIDGIDISKLP---L 1369
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLI----RCINLLErptsGSVLVDGVDLTALSereL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1370 HTLRSRLSIILQDpilfsgsirFNLdpeckctddrLWE---------ALEIA-----QLKNMVKSLpggLDAVVTEGGEN 1435
Cdd:COG1135 78 RAARRKIGMIFQH---------FNL----------LSSrtvaenvalPLEIAgvpkaEIRKRVAEL---LELVGLSDKAD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1436 F-----SVGQRQLFCLARAFVRKSSILIMDEATASIDMA-TENIL---QKVvmtafADR---TVVTIAHRVHTILT-ADL 1502
Cdd:COG1135 136 AypsqlSGGQKQRVGIARALANNPKVLLCDEATSALDPEtTRSILdllKDI-----NRElglTIVLITHEMDVVRRiCDR 210
|
250 260
....*....|....*....|....*....
gi 530398972 1503 VIVMKRGNILEYDT-------PESLLAQE 1524
Cdd:COG1135 211 VAVLENGRIVEQGPvldvfanPQSELTRR 239
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
688-876 |
5.06e-12 |
|
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: 65.81 E-value: 5.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEmqtlegkvhwSNRNRYsvayaaqkpwllnatveenITFGSPFNKQR 767
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA----------SGKARL-------------------ISFLPKFSRNK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 768 YKAVTdacSLQPDIDL----LPFGDQTEigergiNLSGGQRQRICVARALYQNT-NIVF-LDDPFSALDIHLSDHLMQEg 841
Cdd:cd03238 62 LIFID---QLQFLIDVglgyLTLGQKLS------TLSGGELQRVKLASELFSEPpGTLFiLDEPSTGLHQQDINQLLEV- 131
|
170 180 190
....*....|....*....|....*....|....*
gi 530398972 842 iLKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGS 876
Cdd:cd03238 132 -IKGLIDLGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
689-858 |
5.09e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 66.75 E-value: 5.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 689 SNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNR--NRYSVAYAAQKPWL--LNA-----TVEENITF 759
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEpiRRQRDEYHQDLLYLghQPGiktelTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 760 gspfnkqrykavtdACSLQPDIDllpfGDQT-----EIGERGI------NLSGGQRQRICVARALYQNTNIVFLDDPFSA 828
Cdd:PRK13538 98 --------------YQRLHGPGD----DEALwealaQVGLAGFedvpvrQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 530398972 829 LDI--------HLSDHLMQEGIlkflqddkrtLVLVTH 858
Cdd:PRK13538 160 IDKqgvarleaLLAQHAEQGGM----------VILTTH 187
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1299-1511 |
5.57e-12 |
|
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: 66.89 E-value: 5.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIDGIDISKLPlhtLRS 1374
Cdd:cd03301 1 VELENVTKRFGN--VTALDDLNLDIADGEFVVLLGPSGCGKTTT----LRMIagleEPTSGRIYIGGRDVTDLP---PKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1375 R-LSIILQDPILFS-----GSIRFNLD----PEcKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1444
Cdd:cd03301 72 RdIAMVFQNYALYPhmtvyDNIAFGLKlrkvPK-DEIDERVREVAELLQIEHLLDRKPKQL-----------SGGQRQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398972 1445 CLARAFVRKSSILIMDEATASID------MATE-NILQKVVmtafaDRTVVTIAH-RVHTILTADLVIVMKRGNI 1511
Cdd:cd03301 140 ALGRAIVREPKVFLMDEPLSNLDaklrvqMRAElKRLQQRL-----GTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
688-893 |
6.91e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 67.81 E-value: 6.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKS-------SLLLAILGE-----MQTLEGKVHWSNRNRYSVAYaaQKP--WLLNATV 753
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKStiakhmnALLIPSEGKvyvdgLDTSDEENLWDIRNKAGMVF--QNPdnQIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 754 EENITFGsPFNkqrykavtdaCSLQPDidllpfgdqtEIGERGIN-----------------LSGGQRQRICVARALYQN 816
Cdd:PRK13633 104 EEDVAFG-PEN----------LGIPPE----------EIRERVDEslkkvgmyeyrrhaphlLSGGQKQRVAIAGILAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398972 817 TNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIqTKDVEL 893
Cdd:PRK13633 163 PECIIFDEPTAMLDPSGRREVVNT-IKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI-FKEVEM 237
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
672-911 |
7.02e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 68.58 E-value: 7.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFsW--GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRNrysVAYAAQKPWL- 748
Cdd:PRK15079 20 IKDGKQWF-WqpPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKD---LLGMKDDEWRa 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 749 ---------------LNA--TVEENI-----TFGSPFNKQ----RYKAVTDACSLQPDIdllpfgdqteigergIN---- 798
Cdd:PRK15079 96 vrsdiqmifqdplasLNPrmTIGEIIaeplrTYHPKLSRQevkdRVKAMMLKVGLLPNL---------------INryph 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 799 -LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAM 872
Cdd:PRK15079 161 eFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI-----QAQVVNLLQQLQRemglSLIFIAHDLAVVKHiSDRVLVM 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 530398972 873 KDGSVLREGTlkdiqtkDVELYEH-----WKTLMNR---QDQELEKD 911
Cdd:PRK15079 236 YLGHAVELGT-------YDEVYHNplhpyTKALMSAvpiPDPDLERN 275
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
688-886 |
7.10e-12 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 66.94 E-value: 7.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLL--LAILGEMQ----TLEGK-VHWSNRN----RYSVAYAAQK----PwllNAT 752
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLrcINLLEEPDsgtiTVDGEdLTDSKKDinklRRKVGMVFQQfnlfP---HLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 753 VEENITFGsP---FNKQRYKAVTDAcslqpdIDLLpfgDQTEIGERG----INLSGGQRQRICVARALYQNTNIVFLDDP 825
Cdd:COG1126 94 VLENVTLA-PikvKKMSKAEAEERA------MELL---ERVGLADKAdaypAQLSGGQQQRVAIARALAMEPKVMLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398972 826 FSALDIHLSdhlmQE--GILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 886
Cdd:COG1126 164 TSALDPELV----GEvlDVMRDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1299-1525 |
8.08e-12 |
|
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: 67.03 E-value: 8.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSL-SLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLS 1377
Cdd:COG1119 4 LELRNVTVRRGG--KTILDDISWTVKPGEHWAILGPNGAGKSTLlSLITGDLPPTYGNDVRLFGERRGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1378 II---LQDPIL------------FSGSI-RF-NLDPECKCTDDRLWEALEIAQLKNM-VKSLpggldavvteggenfSVG 1439
Cdd:COG1119 82 LVspaLQLRFPrdetvldvvlsgFFDSIgLYrEPTDEQRERARELLELLGLAHLADRpFGTL---------------SQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1440 QRQLFCLARAFVRKSSILIMDEATASIDM-ATENILQkvVMTAFA---DRTVVTIAHRVHTILTA-DLVIVMKRGNILEY 1514
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLgARELLLA--LLDKLAaegAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAA 224
|
250
....*....|.
gi 530398972 1515 DTPESLLAQEN 1525
Cdd:COG1119 225 GPKEEVLTSEN 235
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
688-881 |
1.02e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 66.92 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN------------------------RNRYSVAYAA 743
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqlkvadknqlrllRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 744 QKPWLlNATVEENI------TFGSPFNKQRYKAVTdacslqpdidllpFGDQTEIGERG-----INLSGGQRQRICVARA 812
Cdd:PRK10619 101 FNLWS-HMTVLENVmeapiqVLGLSKQEARERAVK-------------YLAKVGIDERAqgkypVHLSGGQQQRVSIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 813 LYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREG 881
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDPELVGEVLR--IMQQLAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEG 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
688-858 |
1.10e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 69.32 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRNRysVAYAAQKPWLL-NATVEENITFG-SPFNK 765
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLR--IGYLPQEPPLDdDLTVLDTVLDGdAELRA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 766 --QRYKAVTDACSlQPDIDLLPFGD-QTEIGER----------------GI----------NLSGGQRQRICVARALYQN 816
Cdd:COG0488 92 leAELEELEAKLA-EPDEDLERLAElQEEFEALggweaearaeeilsglGFpeedldrpvsELSGGWRRRVALARALLSE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 530398972 817 TNIVFLDDPFSALDIhlsdhlmqEGIL---KFLQDDKRTLVLVTH 858
Cdd:COG0488 171 PDLLLLDEPTNHLDL--------ESIEwleEFLKNYPGTVLVVSH 207
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
684-891 |
1.22e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 66.73 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQT-LEGKV--------HWSNRN-RYSVAYAAQK-PWLLNAT 752
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLL-KMLGRHQPpSEGEIlldaqpleSWSSKAfARKVAYLPQQlPAAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 753 VEENITFG--------SPFNKQRYKAVTDACSLqpdIDLLPFGdqteigERGIN-LSGGQRQRICVARALYQNTNIVFLD 823
Cdd:PRK10575 102 VRELVAIGrypwhgalGRFGAADREKVEEAISL---VGLKPLA------HRLVDsLSGGERQRAWIAMLVAQDSRCLLLD 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 824 DPFSALDI-HLSDHLMQegILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDIQTKDV 891
Cdd:PRK10575 173 EPTSALDIaHQVDVLAL--VHRLSQERGLTVIAVLHDINMAArYCDYLVALRGGEMIAQGTPAELMRGET 240
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
672-895 |
1.31e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 67.04 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWG--SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH-----------WSNRNRYS 738
Cdd:PRK13642 5 LEVENLVFKYEkeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKidgelltaenvWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 739 VAYAAQKPWLLNATVEENITFGSPFN----KQRYKAVTDACSLqpdIDLLPFgdQTEIGERginLSGGQRQRICVARALY 814
Cdd:PRK13642 85 MVFQNPDNQFVGATVEDDVAFGMENQgiprEEMIKRVDEALLA---VNMLDF--KTREPAR---LSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 815 QNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVL-VTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVEL 893
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMR--VIHEIKEKYQLTVLsITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDM 234
|
..
gi 530398972 894 YE 895
Cdd:PRK13642 235 VE 236
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1299-1513 |
1.50e-11 |
|
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: 65.24 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLS--LAFFRMVDIFDGKIVIDGIDISKLPLHtLRSRL 1376
Cdd:cd03217 1 LEIKDLHVSVGG--KEILKGVNLTIKKGEVHALMGPNGSGKSTLAktIMGHPKYEVTEGEILFKGEDITDLPPE-ERARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1377 SIIL--QDPILFSGsirfnldpeckctddrlwealeiAQLKNMVKSLpggldavvtegGENFSVGQRQLFCLARAFVRKS 1454
Cdd:cd03217 78 GIFLafQYPPEIPG-----------------------VKNADFLRYV-----------NEGFSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398972 1455 SILIMDEATASIDMATENILQKVVMT-AFADRTVVTIAH--RVHTILTADLVIVMKRGNILE 1513
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVK 185
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
675-888 |
1.67e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 66.63 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 675 TNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRNRYSVAYAAQK--------- 745
Cdd:PRK10419 15 HGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKafrrdiqmv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 746 ----PWLLNA--TVEENItfGSPF----------NKQRYKAVTDACSLQPDI-DLLPfgdqteigergINLSGGQRQRIC 808
Cdd:PRK10419 95 fqdsISAVNPrkTVREII--REPLrhllsldkaeRLARASEMLRAVDLDDSVlDKRP-----------PQLSGGQLQRVC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 809 VARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKRTL----VLVTHKL---QYLTHAdwIIAMKDGSVLREG 881
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVL-----QAGVIRLLKKLQQQFgtacLFITHDLrlvERFCQR--VMVMDNGQIVETQ 234
|
....*..
gi 530398972 882 TLKDIQT 888
Cdd:PRK10419 235 PVGDKLT 241
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1299-1497 |
1.77e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 66.21 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI-----FDGKIVIDGIDI--SKLPLHT 1371
Cdd:PRK14258 8 IKVNNLSFYYDT--QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELesevrVEGRVEFFNQNIyeRRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1372 LRSRLSIILQDPILFSGSIRFNLDPECKCT--------DDRLWEALEIAQLKNMVKSlpggldaVVTEGGENFSVGQRQL 1443
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNVAYGVKIVgwrpkleiDDIVESALKDADLWDEIKH-------KIHKSALDLSGGQQQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 530398972 1444 FCLARAFVRKSSILIMDEATASID----MATENILQKVVMTafADRTVVTIAHRVHTI 1497
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLR--SELTMVIVSHNLHQV 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1299-1532 |
1.78e-11 |
|
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: 65.72 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHtlRS 1374
Cdd:cd03300 1 IELENVSKFYGG--FVALDGVSLDIKEGEFFTLLGPSGCGKTTL----LRLIAGFEtptsGEILLDGKDITNLPPH--KR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1375 RLSIILQDPILF-----SGSIRFNLD----PEcKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 1445
Cdd:cd03300 73 PVNTVFQNYALFphltvFENIAFGLRlkklPK-AEIKERVAEALDLVQLEGYANRKPSQL-----------SGGQQQRVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1446 LARAFVRKSSILIMDEATASIDMATENILQkVVMTAFADRTVVTIAHRVH----TILTADLVIVMKRGNILEYDTPESLL 1521
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDLKLRKDMQ-LELKRLQKELGITFVFVTHdqeeALTMSDRIAVMNKGKIQQIGTPEEIY 219
|
250
....*....|..
gi 530398972 1522 AQENGVF-ASFV 1532
Cdd:cd03300 220 EEPANRFvADFI 231
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
688-895 |
2.27e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 66.31 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV---------HWSNRN----RYSVAYAAQKP--WLLNAT 752
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVrvddtlitsTSKNKDikqiRKKVGLVFQFPesQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 753 VEENITFGsPFNKQRYKAVTDACSLQpdiDLLPFGDQTEIGERG-INLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 831
Cdd:PRK13649 103 VLKDVAFG-PQNFGVSQEEAEALARE---KLALVGISESLFEKNpFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398972 832 HLSDHLMQegILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDIqTKDVELYE 895
Cdd:PRK13649 179 KGRKELMT--LFKKLHQSGMTIVLVTHLMDDVAnYADFVYVLEKGKLVLSGKPKDI-FQDVDFLE 240
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
672-887 |
2.73e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 66.26 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWGSGLAT----LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRNR----------- 736
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 737 YSVAYAAQKPW------------------------LLNATVEENITFGsPFN--------KQRYKAVTDACSLqpDIDLL 784
Cdd:PRK13651 83 VLEKLVIQKTRfkkikkikeirrrvgvvfqfaeyqLFEQTIEKDIIFG-PVSmgvskeeaKKRAAKYIELVGL--DESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 785 ---PFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQ 861
Cdd:PRK13651 160 qrsPF-----------ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKQGKTIILVTHDLD 226
|
250 260 270
....*....|....*....|....*....|.
gi 530398972 862 Y-LTHADWIIAMKDGSVLREG----TLKDIQ 887
Cdd:PRK13651 227 NvLEWTKRTIFFKDGKIIKDGdtydILSDNK 257
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1299-1522 |
2.85e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 65.88 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLS 1377
Cdd:PRK13642 5 LEVENLVFKYEKESDvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1378 IILQDPI-LFSGSIrfnldpeckcTDDRLWEALEIAQL--KNMVKSLPGGLDAV-----VTEGGENFSVGQRQLFCLARA 1449
Cdd:PRK13642 85 MVFQNPDnQFVGAT----------VEDDVAFGMENQGIprEEMIKRVDEALLAVnmldfKTREPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530398972 1450 FVRKSSILIMDEATASIDMATENILQKVVMtAFADR---TVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLA 1522
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIH-EIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1325-1513 |
3.15e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.96 E-value: 3.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1325 PGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSRLSIILQDPILfsgsirfNLDPEcKCT 1401
Cdd:PRK10261 349 PGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPYA-------SLDPR-QTV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1402 DDRLWEALEIAQL---KNMVKSLPGGLDAV------VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE- 1471
Cdd:PRK10261 421 GDSIMEPLRVHGLlpgKAAAARVAWLLERVgllpehAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRg 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 530398972 1472 ---NI---LQKVVMTAFA----DRTVVT-IAHRvhtiltadlVIVMKRGNILE 1513
Cdd:PRK10261 501 qiiNLlldLQRDFGIAYLfishDMAVVErISHR---------VAVMYLGQIVE 544
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1298-1532 |
3.41e-11 |
|
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: 65.05 E-value: 3.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1298 EIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLhtlRSR-L 1376
Cdd:cd03296 2 SIEVRNVSKRFGD--FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV---QERnV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1377 SIILQDPILF-----SGSIRFNLD-------PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1444
Cdd:cd03296 77 GFVFQHYALFrhmtvFDNVAFGLRvkprserPPEAEIRAKVHELLKLVQLDWLADRYPAQL-----------SGGQRQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1445 CLARAFVRKSSILIMDEATASIDMATENILQKVVmTAFADRTVVTIAHRVH----TILTADLVIVMKRGNILEYDTPESL 1520
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRRWL-RRLHDELHVTTVFVTHdqeeALEVADRVVVMNKGRIEQVGTPDEV 224
|
250
....*....|...
gi 530398972 1521 LAQENGVF-ASFV 1532
Cdd:cd03296 225 YDHPASPFvYSFL 237
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1299-1524 |
3.67e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 65.25 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI-----FDGKIVIDGIDISKLPLHTL- 1372
Cdd:PRK14267 5 IETVNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELneearVEGEVRLFGRNIYSPDVDPIe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1373 -RSRLSIILQDPILF---------SGSIRFN-LDPECKCTDDRLWEALEIAQL----KNMVKSLPGgldavvteggeNFS 1437
Cdd:PRK14267 83 vRREVGMVFQYPNPFphltiydnvAIGVKLNgLVKSKKELDERVEWALKKAALwdevKDRLNDYPS-----------NLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1438 VGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR-VHTILTADLVIVMKRGNILE--- 1513
Cdd:PRK14267 152 GGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEvgp 231
|
250
....*....|....*
gi 530398972 1514 ----YDTPESLLAQE 1524
Cdd:PRK14267 232 trkvFENPEHELTEK 246
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
684-858 |
3.80e-11 |
|
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: 63.92 E-value: 3.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHW----SNRNRY----SVAYAAQKPWLLNA-TVE 754
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWngtpLAEQRDepheNILYLGHLPGLKPElSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 755 ENITFGSPFNKQRYKAVTDACslqpdidllpfgdqTEIGERGIN------LSGGQRQRICVARALYQNTNIVFLDDPFSA 828
Cdd:TIGR01189 92 ENLHFWAAIHGGAQRTIEDAL--------------AAVGLTGFEdlpaaqLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 530398972 829 LDI--------HLSDHLMQEGIlkflqddkrtLVLVTH 858
Cdd:TIGR01189 158 LDKagvallagLLRAHLARGGI----------VLLTTH 185
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
688-862 |
4.08e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 64.73 E-value: 4.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI------------LGEMQTLEGKVhwSNRN-RYSVAYAAQKPWLL-NATV 753
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitsgdliVDGLKVNDPKV--DERLiRQEAGMVFQQFYLFpHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 754 EENITFGSpfnkQRYKAVTDACSLQPDIDLLpfgDQTEIGERG----INLSGGQRQRICVARALYQNTNIVFLDDPFSAL 829
Cdd:PRK09493 95 LENVMFGP----LRVRGASKEEAEKQARELL---AKVGLAERAhhypSELSGGQQQRVAIARALAVKPKLMLFDEPTSAL 167
|
170 180 190
....*....|....*....|....*....|...
gi 530398972 830 DIHLSDHLMQegILKFLQDDKRTLVLVTHKLQY 862
Cdd:PRK09493 168 DPELRHEVLK--VMQDLAEEGMTMVIVTHEIGF 198
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1315-1524 |
5.10e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.53 E-value: 5.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1315 VLKHVKAYIKPGQKVGICGRTGSGKSSlslAFFRMVDIF---DGKIVIDGIDISKLPLHTlRSRLSI--ILQDPILFSG- 1388
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTT---TFYMVVGIVprdAGNIIIDDEDISLLPLHA-RARRGIgyLPQEASIFRRl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1389 ----------SIRFNLDPECKctDDRLWEALEIAQLKNMVKSLpggldavvtegGENFSVGQRQLFCLARAFVRKSSILI 1458
Cdd:PRK10895 94 svydnlmavlQIRDDLSAEQR--EDRANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398972 1459 MDEATASIDMATENILQKVVmTAFADR--TVVTIAHRV-HTILTADLVIVMKRGNILEYDTPESLLAQE 1524
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRII-EHLRDSglGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
669-877 |
5.37e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.01 E-value: 5.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 669 DIAIKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRNRysVAYAAQKPWL 748
Cdd:COG0488 313 KKVLELEGLSKSYG-DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVK--IGYFDQHQEE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 749 L--NATVEENITFGSPFNKQRYkaVTDACSlqpdiDLLpF-GDQ--TEIGergiNLSGGQRQRICVARALYQNTNIVFLD 823
Cdd:COG0488 390 LdpDKTVLDELRDGAPGGTEQE--VRGYLG-----RFL-FsGDDafKPVG----VLSGGEKARLALAKLLLSPPNVLLLD 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 530398972 824 DPFSALDIHlsdhlMQEGILKFLQDDKRTLVLVTHKLQYL-THADWIIAMKDGSV 877
Cdd:COG0488 458 EPTNHLDIE-----TLEALEEALDDFPGTVLLVSHDRYFLdRVATRILEFEDGGV 507
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1299-1525 |
5.83e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 65.21 E-value: 5.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1378
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1379 ILQDP--ILFS---------GSIRFNLDPECkcTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLA 1447
Cdd:PRK13652 83 VFQNPddQIFSptveqdiafGPINLGLDEET--VAHRVSSALHMLGLEELRDRVPHHL-----------SGGEKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1448 RAFVRKSSILIMDEATASID-MATENILQkvVMTAFADR---TVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLA 1522
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDpQGVKELID--FLNDLPETygmTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFL 227
|
...
gi 530398972 1523 QEN 1525
Cdd:PRK13652 228 QPD 230
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
683-891 |
1.45e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.58 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 683 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNR--NRYSVAYAA--------QKPWLLNA- 751
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInyNKLDHKLAAqlgigiiyQELSVIDEl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 752 TVEENITFGS-PFNKQRYKAVTDACSLQ--PDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 828
Cdd:PRK09700 96 TVLENLYIGRhLTKKVCGVNIIDWREMRvrAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398972 829 LDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQTKDV 891
Cdd:PRK09700 176 LTNKEVDYLFL--IMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDVSNDDI 237
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
688-896 |
1.65e-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: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEM-----QTLE------GKVH-WSNRNRYSVAYAA-QKPWLLNATVE 754
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpptygNDVRlfgerrGGEDvWELRKRIGLVSPAlQLRFPRDETVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 755 ENIT---FGSPFnkqRYKAVTDAcslqpDI----DLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPF 826
Cdd:COG1119 99 DVVLsgfFDSIG---LYREPTDE-----QRerarELLELLGLAHLADRPFGtLSQGEQRRVLIARALVKDPELLILDEPT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 827 SALDIHlsdhlMQEGILKFL----QDDKRTLVLVTHKLQYL----THAdwiIAMKDGSVLREGTLKDIQTKDV--ELYEH 896
Cdd:COG1119 171 AGLDLG-----ARELLLALLdklaAEGAPTLVLVTHHVEEIppgiTHV---LLLKDGRVVAAGPKEEVLTSENlsEAFGL 242
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
666-877 |
1.83e-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: 63.33 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 666 ETEDIAIKVTNGyfswgsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAIL------GEMQtLEGkVHWSN----RN 735
Cdd:cd03289 4 TVKDLTAKYTEG------GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLrllnteGDIQ-IDG-VSWNSvplqKW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 736 RYSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQ 815
Cdd:cd03289 76 RKAFGVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398972 816 NTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSV 877
Cdd:cd03289 156 KAKILLLDEPSAHLD-PITYQVIRKTLKQAFAD--CTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
672-881 |
1.96e-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: 62.21 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWGSGLAtLSNIDIRIPTGqLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN--------RYSVAYAA 743
Cdd:cd03264 1 LQLENLTKRYGKKRA-LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDvlkqpqklRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 744 QKP-WLLNATVEENITF-----GSPfNKQRYKAVTDACSLqpdIDLLPFGDQtEIGErginLSGGQRQRICVARALYQNT 817
Cdd:cd03264 79 QEFgVYPNFTVREFLDYiawlkGIP-SKEVKARVDEVLEL---VNLGDRAKK-KIGS----LSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398972 818 NIVFLDDPFSALD----IHLSDHLMQEGilkflqdDKRTLVLVTHKLQ-YLTHADWIIAMKDGSVLREG 881
Cdd:cd03264 150 SILIVDEPTAGLDpeerIRFRNLLSELG-------EDRIVILSTHIVEdVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
1023-1192 |
2.03e-10 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 63.60 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1023 VAGFSILCGAGIFLclvTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLT 1102
Cdd:cd18552 45 IIGLFLLRGLASYL---QTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1103 RSTLLCLSAIGMISYA----TPVFLVALLPLGVAFYFIQKYFRVASKDLQE-LDDSTQlpllcHFSETAEGLTTIRAFRH 1177
Cdd:cd18552 122 RDPLTVIGLLGVLFYLdwklTLIALVVLPLAALPIRRIGKRLRKISRRSQEsMGDLTS-----VLQETLSGIRVVKAFGA 196
|
170
....*....|....*
gi 530398972 1178 ETRFKQRMLELTDTN 1192
Cdd:cd18552 197 EDYEIKRFRKANERL 211
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
688-896 |
2.21e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 61.77 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTL--EGKVHWSNRNrysvayaaqkpwLLNATVEEN------ITF 759
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGED------------ITDLPPEERarlgifLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 760 GSPFnkqRYKAVTDAcslqpdiDLLpfgdqteigeRGIN--LSGGQRQRICVARALYQNTNIVFLDDPFSALDIhlsDHL 837
Cdd:cd03217 84 QYPP---EIPGVKNA-------DFL----------RYVNegFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI---DAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398972 838 -MQEGILKFLQDDKRTLVLVTHKLQYLTH--ADWIIAMKDGSVLREGtlkdiqtkDVELYEH 896
Cdd:cd03217 141 rLVAEVINKLREEGKSVLIITHYQRLLDYikPDRVHVLYDGRIVKSG--------DKELALE 194
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
688-886 |
2.35e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 64.67 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV-------------HWSNRNRYSVAYAAQKPWLL-NATV 753
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVlidgvdiakisdaELREVRRKKIAMVFQSFALMpHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 754 EENITFGS-----PFNKQRYKAVtDACSlQPDIDLLPFGDQTEigerginLSGGQRQRICVARALYQNTNIVFLDDPFSA 828
Cdd:PRK10070 124 LDNTAFGMelagiNAEERREKAL-DALR-QVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 530398972 829 LDIHLSDHlMQEGILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREGTLKDI 886
Cdd:PRK10070 195 LDPLIRTE-MQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1311-1520 |
2.55e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.96 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1311 NLKPVlKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL---PLHTLRSRLSIILQDPiLFS 1387
Cdd:PRK15079 33 TLKAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMkddEWRAVRSDIQMIFQDP-LAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1388 GSIRFNLdpeckctDDRLWEALEI-------AQLKNMVKSL---PGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSIL 1457
Cdd:PRK15079 111 LNPRMTI-------GEIIAEPLRTyhpklsrQEVKDRVKAMmlkVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1458 IMDEATASIDMATE----NILQKvvMTAFADRTVVTIAHR---VHTIltADLVIVMKRGNILEYDTPESL 1520
Cdd:PRK15079 184 ICDEPVSALDVSIQaqvvNLLQQ--LQREMGLSLIFIAHDlavVKHI--SDRVLVMYLGHAVELGTYDEV 249
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
690-886 |
2.66e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 63.74 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 690 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNR-------------NRYSVAYAAQKPWLL-NATVEE 755
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekgiclppEKRRIGYVFQDARLFpHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 756 NITFG-SPFNKQRYKAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 834
Cdd:PRK11144 96 NLRYGmAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 530398972 835 DHLMQegILKFLQDDKRTLVL-VTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 886
Cdd:PRK11144 165 RELLP--YLERLAREINIPILyVSHSLDEILRlADRVVVLEQGKVKAFGPLEEV 216
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1303-1522 |
2.68e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 63.10 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1303 DLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG--IDISKLPLHTLRSRLSIIL 1380
Cdd:PRK13638 6 DLWFRYQD--EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1381 QDP---ILFS---GSIRFNLD----PECKCTDdRLWEALEIAQLKNMVKslpggldavvtEGGENFSVGQRQLFCLARAF 1450
Cdd:PRK13638 84 QDPeqqIFYTdidSDIAFSLRnlgvPEAEITR-RVDEALTLVDAQHFRH-----------QPIQCLSHGQKKRVAIAGAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398972 1451 VRKSSILIMDEATASIDMATEN----ILQKVVMTAfadRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLA 1522
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTqmiaIIRRIVAQG---NHVIISSHDIDLIYeISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
670-897 |
2.86e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 62.92 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 670 IAIKVTNGYFSWGSGLAT--LSNIDIRIPTGQLTMIVGQVGCGKSSLL-------------LAILGEMQTLEGkvhwSNR 734
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMqhfnallkpssgtITIAGYHITPET----GNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 735 N----RYSVAYAAQKP--WLLNATVEENITFGsPFN------KQRYKAVT--DACSLQPD-IDLLPFgdqteigergiNL 799
Cdd:PRK13641 79 NlkklRKKVSLVFQFPeaQLFENTVLKDVEFG-PKNfgfsedEAKEKALKwlKKVGLSEDlISKSPF-----------EL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 800 SGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDGSVL 878
Cdd:PRK13641 147 SGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQ--LFKDYQKAGHTVILVTHNMDDVAeYADDVLVLEHGKLI 224
|
250
....*....|....*....
gi 530398972 879 REGTLKDIQTKDVELYEHW 897
Cdd:PRK13641 225 KHASPKEIFSDKEWLKKHY 243
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
686-888 |
3.38e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 62.37 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 686 ATLSNIDIRIPTGQLTMIVGQVGCGKSSLL------LAILGEMQTLEGKVHWSNRN---------RYSVAYAAQKP-WLL 749
Cdd:PRK14246 24 AILKDITIKIPNNSIFGIMGPSGSGKSTLLkvlnrlIEIYDSKIKVDGKVLYFGKDifqidaiklRKEVGMVFQQPnPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 750 NATVEENITFgsPF------NKQRYKAVTDACslqpdidLLPFGDQTEIGER----GINLSGGQRQRICVARALYQNTNI 819
Cdd:PRK14246 104 HLSIYDNIAY--PLkshgikEKREIKKIVEEC-------LRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKV 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398972 820 VFLDDPFSALDIhlsdhLMQEGILKFLQDDKR--TLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQT 888
Cdd:PRK14246 175 LLMDEPTSMIDI-----VNSQAIEKLITELKNeiAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFT 241
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1331-1517 |
3.72e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 63.33 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1331 ICGRTGSGKSSLSLAF----------FRMVDIFDG-KIVIDGIDISKLP-----LHTLRSRLSIILQDP--ILFSGSIRf 1392
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFnglikskygtIQVGDIYIGdKKNNHELITNPYSkkiknFKELRRRVSMVFQFPeyQLFKDTIE- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1393 nldpeckctDDRLWEALEIAQLKNMVKSLPG------GLDAVVTEGGE-NFSVGQRQLFCLARAFVRKSSILIMDEATAS 1465
Cdd:PRK13631 136 ---------KDIMFGPVALGVKKSEAKKLAKfylnkmGLDDSYLERSPfGLSGGQKRRVAIAGILAIQPEILIFDEPTAG 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 530398972 1466 IDMATENILQKVVMTAFAD-RTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTP 1517
Cdd:PRK13631 207 LDPKGEHEMMQLILDAKANnKTVFVITHTMEHVLeVADEVIVMDKGKILKTGTP 260
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
688-883 |
3.93e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 61.76 E-value: 3.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQT-LEGKVHWSNRNRYSVAYAAqKPWLLNA--------------- 751
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLL-HLLGGLDTpTSGDVIFNGQPMSKLSSAA-KAELRNQklgfiyqfhhllpdf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 752 TVEENITFgsPF---NKQRYKAVTDACSLqpdidLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 828
Cdd:PRK11629 103 TALENVAM--PLligKKKPAEINSRALEM-----LAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 530398972 829 LDIHLSDHLMQegILKFLQDDKRTLVL-VTHKLQYLTHADWIIAMKDGSVLREGTL 883
Cdd:PRK11629 176 LDARNADSIFQ--LLGELNRLQGTAFLvVTHDLQLAKRMSRQLEMRDGRLTAELSL 229
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1316-1522 |
3.99e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.50 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1316 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPI----------- 1384
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPStslnprqrisq 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1385 LFSGSIRFNLDPECKCTDDRLWEAL-EIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEAT 1463
Cdd:PRK15112 109 ILDFPLRLNTDLEPEQREKQIIETLrQVGLLPDHASYYPHML-----------APGQKQRLGLARALILRPKVIIADEAL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398972 1464 ASIDMATENILQKVVMTAFADRTVVTIAHRVHTILT---ADLVIVMKRGNILEYDTPESLLA 1522
Cdd:PRK15112 178 ASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMkhiSDQVLVMHQGEVVERGSTADVLA 239
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
799-886 |
4.01e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 62.16 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 799 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD---HLMQEgilkfLQDDKR-TLVLVTHKLQYLTH-ADWIIAMK 873
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSqiiNLMLE-----LQEKLGiSYIYVSQHLGIVKHiSDKVLVMH 224
|
90
....*....|...
gi 530398972 874 DGSVLREGTLKDI 886
Cdd:COG4167 225 QGEVVEYGKTAEV 237
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
1052-1180 |
4.27e-10 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 62.53 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1052 AKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATP-VFLVALL--- 1127
Cdd:cd18573 73 VARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPkLTLVMLLvvp 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 530398972 1128 PLGVAFYFIQKYFRVASKDLQE-LDDSTQLpllchfsetAE----GLTTIRAFRHETR 1180
Cdd:cd18573 153 PIAVGAVFYGRYVRKLSKQVQDaLADATKV---------AEerlsNIRTVRAFAAERK 201
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
687-886 |
5.07e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 62.34 E-value: 5.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 687 TLSNIDIRIPTGQLTMIVGQVGCGKSSL------LLAI------LGEMQTLEGKVhWSNRNRysVAYAAQKP--WLLNAT 752
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLakllngLLLPeagtitVGGMVLSEETV-WDVRRQ--VGMVFQNPdnQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 753 VEENITFGSPFN----KQRYKAVTDACSLqpdIDLLPFGDQTEIgergiNLSGGQRQRICVARALYQNTNIVFLDDPFSA 828
Cdd:PRK13635 99 VQDDVAFGLENIgvprEEMVERVDQALRQ---VGMEDFLNREPH-----RLSGGQKQRVAIAGVLALQPDIIILDEATSM 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 530398972 829 LDIHLSDHLMqeGILKFLQDDKRTLVL-VTHKLQYLTHADWIIAMKDGSVLREGTLKDI 886
Cdd:PRK13635 171 LDPRGRREVL--ETVRQLKEQKGITVLsITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
687-877 |
5.52e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 62.06 E-value: 5.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 687 TLSNIDIRIPTGQLTMIVGQVGCGKSS-------LLLA------ILGEMQTLEGKvhWSNRNRYSVAYAAQKPWLLNATV 753
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTtvrlidgLLEAesgqiiIDGDLLTEENV--WDIRHKIGMVFQNPDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 754 EENITFGSPfNK-----QRYKAVTDACSLqpdIDLLPFGDQTEIgergiNLSGGQRQRICVARALYQNTNIVFLDDPFSA 828
Cdd:PRK13650 100 EDDVAFGLE-NKgipheEMKERVNEALEL---VGMQDFKEREPA-----RLSGGQKQRVAIAGAVAMRPKIIILDEATSM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 530398972 829 LDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSV 877
Cdd:PRK13650 171 LDPEGRLELIKT-IKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1300-1470 |
5.89e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 60.96 E-value: 5.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1300 KIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLsLAF--------FRmvdiFDGKIVIDGIDISKLPlhT 1371
Cdd:COG4136 3 SLENLTITLGG--RPLLAPLSLTVAPGEILTLMGPSGSGKSTL-LAAiagtlspaFS----ASGEVLLNGRRLTALP--A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1372 LRSRLSIILQDPILFS-----GSIRFNLDPECKCTD--DRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1444
Cdd:COG4136 74 EQRRIGILFQDDLLFPhlsvgENLAFALPPTIGRAQrrARVEQALEEAGLAGFADRDPATL-----------SGGQRARV 142
|
170 180
....*....|....*....|....*.
gi 530398972 1445 CLARAFVRKSSILIMDEATASIDMAT 1470
Cdd:COG4136 143 ALLRALLAEPRALLLDEPFSKLDAAL 168
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1299-1524 |
6.99e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 62.94 E-value: 6.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1378
Cdd:PRK09536 4 IDVSDLSVEFGD--TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1379 ILQDPilfsgSIRFNLDPE----------------CKCTDDRLWE-ALEiaqlknmvkslPGGLDAVVTEGGENFSVGQR 1441
Cdd:PRK09536 82 VPQDT-----SLSFEFDVRqvvemgrtphrsrfdtWTETDRAAVErAME-----------RTGVAQFADRPVTSLSGGER 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1442 QLFCLARAFVRKSSILIMDEATASIDMATE-NILQKVVMTAFADRTVVTIAHRVHtiLTA---DLVIVMKRGNILEYDTP 1517
Cdd:PRK09536 146 QRVLLARALAQATPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLD--LAArycDELVLLADGRVRAAGPP 223
|
....*..
gi 530398972 1518 ESLLAQE 1524
Cdd:PRK09536 224 ADVLTAD 230
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
671-882 |
8.35e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 60.80 E-value: 8.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 671 AIKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLL--LAIL-----GEMQTLEGKVHWSNRN-------- 735
Cdd:PRK11124 2 SIQLNGINCFYGAHQA-LFDITLDCPQGETLVLLGPSGAGKSSLLrvLNLLemprsGTLNIAGNHFDFSKTPsdkairel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 736 RYSVAYAAQK----PWLlnaTVEENITfGSP-----FNKQryKAVTDACSLQPDIDLLPFGDQTEIgergiNLSGGQRQR 806
Cdd:PRK11124 81 RRNVGMVFQQynlwPHL---TVQQNLI-EAPcrvlgLSKD--QALARAEKLLERLRLKPYADRFPL-----HLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398972 807 ICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGT 882
Cdd:PRK11124 150 VAIARALMMEPQVLLFDEPTAALDPEITAQIVS--IIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGD 224
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1265-1527 |
9.27e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.07 E-value: 9.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1265 AVKKVNSFltmESENYEGTMDPSQVPEHWPQegeIKIHDLCVRYENN---LKPVlkhvKAYIKPGQKVGICGRTGSGKSS 1341
Cdd:PRK10522 295 AFNKLNKL---ALAPYKAEFPRPQAFPDWQT---LELRNVTFAYQDNgfsVGPI----NLTIKRGELLFLIGGNGSGKST 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1342 LSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSirfnLDPECKCTDDRLWEA-LEIAQLKNMVKs 1420
Cdd:PRK10522 365 LAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALVEKwLERLKMAHKLE- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1421 lpggldavvTEGGE----NFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRV 1494
Cdd:PRK10522 440 ---------LEDGRisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEmgKTIFAISHDD 510
|
250 260 270
....*....|....*....|....*....|...
gi 530398972 1495 HTILTADLVIVMKRGNILEYDTPESLLAQENGV 1527
Cdd:PRK10522 511 HYFIHADRLLEMRNGQLSELTGEERDAASRDAV 543
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
685-903 |
1.19e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 61.79 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 685 LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEG-------------------------KVHWSNRNRYSV 739
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgdiyigdkknnhelitnpyskKIKNFKELRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 740 AYAAQKP--WLLNATVEENITFGsPFN--------KQRYKAVTDACSLQPD-IDLLPFGdqteigerginLSGGQRQRIC 808
Cdd:PRK13631 119 SMVFQFPeyQLFKDTIEKDIMFG-PVAlgvkkseaKKLAKFYLNKMGLDDSyLERSPFG-----------LSGGQKRRVA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 809 VARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREGTLKDIQ 887
Cdd:PRK13631 187 IAGILAIQPEILIFDEPTAGLDPKGEHEMMQ--LILDAKANNKTVFVITHTMeHVLEVADEVIVMDKGKILKTGTPYEIF 264
|
250
....*....|....*.
gi 530398972 888 TkDVELYEHWKTLMNR 903
Cdd:PRK13631 265 T-DQHIINSTSIQVPR 279
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
680-896 |
1.20e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 61.78 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 680 SWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNR--NRYSVA----------YAaqkpw 747
Cdd:PRK11650 12 SYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvNELEPAdrdiamvfqnYA----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 748 lL--NATVEENITFG-------SPFNKQRYKAVTDACSLQPDIDLLPfgdqteigeRgiNLSGGQRQRICVARALYQNTN 818
Cdd:PRK11650 87 -LypHMSVRENMAYGlkirgmpKAEIEERVAEAARILELEPLLDRKP---------R--ELSGGQRQRVAMGRAIVREPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 819 iVFL-DDPFSALDIHLSDHLMQEgiLKFLQddKR---TLVLVTH-KLQYLTHADWIIAMKDGSVLREGTlkdiqtkDVEL 893
Cdd:PRK11650 155 -VFLfDEPLSNLDAKLRVQMRLE--IQRLH--RRlktTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGT-------PVEV 222
|
...
gi 530398972 894 YEH 896
Cdd:PRK11650 223 YEK 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1298-1492 |
1.43e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 60.57 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1298 EIKIHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIF-----DGKIVIDGIDI--SKLPLH 1370
Cdd:PRK14243 10 VLRTENLNVYYGSFL--AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIpgfrvEGKVTFHGKNLyaPDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1371 TLRSRLSIILQDPILFSGSIRFNLDPECKCT------DDRLWEALEIAQLKNMVKSlpggldaVVTEGGENFSVGQRQLF 1444
Cdd:PRK14243 88 EVRRRIGMVFQKPNPFPKSIYDNIAYGARINgykgdmDELVERSLRQAALWDEVKD-------KLKQSGLSLSGGQQQRL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 530398972 1445 CLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAH 1492
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTH 208
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1313-1532 |
1.55e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 61.78 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1313 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHtlRSRLSIILQDPILF-- 1386
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTL----LRMLAGFEqptaGQIMLDGVDLSHVPPY--QRPINMMFQSYALFph 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1387 ---SGSIRFNLD----PECKCTDdRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIM 1459
Cdd:PRK11607 106 mtvEQNIAFGLKqdklPKAEIAS-RVNEMLGLVHMQEFAKRKPHQL-----------SGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1460 DEATASID------MATE--NILQKVVMTAfadrtvVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQENGVF-A 1529
Cdd:PRK11607 174 DEPMGALDkklrdrMQLEvvDILERVGVTC------VMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEIYEHPTTRYsA 247
|
...
gi 530398972 1530 SFV 1532
Cdd:PRK11607 248 EFI 250
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1242-1523 |
1.83e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 62.13 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1242 ALTITNYLNWVVRNLADLEVQM--GAVKKVNSFLTMESENYEGTMDPSQVPEHWPQEGEIKIHDLCVRYENNLKPVLKHV 1319
Cdd:TIGR03269 221 SMVLTSHWPEVIEDLSDKAIWLenGEIKEEGTPDEVVAVFMEGVSEVEKECEVEVGEPIIKVRNVSKRYISVDRGVVKAV 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1320 KAY---IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVI----DGIDISKlPLHTLRSR----LSIILQDPILFSG 1388
Cdd:TIGR03269 301 DNVsleVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTK-PGPDGRGRakryIGILHQEYDLYPH 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1389 SIRFnldpeckctdDRLWEAL------EIAQLKNMVKSLPGGLD-----AVVTEGGENFSVGQRQLFCLARAFVRKSSIL 1457
Cdd:TIGR03269 380 RTVL----------DNLTEAIglelpdELARMKAVITLKMVGFDeekaeEILDKYPDELSEGERHRVALAQVLIKEPRIV 449
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398972 1458 IMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLAQ 1523
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSILKAREEmeQTFIIVSHDMDFVLdVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1299-1492 |
1.96e-09 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 57.46 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslaffrmvdifdgkividgidisklplhtlrsrLSI 1378
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTL---------------------------------LKL 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1379 ILQDPILFSGSIRFNldpeckctddrlwEALEIAQLknmvkslpggldavvteggENFSVGQRQLFCLARAFVRKSSILI 1458
Cdd:cd03221 46 IAGELEPDEGIVTWG-------------STVKIGYF-------------------EQLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190
....*....|....*....|....*....|....*...
gi 530398972 1459 MDEATASIDMAT----ENILQKvvmtaFaDRTVVTIAH 1492
Cdd:cd03221 94 LDEPTNHLDLESiealEEALKE-----Y-PGTVILVSH 125
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1316-1527 |
2.01e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 60.56 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1316 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP----LHTLRSRLSIILQDP-------- 1383
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRPVRKRIGMVFQFPesqlfedt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1384 ----ILFsGSIRFNLDPEcKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIM 1459
Cdd:PRK13646 103 vereIIF-GPKNFKMNLD-EVKNYAHRLLMDLGFSRDVMSQSPFQM-----------SGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398972 1460 DEATASIDMATenilQKVVMTAFA------DRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQENGV 1527
Cdd:PRK13646 170 DEPTAGLDPQS----KRQVMRLLKslqtdeNKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKDKKKL 240
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
976-1192 |
2.12e-09 |
|
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: 60.64 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 976 GGFFLLILMIFSKLLKHSVIVAIDYWLATWtseysinntgkadqtyYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNL 1055
Cdd:cd07346 11 ATALGLALPLLTKLLIDDVIPAGDLSLLLW----------------IALLLLLLALLRALLSYLRRYLAARLGQRVVFDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1056 HHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIG-MISYATPVFLVALLPL---GV 1131
Cdd:cd07346 75 RRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALViLFYLNWKLTLVALLLLplyVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398972 1132 AFYFIQKYFRVASKDLQE-LDDSTQlpllcHFSETAEGLTTIRAFRHETRFKQRMLELTDTN 1192
Cdd:cd07346 155 ILRYFRRRIRKASREVREsLAELSA-----FLQESLSGIRVVKAFAAEEREIERFREANRDL 211
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1314-1511 |
2.32e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.61 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1314 PVLKHVKAYIKPGQKVGICGRTGSGKSSLS--LAFFRMVDIfdGKIVIDGIDISKL-PLHTLRSRLSIILQDPILFSG-- 1388
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMkiIAGIVPPDS--GTLEIGGNPCARLtPAKAHQLGIYLVPQEPLLFPNls 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1389 ---SIRFNLdPEckctddrlwEALEIAQLKNMVKSLPGGLDAVVTEGgeNFSVGQRQLFCLARAFVRKSSILIMDEATAS 1465
Cdd:PRK15439 103 vkeNILFGL-PK---------RQASMQKMKQLLAALGCQLDLDSSAG--SLEVADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 530398972 1466 IDMA-TENILQKVVMTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNI 1511
Cdd:PRK15439 171 LTPAeTERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTI 218
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1298-1524 |
2.34e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 60.03 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1298 EIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLS 1377
Cdd:PRK11231 2 TLRTENLTVGYGT--KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1378 IILQDPILFSG-SIR----------FNLDPECKCTDDRLWE-ALEIAQLKNMVkslpgglDAVVTEggenFSVGQRQLFC 1445
Cdd:PRK11231 80 LLPQHHLTPEGiTVRelvaygrspwLSLWGRLSAEDNARVNqAMEQTRINHLA-------DRRLTD----LSGGQRQRAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1446 LARAFVRKSSILIMDEATASIDMATENILQKVV-MTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQ 1523
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMrELNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMTP 228
|
.
gi 530398972 1524 E 1524
Cdd:PRK11231 229 G 229
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
978-1190 |
2.67e-09 |
|
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: 60.11 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 978 FFLLILMIFSKLLkhsvIVAIDYWLATWTSEYSINNTGKADQTY-YVAGFSILCGAGIFLCLVTSLTVEWMGLTAA---- 1052
Cdd:cd18547 2 ILVIILAIISTLL----SVLGPYLLGKAIDLIIEGLGGGGGVDFsGLLRILLLLLGLYLLSALFSYLQNRLMARVSqrtv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1053 KNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIG-MISYATPVFLVALLPLGV 1131
Cdd:cd18547 78 YDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLImMLYISPLLTLIVLVTVPL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530398972 1132 AFYFI-------QKYFRVASKDLQELDDSTQlpllchfsETAEGLTTIRAFRHETRFKQRMLELTD 1190
Cdd:cd18547 158 SLLVTkfiakrsQKYFRKQQKALGELNGYIE--------EMISGQKVVKAFNREEEAIEEFDEINE 215
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1314-1521 |
2.91e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 59.34 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1314 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDI--SKLPLHTLRSRLSIILQdpilfsgsiR 1391
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEAGMVFQ---------Q 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1392 FNLDPECKCTDDRLWEALEI-----AQLKNMVKSLPG--GLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA 1464
Cdd:PRK09493 86 FYLFPHLTALENVMFGPLRVrgaskEEAEKQARELLAkvGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398972 1465 SIDmatENILQKV--VMTAFADR----TVVT----IAHRVHTILtadlvIVMKRGNILEYDTPESLL 1521
Cdd:PRK09493 166 ALD---PELRHEVlkVMQDLAEEgmtmVIVTheigFAEKVASRL-----IFIDKGRIAEDGDPQVLI 224
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
685-875 |
3.76e-09 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 58.98 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 685 LATLSNIDIRIPTGQLTMIVGQVGCGKSSLL--LAILgEMQTlEGKVHWSN--------------RNRySVAYAAQKPWL 748
Cdd:COG4181 25 LTILKGISLEVEAGESVAIVGASGSGKSTLLglLAGL-DRPT-SGTVRLAGqdlfaldedararlRAR-HVGFVFQSFQL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 749 LNA-TVEENIT-----FGSPFNKQRYKAVTDACSLQPDIDLLPfgDQteigerginLSGGQRQRICVARALYQNTNIVFL 822
Cdd:COG4181 102 LPTlTALENVMlplelAGRRDARARARALLERVGLGHRLDHYP--AQ---------LSGGEQQRVALARAFATEPAILFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 530398972 823 DDPFSALDIHLSDHLMQegiLKF-LQDDKR-TLVLVTHKLQYLTHADWIIAMKDG 875
Cdd:COG4181 171 DEPTGNLDAATGEQIID---LLFeLNRERGtTLVLVTHDPALAARCDRVLRLRAG 222
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
703-934 |
4.31e-09 |
|
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: 61.10 E-value: 4.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 703 IVGQVGCGKSSLLLAILGEMQTLEGKVhWSNRNrYSVAYAAQKPWL-LNATVEENITFGSPFNKQ---RYKAVTDACS-- 776
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEA-RPQPG-IKVGYLPQEPQLdPTKTVRENVEEGVAEIKDaldRFNEISAKYAep 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 777 -------------LQPDIDL------------------LPFGDQtEIGergiNLSGGQRQRICVARALYQNTNIVFLDDP 825
Cdd:TIGR03719 114 dadfdklaaeqaeLQEIIDAadawdldsqleiamdalrCPPWDA-DVT----KLSGGERRRVALCRLLLSKPDMLLLDEP 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 826 fsaldihlSDHLMQEGIL---KFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDG-SVLREGTlkdiqtkdvelYEHW--- 897
Cdd:TIGR03719 189 --------TNHLDAESVAwleRHLQEYPGTVVAVTHDRYFLDNvAGWILELDRGrGIPWEGN-----------YSSWleq 249
|
250 260 270
....*....|....*....|....*....|....*....
gi 530398972 898 KTlmNRQDQElEKDMEADQTTLERKT--LRRAMYSREAK 934
Cdd:TIGR03719 250 KQ--KRLEQE-EKEESARQKTLKRELewVRQSPKGRQAK 285
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1299-1470 |
4.37e-09 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 58.60 E-value: 4.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVDIFD-GKIVIDGIDISKL---PLHTL 1372
Cdd:COG4181 9 IELRGLTKTVGTGAGELtiLKGISLEVEAGESVAIVGASGSGKSTL-LGLLAGLDRPTsGTVRLAGQDLFALdedARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1373 RSR-LSIILQD---------------PILFSGsirfnlDPECKctdDRLWEALEIAQLKNMVKSLPGGLdavvtEGGEnf 1436
Cdd:COG4181 88 RARhVGFVFQSfqllptltalenvmlPLELAG------RRDAR---ARARALLERVGLGHRLDHYPAQL-----SGGE-- 151
|
170 180 190
....*....|....*....|....*....|....
gi 530398972 1437 svgqRQLFCLARAFVRKSSILIMDEATASIDMAT 1470
Cdd:COG4181 152 ----QQRVALARAFATEPAILFADEPTGNLDAAT 181
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1315-1527 |
5.16e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 58.94 E-value: 5.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1315 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG--IDISKLPLHTLRSRLSIILQDP--ILFSGSI 1390
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTVGIVFQNPddQLFAPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1391 R-------FNLdpeckctddrlweALEIAQLKNMVKSlpgGLDAVVTEGGEN-----FSVGQRQLFCLARAFVRKSSILI 1458
Cdd:PRK13639 97 EedvafgpLNL-------------GLSKEEVEKRVKE---ALKAVGMEGFENkpphhLSGGQKKRVAIAGILAMKPEIIV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398972 1459 MDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTI-LTADLVIVMKRGNILEYDTPESLLAQENGV 1527
Cdd:PRK13639 161 LDEPTSGLDpMGASQIMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDIETI 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1299-1518 |
5.37e-09 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 58.60 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYeNNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIF----DGKIVIDGIDISKLPLHtLRS 1374
Cdd:cd03219 1 LEVRGLTKRF-GGLV-ALDDVSFSVRPGEIHGLIGPNGAGKTTL----FNLISGFlrptSGSVLFDGEDITGLPPH-EIA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1375 RLSII--LQDPILFSG-SIRFNLD-----------------PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvtegge 1434
Cdd:cd03219 74 RLGIGrtFQIPRLFPElTVLENVMvaaqartgsglllararREEREARERAEELLERVGLADLADRPAGEL--------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1435 nfSVGQRQLFCLARAFVRKSSILIMDEATASIDMA-TENILQKVVMTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNIL 1512
Cdd:cd03219 145 --SYGQQRRLEIARALATDPKLLLLDEPAAGLNPEeTEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVI 222
|
....*.
gi 530398972 1513 EYDTPE 1518
Cdd:cd03219 223 AEGTPD 228
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
800-886 |
7.87e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 59.21 E-value: 7.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 800 SGGQRQRICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKRTL----VLVTHKLQYLTH-ADWIIAMKD 874
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSV-----QAQVLNLMMDLQQELglsyVFISHDLSVVEHiADEVMVMYL 230
|
90
....*....|..
gi 530398972 875 GSVLREGTLKDI 886
Cdd:PRK11308 231 GRCVEKGTKEQI 242
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
688-886 |
1.25e-08 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 58.55 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLL--LAILgEMQTlEGKVHWSNRN------------RYSVAYAAQKPWLLNA-T 752
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIrcINLL-ERPT-SGSVLVDGVDltalserelraaRRKIGMIFQHFNLLSSrT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 753 VEENITF-----GSPfNKQRYKAVTDacslqpdidLLPFgdqTEIGERG----INLSGGQRQRICVARALYQNTNIVFLD 823
Cdd:COG1135 99 VAENVALpleiaGVP-KAEIRKRVAE---------LLEL---VGLSDKAdaypSQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398972 824 DPFSALDIHLSDhlmqeGILKFLQDDKR----TLVLVTH------KLqylthADWIIAMKDGSVLREGTLKDI 886
Cdd:COG1135 166 EATSALDPETTR-----SILDLLKDINRelglTIVLITHemdvvrRI-----CDRVAVLENGRIVEQGPVLDV 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
688-880 |
1.49e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 57.40 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV--------HWS--NRNRYsVAYAAQKPwLL----NATV 753
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIlidgkdvtKLPeyKRAKY-IGRVFQDP-MMgtapSMTI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 754 EENI----------TFGSPFNKQRYKAVTDACSlqpDIDL-----LpfgdQTEIGergiNLSGGQRQRICVARALYQNTN 818
Cdd:COG1101 100 EENLalayrrgkrrGLRRGLTKKRRELFRELLA---TLGLglenrL----DTKVG----LLSGGQRQALSLLMATLTKPK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398972 819 IVFLDDPFSALDIHLSDHLMQegiL--KFLQDDKRTLVLVTHKLQY-LTHADWIIAMKDGSVLRE 880
Cdd:COG1101 169 LLLLDEHTAALDPKTAALVLE---LteKIVEENNLTTLMVTHNMEQaLDYGNRLIMMHEGRIILD 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
684-892 |
1.60e-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: 59.07 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG--EMQTLEGKVHWS----------NRNRYSVAYAAQKPWLL-N 750
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSgsplkasnirDTERAGIVIIHQELTLVpE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 751 ATVEENITFGS----PFNKQRYKAVTDAC-SLQPDIDLLPFGDQTEIGERGinlsGGQRQRICVARALYQNTNIVFLDDP 825
Cdd:TIGR02633 93 LSVAENIFLGNeitlPGGRMAYNAMYLRAkNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530398972 826 FSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLqylthaDWIIAMKDG-SVLREGtlKDIQTKDVE 892
Cdd:TIGR02633 169 SSSLTEKETEILLD--IIRDLKAHGVACVYISHKL------NEVKAVCDTiCVIRDG--QHVATKDMS 226
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
691-881 |
2.00e-08 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 56.61 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 691 IDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ------TLEG-KVHWSN---RNRYSVAYAAQK--PWLlnaTVEENIT 758
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEpdagfaTVDGfDVVKEPaeaRRRLGFVSDSTGlyDRL---TARENLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 759 FGSPFNKQRYKAVTDAcsLQPDIDLLPFGDQTEigERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLM 838
Cdd:cd03266 101 YFAGLYGLKGDELTAR--LEELADRLGMEELLD--RRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 530398972 839 QegILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREG 881
Cdd:cd03266 177 E--FIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1323-1531 |
2.20e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 57.81 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1323 IKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIDGIDISKlplHTLRSR-LSIILQDPILFSG-SIRFNL-- 1394
Cdd:PRK11432 29 IKQGTMVTLLGPSGCGKTTV----LRLVagleKPTEGQIFIDGEDVTH---RSIQQRdICMVFQSYALFPHmSLGENVgy 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1395 --------DPECKctdDRLWEALEIAQLKnmvkslpGGLDAVVteggENFSVGQRQLFCLARAFVRKSSILIMDEATASI 1466
Cdd:PRK11432 102 glkmlgvpKEERK---QRVKEALELVDLA-------GFEDRYV----DQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398972 1467 D------MaTENI--LQKVVmtafaDRTVVTIAH-RVHTILTADLVIVMKRGNILEYDTPESLLAQENGVF-ASF 1531
Cdd:PRK11432 168 DanlrrsM-REKIreLQQQF-----NITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFmASF 236
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
684-881 |
2.23e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.38 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN-RYSVAYAAqkpwlLNA----------- 751
Cdd:PRK11288 16 GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEmRFASTTAA-----LAAgvaiiyqelhl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 752 ----TVEENITFGS-P-----FNKQRYKAVTDACSLQPDIDLLPfgdQTEIGErginLSGGQRQRICVARALYQNTNIVF 821
Cdd:PRK11288 91 vpemTVAENLYLGQlPhkggiVNRRLLNYEAREQLEHLGVDIDP---DTPLKY----LSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398972 822 LDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLqylthaDWIIAMKDG-SVLREG 881
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFR--VIRELRAEGRVILYVSHRM------EEIFALCDAiTVFKDG 216
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1299-1525 |
2.28e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 56.70 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1378
Cdd:PRK13548 3 LEARNLSVRLGG--RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1379 ILQDPIL-FSGS----IRFNLDP--ECKCTDDRLWEA----LEIAQLKNmvKSLPggldavVTEGGENfsvgQR-QlfcL 1446
Cdd:PRK13548 81 LPQHSSLsFPFTveevVAMGRAPhgLSRAEDDALVAAalaqVDLAHLAG--RDYP------QLSGGEQ----QRvQ---L 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1447 ARAFVR------KSSILIMDEATASIDMATenilQKVVMTA---FADR---TVVTIAHRVH-TILTADLVIVMKRGNILE 1513
Cdd:PRK13548 146 ARVLAQlwepdgPPRWLLLDEPTSALDLAH----QHHVLRLarqLAHErglAVIVVLHDLNlAARYADRIVLLHQGRLVA 221
|
250
....*....|..
gi 530398972 1514 YDTPESLLAQEN 1525
Cdd:PRK13548 222 DGTPAEVLTPET 233
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
685-880 |
2.44e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 56.33 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 685 LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLlAIL--------GEMQTLEGKVHWSNRNRYS------VAYAAQKPWL-- 748
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLL-AILaglddgssGEVSLVGQPLHQMDEEARAklrakhVGFVFQSFMLip 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 749 -LNATveENITFGSPFnkqryKAVTDACSLQPDIDLLpfgDQTEIGER----GINLSGGQRQRICVARALYQNTNIVFLD 823
Cdd:PRK10584 102 tLNAL--ENVELPALL-----RGESSRQSRNGAKALL---EQLGLGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 530398972 824 DPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSvLRE 880
Cdd:PRK10584 172 EPTGNLDRQTGDKIA-DLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQ-LQE 226
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1299-1515 |
2.48e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 56.71 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYenNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI-----FDGKIVIDGIDISKLPLHT-- 1371
Cdd:PRK14239 6 LQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNIYSPRTDTvd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1372 LRSRLSIILQDPILFSGSI--------RFNLDPECKCTDDRLWEALEIAQLKNMVKSlpggldaVVTEGGENFSVGQRQL 1443
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIyenvvyglRLKGIKDKQVLDEAVEKSLKGASIWDEVKD-------RLHDSALGLSGGQQQR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398972 1444 FCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTI-LTADLVIVMKRGNILEYD 1515
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYN 229
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
688-886 |
2.61e-08 |
|
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: 56.40 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV----------HWSNRNRYSVAYAAQKPWLL-NATVEEN 756
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqditklPMHKRARLGIGYLPQEASIFrKLTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 757 I-----TFGSPFNKQRYKAVtdacSLQPDIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD- 830
Cdd:cd03218 96 IlavleIRGLSKKEREEKLE----ELLEEFHITHLRKS-----KASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDp 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 831 IHLSDhlMQEgILKFLQdDKRTLVLVT----HKLQYLTHADWIIamKDGSVLREGTLKDI 886
Cdd:cd03218 167 IAVQD--IQK-IIKILK-DRGIGVLITdhnvRETLSITDRAYII--YEGKVLAEGTPEEI 220
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
688-881 |
3.07e-08 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 55.75 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNR-----NRYSVAYAAQKPWL-LNATVEEN-ITFG 760
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaARNRIGYLPEERGLyPKMKVIDQlVYLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 761 SPFNKQRYKAVTDACSLQPDIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQE 840
Cdd:cd03269 96 QLKGLKKEEARRRIDEWLERLELSEYANK-----RVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 530398972 841 giLKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREG 881
Cdd:cd03269 171 --IRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
683-859 |
3.19e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 58.22 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 683 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGKVHWSNRnRYSVAYAAQKPWLLNATVEENITFGSP 762
Cdd:TIGR00954 463 NGDVLIESLSFEVPSGNNLLICGPNGCGKSSLF-RILGELWPVYGGRLTKPA-KGKLFYVPQRPYMTLGTLRDQIIYPDS 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 763 FNKQRYKAVTDAcSLQPDIDLLpfgDQTEIGERGIN----------LSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 832
Cdd:TIGR00954 541 SEDMKRRGLSDK-DLEQILDNV---QLTHILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVD 616
|
170 180
....*....|....*....|....*..
gi 530398972 833 LSDHLMQegilkFLQDDKRTLVLVTHK 859
Cdd:TIGR00954 617 VEGYMYR-----LCREFGITLFSVSHR 638
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
683-892 |
3.27e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.02 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 683 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG--EMQTLEGKVHWSNR----------NRYSVAYAAQKPWLL- 749
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyPHGTYEGEIIFEGEelqasnirdtERAGIAIIHQELALVk 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 750 NATVEENITFGS---PFNKQRYKAVTDACS-----LQPDIDllpfgdqteIGERGINLSGGQRQRICVARALYQNTNIVF 821
Cdd:PRK13549 96 ELSVLENIFLGNeitPGGIMDYDAMYLRAQkllaqLKLDIN---------PATPVGNLGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398972 822 LDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLqylthaDWIIAMKDG-SVLREGtlKDIQTKDVE 892
Cdd:PRK13549 167 LDEPTASLTESETAVLLD--IIRDLKAHGIACIYISHKL------NEVKAISDTiCVIRDG--RHIGTRPAA 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1314-1518 |
3.53e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 57.72 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1314 PVLKHVKAYIKPGQKVGICGRTGSGKSSLS--LA-FFRMvDifDGKIVIDGIDISKL-PLHTLRSRLSIILQDPILFSG- 1388
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMkiLSgVYQP-D--SGEILLDGEPVRFRsPRDAQAAGIAIIHQELNLVPNl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1389 SIRFNL------------DpeckctddrlWEALeIAQLKNMVKSLpgGLD----AVVteggENFSVGQRQLFCLARAFVR 1452
Cdd:COG1129 95 SVAENIflgreprrggliD----------WRAM-RRRARELLARL--GLDidpdTPV----GDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398972 1453 KSSILIMDEATASIDMA-TENILQkvVMTAFADR--TVVTIAHRVHTILT-ADLVIVMKRG-NILEYDTPE 1518
Cdd:COG1129 158 DARVLILDEPTASLTEReVERLFR--IIRRLKAQgvAIIYISHRLDEVFEiADRVTVLRDGrLVGTGPVAE 226
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1326-1523 |
4.10e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 57.04 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1326 GQKVGICGRTGSGKSSLSLAFFRMV---DIFDGKIVIDGIDISKLP---LHTLRS-RLSIILQDPILfsgsirfNLDPEC 1398
Cdd:PRK09473 42 GETLGIVGESGSGKSQTAFALMGLLaanGRIGGSATFNGREILNLPekeLNKLRAeQISMIFQDPMT-------SLNPYM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1399 KCTDdrlwEALEIAQL-KNMVKSLP-----GGLDAV--------VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA 1464
Cdd:PRK09473 115 RVGE----QLMEVLMLhKGMSKAEAfeesvRMLDAVkmpearkrMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTT 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398972 1465 SID-------MATENILQKVVMTAfadrtVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLAQ 1523
Cdd:PRK09473 191 ALDvtvqaqiMTLLNELKREFNTA-----IIMITHDLGVVAgICDKVLVMYAGRTMEYGNARDVFYQ 252
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
688-886 |
4.18e-08 |
|
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: 56.99 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG---EMQTLEGKVHWSNRNrysvayaaqkpwLLNATVEEnitfgspFN 764
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGED------------LLKLSEKE-------LR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 765 KQRYKAV--------TdacSLQPdidLLPFGDQ-------------TEIGER--------GIN------------LSGGQ 803
Cdd:COG0444 82 KIRGREIqmifqdpmT---SLNP---VMTVGDQiaeplrihgglskAEARERaiellervGLPdperrldrypheLSGGM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 804 RQRICVARALYQNTNIVFLDDPFSALDIhlsdhLMQEGILKFLQDDKR----TLVLVTHKL---QYLthADWIIAMKDGS 876
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDV-----TIQAQILNLLKDLQRelglAILFITHDLgvvAEI--ADRVAVMYAGR 228
|
250
....*....|
gi 530398972 877 VLREGTLKDI 886
Cdd:COG0444 229 IVEEGPVEEL 238
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
683-877 |
4.35e-08 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 54.75 E-value: 4.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 683 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNR--NRYSVAYAAQKP------------WL 748
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvTRRSPRDAIRAGiayvpedrkregLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 749 LNATVEENITFGSPfnkqrykavtdacslqpdidllpfgdqteigerginLSGGQRQRICVARALYQNTNIVFLDDPFSA 828
Cdd:cd03215 91 LDLSVAENIALSSL------------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 530398972 829 LDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSV 877
Cdd:cd03215 135 VDVGAKAEIYR--LIRELADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
671-881 |
5.14e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 56.26 E-value: 5.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 671 AIKVTNGYfswgSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQT------------LEGKVHWSNRN--- 735
Cdd:PRK14271 24 AVNLTLGF----AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFL-RTLNRMNDkvsgyrysgdvlLGGRSIFNYRDvle 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 736 -RYSVAYAAQKPWLLNATVEENITFGSPFNK----QRYKAVTDACSLQPDI-DLLpfgdQTEIGERGINLSGGQRQRICV 809
Cdd:PRK14271 99 fRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKlvprKEFRGVAQARLTEVGLwDAV----KDRLSDSPFRLSGGQQQLLCL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398972 810 ARALYQNTNIVFLDDPFSALDIHLSdhlmqEGILKFLQD--DKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREG 881
Cdd:PRK14271 175 ARTLAVNPEVLLLDEPTSALDPTTT-----EKIEEFIRSlaDRLTVIIVTHNLaQAARISDRAALFFDGRLVEEG 244
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1303-1515 |
5.25e-08 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 54.99 E-value: 5.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1303 DLCVRYENNLKPVlkHVK-AYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIDG---IDISK---LPLHt 1371
Cdd:cd03297 1 MLCVDIEKRLPDF--TLKiDFDLNEEVTGIFGASGAGKSTL----LRCIagleKPDGGTIVLNGtvlFDSRKkinLPPQ- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1372 lRSRLSIILQDPILFSG-SIRFNLD---PECKCTDDRLW--EALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 1445
Cdd:cd03297 74 -QRKIGLVFQQYALFPHlNVRENLAfglKRKRNREDRISvdELLDLLGLDHLLNRYPAQL-----------SGGEKQRVA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398972 1446 LARAFVRKSSILIMDEATASIDMATENILQKVV--MTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYD 1515
Cdd:cd03297 142 LARALAAQPELLLLDEPFSALDRALRLQLLPELkqIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
684-909 |
5.38e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 57.50 E-value: 5.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG--EMQTLEGKVhwsnrnRYSVAYAAQKPWLL------------ 749
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRI------IYHVALCEKCGYVErpskvgepcpvc 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 750 -NATVEENITFGSPFNKQRY---------------------------KAVTDA-----CSLQPDIDLLpfgDQTEIGER- 795
Cdd:TIGR03269 86 gGTLEPEEVDFWNLSDKLRRrirkriaimlqrtfalygddtvldnvlEALEEIgyegkEAVGRAVDLI---EMVQLSHRi 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 796 ---GINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDhLMQEGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIA 871
Cdd:TIGR03269 163 thiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAK-LVHNALEEAVKASGISMVLTSHWPEVIEDlSDKAIW 241
|
250 260 270
....*....|....*....|....*....|....*...
gi 530398972 872 MKDGSVLREGTLKDIQTKDVELYEhwktlMNRQDQELE 909
Cdd:TIGR03269 242 LENGEIKEEGTPDEVVAVFMEGVS-----EVEKECEVE 274
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1299-1522 |
5.81e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 57.12 E-value: 5.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVDIFD---GKIV----------------- 1358
Cdd:TIGR03269 1 IEVKNLTKKFDG--KEVLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMDQYEptsGRIIyhvalcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1359 ----------------IDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFnLDPECKCTDDRLWEALE----IAQLKNMV 1418
Cdd:TIGR03269 78 vgepcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTV-LDNVLEALEEIGYEGKEavgrAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1419 KslpggLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHT 1496
Cdd:TIGR03269 157 Q-----LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEV 231
|
250 260
....*....|....*....|....*..
gi 530398972 1497 IL-TADLVIVMKRGNILEYDTPESLLA 1522
Cdd:TIGR03269 232 IEdLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1315-1518 |
6.44e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 56.63 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1315 VLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLplHTLRSRLSIILQDPILF---- 1386
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTL----LRIIAGLEhqtsGHIRFHGTDVSRL--HARDRKVGFVFQHYALFrhmt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1387 -SGSIRFNLD-------PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILI 1458
Cdd:PRK10851 91 vFDNIAFGLTvlprrerPNAAAIKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398972 1459 MDEATASIDMATENILQKVVMTAFADR--TVVTIAH-RVHTILTADLVIVMKRGNILEYDTPE 1518
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
688-861 |
7.41e-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: 55.03 E-value: 7.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH------WSNRNRY----SVAYAaQKPWL--------- 748
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvaglvpWKRRKKFlrriGVVFG-QKTQLwwdlpvids 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 749 --LNATVeenitFGSPfnKQRYKAVTDACSlqpdiDLLPFGDQTEIGERgiNLSGGQRQRICVARALYQNTNIVFLDDPF 826
Cdd:cd03267 116 fyLLAAI-----YDLP--PARFKKRLDELS-----ELLDLEELLDTPVR--QLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 530398972 827 SALDIHlsdhlMQEGILKFLQDDKR----TLVLVTHKLQ 861
Cdd:cd03267 182 IGLDVV-----AQENIRNFLKEYNRergtTVLLTSHYMK 215
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
697-858 |
7.64e-08 |
|
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: 53.15 E-value: 7.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 697 TGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnrnrysvayaaqkpwllnatveenitfgspfnkqrykaVTDACS 776
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV-----------------------------------------IYIDGE 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 777 LQPDIDLLpFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEG----ILKFLQDDKRT 852
Cdd:smart00382 40 DILEEVLD-QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrlLLLLKSEKNLT 118
|
....*.
gi 530398972 853 LVLVTH 858
Cdd:smart00382 119 VILTTN 124
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1306-1506 |
7.70e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 54.72 E-value: 7.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1306 VRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPIL 1385
Cdd:PRK10247 13 VGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1386 FSGSIRFNLD-PeckctddrlWEALEIA-QLKNMVKSLP--GGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDE 1461
Cdd:PRK10247 93 FGDTVYDNLIfP---------WQIRNQQpDPAIFLDDLErfALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 530398972 1462 ATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILTADLVIVM 1506
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVITL 210
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1299-1524 |
8.28e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.03 E-value: 8.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLS--LAFFRMVDIFDGKIVIDGIDISKLPlHTLRSRL 1376
Cdd:CHL00131 8 LEIKNLHASVNEN--EILKGLNLSINKGEIHAIMGPNGSGKSTLSkvIAGHPAYKILEGDILFKGESILDLE-PEERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1377 SIIL--QDPILFSGS-----IRFNLDPECKCTDDRLWEALE----IAQLKNMVKSLPGGLDAVVTEGgenFSVGQRQLFC 1445
Cdd:CHL00131 85 GIFLafQYPIEIPGVsnadfLRLAYNSKRKFQGLPELDPLEfleiINEKLKLVGMDPSFLSRNVNEG---FSGGEKKRNE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1446 LARAFVRKSSILIMDEATASIDM-ATENILQKVVMTAFADRTVVTIAH--RVHTILTADLVIVMKRGNILEydTPESLLA 1522
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDIdALKIIAEGINKLMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIK--TGDAELA 239
|
..
gi 530398972 1523 QE 1524
Cdd:CHL00131 240 KE 241
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
1055-1269 |
9.81e-08 |
|
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: 55.26 E-value: 9.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1055 LHHNLLNKiilgPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGM---ISYA-TPVFLVALLPLG 1130
Cdd:cd18557 75 LFSSLLRQ----EIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIIlfiLSWKlTLVLLLVIPLLL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1131 VAFYFIQKYFRVASKDLQE-LDDSTQlpllcHFSETAEGLTTIRAF----RHETRFKQRMLELTDTNN---IAYLFLSAA 1202
Cdd:cd18557 151 IASKIYGRYIRKLSKEVQDaLAKAGQ-----VAEESLSNIRTVRSFsaeeKEIRRYSEALDRSYRLARkkaLANALFQGI 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398972 1203 NRWLEvrtdYLGACIVLtasiasisgSSNSGLVGLG----------LLYALTITNYLNWVVRNLADLEVQMGAVKKV 1269
Cdd:cd18557 226 TSLLI----YLSLLLVL---------WYGGYLVLSGqltvgeltsfILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
688-872 |
1.21e-07 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 54.19 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLllailgEMQTL--EGkvhwsnRNRY--SV-AYAAQ------KPWLLNAT---- 752
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSL------AFDTIyaEG------QRRYveSLsAYARQflgqmdKPDVDSIEglsp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 753 ---VEENITFGSPfnKQRYKAVTDACS----------LQPDIDLLpfgdqTEIG------ERGIN-LSGGQRQRICVARA 812
Cdd:cd03270 79 aiaIDQKTTSRNP--RSTVGTVTEIYDylrllfarvgIRERLGFL-----VDVGlgyltlSRSAPtLSGGEAQRIRLATQ 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398972 813 LYQN-TNIVF-LDDPFSALdiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAM 872
Cdd:cd03270 152 IGSGlTGVLYvLDEPSIGL--HPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDI 211
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
639-858 |
1.36e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 55.22 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 639 PKTINRKQPGRYHLDSYEQSTRRlrPAETEDIAIKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI 718
Cdd:PRK13536 11 PRRLELSPIERKHQGISEAKASI--PGSMSTVAIDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 719 LGEMQTLEGK-----VHWSNRNRYSVAYAAQKPWLLNA----TVEEN-ITFGSPF--NKQRYKAVTDAcslqpdidLLPF 786
Cdd:PRK13536 88 LGMTSPDAGKitvlgVPVPARARLARARIGVVPQFDNLdlefTVRENlLVFGRYFgmSTREIEAVIPS--------LLEF 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398972 787 GD-QTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDDKrTLVLVTH 858
Cdd:PRK13536 160 ARlESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-ARHLIWERLRSLLARGK-TILLTTH 230
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
367-605 |
1.40e-07 |
|
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: 54.86 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 367 TFLQASYYVTIETGI--NLRGALlamiYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFLF-LCPNLWAMPVQIIM 443
Cdd:cd07346 56 SYLRRYLAARLGQRVvfDLRRDL----FRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSsGLLQLLSDVLTLIG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 444 GVILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWE----HIFCKSVE 519
Cdd:cd07346 130 ALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEereiERFREANR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 520 ETRMKELSSLKTFALYTSLSIFMNAAIPIAAVL--ATFVthayaSGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVK 597
Cdd:cd07346 210 DLRDANLRAARLSALFSPLIGLLTALGTALVLLygGYLV-----LQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQ 284
|
....*...
gi 530398972 598 AIISVQKL 605
Cdd:cd07346 285 ALASLERI 292
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1301-1492 |
1.74e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 55.84 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1301 IHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVID-GIDISKLPlhtlrsr 1375
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTL----LKILagelEPDSGEVSIPkGLRIGYLP------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1376 lsiilQDPILFSG-SIRFNL----------------------DPECKCTD-DRLWEALEIA---QLKNMVKSLPGGL--- 1425
Cdd:COG0488 68 -----QEPPLDDDlTVLDTVldgdaelraleaeleeleaklaEPDEDLERlAELQEEFEALggwEAEARAEEILSGLgfp 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1426 ----DAVVTEggenFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT----ENILQK----VVMT----AFADRTVVT 1489
Cdd:COG0488 143 eedlDRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFLKNypgtVLVVshdrYFLDRVATR 218
|
...
gi 530398972 1490 IAH 1492
Cdd:COG0488 219 ILE 221
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
703-860 |
1.81e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 54.74 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 703 IVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRNRYSVAYAAQKPwlLNATVEenITFGSPFNkqrykavtdacSLQP--- 779
Cdd:COG4608 49 LVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRP--LRRRMQ--MVFQDPYA-----------SLNPrmt 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 780 --DIDLLPF-----GDQTEIGER--------GIN----------LSGGQRQRICVARALYQNTNIVFLDDPFSALDihLS 834
Cdd:COG4608 114 vgDIIAEPLrihglASKAERRERvaellelvGLRpehadrypheFSGGQRQRIGIARALALNPKLIVCDEPVSALD--VS 191
|
170 180 190
....*....|....*....|....*....|
gi 530398972 835 dhlMQEGILKFLQDDKR----TLVLVTHKL 860
Cdd:COG4608 192 ---IQAQVLNLLEDLQDelglTYLFISHDL 218
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
666-890 |
2.14e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 54.04 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 666 ETEDIAikvtngyFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV-----HWSNRN----R 736
Cdd:PRK13652 5 ETRDLC-------YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVlirgePITKENirevR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 737 YSVAYAAQKP--WLLNATVEENITFGsPFN--------KQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQR 806
Cdd:PRK13652 78 KFVGLVFQNPddQIFSPTVEQDIAFG-PINlgldeetvAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 807 ICVARALYQNTNIVFLDDPFSALDIHLSDHLmqegiLKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAMKDGSVLREG 881
Cdd:PRK13652 146 VAIAGVIAMEPQVLVLDEPTAGLDPQGVKEL-----IDFLNDLPEtygmTVIFSTHQLDLVPEmADYIYVMDKGRIVAYG 220
|
....*....
gi 530398972 882 TLKDIQTKD 890
Cdd:PRK13652 221 TVEEIFLQP 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1301-1520 |
2.17e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.63 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1301 IHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKI-------------VIDGIDIS 1365
Cdd:PRK10261 15 VENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1366 KLPLHTLR-SRLSIILQDPIL-----------FSGSIRFNLD---PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvt 1430
Cdd:PRK10261 95 AAQMRHVRgADMAMIFQEPMTslnpvftvgeqIAESIRLHQGasrEEAMVEAKRMLDQVRIPEAQTILSRYPHQL----- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1431 eggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE-NILQKV-VMTAFADRTVVTIAHRVHTIL-TADLVIVMK 1507
Cdd:PRK10261 170 ------SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQaQILQLIkVLQKEMSMGVIFITHDMGVVAeIADRVLVMY 243
|
250
....*....|...
gi 530398972 1508 RGNILEYDTPESL 1520
Cdd:PRK10261 244 QGEAVETGSVEQI 256
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
672-882 |
2.23e-07 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 53.53 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 672 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN--------RYSVAYAA 743
Cdd:cd03265 1 IEVENLVKKYGDFEA-VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDvvreprevRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 744 QKPWLLNA-TVEENI-TFGSPFNKQRYKAVTDACSLQPDIDLLPFGDqteigERGINLSGGQRQRICVARALYQNTNIVF 821
Cdd:cd03265 80 QDLSVDDElTGWENLyIHARLYGVPGAERRERIDELLDFVGLLEAAD-----RLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398972 822 LDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHklqYLTHA----DWIIAMKDGSVLREGT 882
Cdd:cd03265 155 LDEPTIGLDPQTRAHVW-EYIEKLKEEFGMTILLTTH---YMEEAeqlcDRVAIIDHGRIIAEGT 215
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
684-875 |
2.34e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 53.34 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN------------RYSVAYAAQKPWLL-N 750
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrlknrevpflRRQIGMIFQDHHLLmD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 751 ATVEENITF-----GSPFN--KQRYKAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARALYQNTNIVFLD 823
Cdd:PRK10908 94 RTVYDNVAIpliiaGASGDdiRRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNKPAVLLAD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 530398972 824 DPFSALDIHLSdhlmqEGILKFLQDDKR---TLVLVTHKLQYLTHADW-IIAMKDG 875
Cdd:PRK10908 163 EPTGNLDDALS-----EGILRLFEEFNRvgvTVLMATHDIGLISRRSYrMLTLSDG 213
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1316-1499 |
2.41e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 53.34 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1316 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL---PLHTLRSRLSIILQD---------- 1382
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrEVPFLRRQIGMIFQDhhllmdrtvy 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1383 -----PILFSGSirfnldpeckCTDD---RLWEALEIAQLKNMVKSLPggldaVVTEGGENFSVGqrqlfcLARAFVRKS 1454
Cdd:PRK10908 98 dnvaiPLIIAGA----------SGDDirrRVSAALDKVGLLDKAKNFP-----IQLSGGEQQRVG------IARAVVNKP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 530398972 1455 SILIMDEATASIDMA-TENILQ------KVVMTAF-ADRTVVTIAHRVHTILT 1499
Cdd:PRK10908 157 AVLLADEPTGNLDDAlSEGILRlfeefnRVGVTVLmATHDIGLISRRSYRMLT 209
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
1021-1269 |
2.85e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 54.09 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1021 YYVAGFSILCG------AGIFLcLVTSLTVEWMGLTaaknLHHNLLNKiilgPIRFFDTTPLGLILNRFSADTNIIDQHI 1094
Cdd:cd18572 40 LLLLLLSVLSGlfsglrGGCFS-YAGTRLVRRLRRD----LFRSLLRQ----DIAFFDATKTGELTSRLTSDCQKVSDPL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1095 PPTLESLTRSTLLCLSAIGMISYATP----VFLVALLPLGVAFYFIQKYFRVASKDLQElddstqlpLLCHFSETAE--- 1167
Cdd:cd18572 111 STNLNVFLRNLVQLVGGLAFMFSLSWrltlLAFITVPVIALITKVYGRYYRKLSKEIQD--------ALAEANQVAEeal 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1168 -GLTTIRAFRHET----RFKQRMLELTDTN---NIAYLFLSAANRWLevrtDYLGACIVLtasiasisgssnsgLVGLGL 1239
Cdd:cd18572 183 sNIRTVRSFATEErearRYERALDKALKLSvrqALAYAGYVAVNTLL----QNGTQVLVL--------------FYGGHL 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 530398972 1240 ---------------LYALTITNYLNWVVRNLADLEVQMGAVKKV 1269
Cdd:cd18572 245 vlsgrmsagqlvtfmLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1299-1383 |
2.94e-07 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 55.08 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRY--ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVD----IFDGKIVIDGIDISKLPLHTL 1372
Cdd:COG4172 7 LSVEDLSVAFgqGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPdpaaHPSGSILFDGQDLLGLSEREL 86
|
90
....*....|....*
gi 530398972 1373 R----SRLSIILQDP 1383
Cdd:COG4172 87 RrirgNRIAMIFQEP 101
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
683-830 |
3.43e-07 |
|
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: 52.26 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 683 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI---LGEMQTLEGKVHWSN--------RNRYSVAYAAQK----PW 747
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGipykefaeKYPGEIIYVSEEdvhfPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 748 LlnaTVEENITFgspfnkqrykavtdACSLQpdidllpfGDQTEigeRGInlSGGQRQRICVARALYQNTNIVFLDDPFS 827
Cdd:cd03233 98 L---TVRETLDF--------------ALRCK--------GNEFV---RGI--SGGERKRVSIAEALVSRASVLCWDNSTR 147
|
...
gi 530398972 828 ALD 830
Cdd:cd03233 148 GLD 150
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
688-882 |
4.41e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.57 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV--------HWSNRN--RYSVAYAAQKPWLLN-ATVEEN 756
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIvfdgkditDWQTAKimREAVAIVPEGRRVFSrMTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 757 ITFGSPF-NKQRYKAvtdacSLQPDIDLLPFGDQTEIgERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD----I 831
Cdd:PRK11614 101 LAMGGFFaERDQFQE-----RIKWVYELFPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLApiiiQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 530398972 832 HLSDHLMQegilkfLQDDKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREGT 882
Cdd:PRK11614 175 QIFDTIEQ------LREQGMTIFLVEQNAnQALKLADRGYVLENGHVVLEDT 220
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
688-886 |
4.45e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 53.65 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI-LGEMQTlEGKVHWSNRN------------RYSVAYAAQKPWLLNA-TV 753
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCInLLERPT-SGRVLVDGQDltalsekelrkaRRQIGMIFQHFNLLSSrTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 754 EENITF-----GSPfNKQRYKAVTDacslqpdidLLPFGDQTEIGER-GINLSGGQRQRICVARALYQNTNIVFLDDPFS 827
Cdd:PRK11153 100 FDNVALplelaGTP-KAEIKARVTE---------LLELVGLSDKADRyPAQLSGGQKQRVAIARALASNPKVLLCDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398972 828 ALDIHLSDhlmqeGILKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 886
Cdd:PRK11153 170 ALDPATTR-----SILELLKDINRelglTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGTVSEV 228
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1315-1522 |
5.49e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 52.44 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1315 VLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVD---IFDGKIVIDG---IDISKLPLHTLRSRLSIILQDpilf 1386
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLlrCINLLEQPEagtIRVGDITIDTarsLSQQKGLIRQLRQHVGFVFQN---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1387 sgsirFNLDPEckctddrlWEALE-IAQLKNMVKSLPGG---------LDAVVTEGGEN-----FSVGQRQLFCLARAFV 1451
Cdd:PRK11264 94 -----FNLFPH--------RTVLEnIIEGPVIVKGEPKEeatararelLAKVGLAGKETsyprrLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398972 1452 RKSSILIMDEATASID--MATEnILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLA 1522
Cdd:PRK11264 161 MRPEVILFDEPTSALDpeLVGE-VLNTIRQLAQEKRTMVIVTHEMSFARdVADRAIFMDQGRIVEQGPAKALFA 233
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1313-1522 |
6.68e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 52.79 E-value: 6.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1313 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI-----FDGKIVIDGIDI-SKLPLHTLRSRLSIILQDPILF 1386
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1387 SGSIRFNLDPECKCtdDRLWEALEIAQLKNMVKSLPGGLDAV---VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEAT 1463
Cdd:PRK14271 114 PMSIMDNVLAGVRA--HKLVPRKEFRGVAQARLTEVGLWDAVkdrLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398972 1464 ASIDMATENILQKVVMTaFADR-TVVTIAHRV-HTILTADLVIVMKRGNILEYDTPESLLA 1522
Cdd:PRK14271 192 SALDPTTTEKIEEFIRS-LADRlTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
690-886 |
7.90e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 52.82 E-value: 7.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 690 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGeMQTLEGKV-----HWSNRNRYSVAyAAQKPWLLNATVEenITFGSPFN 764
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSVSSLAIMG-LIDYPGRVmaeklEFNGQDLQRIS-EKERRNLVGAEVA--MIFQDPMT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 765 K---------QRYKAV------TDACSLQPDIDLLpfgdqTEIG----ERGIN-----LSGGQRQRICVARALYQNTNIV 820
Cdd:PRK11022 101 SlnpcytvgfQIMEAIkvhqggNKKTRRQRAIDLL-----NQVGipdpASRLDvyphqLSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398972 821 FLDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 886
Cdd:PRK11022 176 IADEPTTALDVTIQAQII-ELLLELQQKENMALVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDI 241
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
688-881 |
7.95e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 52.32 E-value: 7.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHW-------SNRN----RYSVAYAAQKP--WLLNATVE 754
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWqgkpldySKRGllalRQQVATVFQDPeqQIFYTDID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 755 ENITFgspfnKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 833
Cdd:PRK13638 97 SDIAF-----SLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 530398972 834 SDHLMqeGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREG 881
Cdd:PRK13638 172 RTQMI--AIIRRIVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHG 218
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
688-882 |
8.50e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 52.23 E-value: 8.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAIL----------GEMQTLEGKVHWSNRNRYSVAYAAQKPwlLNATVEEN- 756
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLypalarrlhlKKEQPGNHDRIEGLEHIDKVIVIDQSP--IGRTPRSNp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 757 ITF----------------GSPFNKQ----RYKAVTDACSLQPDID------------------LLPFG-DQTEIGERGI 797
Cdd:cd03271 89 ATYtgvfdeirelfcevckGKRYNREtlevRYKGKSIADVLDMTVEealeffenipkiarklqtLCDVGlGYIKLGQPAT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 798 NLSGGQRQRICVARALYQNTN---IVFLDDPFSALdiHLSD--HLMQegILKFLQDDKRTLVLVTHKLQYLTHADWIIAM 872
Cdd:cd03271 169 TLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGL--HFHDvkKLLE--VLQRLVDKGNTVVVIEHNLDVIKCADWIIDL 244
|
250
....*....|....*.
gi 530398972 873 ------KDGSVLREGT 882
Cdd:cd03271 245 gpeggdGGGQVVASGT 260
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
676-858 |
8.95e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 51.09 E-value: 8.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 676 NGYFSW----------GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLL--LAILGEMQTLEGKVHWSNRN-----RYS 738
Cdd:cd03232 1 GSVLTWknlnytvpvkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLdvLAGRKTAGVITGEILINGRPldknfQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 739 VAYAAQKPWLL-NATVEENITFgspfnkqrykavtDACSlqpdidllpfgdqteigeRGINLSggQRQRICVARALYQNT 817
Cdd:cd03232 81 TGYVEQQDVHSpNLTVREALRF-------------SALL------------------RGLSVE--QRKRLTIGVELAAKP 127
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 530398972 818 NIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTH 858
Cdd:cd03232 128 SILFLDEPTSGLDSQAAYNIVR--FLKKLADSGQAILCTIH 166
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
673-934 |
1.25e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.25 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 673 KVTNGYfswGSGLaTLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRNRysVAYAAQKPW-LLNA 751
Cdd:PRK10636 317 KVSAGY---GDRI-ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIK--LGYFAQHQLeFLRA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 752 tvEEnitfgSPFnkQRYKAVTDACSLQPDIDLL-PFGDQ----TEIGERginLSGGQRQRICVARALYQNTNIVFLDDPF 826
Cdd:PRK10636 391 --DE-----SPL--QHLARLAPQELEQKLRDYLgGFGFQgdkvTEETRR---FSGGEKARLVLALIVWQRPNLLLLDEPT 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 827 SALDIHLSDHLMQ-----EGILKFLQDDKRTLVLVTHKLqYLTHadwiiamkDGSVlregtlkDIQTKDVELYEHWktLM 901
Cdd:PRK10636 459 NHLDLDMRQALTEalidfEGALVVVSHDRHLLRSTTDDL-YLVH--------DGKV-------EPFDGDLEDYQQW--LS 520
|
250 260 270
....*....|....*....|....*....|...
gi 530398972 902 NRQDQELEKDMEADQTTLERKTLRRAMYSREAK 934
Cdd:PRK10636 521 DVQKQENQTDEAPKENNANSAQARKDQKRREAE 553
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1299-1514 |
1.40e-06 |
|
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: 50.74 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV-DIF---DGKIVIDGIDISKLPLHT--- 1371
Cdd:cd03269 1 LEVENVTKRFGR--VTALDDISFSVEKGEIFGLLGPNGAGKTTT----IRMIlGIIlpdSGEVLFDGKPLDIAARNRigy 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1372 ------LRSRLSIilQDPILFSGSIRfNLDP-ECKCTDDRLWEALEIAQLKNmvKSLpggldavvteggENFSVGQRQLF 1444
Cdd:cd03269 75 lpeergLYPKMKV--IDQLVYLAQLK-GLKKeEARRRIDEWLERLELSEYAN--KRV------------EELSKGNQQKV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398972 1445 CLARAFVRKSSILIMDEATASIDMATENILQKVVMT-AFADRTVVTIAHRVHTI-LTADLVIVMKRGNILEY 1514
Cdd:cd03269 138 QFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLY 209
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
660-886 |
1.69e-06 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 52.50 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 660 RRLRPAETEDIAIKVTN---GYFSWGSGLA-TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH----- 730
Cdd:TIGR03269 268 EKECEVEVGEPIIKVRNvskRYISVDRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgd 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 731 -W--------SNRNRYS--VAYAAQKPWLL-NATVEENIT----FGSPFNKQRYKAVtdacslqpdIDLLPFGDQTEIGE 794
Cdd:TIGR03269 348 eWvdmtkpgpDGRGRAKryIGILHQEYDLYpHRTVLDNLTeaigLELPDELARMKAV---------ITLKMVGFDEEKAE 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 795 RGIN-----LSGGQRQRICVARALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQY-LTHADW 868
Cdd:TIGR03269 419 EILDkypdeLSEGERHRVALAQVLIKEPRIVILDEPTGTMD-PITKVDVTHSILKAREEMEQTFIIVSHDMDFvLDVCDR 497
|
250
....*....|....*...
gi 530398972 869 IIAMKDGSVLREGTLKDI 886
Cdd:TIGR03269 498 AALMRDGKIVKIGDPEEI 515
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
800-881 |
1.76e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.40 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 800 SGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKR-TLVLVTHKLQY---LTHAdwIIAMKDG 875
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILA--LLKSLQQKHQlAYLFISHDLHVvraLCHQ--VIVLRQG 502
|
....*.
gi 530398972 876 SVLREG 881
Cdd:PRK15134 503 EVVEQG 508
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
647-831 |
1.85e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.55 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 647 PGRYHLDSYEQSTRRLRPAETEDIA-----IKVTN--GYFSWGSGL--------ATLSNIDIRIPTGQLTMIVGQVGCGK 711
Cdd:PRK10261 284 PRRFPLISLEHPAKQEPPIEQDTVVdgepiLQVRNlvTRFPLRSGLlnrvtrevHAVEKVSFDLWPGETLSLVGESGSGK 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 712 SSLLLAILGEMQTLEGKVHWSNRN------------RYSVAYAAQKPWllnATVEENITFG-SPFNKQRYKAVTDACSLQ 778
Cdd:PRK10261 364 STTGRALLRLVESQGGEIIFNGQRidtlspgklqalRRDIQFIFQDPY---ASLDPRQTVGdSIMEPLRVHGLLPGKAAA 440
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 530398972 779 PDIDLL--PFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDI 831
Cdd:PRK10261 441 ARVAWLleRVGLLPEHAWRYPHeFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1313-1532 |
1.92e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 51.87 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1313 KPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDifDGKIVIDGIDISKLP-----LHTlrsrlsiILQDPIL 1385
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVlrLIAGFETPD--SGRIMLDGQDITHVPaenrhVNT-------VFQSYAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1386 FSG-SIRFNLDPECKC-------TDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSIL 1457
Cdd:PRK09452 98 FPHmTVFENVAFGLRMqktpaaeITPRVMEALRMVQLEEFAQRKPHQL-----------SGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1458 IMDEATASID------MATE-NILQKVVMTAFadrtvVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQENGVF- 1528
Cdd:PRK09452 167 LLDESLSALDyklrkqMQNElKALQRKLGITF-----VFVTHDQEEALTmSDRIVVMRDGRIEQDGTPREIYEEPKNLFv 241
|
....
gi 530398972 1529 ASFV 1532
Cdd:PRK09452 242 ARFI 245
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
703-869 |
2.15e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.43 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 703 IVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRnrYSVAYAAQKPWL-LNATVEENIT--FGSPFNKQ-RYKAVTDACS-- 776
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPAPG--IKVGYLPQEPQLdPEKTVRENVEegVAEVKAALdRFNEIYAAYAep 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 777 -------------LQPDIDL------------------LPFGDqTEIGergiNLSGGQRQRICVARALYQNTNIVFLDDP 825
Cdd:PRK11819 116 dadfdalaaeqgeLQEIIDAadawdldsqleiamdalrCPPWD-AKVT----KLSGGERRRVALCRLLLEKPDMLLLDEP 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 530398972 826 fsaldihlSDHLMQEGIL---KFLQDDKRTLVLVTHKLQYLTH-ADWI 869
Cdd:PRK11819 191 --------TNHLDAESVAwleQFLHDYPGTVVAVTHDRYFLDNvAGWI 230
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1306-1515 |
2.24e-06 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 50.41 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1306 VRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslaffrmVDIFDGKIVIDGIDISKLPL------HTLRSRLSII 1379
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTT-------LKILSGLLQPTSGEVRVAGLvpwkrrKKFLRRIGVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1380 L------------QDPILFSGSIrFNLDP-ECKCTDDRLWEALEIAQLknmvkslpggLDAVVteggENFSVGQRQLFCL 1446
Cdd:cd03267 100 FgqktqlwwdlpvIDSFYLLAAI-YDLPPaRFKKRLDELSELLDLEEL----------LDTPV----RQLSLGQRMRAEI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398972 1447 ARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILT-ADLVIVMKRGNILeYD 1515
Cdd:cd03267 165 AAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLL-YD 235
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1325-1523 |
2.30e-06 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 51.64 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1325 PGQKV-GICGRTGSGKSSLslafFRMV------DifDGKIVIDG---IDISK---LPLHtlRSRLSIILQDPILFSG-SI 1390
Cdd:COG4148 23 PGRGVtALFGPSGSGKTTL----LRAIaglerpD--SGRIRLGGevlQDSARgifLPPH--RRRIGYVFQEARLFPHlSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1391 RFNLD--------PECKCTDDRLWEALEIAQLknmVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEA 1462
Cdd:COG4148 95 RGNLLygrkraprAERRISFDEVVELLGIGHL---LDRRPATL-----------SGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398972 1463 TASIDMATEN----ILQKVvmtafADRT---VVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQ 1523
Cdd:COG4148 161 LAALDLARKAeilpYLERL-----RDELdipILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
798-881 |
2.62e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.95 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 798 NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQ-YLTHADWIiamkdgS 876
Cdd:COG3845 141 DLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFE--ILRRLAAEGKSIIFITHKLReVMAIADRV------T 212
|
....*
gi 530398972 877 VLREG 881
Cdd:COG3845 213 VLRRG 217
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
688-935 |
2.84e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.42 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ----TLEGKVHWS--------NRNRYSVAYAAQK----PWLlna 751
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDgitpeeikKHYRGDVVYNAETdvhfPHL--- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 752 TVEENITFG----SPFNkqRYKAVT--DACSLQPDIDLLPFG----DQTEIGE---RGInlSGGQRQRICVARALYQNTN 818
Cdd:TIGR00956 154 TVGETLDFAarckTPQN--RPDGVSreEYAKHIADVYMATYGlshtRNTKVGNdfvRGV--SGGERKRVSIAEASLGGAK 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 819 IVFLDDPFSALD--------------IHLSDHLMQEGILKFLQD-----DKRTLV---------LVTHKLQYL------- 863
Cdd:TIGR00956 230 IQCWDNATRGLDsatalefiralktsANILDTTPLVAIYQCSQDayelfDKVIVLyegyqiyfgPADKAKQYFekmgfkc 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 864 ----THADWIIAMKDGS--VLREGTLKDIQTKDVELYEHWKTLMNRqdQELEKDMEA----DQTTLERKTLRRAMYSREA 933
Cdd:TIGR00956 310 pdrqTTADFLTSLTSPAerQIKPGYEKKVPRTPQEFETYWRNSPEY--AQLMKEIDEyldrCSESDTKEAYRESHVAKQS 387
|
..
gi 530398972 934 KA 935
Cdd:TIGR00956 388 KR 389
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
688-858 |
3.75e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 51.59 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI----LGEMQ-----TLEGKVHWSNRNRYSVAYAAQKPWLLNA-TVEENI 757
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrsPKGVKgsgsvLLNGMPIDAKEMRAISAYVQQDDLFIPTlTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 758 TFGSPF----------NKQRYKAVTDACSLQPDIDllpfgdqTEIGERGI--NLSGGQRQRICVARALYQNTNIVFLDDP 825
Cdd:TIGR00955 121 MFQAHLrmprrvtkkeKRERVDEVLQALGLRKCAN-------TRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190
....*....|....*....|....*....|...
gi 530398972 826 FSALDIHLSDHLMQegILKFLQDDKRTLVLVTH 858
Cdd:TIGR00955 194 TSGLDSFMAYSVVQ--VLKGLAQKGKTIICTIH 224
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
694-869 |
5.36e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 49.67 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 694 RIPT---GQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV----HWSNRNRYSVAYAAQKpwLLNATVEENItfgSPFNKQ 766
Cdd:cd03236 19 RLPVpreGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppDWDEILDEFRGSELQN--YFTKLLEGDV---KVIVKP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 767 RY-----KAVTDACslqpdIDLLPFGDQTE-------------IGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFS 827
Cdd:cd03236 94 QYvdlipKAVKGKV-----GELLKKKDERGkldelvdqlelrhVLDRNIdQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 530398972 828 ALDIHlsDHLMQEGILKFLQDDKRTLVLVTHKLQYLTH-ADWI 869
Cdd:cd03236 169 YLDIK--QRLNAARLIRELAEDDNYVLVVEHDLAVLDYlSDYI 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
799-886 |
5.75e-06 |
|
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: 50.84 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 799 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKRT----LVLVTHKLQYLTH-ADWIIAMK 873
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTV-----QAQILDLLKDLQRElgmaLLLITHDLGVVRRfADRVAVMR 231
|
90
....*....|...
gi 530398972 874 DGSVLREGTLKDI 886
Cdd:COG4172 232 QGEIVEQGPTAEL 244
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1323-1478 |
6.58e-06 |
|
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: 50.59 E-value: 6.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1323 IKPGQKVGICGRTGSGKSSLS--LAFFRMVDIFDGKIVIDGIDISKLPLH-TLRSRLSIILQDPILFSG-SIRFN--LDP 1396
Cdd:TIGR02633 24 VRPGECVGLCGENGAGKSTLMkiLSGVYPHGTWDGEIYWSGSPLKASNIRdTERAGIVIIHQELTLVPElSVAENifLGN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1397 ECKCTDDRLWEALEIAQLKNMVKSLPggLDAV-VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQ 1475
Cdd:TIGR02633 104 EITLPGGRMAYNAMYLRAKNLLRELQ--LDADnVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILL 181
|
...
gi 530398972 1476 KVV 1478
Cdd:TIGR02633 182 DII 184
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1309-1517 |
6.78e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.00 E-value: 6.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1309 ENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLslaffrmVDIFDGKIV---IDG-IDISKLP-LHTLRSRLS------ 1377
Cdd:PLN03140 890 EDRLQ-LLREVTGAFRPGVLTALMGVSGAGKTTL-------MDVLAGRKTggyIEGdIRISGFPkKQETFARISgyceqn 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1378 ------IILQDPILFSGSIRfnLDPECKCTD-----DRLWEALEIAQLKNMVKSLPGgldavVTeggeNFSVGQRQLFCL 1446
Cdd:PLN03140 962 dihspqVTVRESLIYSAFLR--LPKEVSKEEkmmfvDEVMELVELDNLKDAIVGLPG-----VT----GLSTEQRKRLTI 1030
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398972 1447 ARAFVRKSSILIMDEATASIDMATENILQKVVM-TAFADRTVVTIAHRVHT-ILTA-DLVIVMKRGNILEYDTP 1517
Cdd:PLN03140 1031 AVELVANPSIIFMDEPTSGLDARAAAIVMRTVRnTVDTGRTVVCTIHQPSIdIFEAfDELLLMKRGGQVIYSGP 1104
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
688-881 |
7.78e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 48.80 E-value: 7.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMqtlegkvhwSNRNRYSVAYAAQKPWLLNATVEENITFGSPFNKQr 767
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL---------KGTPVAGCVDVPDNQFGREASLIDAIGRKGDFKDA- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 768 yKAVTDACSLQPDIDLL-PFGdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSdHLMQEGILKFL 846
Cdd:COG2401 116 -VELLNAVGLSDAVLWLrRFK----------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA-KRVARNLQKLA 183
|
170 180 190
....*....|....*....|....*....|....*
gi 530398972 847 QDDKRTLVLVTHklqyltHADWIIAMKDGSVLREG 881
Cdd:COG2401 184 RRAGITLVVATH------HYDVIDDLQPDLLIFVG 212
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
998-1209 |
9.93e-06 |
|
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: 49.02 E-value: 9.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 998 IDYWLATwtseysiNNTGKADQTyyvagFSILCGAGIFLCLVTSL---TVEWMGLTAAKNLHHNLLNKIILGPIRFFDTT 1074
Cdd:cd18575 23 IDQGFAA-------GNTALLNRA-----FLLLLAVALVLALASALrfyLVSWLGERVVADLRKAVFAHLLRLSPSFFETT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1075 PLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATP---VFLVALLPLGVA-FYFIQKYFRVASKDLQE- 1149
Cdd:cd18575 91 RTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPkltLLVLLVIPLVVLpIILFGRRVRRLSRASQDr 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1150 LDDSTQlpllcHFSETAEGLTTIRAFRHETRFKQRMLELTDTNniaylfLSAANRWLEVR 1209
Cdd:cd18575 171 LADLSA-----FAEETLSAIKTVQAFTREDAERQRFATAVEAA------FAAALRRIRAR 219
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
684-875 |
1.21e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRnrySVAYAAQKPWLLNA------------ 751
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK---EIDFKSSKEALENGismvhqelnlvl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 752 --TVEENITFG-----SPF--NKQRYKAvTDACSLQPDIDLLPfgdqteiGERGINLSGGQRQRICVARALYQNTNIVFL 822
Cdd:PRK10982 87 qrSVMDNMWLGryptkGMFvdQDKMYRD-TKAIFDELDIDIDP-------RAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 530398972 823 DDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDG 875
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFT--IIRKLKERGCGIVYISHKMEEIFQlCDEITILRDG 210
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
690-858 |
1.46e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 48.65 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 690 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN-----RNRYSVAYAAQKPWLLNA----TVEENI-TF 759
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpsRARHARQRVGVVPQFDNLdpdfTVRENLlVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 760 GspfnkqRYKAVTDACSLQPDIDLLPFGD-----QTEIGErginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlS 834
Cdd:PRK13537 105 G------RYFGLSAAAARALVPPLLEFAKlenkaDAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ-A 173
|
170 180
....*....|....*....|....
gi 530398972 835 DHLMQEGiLKFLQDDKRTLVLVTH 858
Cdd:PRK13537 174 RHLMWER-LRSLLARGKTILLTTH 196
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
688-885 |
1.47e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 49.88 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ--TLEGKVHWSNRNRYS-----VAYAAQKPWLL-NATVEENITF 759
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQgnNFTGTILANNRKPTKqilkrTGFVTQDDILYpHLTVRETLVF 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 760 GS----PFNKQRYKAVTDACSLQPDIDLLPFGDqTEIGE---RGInlSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 832
Cdd:PLN03211 164 CSllrlPKSLTKQEKILVAESVISELGLTKCEN-TIIGNsfiRGI--SGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 530398972 833 LSDHLMQegILKFLQDDKRTLVLVTHKLQYLTHA--DWIIAMKDGSVLREGTLKD 885
Cdd:PLN03211 241 AAYRLVL--TLGSLAQKGKTIVTSMHQPSSRVYQmfDSVLVLSEGRCLFFGKGSD 293
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
752-886 |
1.52e-05 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 48.10 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 752 TVEENI-----TFGSPFNKQRYKAVtdacSLQPDIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPF 826
Cdd:COG1137 94 TVEDNIlavleLRKLSKKEREERLE----ELLEEFGITHLRKS-----KAYSLSGGERRRVEIARALATNPKFILLDEPF 164
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398972 827 SALD-IHLSDhlMQEgILKFLQDdkRTL-VLVT-HK----LQ-----YLthadwiiaMKDGSVLREGTLKDI 886
Cdd:COG1137 165 AGVDpIAVAD--IQK-IIRHLKE--RGIgVLITdHNvretLGicdraYI--------ISEGKVLAEGTPEEI 223
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
680-881 |
1.62e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 48.38 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 680 SWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRNRYSVAYA----AQKPWLLN---AT 752
Cdd:PRK11701 15 LYGPRKG-CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYalseAERRRLLRtewGF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 753 VEEN--------ITFGSP------------FNKQRYKAVT--DACSLQPD-IDLLP--FgdqteigerginlSGGQRQRI 807
Cdd:PRK11701 94 VHQHprdglrmqVSAGGNigerlmavgarhYGDIRATAGDwlERVEIDAArIDDLPttF-------------SGGMQQRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 808 CVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLqddkRTLV--------LVTHKL---QYLTHAdwIIAMKDGS 876
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLDVSV-----QARLLDLL----RGLVrelglavvIVTHDLavaRLLAHR--LLVMKQGR 229
|
....*
gi 530398972 877 VLREG 881
Cdd:PRK11701 230 VVESG 234
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
685-886 |
2.04e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.08 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 685 LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH-----WSNRNRYSV------------------AY 741
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmlLRRRSRQVIelseqsaaqmrhvrgadmAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 742 AAQKPWL-LNA--TVEENITFGSPFNK--QRYKAVTDACSLqpdIDLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQ 815
Cdd:PRK10261 109 IFQEPMTsLNPvfTVGEQIAESIRLHQgaSREEAMVEAKRM---LDQVRIPEAQTILSRYPHqLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398972 816 NTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRT-LVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 886
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQ--LIKVLQKEMSMgVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQI 256
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
695-870 |
2.08e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.80 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 695 IPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWsnrNRYSVAYAAQKpwllnatveenitfgspfnkqrykavtda 774
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW---DGITPVYKPQY----------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 775 cslqpdidllpfgdqteigergINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQeGILKFLQDDKRTLV 854
Cdd:cd03222 70 ----------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAAR-AIRRLSEEGKKTAL 126
|
170
....*....|....*..
gi 530398972 855 LVTHKLQYLTH-ADWII 870
Cdd:cd03222 127 VVEHDLAVLDYlSDRIH 143
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
794-886 |
2.59e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.86 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 794 ERGIN-LSGGQRQRICVARAL-YQNTNIVF-LDDPfsALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWII 870
Cdd:TIGR00630 483 SRAAGtLSGGEAQRIRLATQIgSGLTGVLYvLDEP--SIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVI 560
|
90 100
....*....|....*....|..
gi 530398972 871 AM------KDGSVLREGTLKDI 886
Cdd:TIGR00630 561 DIgpgageHGGEVVASGTPEEI 582
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1297-1512 |
2.82e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 48.72 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1297 GEIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDIFDGKIVIDGIDISKlplHTLRs 1374
Cdd:PLN03211 67 HKPKISDETRQIQE--RTILNGVTGMASPGEILAVLGPSGSGKSTLlnALAGRIQGNNFTGTILANNRKPTK---QILK- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1375 RLSIILQDPILFSG-SIRFNLdpeCKCTDDRLWEALEiAQLKNMVKslpgglDAVVTEGG----EN----------FSVG 1439
Cdd:PLN03211 141 RTGFVTQDDILYPHlTVRETL---VFCSLLRLPKSLT-KQEKILVA------ESVISELGltkcENtiignsfirgISGG 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530398972 1440 QRQLFCLARAFVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIAH----RVHTILtaDLVIVMKRGNIL 1512
Cdd:PLN03211 211 ERKRVSIAHEMLINPSLLILDEPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHqpssRVYQMF--DSVLVLSEGRCL 286
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1323-1518 |
2.91e-05 |
|
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: 47.34 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1323 IKPGQKVGICGRTGSGKSSLslafFRMV------DifDGKIVIDGIDISKLPLHtLRSRLSII--LQDPILFSG------ 1388
Cdd:COG0411 27 VERGEIVGLIGPNGAGKTTL----FNLItgfyrpT--SGRILFDGRDITGLPPH-RIARLGIArtFQNPRLFPEltvlen 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1389 --------------SIRFNLDP---ECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFV 1451
Cdd:COG0411 100 vlvaaharlgrgllAALLRLPRarrEEREARERAEELLERVGLADRADEPAGNL-----------SYGQQRRLEIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1452 RKSSILIMDEATASIDMA-TENILQKVV-MTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPE 1518
Cdd:COG0411 169 TEPKLLLLDEPAAGLNPEeTEELAELIRrLRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPA 238
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1275-1493 |
3.73e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 48.21 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1275 MESENYEGTMDP--------SQVPEHWPQEGEIKIHDLCVRYEN------NLKPVLKHVKAYIKPGQKVGICGRTGSGKS 1340
Cdd:TIGR00954 413 VKSGNFKRPRVEeiesgregGRNSNLVPGRGIVEYQDNGIKFENiplvtpNGDVLIESLSFEVPSGNNLLICGPNGCGKS 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1341 SLslafFRMVD----IFDGKIVIDG----IDISKLPLHTLRSrlsiiLQDPILFSGSIrfnLDPECK-CTDDRLWEALEI 1411
Cdd:TIGR00954 493 SL----FRILGelwpVYGGRLTKPAkgklFYVPQRPYMTLGT-----LRDQIIYPDSS---EDMKRRgLSDKDLEQILDN 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1412 AQLKNMVKSlPGGLDAVvTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA--SIDM--ATENILQKVVMTAFadrtv 1487
Cdd:TIGR00954 561 VQLTHILER-EGGWSAV-QDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSavSVDVegYMYRLCREFGITLF----- 633
|
....*.
gi 530398972 1488 vTIAHR 1493
Cdd:TIGR00954 634 -SVSHR 638
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
688-877 |
3.78e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.35 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRNrySVAYAAQKPwllNATVEENITfgspfnkqr 767
Cdd:PRK15064 335 FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENA--NIGYYAQDH---AYDFENDLT--------- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 768 ykaVTDACSL--QPDID----------LLpFGdQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPfsaldihlSD 835
Cdd:PRK15064 401 ---LFDWMSQwrQEGDDeqavrgtlgrLL-FS-QDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP--------TN 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 530398972 836 HLMQEGI--LKF-LQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSV 877
Cdd:PRK15064 468 HMDMESIesLNMaLEKYEGTLIFVSHDREFVSSlATRIIEITPDGV 513
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
683-860 |
4.09e-05 |
|
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: 48.47 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 683 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN--------RYSVAYAAQKPWLLN-ATV 753
Cdd:TIGR01257 941 SGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDietnldavRQSLGMCPQHNILFHhLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 754 EENITFGSPFNKQRYkavtDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHl 833
Cdd:TIGR01257 1021 AEHILFYAQLKGRSW----EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY- 1095
|
170 180
....*....|....*....|....*..
gi 530398972 834 SDHLMQEGILKFlqDDKRTLVLVTHKL 860
Cdd:TIGR01257 1096 SRRSIWDLLLKY--RSGRTIIMSTHHM 1120
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
698-858 |
4.14e-05 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 47.02 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 698 GQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRnrySVAYaaqKPWLLNA----TVEENItfgspfnkqrYKAVTD 773
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD---TVSY---KPQYIKAdyegTVRDLL----------SSITKD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 774 ACS---LQPDIdLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlsDHLMQEGILK-FLQDD 849
Cdd:cd03237 89 FYThpyFKTEI-AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE--QRLMASKVIRrFAENN 165
|
....*....
gi 530398972 850 KRTLVLVTH 858
Cdd:cd03237 166 EKTAFVVEH 174
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1304-1469 |
4.61e-05 |
|
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: 46.20 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1304 LCVRYEnnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDP 1383
Cdd:TIGR01189 7 ACSRGE---RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1384 ILFSGSIRFNLD---PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMD 1460
Cdd:TIGR01189 84 LKPELSALENLHfwaAIHGGAQRTIEDALAAVGLTGFEDLPAAQL-----------SAGQQRRLALARLWLSRRPLWILD 152
|
....*....
gi 530398972 1461 EATASIDMA 1469
Cdd:TIGR01189 153 EPTTALDKA 161
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
977-1197 |
5.06e-05 |
|
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: 47.00 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 977 GFFLLILMIFSKLLKHSVI-VAIDywlatwtsEYSINNTGKADQTYYVAGFSILCGAGIFLCL-VTSLTVEWMGLTAAKN 1054
Cdd:cd18544 4 ALLLLLLATALELLGPLLIkRAID--------DYIVPGQGDLQGLLLLALLYLGLLLLSFLLQyLQTYLLQKLGQRIIYD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1055 LHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISY----ATPVFLVALLPLG 1130
Cdd:cd18544 76 LRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLlnwrLALISLLVLPLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398972 1131 VAFYFIQKYFRVASKDLQEL--DDSTQLpllchfSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYL 1197
Cdd:cd18544 156 LATYLFRKKSRKAYREVREKlsRLNAFL------QESISGMSVIQLFNREKREFEEFDEINQEYRKANL 218
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
698-891 |
5.88e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 46.46 E-value: 5.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 698 GQLTMIVGQVGCGKSSLLLAILGeMQTLEGKVHWSNRN----------RYSVAYAAQKPWLLNATVEENITFGSPFNKQR 767
Cdd:PRK03695 22 GEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPleawsaaelaRHRAYLSQQQTPPFAMPVFQYLTLHQPDKTRT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 768 Y---KAVTDACSLQPDIDLLPfgdqteigeRGIN-LSGGQRQRICVARALYQ-------NTNIVFLDDPFSALDI----- 831
Cdd:PRK03695 101 EavaSALNEVAEALGLDDKLG---------RSVNqLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVaqqaa 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398972 832 --HLSDHLMQEGIlkflqddkrTLVLVTHKLQY-LTHADWIIAMKDGSVLREGTLKDIQTKDV 891
Cdd:PRK03695 172 ldRLLSELCQQGI---------AVVMSSHDLNHtLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
688-830 |
7.31e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.63 E-value: 7.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRNRYSVayaaQKPWL----------LNATVEENI 757
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI----AKPYCtyighnlglkLEMTVFENL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398972 758 TFGSPFnkqrYKAVTdacSLQPDIDLLPFGDQteIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD 830
Cdd:PRK13541 92 KFWSEI----YNSAE---TLYAAIHYFKLHDL--LDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1323-1524 |
7.98e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 47.13 E-value: 7.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1323 IKPGQKVGICGRTGSGKSSLSLAFFRMVD-IFDGKIVIDG--IDIsKLPLHTLRSRLSIILQD-------PIL------- 1385
Cdd:TIGR02633 283 LRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGkpVDI-RNPAQAIRAGIAMVPEDrkrhgivPILgvgknit 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1386 ------FSGSIRFNLDPECKCTDdrlwEALEIAQLKNMVKSLP-GGLdavvteggenfSVGQRQLFCLARAFVRKSSILI 1458
Cdd:TIGR02633 362 lsvlksFCFKMRIDAAAELQIIG----SAIQRLKVKTASPFLPiGRL-----------SGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530398972 1459 MDEATASIDM-ATENILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNiLEYDTPESLLAQE 1524
Cdd:TIGR02633 427 LDEPTRGVDVgAKYEIYKLINQLAQEGVAIIVVSSELAEVLgLSDRVLVIGEGK-LKGDFVNHALTQE 493
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1299-1515 |
8.51e-05 |
|
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: 45.60 E-value: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNLKP--------------------VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIV 1358
Cdd:cd03220 1 IELENVSKSYPTYKGGssslkklgilgrkgevgefwALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1359 IDGIDISKLPLHT-LRSRLSIIlqDPILFSGSIrFNLDPecKCTDDRLWEALEIAQLKNMvkslpggLDAVVteggENFS 1437
Cdd:cd03220 81 VRGRVSSLLGLGGgFNPELTGR--ENIYLNGRL-LGLSR--KEIDEKIDEIIEFSELGDF-------IDLPV----KTYS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1438 VGQ--RQLFCLARAFvrKSSILIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTIL-TADLVIVMKRGNILE 1513
Cdd:cd03220 145 SGMkaRLAFAIATAL--EPDILLIDEVLAVGDAAFQEKCQRRLRELLKQgKTVILVSHDPSSIKrLCDRALVLEKGKIRF 222
|
..
gi 530398972 1514 YD 1515
Cdd:cd03220 223 DG 224
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
723-882 |
8.54e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 47.32 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 723 QTLEgkVHWSNRNRYSVayaaqkpwlLNATVEENITFGSPFNKQRYKavtdacsLQPDIDL-LPFgdqTEIGERGINLSG 801
Cdd:TIGR00630 774 ETLE--VKYKGKNIADV---------LDMTVEEAYEFFEAVPSISRK-------LQTLCDVgLGY---IRLGQPATTLSG 832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 802 GQRQRICVARALYQNTN---IVFLDDPFSALdiHLSD--HLMQegILKFLQDDKRTLVLVTHKLQYLTHADWII------ 870
Cdd:TIGR00630 833 GEAQRIKLAKELSKRSTgrtLYILDEPTTGL--HFDDikKLLE--VLQRLVDKGNTVVVIEHNLDVIKTADYIIdlgpeg 908
|
170
....*....|..
gi 530398972 871 AMKDGSVLREGT 882
Cdd:TIGR00630 909 GDGGGTVVASGT 920
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1046-1188 |
8.74e-05 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 46.32 E-value: 8.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1046 WMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATP---VF 1122
Cdd:cd18576 62 RVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWkltLL 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398972 1123 LVALLP-LGVAFYFIQKYFRVASKDLQ-ELDDSTQlpllcHFSETAEGLTTIRAFRHE----TRFKQRMLEL 1188
Cdd:cd18576 142 MLATVPvVVLVAVLFGRRIRKLSKKVQdELAEANT-----IVEETLQGIRVVKAFTREdyeiERYRKALERV 208
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1323-1513 |
1.12e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 46.27 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1323 IKPGQKVGICGRTGSGKSSLSLAFFRMVDiFDGKIV-----IDGIDISKLPLHTLR----SRLSIILQDPILfsgsirfN 1393
Cdd:PRK11022 30 VKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMaekleFNGQDLQRISEKERRnlvgAEVAMIFQDPMT-------S 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1394 LDPeCKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEG-----------GENFSVGQRQLFCLARAFVRKSSILIMDEA 1462
Cdd:PRK11022 102 LNP-CYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGipdpasrldvyPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1463 TASIDMATE--------NILQKVVMtafadrTVVTIAHRVHTIL-TADLVIVMKRGNILE 1513
Cdd:PRK11022 181 TTALDVTIQaqiielllELQQKENM------ALVLITHDLALVAeAAHKIIVMYAGQVVE 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1299-1515 |
1.13e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 46.60 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRM----VDIFDGKIVI-DGIDISKLPlhtlr 1373
Cdd:COG0488 316 LELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTL----LKLlageLEPDSGTVKLgETVKIGYFD----- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1374 srlsiilQDpilfsgsiRFNLDPeckctDDRLWEAL-------EIAQLKNMVKSL--PGglDAVVTEGGeNFSVGQRQLF 1444
Cdd:COG0488 385 -------QH--------QEELDP-----DKTVLDELrdgapggTEQEVRGYLGRFlfSG--DDAFKPVG-VLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398972 1445 CLARAFVRKSSILIMDEATASIDMATENILQKVVMTaFaDRTVVTIAH------RVhtiltADLVIVMKRGNILEYD 1515
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDD-F-PGTVLLVSHdryfldRV-----ATRILEFEDGGVREYP 511
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1325-1504 |
1.19e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.90 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1325 PGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIdgIDISKLPLHTLRSRLSIILQDPILFSGSIRfnldpeckctddr 1404
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--IDGEDILEEVLDQLLLIIVGGKKASGSGEL------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1405 lwealeiaqlknmvkslpggldavvteggenfsvGQRQLFclARAFVRKSSILIMDEATASIDMATENILQKVVMTAF-- 1482
Cdd:smart00382 66 ----------------------------------RLRLAL--ALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLll 109
|
170 180
....*....|....*....|....*..
gi 530398972 1483 -----ADRTVVTIAHRVHTILTADLVI 1504
Cdd:smart00382 110 llkseKNLTVILTTNDEKDLGPALLRR 136
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1313-1467 |
1.30e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 45.98 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1313 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKlPLHTLRSRLSIILQdpilFSgsirf 1392
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQ----FD----- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1393 NLDPECKCTDD------------RLWEA-----LEIAQLKNMVkslpgglDAVVTEggenFSVGQRQLFCLARAFVRKSS 1455
Cdd:PRK13536 124 NLDLEFTVRENllvfgryfgmstREIEAvipslLEFARLESKA-------DARVSD----LSGGMKRRLTLARALINDPQ 192
|
170
....*....|..
gi 530398972 1456 ILIMDEATASID 1467
Cdd:PRK13536 193 LLILDEPTTGLD 204
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
799-875 |
1.57e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.24 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 799 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAMK 873
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSV-----QAQILQLLRELQQelnmGLLFITHNLSIVRKlADRVAVMQ 231
|
..
gi 530398972 874 DG 875
Cdd:PRK15134 232 NG 233
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
1047-1190 |
1.73e-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: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1047 MGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADT----NIIDQHIPptlESLTRSTLLCLSAIGMISYATPVF 1122
Cdd:cd18551 63 TGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTtllrELITSGLP---QLVTGVLTVVGAVVLMFLLDWVLT 139
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398972 1123 LVALLPLGVAF---YFIQKYFRVASKDLQE-LDDSTQlpllcHFSETAEGLTTIRAFRHETRFKQRMLELTD 1190
Cdd:cd18551 140 LVTLAVVPLAFliiLPLGRRIRKASKRAQDaLGELSA-----ALERALSAIRTVKASNAEERETKRGGEAAE 206
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
1055-1184 |
1.77e-04 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 45.32 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1055 LHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIG---MISYA-TPVFLVALLPLG 1130
Cdd:cd18780 77 LRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVfmfTTSWKlTLVMLSVVPPLS 156
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 530398972 1131 VAFYFIQKYFRVASKDLQ-ELDDStqlpllchfSETAE----GLTTIRAFRHETRFKQR 1184
Cdd:cd18780 157 IGAVIYGKYVRKLSKKFQdALAAA---------STVAEesisNIRTVRSFAKETKEVSR 206
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
796-898 |
1.78e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 44.88 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 796 GINLSGGQRQRICVARALYQNTNIVFLDDPFSALD-IHLSDhlmQEGILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMK 873
Cdd:PRK10895 135 GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDpISVID---IKRIIEHLRDSGLGVLITDHNVrETLAVCERAYIVS 211
|
90 100
....*....|....*....|....*....
gi 530398972 874 DGSVLREGT----LKDIQTKDVELYEHWK 898
Cdd:PRK10895 212 QGHLIAHGTpteiLQDEHVKRVYLGEDFR 240
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1425-1509 |
2.22e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 45.79 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1425 LDAVVteggENFSVGQRQLFCLARAFVRKSSILIMDEATASI-DMATENILQkvVMTAFAD--RTVVTIAHRVHTILT-A 1500
Cdd:COG3845 135 PDAKV----EDLSVGEQQRVEILKALYRGARILILDEPTAVLtPQEADELFE--ILRRLAAegKSIIFITHKLREVMAiA 208
|
....*....
gi 530398972 1501 DLVIVMKRG 1509
Cdd:COG3845 209 DRVTVLRRG 217
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
703-831 |
3.36e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.18 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 703 IVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRnrysVAYaaqKPWLL----NATVEE---NIT--FGSPFnkqrykavtd 773
Cdd:PRK13409 370 IVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK----ISY---KPQYIkpdyDGTVEDllrSITddLGSSY---------- 432
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 530398972 774 acsLQPDIdLLPFGdQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDI 831
Cdd:PRK13409 433 ---YKSEI-IKPLQ-LERLLDKNVKdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 486
|
|
| PduV-EutP |
pfam10662 |
Ethanolamine utilization - propanediol utilization; Members of this family function in ... |
701-804 |
4.23e-04 |
|
Ethanolamine utilization - propanediol utilization; Members of this family function in ethanolamine and propanediol degradation pathways. PduV may be involved in the association of the bacterial microcompartments (BMCs) to filaments.
Pssm-ID: 402341 [Multi-domain] Cd Length: 137 Bit Score: 41.88 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 701 TMIVGQVGCGKSSLLLAILGE------MQTLEgkvhWS------------NRNRYSV----AYAAQKPWLL-NATVEENI 757
Cdd:pfam10662 4 IMLIGPTGCGKTTLCQALSGEelkykkTQAIE----FYdnaidtpgeyleNRRYYSAlivtSADADVIALVqDATEPEST 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 530398972 758 ---TFGSPFNKQRYKAVTdacslqpDIDLLPFGDQTEIGERGINLSGGQR 804
Cdd:pfam10662 80 fppGFASMFNKPVIGIIT-------KIDLAKDEANIEIAEEWLSLAGAQK 122
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1304-1517 |
5.66e-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: 45.00 E-value: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1304 LCVR-----YENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIsKLPLHTLRSRLSI 1378
Cdd:TIGR01257 929 VCVKnlvkiFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGM 1007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1379 ILQDPILF-----SGSIRFNLDpeckcTDDRLWEALEIaQLKNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLARAFVRK 1453
Cdd:TIGR01257 1008 CPQHNILFhhltvAEHILFYAQ-----LKGRSWEEAQL-EMEAMLEDT--GLHHKRNEEAQDLSGGMQRKLSVAIAFVGD 1079
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398972 1454 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRV-HTILTADLVIVMKRGNILEYDTP 1517
Cdd:TIGR01257 1080 AKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMdEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
703-831 |
6.32e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 44.39 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 703 IVGQVGCGKSSL--LLAilGEMQTLEGKVHWSNRnrysVAYaaqKPWLLNA----TVEENItfgspfnkqrYKAVTDacs 776
Cdd:COG1245 371 IVGPNGIGKTTFakILA--GVLKPDEGEVDEDLK----ISY---KPQYISPdydgTVEEFL----------RSANTD--- 428
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530398972 777 lqpdidllPFGD---QTEIGER-GI---------NLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 831
Cdd:COG1245 429 --------DFGSsyyKTEIIKPlGLeklldknvkDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
688-868 |
6.79e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 42.63 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRN--RYSVAYAAQ----------KPWLlnaTVEE 755
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSikKDLCTYQKQlcfvghrsgiNPYL---TLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 756 NITFGSPFNKQRYKaVTDAC---SLQPDIDlLPFGdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALdih 832
Cdd:PRK13540 94 NCLYDIHFSPGAVG-ITELCrlfSLEHLID-YPCG----------LLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL--- 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 530398972 833 lsDHLMQEGILKFLQDDKR---TLVLVTHKLQYLTHADW 868
Cdd:PRK13540 159 --DELSLLTIITKIQEHRAkggAVLLTSHQDLPLNKADY 195
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1325-1468 |
7.68e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 43.71 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1325 PGQKV-GICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG---IDISK---LPLHtlRSRLSIILQDPILFSG-SIRFNLDP 1396
Cdd:PRK11144 22 PAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgicLPPE--KRRIGYVFQDARLFPHyKVRGNLRY 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530398972 1397 ECKCTD----DRLWEALEIAQLknmVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDM 1468
Cdd:PRK11144 100 GMAKSMvaqfDKIVALLGIEPL---LDRYPGSL-----------SGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
688-845 |
7.91e-04 |
|
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: 43.77 E-value: 7.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNRNRysVAYAAQKPWLL--NATVEENITFGSpfnk 765
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVK--LAYVDQSRDALdpNKTVWEEISGGL---- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 766 qrykavtdacslqpdidllpfgDQTEIGERGIN---------------------LSGGQRQRICVARALYQNTNIVFLDD 824
Cdd:TIGR03719 412 ----------------------DIIKLGKREIPsrayvgrfnfkgsdqqkkvgqLSGGERNRVHLAKTLKSGGNVLLLDE 469
|
170 180
....*....|....*....|.
gi 530398972 825 PFSALDIHLSDHLmQEGILKF 845
Cdd:TIGR03719 470 PTNDLDVETLRAL-EEALLNF 489
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1299-1467 |
9.28e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 43.26 E-value: 9.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1299 IKIHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTlRSRLSI 1378
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1379 ILQdpilFSgsirfNLDPECKCTDDRL----WEALEIAQLKNMVKSL------PGGLDAVVTEggenFSVGQRQLFCLAR 1448
Cdd:PRK13537 85 VPQ----FD-----NLDPDFTVRENLLvfgrYFGLSAAAARALVPPLlefaklENKADAKVGE----LSGGMKRRLTLAR 151
|
170
....*....|....*....
gi 530398972 1449 AFVRKSSILIMDEATASID 1467
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLD 170
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
1067-1202 |
9.89e-04 |
|
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: 42.78 E-value: 9.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1067 PIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIG-MISYATPVFLVALLPL---GVAFYFIQKYFRV 1142
Cdd:cd18541 87 SPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVmMFTISPKLTLIALLPLpllALLVYRLGKKIHK 166
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398972 1143 ASKDLQE----LDDSTQlpllchfsETAEGLTTIRAFRHETRFKQRMLELTDTN---NIAYLFLSAA 1202
Cdd:cd18541 167 RFRKVQEafsdLSDRVQ--------ESFSGIRVIKAFVQEEAEIERFDKLNEEYvekNLRLARVDAL 225
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
800-886 |
1.19e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 42.79 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 800 SGGQRQRICVARALYQNTNIVFLDDPFSALDIhlsdhLMQEGILKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAMKD 874
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDV-----TVQAQIMTLLNELKRefntAIIMITHDLGVVAGiCDKVLVMYA 237
|
90
....*....|..
gi 530398972 875 GSVLREGTLKDI 886
Cdd:PRK09473 238 GRTMEYGNARDV 249
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
1012-1204 |
1.23e-03 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 42.79 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1012 NNTGKADQTYYVAGFSILCGAGIFLCL------VTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSA 1085
Cdd:cd18554 32 GSSLTLDEKVYKLFTIIGIMFFIFLILrppveyYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVIN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1086 DTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVA---LLPL-GVAFYFIQKYFRVASKDL-QELDDstqlpLLC 1160
Cdd:cd18554 112 DVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVslvIFPFyILAVKYFFGRLRKLTKERsQALAE-----VQG 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 530398972 1161 HFSETAEGLTTIRAFRHETRFKQrmlELTDTNNiayLFLSAANR 1204
Cdd:cd18554 187 FLHERIQGMSVIKSFALEKHEQK---QFDKRNG---HFLTRALK 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1326-1483 |
1.68e-03 |
|
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: 41.32 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1326 GQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECK-CTDDR 1404
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHAdHSDEQ 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398972 1405 LWEALEIAQLkNMVKSLPGGldavvteggeNFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILqkvvMTAFA 1483
Cdd:cd03231 106 VEEALARVGL-NGFEDRPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF----AEAMA 169
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
799-886 |
1.80e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 42.08 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 799 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD---HLMQEgilkfLQDDKR-TLVLVTHKLQYLTH-ADWIIAMK 873
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSqliNLMLE-----LQEKQGiSYIYVTQHLGMMKHiSDQVLVMH 224
|
90
....*....|...
gi 530398972 874 DGSVLREGTLKDI 886
Cdd:PRK15112 225 QGEVVERGSTADV 237
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
1058-1220 |
2.54e-03 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 41.53 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1058 NLLNK-IILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTllcLSAIGMI------SYATPVFLVALLPL- 1129
Cdd:cd18784 73 NLLFRsIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSL---VKAIGVIvfmfklSWQLSLVTLIGLPLi 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1130 -GVAFYFiQKYFRVASKDLQeldDStqlplLCHFSETAE----GLTTIRAFRHET----RFK---QRMLELTDTNNIAYL 1197
Cdd:cd18784 150 aIVSKVY-GDYYKKLSKAVQ---DS-----LAKANEVAEetisSIRTVRSFANEDgeanRYSeklKDTYKLKIKEALAYG 220
|
170 180
....*....|....*....|....*..
gi 530398972 1198 FLSAANRWLE----VRTDYLGACIVLT 1220
Cdd:cd18784 221 GYVWSNELTElaltVSTLYYGGHLVIT 247
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
800-863 |
2.76e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 2.76e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398972 800 SGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLmQEGILKFlqddKRTLVLVTHKLQYL 863
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWL-ETYLLKW----PKTFIVVSHAREFL 404
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
794-927 |
3.51e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 794 ERGIN-LSGGQRQRICVARAL-YQNTNIVF-LDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTHADWII 870
Cdd:PRK00635 471 ERALAtLSGGEQERTALAKHLgAELIGITYiLDEPSIGLHPQDTHKLIN--VIKKLRDQGNTVLLVEHDEQMISLADRII 548
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398972 871 ------AMKDGSVLREGTLKDIQTKDVELYEHWKtlmnRQDQELEKDmEADQTTLERKTLRRA 927
Cdd:PRK00635 549 digpgaGIFGGEVLFNGSPREFLAKSDSLTAKYL----RQELTIPIP-EKRTNSLGTLTLSKA 606
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
688-873 |
3.62e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 39.65 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILgemqtlegkvhwsnrnrysvayaaqkpwlLNATVEENITFGSPFNKQR 767
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILDAIG-----------------------------LALGGAQSATRRRSGVKAG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 768 YKavtdacSLQPDIDLLPFGDQteigerginLSGGQRQRICVARAL----YQNTNIVFLDDPFSALDIHLSDHLMqEGIL 843
Cdd:cd03227 62 CI------VAAVSAELIFTRLQ---------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALA-EAIL 125
|
170 180 190
....*....|....*....|....*....|
gi 530398972 844 KFLqDDKRTLVLVTHKLQYLTHADWIIAMK 873
Cdd:cd03227 126 EHL-VKGAQVIVITHLPELAELADKLIHIK 154
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
798-860 |
3.72e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 41.69 E-value: 3.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398972 798 NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhlSDHLMQEGILKFLQDDKRTLVLVTHKL 860
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI--YQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
792-895 |
4.71e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 41.76 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 792 IGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHK--LQYLTHADW 868
Cdd:PLN03140 1012 VGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRT--VRNTVDTGRTVVCTIHQpsIDIFEAFDE 1089
|
90 100
....*....|....*....|....*...
gi 530398972 869 IIAMK-DGSVLREGTLKDIQTKDVELYE 895
Cdd:PLN03140 1090 LLLMKrGGQVIYSGPLGRNSHKIIEYFE 1117
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1323-1511 |
5.23e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.05 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1323 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG--IDISKlPLHTLRSrlSIIL------QDPILFSGSIRFNL 1394
Cdd:PRK11288 276 VRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRS-PRDAIRA--GIMLcpedrkAEGIIPVHSVADNI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1395 DPECK-------CTDDRLWEA----LEIAQLKnmVKSlPGGLDAVVteggeNFSVGQRQLFCLARAFVRKSSILIMDEAT 1463
Cdd:PRK11288 353 NISARrhhlragCLINNRWEAenadRFIRSLN--IKT-PSREQLIM-----NLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 530398972 1464 ASIDM-ATENILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNI 1511
Cdd:PRK11288 425 RGIDVgAKHEIYNVIYELAAQGVAVLFVSSDLPEVLgVADRIVVMREGRI 474
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
790-831 |
6.64e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.95 E-value: 6.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 530398972 790 TEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 831
Cdd:PRK13409 203 ENILDRDIsELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
792-903 |
7.12e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 792 IGERGINLSGGQRQRICVARALY---QNTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLTHADW 868
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQ--LRTLVSLGHSVIYIDHDPALLKQADY 1770
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 530398972 869 IIAM------KDGSVLREGTLKDIQ-TKDVELyehwKTLMNR 903
Cdd:PRK00635 1771 LIEMgpgsgkTGGKILFSGPPKDISaSKDSLL----KTYMCN 1808
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1331-1492 |
7.20e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.51 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1331 ICGRTGSGKSSLslaffrmvdifdgkivIDGIDISKLPLHTLRSRLSIILQDPIlFSGSIRFNLDPECKCTDDRLWEAL- 1409
Cdd:cd03240 27 IVGQNGAGKTTI----------------IEALKYALTGELPPNSKGGAHDPKLI-REGEVRAQVKLAFENANGKKYTITr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1410 EIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFC------LARAFVRKSSILIMDEATASIDmaTENILQKVV----- 1478
Cdd:cd03240 90 SLAILENVIFCHQGESNWPLLDMRGRCSGGEKVLASliirlaLAETFGSNCGILALDEPTTNLD--EENIEESLAeiiee 167
|
170
....*....|....
gi 530398972 1479 MTAFADRTVVTIAH 1492
Cdd:cd03240 168 RKSQKNFQLIVITH 181
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
1030-1196 |
7.83e-03 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 40.01 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1030 CGAGIFLCLVTSLTvewmgltaaKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCL 1109
Cdd:cd18590 55 LRGGLFMCTLSRLN---------LRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1110 SAIG-MISYATPVFLVALL--PLGVAfyfIQK----YFRVASKDLQE-LDDSTQLPllchfSETAEGLTTIRAFRHET-- 1179
Cdd:cd18590 126 GMLGfMLSLSWQLTLLTLIemPLTAI---AQKvyntYHQKLSQAVQDsIAKAGELA-----REAVSSIRTVRSFKAEEee 197
|
170 180
....*....|....*....|..
gi 530398972 1180 --RFKQ---RMLELTDTNNIAY 1196
Cdd:cd18590 198 acRYSEaleRTYNLKDRRDTVR 219
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
1060-1184 |
8.33e-03 |
|
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: 40.12 E-value: 8.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 1060 LNKIILGPIRFFDTTPLGLILNRFSaDTNIIDQHIPPTLESLTRSTLLCL-SAIGMISYATPVFLVALLPL---GVAFYF 1135
Cdd:cd18570 82 FKHLLKLPLSFFETRKTGEIISRFN-DANKIREAISSTTISLFLDLLMVIiSGIILFFYNWKLFLITLLIIplyILIILL 160
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 530398972 1136 IQKYFRVASKDLQELDDSTQlpllCHFSETAEGLTTIRAFRHETRFKQR 1184
Cdd:cd18570 161 FNKPFKKKNREVMESNAELN----SYLIESLKGIETIKSLNAEEQFLKK 205
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
688-881 |
8.38e-03 |
|
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: 39.44 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsNRNRySVAyaaqkpWLL--------NATVEENITF 759
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV---TVRG-RVS------SLLglgggfnpELTGRENIYL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398972 760 -GS------PFNKQRYKAVTDACSLQPDIDlLPFGdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 832
Cdd:cd03220 108 nGRllglsrKEIDEKIDEIIEFSELGDFID-LPVK----------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 530398972 833 LSDHlMQEGILKFLQDDkRTLVLVTHKLQYL-THADWIIAMKDGSVLREG 881
Cdd:cd03220 177 FQEK-CQRRLRELLKQG-KTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| |
