|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
222-1499 |
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: 842.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 222 LLSKATYWWMNTLIISAHKKPIDLKAIGKLPIAMRAVTNYVCLKDAYEEQKKKVADHP---------------------- 279
Cdd:TIGR00957 209 FLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKECKKTRKQPvsavygkkdpskpkgssqldan 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 280 -------------NRTPSIWLAMYRAFGRPILLSSTFRYLADLLGFAGPLCISGIVQRVNETQNGTnnttgisetlsske 346
Cdd:TIGR00957 289 eevealivksphkPRKPSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPD-------------- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 347 flENAYVLAVLLFLALILQRTFLQASYYVTIETGINLRGALLAMIYNKILRLStsNLSMGEMTLGQINNLVAIETNQLMW 426
Cdd:TIGR00957 355 --WQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVIT--NSARKSSTVGEIVNLMSVDAQRFMD 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 427 FLFLCPNLWAMPVQIIMGVILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLK 506
Cdd:TIGR00957 431 LATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLK 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 507 LYAWEHIFCKSVEETRMKELSSLKTFALYTSLSIFMNAAIPIAAVLATFVTHAYASGNNLKPAE-AFASLSLFHILVTPL 585
Cdd:TIGR00957 511 LYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENNILDAEkAFVSLALFNILRFPL 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 586 FLLSTVVRFAVKAIISVQKLNEFLLSDEIgddswrtgesslpfesckkhtgvQPKTINRkqpgryhldsyeqstRRLRPA 665
Cdd:TIGR00957 591 NILPMVISSIVQASVSLKRLRIFLSHEEL-----------------------EPDSIER---------------RTIKPG 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 666 ETEDIAIKvtNGYFSWGSGLA-TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH------------W- 731
Cdd:TIGR00957 633 EGNSITVH--NATFTWARDLPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHmkgsvayvpqqaWi 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 732 -----------------SKYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 794
Cdd:TIGR00957 711 qndslrenilfgkalneKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSA 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 795 LDIHLSDHLMQ-----EGILKflqddKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEHWKTLMNR 869
Cdd:TIGR00957 791 VDAHVGKHIFEhvigpEGVLK-----NKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPD 865
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 870 QDQElekDMEADQTTL------ERKTLRRAMY-----SREAKAQMEDEDEEEEEEEDEDDNMSTVMRLRTKMP-WKTC-- 935
Cdd:TIGR00957 866 EQQG---HLEDSWTALvsgegkEAKLIENGMLvtdvvGKQLQRQLSASSSDSGDQSRHHGSSAELQKAEAKEEtWKLMea 942
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 936 -------------WRYLTSGGFFLLILMIFSKLLKHSVIVAIDYWLATWTSEYSINNTgKADQTYYV---AGFSILCGAG 999
Cdd:TIGR00957 943 dkaqtgqvelsvyWDYMKAIGLFITFLSIFLFVCNHVSALASNYWLSLWTDDPMVNGT-QNNTSLRLsvyGALGILQGFA 1021
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1000 IFLclvTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIG 1079
Cdd:TIGR00957 1022 VFG---YSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALI 1098
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1080 MISYATPVFLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNN 1159
Cdd:TIGR00957 1099 VILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQ 1178
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1160 IAYLFLSAANRWLEVRTDYLGACIVL--TASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNS 1237
Cdd:TIGR00957 1179 KAYYPSIVANRWLAVRLECVGNCIVLfaALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKE 1258
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1238 FLTMESENyEGTMDPSQVPEHWPQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVD 1317
Cdd:TIGR00957 1259 YSETEKEA-PWQIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINE 1337
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1318 IFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTE 1397
Cdd:TIGR00957 1338 SAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAE 1417
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1398 GGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNI 1477
Cdd:TIGR00957 1418 GGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEV 1497
|
1370 1380
....*....|....*....|..
gi 530398974 1478 LEYDTPESLLAQEnGVFASFVR 1499
Cdd:TIGR00957 1498 AEFGAPSNLLQQR-GIFYSMAK 1518
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
220-1500 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 722.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 220 VNLLSKATYWWMNTLIISAHKKPIDLKAIGKLPIAMRAVTNYVCLKDAYEEQKKKvadhpnrtPSIWL--AMYRAFGRPI 297
Cdd:PLN03130 232 ANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKK--------PKPWLlrALNNSLGGRF 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 298 LLSSTFRYLADLLGFAGPLCISGIVQRVnetQNGTNNTTGISETLSskeflenayvlavllflalilqrTFLQASYYVTI 377
Cdd:PLN03130 304 WLGGFFKIGNDLSQFVGPLLLNLLLESM---QNGEPAWIGYIYAFS-----------------------IFVGVVLGVLC 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 378 E---------TGINLRGALLAMIYNKILRLStsNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILL 448
Cdd:PLN03130 358 EaqyfqnvmrVGFRLRSTLVAAVFRKSLRLT--HEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 449 YNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSS 528
Cdd:PLN03130 436 YQQLGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSW 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 529 LKTFALYTSLSIFMNAAIPIAAVLATFVTHAYASGNnLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKLNEF 608
Cdd:PLN03130 516 FRKAQLLSAFNSFILNSIPVLVTVVSFGVFTLLGGD-LTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEEL 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 609 LLSDEigddswRTGESSLPFESCkkhtgvqpktinrkQPgryhldsyeqstrrlrpaetediAIKVTNGYFSWGSGL--A 686
Cdd:PLN03130 595 LLAEE------RVLLPNPPLEPG--------------LP-----------------------AISIKNGYFSWDSKAerP 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 687 TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEG-------------KVHW------------------SKYK 735
Cdd:PLN03130 632 TLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDasvvirgtvayvpQVSWifnatvrdnilfgspfdpERYE 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 736 AVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQdd 815
Cdd:PLN03130 712 RAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELR-- 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 816 KRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIqTKDVELYehwKTLMNR---------------QDQELEKDMEA 880
Cdd:PLN03130 790 GKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEEL-SNNGPLF---QKLMENagkmeeyveengeeeDDQTSSKPVAN 865
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 881 DQTTLERKTLRRAMYSREAKAQMededeeeeeeededdnMSTVMRLRTKMPWKTCWRYLTS-GGFFLLILMIFSKLLKHS 959
Cdd:PLN03130 866 GNANNLKKDSSSKKKSKEGKSVL----------------IKQEERETGVVSWKVLERYKNAlGGAWVVMILFLCYVLTEV 929
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 960 VIVAIDYWLATWTSEYSINNTGKAdqtYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDT 1039
Cdd:PLN03130 930 FRVSSSTWLSEWTDQGTPKTHGPL---FYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHT 1006
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1040 TPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQKYFRVASKDLQELDDS 1119
Cdd:PLN03130 1007 NPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVKRLDSI 1086
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1120 TQLPLLCHFSETAEGLTTIRAFRHetrfKQRMLELTDT---NNIAYLFLS-AANRWLEVRTDYLGACIV-LTASIA---- 1190
Cdd:PLN03130 1087 TRSPVYAQFGEALNGLSTIRAYKA----YDRMAEINGRsmdNNIRFTLVNmSSNRWLAIRLETLGGLMIwLTASFAvmqn 1162
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1191 --SISGSSNSGLVGLGLLYALTITNYLNWVVRnLADL-EVQMGAVKKVNSFLTMESENyEGTMDPSQVPEHWPQEGEIKI 1267
Cdd:PLN03130 1163 grAENQAAFASTMGLLLSYALNITSLLTAVLR-LASLaENSLNAVERVGTYIDLPSEA-PLVIENNRPPPGWPSSGSIKF 1240
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1268 HDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQ 1347
Cdd:PLN03130 1241 EDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQ 1320
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1348 DPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDE 1427
Cdd:PLN03130 1321 APVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDE 1400
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398974 1428 ATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQENGVFASFVRA 1500
Cdd:PLN03130 1401 ATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQS 1473
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
221-1500 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 689.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 221 NLLSKATYWWMNTLIISAHKKPIDLKAIGKLPIAMRAVTNYVCLKDAYEEQkkkvadhpNRTPSIWL--AMYRAFGRPIL 298
Cdd:PLN03232 233 SIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEE--------SRRPKPWLlrALNNSLGGRFW 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 299 LSSTFRYLADLLGFAGPLCISGIVQRVNEtqngtNNTTGISETLSSKEFLENAYVlavllflalilqrTFLQASYYVTI- 377
Cdd:PLN03232 305 LGGIFKIGHDLSQFVGPVILSHLLQSMQE-----GDPAWVGYVYAFLIFFGVTFG-------------VLCESQYFQNVg 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 378 ETGINLRGALLAMIYNKILRLStsNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSAL 457
Cdd:PLN03232 367 RVGFRLRSTLVAAIFHKSLRLT--HEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 458 VGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTS 537
Cdd:PLN03232 445 FGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSA 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 538 LSIFMNAAIPIAAVLATFVTHAYASGNnLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKLNEFLLSDEigdd 617
Cdd:PLN03232 525 FNSFILNSIPVVVTLVSFGVFVLLGGD-LTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEE---- 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 618 swRTGESSLPFesckkhtgvqpktinrkQPGRyhldsyeqstrrlrPAetediaIKVTNGYFSWGSGLA--TLSNIDIRI 695
Cdd:PLN03232 600 --RILAQNPPL-----------------QPGA--------------PA------ISIKNGYFSWDSKTSkpTLSDINLEI 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 696 PTGQLTMIVGQVGCGKSSLLLAILGEMQTLEG-------------KVHW------------------SKYKAVTDACSLQ 744
Cdd:PLN03232 641 PVGSLVAIVGGTGEGKTSLISAMLGELSHAETssvvirgsvayvpQVSWifnatvrenilfgsdfesERYWRAIDVTALQ 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 745 PDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDdkRTLVLVTH 824
Cdd:PLN03232 721 HDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKG--KTRVLVTN 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 825 KLQYLTHADWIIAMKDGSVLREGTLKDIqTKDVELYehwKTLM------------NRQDQELEKDMEADQTTLERKTLRR 892
Cdd:PLN03232 799 QLHFLPLMDRIILVSEGMIKEEGTFAEL-SKSGSLF---KKLMenagkmdatqevNTNDENILKLGPTVTIDVSERNLGS 874
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 893 AMYSREAKAQMededeeeeeeededdnMSTVMRLRTKMPWKTCWRYLTS-GGFFLLILMIFSKLLKHSVIVAIDYWLATW 971
Cdd:PLN03232 875 TKQGKRGRSVL----------------VKQEERETGIISWNVLMRYNKAvGGLWVVMILLVCYLTTEVLRVSSSTWLSIW 938
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 972 TSEYSINNTGKAdqtYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSA 1051
Cdd:PLN03232 939 TDQSTPKSYSPG---FYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSK 1015
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1052 DTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSET 1131
Cdd:PLN03232 1016 DIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEA 1095
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1132 AEGLTTIRAFRHETRFKQRMLELTDtNNIAY-LFLSAANRWLEVRTDYLGACIV-LTASIASISGSSNSGLVG----LGL 1205
Cdd:PLN03232 1096 LNGLSSIRAYKAYDRMAKINGKSMD-NNIRFtLANTSSNRWLTIRLETLGGVMIwLTATFAVLRNGNAENQAGfastMGL 1174
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1206 L--YALTITNYLNWVVRNLADLEVQMGAVKKVNSFLTMESENyEGTMDPSQVPEHWPQEGEIKIHDLCVRYENNLKPVLK 1283
Cdd:PLN03232 1175 LlsYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEA-TAIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLH 1253
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1284 HVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPE 1363
Cdd:PLN03232 1254 GLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPF 1333
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1364 CKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKV 1443
Cdd:PLN03232 1334 SEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRT 1413
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*..
gi 530398974 1444 VMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQENGVFASFVRA 1500
Cdd:PLN03232 1414 IREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHS 1470
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
365-1500 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 626.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 365 QRTFLQASYYVTIETGINLRGALLAMIYNKILRLSTSNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMG 444
Cdd:PTZ00243 298 QSVCLHRFYYISIRCGLQYRSALNALIFEKCFTISSKSLAQPDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLS 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 445 VILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMK 524
Cdd:PTZ00243 378 ILLLSRLVGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRAR 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 525 ELSSLKTFALYTSLSIFMNAAIPIAAVLATFVTHaYASGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQK 604
Cdd:PTZ00243 458 ELRYLRDVQLARVATSFVNNATPTLMIAVVFTVY-YLLGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKR 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 605 LNEFLLSDE-----IGD--DSWRTGESS----------------------LPF------------------ESCKKHTGV 637
Cdd:PTZ00243 537 ISTFLECDNatcstVQDmeEYWREQREHstacqlaavlenvdvtafvpvkLPRapkvktsllsralrmlccEQCRPTKRH 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 638 QPKTI---------------NRKQPGRYHLDSyEQSTrrlrPAETEDIAIKVTNGYFSWGSGLaTLSNIDIRIPTGQLTM 702
Cdd:PTZ00243 617 PSPSVvvedtdygspssasrHIVEGGTGGGHE-ATPT----SERSAKTPKMKTDDFFELEPKV-LLRDVSVSVPRGKLTV 690
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 703 IVGQVGCGKSSLLLAILGEMQTLEGKVHWSKYKA---------------------------VTDA---CSLQPDIDLLPF 752
Cdd:PTZ00243 691 VLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAyvpqqawimnatvrgnilffdeedaarLADAvrvSQLEADLAQLGG 770
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 753 GDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHA 832
Cdd:PTZ00243 771 GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAG--KTRVLATHQVHVVPRA 848
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 833 DWIIAMKDGSVLREGTLKD-IQTKdveLYEHWKT-LMNRQDQElEKDMEADQTTLER-KTLRRAMYSREAKAQMEDEDEE 909
Cdd:PTZ00243 849 DYVVALGDGRVEFSGSSADfMRTS---LYATLAAeLKENKDSK-EGDADAEVAEVDAaPGGAVDHEPPVAKQEGNAEGGD 924
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 910 EEEEEDEDDNMSTVMRLRTKM-PWKTCWRYLTS-GGFFLLILMIFSKLLKHSVIVAIDYWLATWTSeysiNNTGKADQTY 987
Cdd:PTZ00243 925 GAALDAAAGRLMTREEKASGSvPWSTYVAYLRFcGGLHAAGFVLATFAVTELVTVSSGVWLSMWST----RSFKLSAATY 1000
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 988 -YV-AGFSILCGAGIFLCLVTSLTVEWMGltaAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLE 1065
Cdd:PTZ00243 1001 lYVyLGIVLLGTFSVPLRFFLSYEAMRRG---SRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYL 1077
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1066 SLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHET 1145
Cdd:PTZ00243 1078 YLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAH 1157
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1146 RFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACIVLT------ASIASISGSSNSGLVGLGLLYALTITNYLNWVV 1219
Cdd:PTZ00243 1158 LVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVialigvIGTMLRATSQEIGLVSLSLTMAMQTTATLNWLV 1237
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1220 RNLADLEVQMGAVKKVNSF--------------LTMESENYEGT---------MDPSQVPEHWP---QEGEIKIHDLCVR 1273
Cdd:PTZ00243 1238 RQVATVEADMNSVERLLYYtdevphedmpeldeEVDALERRTGMaadvtgtvvIEPASPTSAAPhpvQAGSLVFEGVQMR 1317
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1274 YENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFS 1353
Cdd:PTZ00243 1318 YREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFD 1397
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1354 GSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILI-MDEATASI 1432
Cdd:PTZ00243 1398 GTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFIlMDEATANI 1477
|
1210 1220 1230 1240 1250 1260
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530398974 1433 DMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQENGVFASFVRA 1500
Cdd:PTZ00243 1478 DPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVEA 1545
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1263-1502 |
1.99e-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: 516.00 E-value: 1.99e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1263 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1342
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1343 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 1422
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1423 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQENGVFASFVRADM 1502
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVRTDK 257
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
299-605 |
1.71e-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: 425.50 E-value: 1.71e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 299 LSSTFRYLADLLGFAGPLCISGIVQRVNETQNGTNNTTGISET--LSSKEFLENAYVLAVLLFLALILQRTFLQASYYVT 376
Cdd:cd18591 1 LGGILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNSTDKLSVsyVTVEEFFSNGYVLAVILFLALLLQATFSQASYHIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 377 IETGINLRGALLAMIYNKILRLSTSNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSA 456
Cdd:cd18591 81 IREGIRLKTALQAMIYEKALRLSSWNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 457 LVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYT 536
Cdd:cd18591 161 LIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYW 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398974 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 ... |
1263-1483 |
6.69e-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: 398.41 E-value: 6.69e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1263 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1342
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1343 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 1422
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398974 1423 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTP 1483
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
221-1489 |
2.51e-127 |
|
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: 432.80 E-value: 2.51e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 221 NLLSKATYWWMNTLIISAHKKPIDLKAIGKLPIAMRAVTnyvcLKDAYEEQKKKVADHPNRTPSIWLAMYRAFGRPILLS 300
Cdd:TIGR01271 10 NFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADN----LSERLEREWDRELASAKKNPKLLNALRRCFFWRFVFY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 301 STFRYLADLLGFAGPLCISGIVQRVNEtqngtnnttgisetlSSKEFLENAYVLAVLLFLALILQRTFLQASYYVTIETG 380
Cdd:TIGR01271 86 GILLYFGEATKAVQPLLLGRIIASYDP---------------FNAPEREIAYYLALGLCLLFIVRTLLLHPAIFGLHHLG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 381 INLRGALLAMIYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSALVGA 460
Cdd:TIGR01271 151 MQMRIALFSLIYKKTLKLSSRVLD--KISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 461 AVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFAlytSLSI 540
Cdd:TIGR01271 229 GFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIA---YLRY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 541 FMNAAIPIAAVLATF---VTHAYASGNNLKpaEAFASLSLFHIL-VTPLFLLSTVVRFAVKAIISVQKLNEFLLSDEigd 616
Cdd:TIGR01271 306 FYSSAFFFSGFFVVFlsvVPYALIKGIILR--RIFTTISYCIVLrMTVTRQFPGAIQTWYDSLGAITKIQDFLCKEE--- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 617 dsWRTGESSLpfesckkhTGVQPKTINRKQpgryhldSYEQSTRRL-RPAETEDIAIKVTNG----YFSWGSGLAT--LS 689
Cdd:TIGR01271 381 --YKTLEYNL--------TTTEVEMVNVTA-------SWDEGIGELfEKIKQNNKARKQPNGddglFFSNFSLYVTpvLK 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 690 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS------------------------------KYKAVTD 739
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSgrisfspqtswimpgtikdniifglsydeyRYTSVIK 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 740 ACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDdkRTL 819
Cdd:TIGR01271 524 ACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSN--KTR 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 820 VLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKD------------------------------------------- 856
Cdd:TIGR01271 602 ILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRpdfsslllgleafdnfsaerrnsiltetlrrvsidgdstvfsg 681
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 857 ----------------------------------------------------------------------------VELY 860
Cdd:TIGR01271 682 petikqsfkqpppefaekrkqsiilnpiasarkfsfvqmgpqkaqattiedavrepserkfslvpedeqgeeslprGNQY 761
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 861 EHWKTLMNRQDQELEKDMEADQTTLERKTLRRAMYSREAKAQMEDEDEEEEEEEDEDDNMSTVMRLRTKM---------- 930
Cdd:TIGR01271 762 HHGLQHQAQRRQSVLQLMTHSNRGENRREQLQTSFRKKSSITQQNELASELDIYSRRLSKDSVYEISEEIneedlkecfa 841
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 931 ----------PWKTCWRYLTSGG--FFLLI--LMIFSKLLKHSVIVaidYWLATWTSEYSINNTGK-ADQTYYVAGFSIL 995
Cdd:TIGR01271 842 derenvfettTWNTYLRYITTNRnlVFVLIfcLVIFLAEVAASLLG---LWLITDNPSAPNYVDQQhANASSPDVQKPVI 918
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 996 CGAG-----IFLCLVTSLTVEWMG-----------LTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQH 1059
Cdd:TIGR01271 919 ITPTsayyiFYIYVGTADSVLALGffrglplvhtlLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDM 998
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1060 IPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIR 1139
Cdd:TIGR01271 999 LPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIR 1078
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1140 AFRHETRFK---QRMLELTDTNNIAYLflsAANRWLEVRTDYLGACIVLTASIASISGSSNSG-LVGLGLLYALTITNYL 1215
Cdd:TIGR01271 1079 AFGRQSYFEtlfHKALNLHTANWFLYL---STLRWFQMRIDIIFVFFFIAVTFIAIGTNQDGEgEVGIILTLAMNILSTL 1155
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1216 NWVVRNLADLEVQMGAVKKVNSFLTMESENYEGT-------------MDPSQVPEHWPQEGEIKIHDLCVRYENNLKPVL 1282
Cdd:TIGR01271 1156 QWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRPSggggkyqlstvlvIENPHAQKCWPSGGQMDVQGLTAKYTEAGRAVL 1235
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1283 KHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDP 1362
Cdd:TIGR01271 1236 QDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDP 1314
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1363 ECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQK 1442
Cdd:TIGR01271 1315 YEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRK 1394
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|....*..
gi 530398974 1443 VVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1489
Cdd:TIGR01271 1395 TLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNE 1441
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
948-1239 |
1.43e-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: 387.73 E-value: 1.43e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 948 ILMIFSKLLKHSVIVAIDYWLATWTSE----------YSINNTGKADQTYYVAGFSILCGAGIFLCLVTSLTVEWMGLTA 1017
Cdd:cd18602 2 ALVLALALLKQGLRVATDFWLADWTEAnhdvasvvfnITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGELAGLRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1018 AKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGV 1097
Cdd:cd18602 82 ARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIII 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1098 AFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTD 1177
Cdd:cd18602 162 VYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRLD 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530398974 1178 YLGACIVL----TASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFL 1239
Cdd:cd18602 242 YLGAVIVFlaalSSLTAALAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
672-842 |
1.01e-114 |
|
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: 360.11 E-value: 1.01e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS------------------- 732
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSnknesepsfeatrsrnrys 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 733 ----------------------------KYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTN 784
Cdd:cd03290 81 vayaaqkpwllnatveenitfgspfnkqRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 530398974 785 IVFLDDPFSALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGS 842
Cdd:cd03290 161 IVFLDDPFSALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
924-1500 |
7.59e-102 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 338.29 E-value: 7.59e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 924 MRLRTKMPWKTCWRYLtSGGFFLLILMIFSKLLKHSVIVAIDYWLATWTSEYSinNTGKADQTYYVAGFSILCGAGIFLC 1003
Cdd:COG1132 1 MSKSPRKLLRRLLRYL-RPYRGLLILALLLLLLSALLELLLPLLLGRIIDALL--AGGDLSALLLLLLLLLGLALLRALL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1004 -LVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMIS 1082
Cdd:COG1132 78 sYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1083 YATP----VFLVALLPLGVAFYFIQKYFRVASKDLQE-LDDSTQlpllcHFSETAEGLTTIRAFRHETRFKQRMLELTDT 1157
Cdd:COG1132 158 VIDWrlalIVLLVLPLLLLVLRLFGRRLRKLFRRVQEaLAELNG-----RLQESLSGIRVVKAFGREERELERFREANEE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1158 NNIAYLFLSAANRWLEVRTDYLGACIVLTasiasisgssnsgLVGLG-----------------LLYALTITNYLNWVVR 1220
Cdd:COG1132 233 LRRANLRAARLSALFFPLMELLGNLGLAL-------------VLLVGgllvlsgsltvgdlvafILYLLRLFGPLRQLAN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1221 NLADLEVQMGAVKKVNSFLTMESENYEGTmDPSQVPehwPQEGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGR 1300
Cdd:COG1132 300 VLNQLQRALASAERIFELLDEPPEIPDPP-GAVPLP---PVRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1301 TGSGKSSL-SLaFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPECkcTDDRLWEALE 1376
Cdd:COG1132 375 SGSGKSTLvNL-LLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRPDA--TDEEVEEAAK 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1377 IAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTI 1456
Cdd:COG1132 452 AAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVI 531
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 530398974 1457 AHRVHTILTADLVIVMKRGNILEYDTPESLLAQeNGVFASFVRA 1500
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 ... |
1259-1483 |
4.14e-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: 4.14e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1259 WPQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTL 1338
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1339 RSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEiaqlknmvkslpggldavVTEGGENFSVGQRQLFCLARAFVR 1418
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398974 1419 KSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTP 1483
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
672-842 |
9.33e-82 |
|
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: 267.03 E-value: 9.33e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSWGSGLA----TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS--------------- 732
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPgsiayvsqepwiqng 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 733 ---------------KYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 797
Cdd:cd03250 81 tirenilfgkpfdeeRYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 530398974 798 HLSDHLMQEGILKFLQDDKrTLVLVTHKLQYLTHADWIIAMKDGS 842
Cdd:cd03250 161 HVGRHIFENCILGLLLNNK-TRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
943-1238 |
1.21e-81 |
|
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: 270.53 E-value: 1.21e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 943 GFFLLILMIFSKLLKHSVIVAIDYWLATWTSEYSINNTgkadqTYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLH 1022
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSG-----YYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1023 HNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFI 1102
Cdd:cd18580 76 DKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1103 QKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGAC 1182
Cdd:cd18580 156 QRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGAL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 530398974 1183 IV--LTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSF 1238
Cdd:cd18580 236 LAlvVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEY 293
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
989-1499 |
8.76e-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: 282.11 E-value: 8.76e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 989 VAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSaDTNIIDQHIP-PTLESL 1067
Cdd:COG2274 199 AIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTgSLLTAL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1068 TRSTLLCLSAIGMISYATPVFLVALLPLGVAF---YFIQKYFRVASKDLQELDDSTQLpllcHFSETAEGLTTIRAFRHE 1144
Cdd:COG2274 278 LDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVllgLLFQPRLRRLSREESEASAKRQS----LLVETLRGIETIKALGAE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1145 TRFKQRMLELTdtnnIAYLFLSAANRWLEVRTDYLGACIvltasiasisgssnSGLVGLGLLYA---------LTI---- 1211
Cdd:COG2274 354 SRFRRRWENLL----AKYLNARFKLRRLSNLLSTLSGLL--------------QQLATVALLWLgaylvidgqLTLgqli 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1212 -TNYLNWV----VRNLADL--EVQM--GAVKKVNSFLTMESENYEGTmDPSQVPEhwpQEGEIKIHDLCVRYENNLKPVL 1282
Cdd:COG2274 416 aFNILSGRflapVAQLIGLlqRFQDakIALERLDDILDLPPEREEGR-SKLSLPR---LKGDIELENVSFRYPGDSPPVL 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1283 KHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL-- 1360
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItl 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1361 -DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENI 1439
Cdd:COG2274 572 gDPDA--TDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAI 649
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1440 LQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQeNGVFASFVR 1499
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, ... |
945-1226 |
1.60e-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: 258.56 E-value: 1.60e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 945 FLLILMIFskLLKHSVIVAIDYWLATWTSEYSINNTGKADQT-YYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHH 1023
Cdd:cd18603 1 SLLILLLY--LLSQAFSVGSNIWLSEWSDDPALNGTQDTEQRdYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1024 NLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQ 1103
Cdd:cd18603 79 KLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1104 KYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACI 1183
Cdd:cd18603 159 RFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLI 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 530398974 1184 VLTASIASISGSSNSG--LVGLGLLYALTITNYLNWVVRNLADLE 1226
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; ... |
948-1239 |
4.19e-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: 243.14 E-value: 4.19e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 948 ILMIFSKLLKHSVIVAIDYWLATWTSEYSINNTGKADQ---TYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHN 1024
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEvsvLYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1025 LLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQK 1104
Cdd:cd18604 82 LLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1105 YFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACIV 1184
Cdd:cd18604 162 LYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFS 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 530398974 1185 L-TASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFL 1239
Cdd:cd18604 242 FaTAALLVYGPGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1263-1489 |
6.88e-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: 239.82 E-value: 6.88e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1263 GEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1342
Cdd:cd03254 1 GEIEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1343 SIILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 1419
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIrlgRPNA--TDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1420 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1489
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1071-1490 |
2.59e-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: 244.28 E-value: 2.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1071 TLLCLSAIGMISYATPVFLVALLPLGVAF-YFIQKYFRVASKD----LQELDDstqlpllcHFSETAEGLTTIRAFRHET 1145
Cdd:COG4988 146 PLLILVAVFPLDWLSGLILLVTAPLIPLFmILVGKGAAKASRRqwraLARLSG--------HFLDRLRGLTTLKLFGRAK 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1146 RFKQRMLELTDTNNIAYL------FLSAANrwLEVRTdYLGACIVLtasiasisgssnsGLVGLGLLYA-LTITN----- 1213
Cdd:COG4988 218 AEAERIAEASEDFRKRTMkvlrvaFLSSAV--LEFFA-SLSIALVA-------------VYIGFRLLGGsLTLFAalfvl 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1214 ------YLNwvVRNLAdleVQ-------MGAVKKVNSFLTMESEnyegTMDPSQVPEHWPQEGEIKIHDLCVRYENNlKP 1280
Cdd:COG4988 282 llapefFLP--LRDLG---SFyharangIAAAEKIFALLDAPEP----AAPAGTAPLPAAGPPSIELEDVSFSYPGG-RP 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1281 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 1360
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENL 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1361 ---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 1437
Cdd:COG4988 432 rlgRPDA--SDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETE 509
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 530398974 1438 NILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQE 1490
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 |
1.62e-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: 232.76 E-value: 1.62e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 299 LSSTFRYLADLLGFAGPLCISGIVQRVNETQNgtnnttgisetlsskEFLENAYVLAVLLFLALILQRTFLQASYYVTIE 378
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPD---------------EPLSEGYLLALALFLVSLLQSLLLHQYFFLSFR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 379 TGINLRGALLAMIYNKILRLSTSnlSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSALV 458
Cdd:cd18579 66 LGMRVRSALSSLIYRKALRLSSS--ARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 459 GAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTSL 538
Cdd:cd18579 144 GLGVLLLLIPLQAFLAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRAL 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398974 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 ... |
944-1239 |
2.86e-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: 226.64 E-value: 2.86e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 944 FFLLILMIFSKllkhsviVAIDYWLATWTSEYSIN--NTGKADQTYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNL 1021
Cdd:cd18605 5 LLSLILMQASR-------NLIDFWLSYWVSHSNNSffNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1022 HHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYF 1101
Cdd:cd18605 78 HNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1102 IQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGA 1181
Cdd:cd18605 158 IQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGV 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398974 1182 CIV-----LTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFL 1239
Cdd:cd18605 238 LIVtfvalTAVVQHFFGLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
944-1232 |
7.70e-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: 7.70e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 944 FFLLILMIFSKllkhsviVAIDYWLATWTSeysinNTGKADQTYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHH 1023
Cdd:cd18606 5 LLLLILSQFAQ-------VFTNLWLSFWTE-----DFFGLSQGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1024 NLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQ 1103
Cdd:cd18606 73 KALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1104 KYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACI 1183
Cdd:cd18606 153 NYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 530398974 1184 VL--TASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAV 1232
Cdd:cd18606 233 VLivALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSV 283
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1265-1475 |
9.00e-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: 211.47 E-value: 9.00e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1344
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1345 ILQDPILFSGSIRFNLdpeckctddrlwealeiaqlknmvkslpggldavvteggenFSVGQRQLFCLARAFVRKSSILI 1424
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 530398974 1425 MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRG 1475
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
365-605 |
7.21e-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: 7.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 365 QRTFLQASYYVTIETGINLRGALLAMIYNKILRLStsNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMG 444
Cdd:cd18595 51 QSLLLHQYFHRCFRLGMRIRTALTSAIYRKALRLS--NSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 445 VILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMK 524
Cdd:cd18595 129 LYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 525 ELSSLKTFALYTSLSIFMNAAIPIAAVLATFVTHAYASGNN-LKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQ 603
Cdd:cd18595 209 ELKLLKKAAYLNAVSSFLWTCAPFLVSLATFATYVLSDPDNvLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLK 288
|
..
gi 530398974 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, ... |
943-1239 |
1.67e-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: 210.50 E-value: 1.67e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 943 GFFLLILMIFSKLLKHSVIVAIDYWLATW--------------TSEYSINNTGKADQTYYVAGFSILCGAGIFLCLVTSL 1008
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWlkqgsgnttnnvdnSTVDSGNISDNPDLNFYQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1009 TVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVF 1088
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1089 LVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAA 1168
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398974 1169 NRWLEVRTDYLGACIVLTASIASISGSSNS--GLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFL 1239
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLKGSIspAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1265-1496 |
3.76e-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: 3.76e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1344
Cdd:cd03253 1 IEFENVTFAYDPG-RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1345 ILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 1421
Cdd:cd03253 80 VPQDTVLFNDTIGYNIrygRPDA--TDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398974 1422 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAqENGVFAS 1496
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLA-KGGLYAE 231
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1265-1495 |
1.42e-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: 198.99 E-value: 1.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1344
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1345 ILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 1421
Cdd:cd03251 81 VSQDVFLFNDTVAENIaygRPGA--TREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398974 1422 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQeNGVFA 1495
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ-GGVYA 231
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
989-1496 |
1.88e-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: 209.57 E-value: 1.88e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 989 VAGFSILCGAGIFlclVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLT 1068
Cdd:TIGR02203 60 VIGLAVLRGICSF---VSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1069 RSTLLCLSAIGMI---SYATPVFLVALLPL-GVAFYFIQKYFRVASKDLQELD-DSTQLpllchFSETAEGLTTIRAFRH 1143
Cdd:TIGR02203 137 RETLTVIGLFIVLlyySWQLTLIVVVMLPVlSILMRRVSKRLRRISKEIQNSMgQVTTV-----AEETLQGYRVVKLFGG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1144 ETRFKQRmleltdtnniaYLFLSAANRWLEVRTDYLGACI-----VLTASIASISGSSNSGLVGLGLLYALTITNYLNWV 1218
Cdd:TIGR02203 212 QAYETRR-----------FDAVSNRNRRLAMKMTSAGSISspitqLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAM 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1219 ------VRNLADLEVQM----GAVKKVNSFLTMESENYEGTMDPSQVpehwpqEGEIKIHDLCVRYENNLKPVLKHVKAY 1288
Cdd:TIGR02203 281 ialirpLKSLTNVNAPMqrglAAAESLFTLLDSPPEKDTGTRAIERA------RGDVEFRNVTFRYPGRDRPALDSISLV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1289 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPEcK 1365
Cdd:TIGR02203 355 IEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRTE-Q 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1366 CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVM 1445
Cdd:TIGR02203 434 ADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALE 513
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 530398974 1446 TAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQeNGVFAS 1496
Cdd:TIGR02203 514 RLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLAR-NGLYAQ 563
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
368-605 |
3.97e-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: 194.21 E-value: 3.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 368 FLQASYYVTIETGINLRGALLAMIYNKILRLSTSnlSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVIL 447
Cdd:cd18597 59 LLNHFFYRSMLTGAQVRAALTKAIYRKSLRLSGK--SRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIAL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 448 LYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELS 527
Cdd:cd18597 137 LIVNLGPSALVGIGVLILSIPLQGFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELK 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530398974 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 ... |
1280-1500 |
6.17e-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: 6.17e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1280 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFN 1359
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1360 L---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT 1436
Cdd:cd03249 97 IrygKPDA--TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398974 1437 ENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQEnGVFASFVRA 1500
Cdd:cd03249 175 EKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQK-GVYAKLVKA 237
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
367-603 |
6.01e-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: 6.01e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 367 TFLQASYYVTIETGINLRGALLAMIYNKILRL-----------------STSNLSMGEMTLGQINNLVAIETN---QLMW 426
Cdd:cd18596 54 LLDQQYLWIGRRLSVRLRAILTQLIFEKALRRrdksgssksseskkkdkEEDEDEKSSASVGKINNLMSVDANrisEFAA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 427 FLFLcpnLWAMPVQIIMGVILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLK 506
Cdd:cd18596 134 FLHL---LVSAPLQIVIAIVFLYRLLGWSALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIK 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 507 LYAWEHIFCKSVEETRMKELSSLKTFALYTSLSIFMNAAIPIAAVLATFVTHAYASGNNLKPAEAFASLSLFHILVTPLF 586
Cdd:cd18596 211 FFAWERKWEERILEAREEELKWLRKRFLLDLLLSLLWFLIPILVTVVTFATYTLVMGQELTASVAFTSLALFNMLRGPLN 290
|
250
....*....|....*..
gi 530398974 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) ... |
943-1235 |
7.82e-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: 7.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 943 GFFLLILMIFSKLLKHSVIVAIDYWLATWTSEY---------------SINNTGKADQTYYVAGFSILCGAGIFLCLVTS 1007
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLEeklndttdrvqgensTNVDIEDLDRDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1008 LTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPV 1087
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1088 FLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAY-LFLs 1166
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWfLFL- 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398974 1167 AANRWLEVRTDYLGA--CIVLTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKV 1235
Cdd:cd18601 240 ATSRWLAVRLDALCAlfVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERV 310
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
936-1498 |
1.19e-51 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 195.33 E-value: 1.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 936 WRYLTSGGFFLLILMIFSKLLKHSVIVAIDYWLATWTSEYSINNTGKADQTYYVAGFSILCGAGIFLCLvtsltvewMGL 1015
Cdd:TIGR00958 160 WPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNYT--------MAR 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1016 TAAKnLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRS--TLLCLSAIgMIS---YATPVFLV 1090
Cdd:TIGR00958 232 INLR-IREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNlvMLLGLLGF-MLWlspRLTMVTLI 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1091 ALLPLGVAFYFIQKYFRVASKDLQE-LDDSTQLPLlchfsETAEGLTTIRAFRHE----TRFKQ---RMLELTDTNNIAY 1162
Cdd:TIGR00958 310 NLPLVFLAEKVFGKRYQLLSEELQEaVAKANQVAE-----EALSGMRTVRSFAAEegeaSRFKEaleETLQLNKRKALAY 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1163 LFLSAANRWLE----VRTDYLGACIVLTASIASISgssnsgLVGLgLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSF 1238
Cdd:TIGR00958 385 AGYLWTTSVLGmliqVLVLYYGGQLVLTGKVSSGN------LVSF-LLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEY 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1239 L--TMESENyEGTMDPSQVpehwpqEGEIKIHDLCVRYENNL-KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRM 1315
Cdd:TIGR00958 458 LdrKPNIPL-TGTLAPLNL------EGLIEFQDVSFSYPNRPdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNL 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1316 VDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAV 1394
Cdd:TIGR00958 531 YQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLtDTPDEEIMAAAKAANAHDFIMEFPNGYDTE 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1395 VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKvvMTAFADRTVVTIAHRVHTILTADLVIVMKR 1474
Cdd:TIGR00958 611 VGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKK 688
|
570 580
....*....|....*....|....
gi 530398974 1475 GNILEYDTPESLLAQEnGVFASFV 1498
Cdd:TIGR00958 689 GSVVEMGTHKQLMEDQ-GCYKHLV 711
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1263-1491 |
1.30e-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: 1.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1263 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDGKIVIDGIDISKLPLHTLRSRL 1342
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1343 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 1422
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398974 1423 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQEN 1491
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKS 228
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1002-1490 |
3.14e-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: 3.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1002 LCLVTSLTVEWMGLTA-AKNLHHN---LLNKIILG----------------PIRFFDTTPLGLILNRFSADTNIIDQHIP 1061
Cdd:PRK10790 61 LGLVAGLAAAYVGLQLlAAGLHYAqslLFNRAAVGvvqqlrtdvmdaalrqPLSAFDTQPVGQLISRVTNDTEVIRDLYV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1062 PTLESLTRSTLLcLSA--IGMISYATPVFLVALL--PLGVAFYFIQKYF------RVASKdLQELDDStqlpllchFSET 1131
Cdd:PRK10790 141 TVVATVLRSAAL-IGAmlVAMFSLDWRMALVAIMifPAVLVVMVIYQRYstpivrRVRAY-LADINDG--------FNEV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1132 AEGLTTIRAFRHETRFKQRMLELTDTNNIAylflsaanRWLEVRTD--------YLGACIVLTASIASISGSSNSGlVGL 1203
Cdd:PRK10790 211 INGMSVIQQFRQQARFGERMGEASRSHYMA--------RMQTLRLDgfllrpllSLFSALILCGLLMLFGFSASGT-IEV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1204 GLLYALTitNYLNWVVRNLADLE-----VQMGAVKKVNSFLTMESENYEGTMDPSQVpehwpQEGEIKIHDLCVRYENNl 1278
Cdd:PRK10790 282 GVLYAFI--SYLGRLNEPLIELTtqqsmLQQAVVAGERVFELMDGPRQQYGNDDRPL-----QSGRIDIDNVSFAYRDD- 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1279 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRF 1358
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLA 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1359 NLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEN 1438
Cdd:PRK10790 434 NVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQ 513
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 530398974 1439 ILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQE 1490
Cdd:PRK10790 514 AIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQ 565
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1263-1477 |
3.24e-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: 174.31 E-value: 3.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1263 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1342
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1343 SIILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 1419
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNItlgAPLA--DDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 530398974 1420 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNI 1477
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1213-1496 |
1.12e-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: 184.25 E-value: 1.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1213 NYLNWVVR----NLADLEvQMGAVkkvnsfLTMESEnyegTMDPSQVPEHWPQEGEIKIHDLCVRYENNlKPVLKHVKAY 1288
Cdd:COG5265 313 NFLGFVYReirqALADME-RMFDL------LDQPPE----VADAPDAPPLVVGGGEVRFENVSFGYDPE-RPILKGVSFE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1289 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPECk 1365
Cdd:COG5265 381 VPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIaygRPDA- 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1366 cTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVM 1445
Cdd:COG5265 460 -SEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALR 538
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 530398974 1446 TAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQeNGVFAS 1496
Cdd:COG5265 539 EVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQ-GGLYAQ 588
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1239-1502 |
2.66e-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: 184.77 E-value: 2.66e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1239 LTMESENYEGTMDPSQVpehwpqEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDI 1318
Cdd:TIGR03797 432 LEALPEVDEAKTDPGKL------SGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTL----LRLLLG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1319 FD----GKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAV 1394
Cdd:TIGR03797 502 FEtpesGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTV 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1395 VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDmateNILQKVVMTAFA--DRTVVTIAHRVHTILTADLVIVM 1472
Cdd:TIGR03797 582 ISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALD----NRTQAIVSESLErlKVTRIVIAHRLSTIRNADRIYVL 657
|
250 260 270
....*....|....*....|....*....|
gi 530398974 1473 KRGNILEYDTPESLLAQEnGVFASFVRADM 1502
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 |
4.59e-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: 170.81 E-value: 4.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 303 FRYLADLLGFAGPLCISGIVQRVNETQNGTNNTTGISETLSSKEFLenayvlavllflalilqRTFLQASY-YVTIETGI 381
Cdd:cd18598 5 LKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLL-----------------GALLSSHYnFQMNKVSL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 382 NLRGALLAMIYNKILRLSTSnlSMGEMTLGQINNLVAIETNQLMWFlflCPNL---WAMPVQIIMGVILLYNLLGSSALV 458
Cdd:cd18598 68 KVRAALVTAVYRKALRVRSS--SLSKFSTGEIVNLMSTDADRIVNF---CPSFhdlWSLPLQIIVALYLLYQQVGVAFLA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 459 GAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTSL 538
Cdd:cd18598 143 GLVFALVLIPINKWIAKRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDAL 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398974 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 ... |
1273-1498 |
5.55e-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: 5.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1273 RYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILF 1352
Cdd:cd03252 9 RYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1353 SGSIRFNL---DPECKCtdDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEAT 1429
Cdd:cd03252 89 NRSIRDNIalaDPGMSM--ERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398974 1430 ASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAqENGVFASFV 1498
Cdd:cd03252 167 SALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLA-ENGLYAYLY 234
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
1247-1499 |
2.09e-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: 179.37 E-value: 2.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1247 EGTMDPSQVPEHWPQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVID 1326
Cdd:TIGR03796 460 EPEGSAATSEPPRRLSGYVELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFD 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1327 GIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPecKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFS 1403
Cdd:TIGR03796 540 GIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLtlwDP--TIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLS 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1404 VGQRQLFCLARAFVRKSSILIMDEATASIDMATEnilqKVVMTAFADR--TVVTIAHRVHTILTADLVIVMKRGNILEYD 1481
Cdd:TIGR03796 618 GGQRQRLEIARALVRNPSILILDEATSALDPETE----KIIDDNLRRRgcTCIIVAHRLSTIRDCDEIIVLERGKVVQRG 693
|
250
....*....|....*...
gi 530398974 1482 TPESLLAQEnGVFASFVR 1499
Cdd:TIGR03796 694 THEELWAVG-GAYARLIR 710
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
368-605 |
1.66e-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: 1.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 368 FLQASYYVTIETGINLRGALLAMIYNKILRLStsnlSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVIL 447
Cdd:cd18592 55 FFSLTWAISYRTGIRLRGAVLGLLYKKILRLR----SLGDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 448 LYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELS 527
Cdd:cd18592 131 STYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERK 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530398974 528 SLKTFALYTSLSIFMNAAIPIAAVLATFVTHaYASGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 605
Cdd:cd18592 211 ILEKAGYLQSISISLAPIVPVIASVVTFLAH-VALGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1229-1495 |
2.19e-44 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 170.97 E-value: 2.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1229 MGAVKKVNSFLTMESENYEGTMDPSQVpehwpqEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSL 1308
Cdd:PRK11176 312 MAACQTLFAILDLEQEKDEGKRVIERA------KGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTI 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1309 SLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPEC--KCTDDRLWEALEIAQLKNMVKS 1386
Cdd:PRK11176 386 ANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARteQYSREQIEEAARMAYAMDFINK 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1387 LPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTA 1466
Cdd:PRK11176 466 MDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKA 545
|
250 260
....*....|....*....|....*....
gi 530398974 1467 DLVIVMKRGNILEYDTPESLLAQeNGVFA 1495
Cdd:PRK11176 546 DEILVVEDGEIVERGTHAELLAQ-NGVYA 573
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1234-1500 |
1.08e-43 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 168.99 E-value: 1.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1234 KVNSFLTME-----SENYEGTMDPSQVpehwpqEGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSL 1308
Cdd:PRK13657 305 KLEEFFEVEdavpdVRDPPGAIDLGRV------KGAVEFDDVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1309 SLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVK 1385
Cdd:PRK13657 378 INLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIrvgRPDA--TDEEMRAAAERAQAHDFIE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1386 SLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILT 1465
Cdd:PRK13657 456 RKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRN 535
|
250 260 270
....*....|....*....|....*....|....*
gi 530398974 1466 ADLVIVMKRGNILEYDTPESLLAQeNGVFASFVRA 1500
Cdd:PRK13657 536 ADRILVFDNGRVVESGSFDELVAR-GGRFAALLRA 569
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
371-848 |
6.70e-43 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 166.49 E-value: 6.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 371 ASYYVTIETGINLRGALLAMIYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFL-FLCPNLWAMPVQIIMGVILLY 449
Cdd:COG1132 80 LQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFD--RRRTGDLLSRLTNDVDAVEQFLaHGLPQLVRSVVTLIGALVVLF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 450 NLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWE----HIFCKSVEETRMKE 525
Cdd:COG1132 158 VIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREerelERFREANEELRRAN 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 526 LSSLKTFALYTSLSIFMNAAIpIAAVLAtFVTHAYASGNnLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 605
Cdd:COG1132 238 LRAARLSALFFPLMELLGNLG-LALVLL-VGGLLVLSGS-LTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERI 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 606 NEFL-LSDEIGDdswrtGESSLPFesckkhtgvqpktinrkqpgryhldsyeqstrrlrPAETEDIAIK-VTngyFSWGS 683
Cdd:COG1132 315 FELLdEPPEIPD-----PPGAVPL-----------------------------------PPVRGEIEFEnVS---FSYPG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV--------HWSK---------------------- 733
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlidgvdirDLTLeslrrqigvvpqdtflfsgtir 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 734 ---------------YKAVTDACsLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 798
Cdd:COG1132 432 enirygrpdatdeevEEAAKAAQ-AHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTE 510
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 530398974 799 lSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 848
Cdd:COG1132 511 -TEALIQEALERLMKG--RTTIVIAHRLSTIRNADRILVLDDGRIVEQGT 557
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
367-864 |
1.18e-42 |
|
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: 168.09 E-value: 1.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 367 TFLQASYYVTIETGINLRgaLLAMIYNKILRLSTSNL---SMGEMtLGQINNLVAIE---TNQLMWFLFLCPNLWampvq 440
Cdd:COG2274 213 RLLRSYLLLRLGQRIDLR--LSSRFFRHLLRLPLSFFesrSVGDL-ASRFRDVESIReflTGSLLTALLDLLFVL----- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 441 IIMGVILLYNllGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYA--------WEH 512
Cdd:COG2274 285 IFLIVLFFYS--PPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGaesrfrrrWEN 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 513 IFCKSVEetrmKELSSLKTFALYTSLSIFMNAAIPIAAVL--ATFVTHayasgNNLKPAEAFASLSLFHILVTPLF-LLS 589
Cdd:COG2274 363 LLAKYLN----ARFKLRRLSNLLSTLSGLLQQLATVALLWlgAYLVID-----GQLTLGQLIAFNILSGRFLAPVAqLIG 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 590 TVVRFAvKAIISVQKLNEFLlsdeigddswrtgesSLPFEsckkhtgvqpktinrkqpgryhldsyEQSTRRLRPAETED 669
Cdd:COG2274 434 LLQRFQ-DAKIALERLDDIL---------------DLPPE--------------------------REEGRSKLSLPRLK 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 670 IAIKVTNGYFSW-GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV-------------HWSK-- 733
Cdd:COG2274 472 GDIELENVSFRYpGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidlrqidpaSLRRqi 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 734 ------------------------------YKAVTDACsLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 783
Cdd:COG2274 552 gvvlqdvflfsgtirenitlgdpdatdeeiIEAARLAG-LHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNP 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 784 NIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEHW 863
Cdd:COG2274 631 RILILDEATSALDAE-TEAIILENLRRLLKG--RTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELV 707
|
.
gi 530398974 864 K 864
Cdd:COG2274 708 Q 708
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1071-1472 |
1.09e-41 |
|
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: 1.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1071 TLLCLSAIGMISYATPVFLVALLPLgVAFYFIQKYFRVASKDLQELDDSTQLPllCHFSETAEGLTTIRAFRHETRFKQR 1150
Cdd:TIGR02857 132 PLAILAAVFPQDWISGLILLLTAPL-IPIFMILIGWAAQAAARKQWAALSRLS--GHFLDRLRGLPTLKLFGRAKAQAAA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1151 MLELTD--------TNNIAylFLSAANrwLEVRTDyLGACIVLTAsiasisgssnsglVGLGLLY-------ALTI---- 1211
Cdd:TIGR02857 209 IRRSSEeyrertmrVLRIA--FLSSAV--LELFAT-LSVALVAVY-------------IGFRLLAgdldlatGLFVllla 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1212 -TNYLNwvVRNL-ADLEVQMGAVKKVNSFLTMESENyeGTMDPSQVPEHWPQEGEIKIHDLCVRYENNlKPVLKHVKAYI 1289
Cdd:TIGR02857 271 pEFYLP--LRQLgAQYHARADGVAAAEALFAVLDAA--PRPLAGKAPVTAAPASSLEFSGVSVAYPGR-RPALRPVSFTV 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1290 KPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPECkc 1366
Cdd:TIGR02857 346 PPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaRPDA-- 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1367 TDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMT 1446
Cdd:TIGR02857 424 SDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRA 503
|
410 420
....*....|....*....|....*.
gi 530398974 1447 AFADRTVVTIAHRVHTILTADLVIVM 1472
Cdd:TIGR02857 504 LAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
368-606 |
2.71e-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: 151.25 E-value: 2.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 368 FLQASYYVTIETGINLRGALLAMIYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVIL 447
Cdd:cd18594 55 LHHPYFFGLHRYGMQLRIALSSLIYKKTLKLSSSALS--KITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 448 LYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELS 527
Cdd:cd18594 133 LWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 528 SLKTFALYTSLSIFMNAAIPIAAVLATFVTHAyASGNNLKPAEAFASLSLFHILVTPL-FLLSTVVRFAVKAIISVQKLN 606
Cdd:cd18594 213 LIRKAAYIRAFNMAFFFFSPTLVSFATFVPYV-LTGNTLTARKVFTVISLLNALRMTItRFFPESIQTLSESRVSLKRIQ 291
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1021-1500 |
8.46e-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: 156.05 E-value: 8.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1021 LHHNLLNKIILG--------PIRFFDTTPLGLILNRFSADTNIIDqhippTLESLTRSTLLCLSAIGMISYA-----TPV 1087
Cdd:TIGR01193 223 LGQRLSIDIILSyikhlfelPMSFFSTRRTGEIVSRFTDASSIID-----ALASTILSLFLDMWILVIVGLFlvrqnMLL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1088 FLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLpLLCHFSETAEGLTTIRAFRHE-TRFKQ----------RMLELTD 1156
Cdd:TIGR01193 298 FLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAV-LNSSIIEDLNGIETIKSLTSEaERYSKidsefgdylnKSFKYQK 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1157 TNNIAYLFLSAANRWLEVRTDYLGACIVLTASIAsisgssnsglVGLGLLYALTITNYLNwVVRNLADLEVQMGAVK--- 1233
Cdd:TIGR01193 377 ADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLT----------LGQLITFNALLSYFLT-PLENIINLQPKLQAARvan 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1234 -KVNSFLTMESE-NYEGTMDPSQVPEhwpqeGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLA 1311
Cdd:TIGR01193 446 nRLNEVYLVDSEfINKKKRTELNNLN-----GDIVINDVSYSYGYG-SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKL 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1312 FFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL--DPECKCTDDRLWEALEIAQLKNMVKSLPG 1389
Cdd:TIGR01193 520 LVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLllGAKENVSQDEIWAACEIAEIKDDIENMPL 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1390 GLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEnilQKVV--MTAFADRTVVTIAHRVHTILTAD 1467
Cdd:TIGR01193 600 GYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE---KKIVnnLLNLQDKTIIFVAHRLSVAKQSD 676
|
490 500 510
....*....|....*....|....*....|...
gi 530398974 1468 LVIVMKRGNILEYDTPESLLAQeNGVFASFVRA 1500
Cdd:TIGR01193 677 KIIVLDHGKIIEQGSHDELLDR-NGFYASLIHN 708
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1260-1459 |
2.89e-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: 2.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1260 PQEGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLR 1339
Cdd:TIGR02868 330 LGKPTLELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1340 SRLSIILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAF 1416
Cdd:TIGR02868 409 RRVSVCAQDAHLFDTTVRENLrlaRPDA--TDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARAL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 530398974 1417 VRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR 1459
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
667-856 |
9.36e-37 |
|
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: 147.60 E-value: 9.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 667 TEDIAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV-------------HWSK 733
Cdd:COG4988 332 AGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingvdlsdldpaSWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 734 Y-------------------------------KAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQN 782
Cdd:COG4988 412 QiawvpqnpylfagtirenlrlgrpdasdeelEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRD 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398974 783 TNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKD 856
Cdd:COG4988 492 APLLLLDEPTAHLDAE-TEAEILQALRRLAKG--RTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1230-1500 |
1.08e-36 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 148.07 E-value: 1.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1230 GAVKKVNSFLTMESEnyegTMDPSQVPEHWPQEGEIKIHDLCVrYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLS 1309
Cdd:PRK11174 319 GAAESLVTFLETPLA----HPQQGEKELASNDPVTIEAEDLEI-LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1310 ---LAFFRmvdiFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNM 1383
Cdd:PRK11174 394 nalLGFLP----YQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVllgNPDA--SDEQLQQALENAWVSEF 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1384 VKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTI 1463
Cdd:PRK11174 468 LPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDL 547
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 530398974 1464 LTADLVIVMKRGNILE---YDTpeslLAQENGVFASFVRA 1500
Cdd:PRK11174 548 AQWDQIWVMQDGQIVQqgdYAE----LSQAGGLFATLLAH 583
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
672-841 |
1.89e-35 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 132.89 E-value: 1.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSWGSGLA-TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKykavTDACSLQPD---- 746
Cdd:cd03228 1 IEFKNVSFSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDG----VDLRDLDLEslrk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 747 -IDLLP-----FGDqTeIGErgiN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTL 819
Cdd:cd03228 77 nIAYVPqdpflFSG-T-IRE---NiLSGGQRQRIAIARALLRDPPILILDEATSALDPE-TEALILEALRALAKG--KTV 148
|
170 180
....*....|....*....|..
gi 530398974 820 VLVTHKLQYLTHADWIIAMKDG 841
Cdd:cd03228 149 IVIAHRLSTIRDADRIIVLDDG 170
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1260-1495 |
1.90e-35 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 143.81 E-value: 1.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1260 PQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLR 1339
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1340 SRLSIILQDPILFSGSIRFNL---DPEckCTDDRLWEALEIAQLKNMVKSlPGGLDAVVTEGGENFSVGQRQLFCLARAF 1416
Cdd:PRK11160 414 QAISVVSQRVHLFSATLRDNLllaAPN--ASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARAL 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1417 VRKSSILIMDEATASIDMATEN-ILQkVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQENGVFA 1495
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERqILE-LLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQ 569
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1253-1477 |
4.91e-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: 4.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1253 SQVPEHWpqEGEIKIHDLCVRYENNL-KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIS 1331
Cdd:cd03248 2 SLAPDHL--KGIVKFQNVTFAYPTRPdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1332 KLPLHTLRSRLSIILQDPILFSGSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLF 1410
Cdd:cd03248 80 QYEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQsCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398974 1411 CLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNI 1477
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1265-1477 |
1.30e-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: 1.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAffrMVDIF---DGKIVIDGIDISKLPLHTLRSR 1341
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARL---ILGLLrptSGRVRLDGADISQWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1342 LSIILQDPILFSGSIRFNLdpeckctddrlwealeiaqlknmvkslpggldavvteggenFSVGQRQLFCLARAFVRKSS 1421
Cdd:cd03246 78 VGYLPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 530398974 1422 ILIMDEATASIDMATEN-ILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNI 1477
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 |
1.68e-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: 131.57 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 372 SYYVTIETGINLRGALLAMIYNKILRLSTSnlSMGEMTLGQINNLVAIETNQL-MWFLFLcPNLWAMPVQIIMGVILLYN 450
Cdd:cd18593 60 YFFGMQRIGMRLRVACSSLIYRKALRLSQA--ALGKTTVGQIVNLLSNDVNRFdQAVLFL-HYLWVAPLQLIAVIYILWF 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 451 LLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLK 530
Cdd:cd18593 137 EIGWSCLAGLAVLLILIPLQSFFGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVR 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 530398974 531 TFALYTSlsifMNAAIPIAA----VLATFVTHAYaSGNNLKPAEAFASLSLFH 579
Cdd:cd18593 217 RTSFLRA----LNMGLFFVSskliLFLTFLAYIL-LGNILTAERVFVTMALYN 264
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1265-1489 |
3.55e-33 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 136.77 E-value: 3.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCvrYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1344
Cdd:PRK10789 316 VNIRQFT--YPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1345 ILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSIL 1423
Cdd:PRK10789 394 VSQTPFLFSDTVANNIALGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398974 1424 IMDEATASIDMATE-NILQKVVMTAfADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1489
Cdd:PRK10789 474 ILDDALSAVDGRTEhQILHNLRQWG-EGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQ 539
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
688-892 |
1.44e-32 |
|
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: 128.82 E-value: 1.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS------------------------------KYKAV 737
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSgrisfssqfswimpgtikeniifgvsydeyRYKSV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 738 TDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDdkR 817
Cdd:cd03291 133 VKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMAN--K 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 818 TLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEHwktLMNRQdqelekdmEADQTTLERK------TLR 891
Cdd:cd03291 211 TRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSK---LMGYD--------TFDQFSAERRnsilteTLR 279
|
.
gi 530398974 892 R 892
Cdd:cd03291 280 R 280
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1265-1479 |
2.02e-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: 121.65 E-value: 2.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPlHTLRSRLSI 1344
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1345 ILQDPILFSGSIRFNLdpeckctddrlwealeiaqlknmvkslpggldavvtegGENFSVGQRQLFCLARAFVRKSSILI 1424
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 530398974 1425 MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILE 1479
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
651-848 |
5.28e-31 |
|
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: 130.27 E-value: 5.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 651 HLDSYEQSTRRL------RPAETE---------DIAIKVTNGYFSW-GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSL 714
Cdd:COG4987 298 HLGRVRAAARRLnelldaPPAVTEpaepapapgGPSLELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 715 LLAILGEMQTLEGKVHWSKY--------------------------------------------KAVTDACSLQPDIDLL 750
Cdd:COG4987 378 LALLLRFLDPQSGSITLGGVdlrdldeddlrrriavvpqrphlfdttlrenlrlarpdatdeelWAALERVGLGDWLAAL 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 751 PFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDdkRTLVLVTHKLQYLT 830
Cdd:COG4987 458 PDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLAD-LLEALAG--RTVLLITHRLAGLE 534
|
250
....*....|....*...
gi 530398974 831 HADWIIAMKDGSVLREGT 848
Cdd:COG4987 535 RMDRILVLEDGRIVEQGT 552
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1265-1490 |
1.86e-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: 120.90 E-value: 1.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1344
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1345 ILQDPI--LFSGSIR---------FNLDPECkcTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLA 1413
Cdd:COG1122 80 VFQNPDdqLFAPTVEedvafgpenLGLPREE--IRERVEEALELVGLEHLADRPPHEL-----------SGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398974 1414 RAFVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLAQE 1490
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDpRGRRELLELLKRLNKEGKTVIIVTHDLDLVAeLADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
947-1185 |
3.07e-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: 121.60 E-value: 3.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 947 LILMIFSKLLKHSVIVAIDYWLATWTSEYS-INNTGKADQTYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNL 1025
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLpDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1026 LNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQKY 1105
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1106 FRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACIVL 1185
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1266-1475 |
3.47e-30 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 117.35 E-value: 3.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1266 KIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSII 1345
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1346 LQdpilfsgsirfnldpeckctddrlwealeiaqlknmvkslpggldavvteggenFSVGQRQLFCLARAFVRKSSILIM 1425
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 530398974 1426 DEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTILTA-DLVIVMKRG 1475
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1265-1475 |
4.95e-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: 4.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENN---LKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIvidgidisklplhTLRSR 1341
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1342 LSIILQDPILFSGSIRFN------LDPEckctddRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARA 1415
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENilfgkpFDEE------RYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398974 1416 FVRKSSILIMDEATASIDMATEN-ILQKVVMTAFAD-RTVVTIAHRVHTILTADLVIVMKRG 1475
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRhIFENCILGLLLNnKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
672-864 |
6.06e-30 |
|
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: 119.64 E-value: 6.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV---------------------- 729
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSIlidgqdirevtldslrraigvv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 730 ------------HWSKYK--AVTD--------ACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVF 787
Cdd:cd03253 81 pqdtvlfndtigYNIRYGrpDATDeevieaakAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398974 788 LDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEHWK 864
Cdd:cd03253 161 LDEATSALDTH-TEREIQAALRDVSKG--RTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWK 234
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
673-841 |
3.68e-29 |
|
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: 114.65 E-value: 3.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 673 KVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKykavtdacslQPDIDLLPF 752
Cdd:cd00267 1 EIENLSFRYGGRTA-LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG----------KDIAKLPLE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 753 GDQTEIGERGiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTHA 832
Cdd:cd00267 70 ELRRRIGYVP-QLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLE--LLRELAEEGRTVIIVTHDPELAELA 146
|
170
....*....|
gi 530398974 833 -DWIIAMKDG 841
Cdd:cd00267 147 aDRVIVLKDG 156
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
673-847 |
3.76e-29 |
|
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: 115.23 E-value: 3.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 673 KVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH--------WSkYKAVTDACSLQ 744
Cdd:cd03214 1 EVENLSVGYGGRTV-LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILldgkdlasLS-PKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 745 P----DIDLLPFGDqteigeRGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDK-RT 818
Cdd:cd03214 79 PqaleLLGLAHLAD------RPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLE--LLRRLARERgKT 150
|
170 180 190
....*....|....*....|....*....|
gi 530398974 819 LVLVTHKL-QYLTHADWIIAMKDGSVLREG 847
Cdd:cd03214 151 VVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
712-1499 |
4.92e-29 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 127.07 E-value: 4.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 712 SSLLLAILGEMQTLEGK--VHWSKYKAVTDACSLQPDidllpfGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 789
Cdd:PTZ00265 531 SNELIEMRKNYQTIKDSevVDVSKKVLIHDFVSALPD------KYETLVGSNASKLSGGQKQRISIARAIIRNPKILILD 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 790 DPFSALDiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAMK--------DGSVLREGTLKDIQTKD----- 856
Cdd:PTZ00265 605 EATSSLD-NKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLSnrergstvDVDIIGEDPTKDNKENNnknnk 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 857 ---------------------VELYEH----------WKTLMNRQ----------DQELEKDM------------EADQT 883
Cdd:PTZ00265 684 ddnnnnnnnnnnkinnagsyiIEQGTHdalmknkngiYYTMINNQkvsskkssnnDNDKDSDMkssaykdsergyDPDEM 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 884 TLERKTLRRAMySREAKAQMEDEDEEEEEEEDEDDNMSTVMRLRTKMP------WKTCWRY-----------LTSGGFFL 946
Cdd:PTZ00265 764 NGNSKHENESA-SNKKSCKMSDENASENNAGGKLPFLRNLFKRKPKAPnnlrivYREIFSYkkdvtiialsiLVAGGLYP 842
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 947 LILMIFSKLlkhsVIVAIDYW-LATWTSEYSInntgkadqtyyvagFSILCGAGIFLC-LVTSLTVEWMGLTAAKNLHHN 1024
Cdd:PTZ00265 843 VFALLYAKY----VSTLFDFAnLEANSNKYSL--------------YILVIAIAMFISeTLKNYYNNVIGEKVEKTMKRR 904
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1025 LLNKIILGPIRFFDT---TPlGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVflVALLPLGVAFYF 1101
Cdd:PTZ00265 905 LFENILYQEISFFDQdkhAP-GLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPI--VAAVLTGTYFIF 981
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1102 IqKYFRV-----ASKDLQELDDSTQLPLLCHFS-------------ETAEGLTTIRAFRHETRFKQRMLELTDTNN---- 1159
Cdd:PTZ00265 982 M-RVFAIrarltANKDVEKKEINQPGTVFAYNSddeifkdpsfliqEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNkgqk 1060
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1160 --------------IAYLFLSAANRW----------LEVrTDYLGAciVLTASIASISGSSNSGLVGLGLLYALTITNYL 1215
Cdd:PTZ00265 1061 rktlvnsmlwgfsqSAQLFINSFAYWfgsflirrgtILV-DDFMKS--LFTFLFTGSYAGKLMSLKGDSENAKLSFEKYY 1137
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1216 NWVVRNlADLEVQ-MGAVKKVNSFLTmesenyegtmdpsqvpehwpqEGEIKIHDLCVRYENNLK-PVLKHVKAYIKPGQ 1293
Cdd:PTZ00265 1138 PLIIRK-SNIDVRdNGGIRIKNKNDI---------------------KGKIEIMDVNFRYISRPNvPIYKDLTFSCDSKK 1195
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1294 KVGICGRTGSGKSSLSLAFFRMVDIFD----------------------------------------------------- 1320
Cdd:PTZ00265 1196 TTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfkn 1275
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1321 -GKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEG 1398
Cdd:PTZ00265 1276 sGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKfGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPY 1355
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1399 GENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVV--MTAFADRTVVTIAHRVHTILTADLVIVM---- 1472
Cdd:PTZ00265 1356 GKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdIKDKADKTIITIAHRIASIKRSDKIVVFnnpd 1435
|
970 980
....*....|....*....|....*...
gi 530398974 1473 KRGNILE-YDTPESLLAQENGVFASFVR 1499
Cdd:PTZ00265 1436 RTGSFVQaHGTHEELLSVQDGVYKKYVK 1463
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
303-605 |
1.04e-28 |
|
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: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 303 FRYLADLLGFAGPLCISGIVQRVNETQngtnnttgisetlsskEFLENAYVLAVLLFLALILQRTFLQASYYVTIETGIN 382
Cdd:cd18559 5 IKLVLCNHVFSGPSNLWLLLWFDDPVN----------------GPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 383 LRGALLAMIYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSALVGAAV 462
Cdd:cd18559 69 ASRAVHLDLYHKALRSPISFFE--RTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 463 IVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTSLSIFM 542
Cdd:cd18559 147 GLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRL 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398974 543 NAAIPIAAVLATFVTHAYASGNN-LKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 605
Cdd:cd18559 227 WCVGPCIVLFASFFAYVSRHSLAgLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1265-1489 |
1.67e-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: 118.85 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI---FDGKIVIDGIDISKLPLHTLRSR 1341
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1342 LSIILQDPI--LFSGSIRFNLD--PECKCTD-----DRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCL 1412
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGDQIAeaLENLGLSraearARVLELLEAVGLERRLDRYPHQL-----------SGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1413 ARAFVRKSSILIMDEATASIDMATenilQKVVMTAFAD------RTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPES 1485
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTT----QAEILDLLRElqrergTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEE 229
|
....
gi 530398974 1486 LLAQ 1489
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 ... |
1266-1475 |
2.21e-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: 2.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1266 KIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSII 1345
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1346 LQDP--ILFSGSIR----FNLDPECKCTDD---RLWEALEIAQLKNMVKSLPggldavvteggENFSVGQRQLFCLARAF 1416
Cdd:cd03225 81 FQNPddQFFGPTVEeevaFGLENLGLPEEEieeRVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398974 1417 VRKSSILIMDEATASIDMATENILQKVVmTAFADR--TVVTIAHRVHTILT-ADLVIVMKRG 1475
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELL-KKLKAEgkTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1265-1480 |
2.96e-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: 111.44 E-value: 2.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTL---R 1339
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1340 SRLSIILQDPILfsgsirfNLDP------------ECKCTDDRLWEALEIAQLKNMVKSLPGG-LDAVVTEggenFSVGQ 1406
Cdd:cd03257 82 KEIQMVFQDPMS-------SLNPrmtigeqiaeplRIHGKLSKKEARKEAVLLLLVGVGLPEEvLNRYPHE----LSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398974 1407 RQLFCLARAFVRKSSILIMDEATASIDMATE-NILQkvVMTAFADR---TVVTIAHRVHTIL-TADLVIVMKRGNILEY 1480
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQaQILD--LLKKLQEElglTLLFITHDLGVVAkIADRVAVMYAGKIVEE 227
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1262-1489 |
1.07e-26 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 116.77 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1262 EGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAffrMVDIFD---GKIVIDGIDISKLPlhtl 1338
Cdd:COG4618 328 KGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARL---LVGVWPptaGSVRLDGADLSQWD---- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1339 RSRLSIIL----QDPILFSGSI-----RFNlDPeckcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQL 1409
Cdd:COG4618 401 REELGRHIgylpQDVELFDGTIaeniaRFG-DA----DPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1410 FCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLA 1488
Cdd:COG4618 476 IGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
.
gi 530398974 1489 Q 1489
Cdd:COG4618 556 R 556
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
688-860 |
1.90e-26 |
|
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: 110.13 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHW-----SKYKA---------VTDACSLQPDI---DLL 750
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdgrdlASLSRrelarriayVPQEPPAPFGLtvrELV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 751 ---------PFG--------------DQTEIG---ERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlsdHl 803
Cdd:COG1120 97 algryphlgLFGrpsaedreaveealERTGLEhlaDRPVDeLSGGERQRVLIARALAQEPPLLLLDEPTSHLDLA---H- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398974 804 mQEGILKFLQD----DKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREGTLKDIQTKDV--ELY 860
Cdd:COG1120 173 -QLEVLELLRRlareRGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEVLTPELleEVY 235
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1265-1486 |
2.90e-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: 2.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIF-----DGKIVIDGIDISKLPLH--T 1337
Cdd:cd03260 1 IELRDLNVYYGD--KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDVDvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1338 LRSRLSIILQDPILFSGSIRFNLD--------PECKCTDDRLWEALEIAQLKNMVKSLPGGLDavvteggenFSVGQRQL 1409
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAyglrlhgiKLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398974 1410 FCLARAFVRKSSILIMDEATASID-MATENIlQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESL 1486
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDpISTAKI-EELIAELKKEYTIVIVTHNMQQAArVADRTAFLLNGRLVEFGPTEQI 227
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
672-861 |
3.44e-26 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 109.02 E-value: 3.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI--LGEMQtlEGKVHWSKyKAVTDACSLQ----- 744
Cdd:COG4604 2 IEIKNVSKRYG-GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMIsrLLPPD--SGEVLVDG-LDVATTPSRElakrl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 745 ------PDI-------DLLPFG------------DQ------------TEIGERGIN-LSGGQRQRICVARALYQNTNIV 786
Cdd:COG4604 78 ailrqeNHInsrltvrELVAFGrfpyskgrltaeDReiideaiayldlEDLADRYLDeLSGGQRQRAFIAMVLAQDTDYV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398974 787 FLDDPFSALDIHLSDHLMQegILKFLQDDK-RTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQTKDV--ELYE 861
Cdd:COG4604 158 LLDEPLNNLDMKHSVQMMK--LLRRLADELgKTVVIVLHDINFASCyADHIVAMKDGRVVAQGTPEEIITPEVlsDIYD 234
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
371-585 |
4.95e-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: 109.27 E-value: 4.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 371 ASYYVTIETGINLRGALLAMIYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYN 450
Cdd:pfam00664 60 LQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMF 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 451 LLG-SSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSL 529
Cdd:pfam00664 138 YYGwKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAG 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 530398974 530 KTFALYTSLSI-FMNAAIPIAAVLATFVTHAYASGNNLKPAEAFASLSLFHILVTPL 585
Cdd:pfam00664 218 IKKAVANGLSFgITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
966-1233 |
5.25e-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: 5.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 966 YWLATWTSEysiNNTGKADQTY-YVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGL 1044
Cdd:cd18559 20 LWLLLWFDD---PVNGPQEHGQvYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1045 ILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVAlLPLGVAFYFIQKYFRVASKDLQELDDSTQLPL 1124
Cdd:cd18559 97 LVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVG-IPLGLLYVPVNRVYAASSRQLKRLESVSKDPR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1125 LCHFSETAEGLTTIRAFRHETRFKQRMLELTDtNNIAYLFLSAANRWLEVRTDYLGACIV-LTASIASISGSSNSGLVGL 1203
Cdd:cd18559 176 YKLFNETLLGISVIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVRLWCVGPCIVlFASFFAYVSRHSLAGLVAL 254
|
250 260 270
....*....|....*....|....*....|
gi 530398974 1204 GLLYALTITNYLNWVVRNLADLEVQMGAVK 1233
Cdd:cd18559 255 KVFYSLALTTYLNWPLNMSPEVITNIVAAE 284
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
688-843 |
7.19e-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: 105.76 E-value: 7.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV----------HWSKYKAVTdACSLQpDIDLLPfGDQTE 757
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrldgadisqwDPNELGDHV-GYLPQ-DDELFS-GSIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 758 IgergInLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTHADWIIA 837
Cdd:cd03246 95 N----I-LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQ--AIAALKAAGATRIVIAHRPETLASADRILV 167
|
....*.
gi 530398974 838 MKDGSV 843
Cdd:cd03246 168 LEDGRV 173
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
682-848 |
1.25e-25 |
|
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: 106.93 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 682 GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLL-------------------------LAILGEM------------QT 724
Cdd:cd03251 12 GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVnliprfydvdsgrilidghdvrdytLASLRRQiglvsqdvflfnDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 725 LEGKVHWSKYKA----VTDA---CSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 797
Cdd:cd03251 92 VAENIAYGRPGAtreeVEEAaraANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 530398974 798 HlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 848
Cdd:cd03251 172 E-SERLVQAALERLMKN--RTTFVIAHRLSTIENADRIVVLEDGKIVERGT 219
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
673-841 |
1.82e-25 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 105.63 E-value: 1.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 673 KVTNGYFSWGSGL-ATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKyKAVTDACSLQ------- 744
Cdd:cd03225 1 ELKNLSFSYPDGArPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDG-KDLTKLSLKElrrkvgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 745 ----PD--------IDLLPFG------DQTEIGER--------GI---------NLSGGQRQRICVARALYQNTNIVFLD 789
Cdd:cd03225 80 vfqnPDdqffgptvEEEVAFGlenlglPEEEIEERveealelvGLeglrdrspfTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 530398974 790 DPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYL-THADWIIAMKDG 841
Cdd:cd03225 160 EPTAGLDPAGRRELLE--LLKKLKAEGKTIIIVTHDLDLLlELADRVIVLEDG 210
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
667-862 |
2.61e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 106.33 E-value: 2.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 667 TEDIAIKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKYKA---------- 736
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPV-LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPrrarrrigyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 737 -------------VTD--ACSLQPDIDLLPFGDQTE--------------------IGErginLSGGQRQRICVARALYQ 781
Cdd:COG1121 81 pqraevdwdfpitVRDvvLMGRYGRRGLFRRPSRADreavdealervgledladrpIGE----LSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 782 NTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYL-THADWIIAMKDGsVLREGTLKDIQTKDV--E 858
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYE--LLRELRREGKTILVVTHDLGAVrEYFDRVLLLNRG-LVAHGPPEEVLTPENlsR 233
|
....
gi 530398974 859 LYEH 862
Cdd:COG1121 234 AYGG 237
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
932-1239 |
5.59e-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: 107.58 E-value: 5.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 932 WKTCWRYLTSGGFFLLILmIFSKLLKHSVIVAIDYWLATWTSEYSINNTGKAD---QTY---------------YVAGFS 993
Cdd:cd18600 3 WNTYLRYITSHKSLIFVL-ILCLVIFAIEVAASLVGLWLLRSQADRVNTTRPEsssNTYavivtftssyyvfyiYVGVAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 994 ILCGAGIF--LCLVTSLtvewmgLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRST 1071
Cdd:cd18600 82 SLLAMGFFrgLPLVHTL------ITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1072 LLCLSAIGMISYATPVFLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRM 1151
Cdd:cd18600 156 LIVIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1152 LELTDTNNIAYLFLSAANRWLEVRTDYLGAC-IVLTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMG 1230
Cdd:cd18600 236 HKALNLHTANWFLYLSTLRWFQMRIEMIFVIfFTAVTFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMR 315
|
....*....
gi 530398974 1231 AVKKVNSFL 1239
Cdd:cd18600 316 SVSRIFKFI 324
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1282-1430 |
7.04e-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: 101.96 E-value: 7.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1282 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSG-SIRFNL 1360
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398974 1361 DPECKCT-------DDRLWEALEiaQLknmvkSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA 1430
Cdd:pfam00005 81 RLGLLLKglskrekDARAEEALE--KL-----GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
682-843 |
1.11e-24 |
|
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: 110.61 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 682 GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV--------HWskykavtDACSLQP-------D 746
Cdd:COG4618 342 GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsQW-------DREELGRhigylpqD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 747 IDLLP---------FGD--------------------------QTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 791
Cdd:COG4618 415 VELFDgtiaeniarFGDadpekvvaaaklagvhemilrlpdgyDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 530398974 792 FSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSV 843
Cdd:COG4618 495 NSNLDDEGEAALAA--AIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
688-848 |
1.25e-24 |
|
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: 104.16 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAIL-------GEMqTLEGK------VHW----------------------- 731
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLErfydptsGEI-LLDGVdirdlnLRWlrsqiglvsqepvlfdgtiaeni 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 732 --SKYKA----VTDACSL---QPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDH 802
Cdd:cd03249 98 ryGKPDAtdeeVEEAAKKaniHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE-SEK 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 530398974 803 LMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 848
Cdd:cd03249 177 LVQEALDRAMKG--RTTIVIAHRLSTIRNADLIAVLQNGQVVEQGT 220
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
672-848 |
1.29e-24 |
|
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: 103.84 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV------------HW-------- 731
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgidirdisrKSlrsmigvv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 732 ---------------------SKYKAVTDACS---LQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVF 787
Cdd:cd03254 83 lqdtflfsgtimenirlgrpnATDEEVIEAAKeagAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398974 788 LDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 848
Cdd:cd03254 163 LDEATSNIDTE-TEKLIQEALEKLMKG--RTSIIIAHRLSTIKNADKILVLDDGKIIEEGT 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1265-1491 |
1.44e-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: 104.17 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHtLRSRLSI 1344
Cdd:COG4555 2 IEVENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1345 ILQDPILFSG-SIRFNLDPECKCTDDRLWEALEIAQlkNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSIL 1423
Cdd:COG4555 79 LPDERGLYDRlTVRENIRYFAELYGLFDEELKKRIE--ELIELL--GLEEFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1424 IMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLAQEN 1491
Cdd:COG4555 155 LLDEPTNGLDvMARRLLREILRALKKEGKTVLFSSHIMQEVEaLCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
686-847 |
3.49e-24 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 102.28 E-value: 3.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 686 ATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHW---------------------------------- 731
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdgtdirqldpadlrrnigyvpqdvtlfygtlrdn 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 732 --SKYKAVTDACSLQ--------PDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD 801
Cdd:cd03245 98 itLGAPLADDERILRaaelagvtDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 530398974 802 HLMQEgiLKFLQDDKrTLVLVTHKLQYLTHADWIIAMKDGSVLREG 847
Cdd:cd03245 178 RLKER--LRQLLGDK-TLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1265-1489 |
5.00e-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: 108.07 E-value: 5.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNLK---PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTL 1338
Cdd:COG1123 261 LEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1339 RSRLSIILQDPilfSGSirfnLDPECKCTDDrLWEALEI------AQLKNMVKSLpggLDAVvteG----------GEnF 1402
Cdd:COG1123 341 RRRVQMVFQDP---YSS----LNPRMTVGDI-IAEPLRLhgllsrAERRERVAEL---LERV---GlppdladrypHE-L 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1403 SVGQRQLFCLARAFVRKSSILIMDEATASIDMATenilQKVVMTAFAD------RTVVTIAHRVHTILT-ADLVIVMKRG 1475
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALDVSV----QAQILNLLRDlqrelgLTYLFISHDLAVVRYiADRVAVMYDG 481
|
250
....*....|....
gi 530398974 1476 NILEYDTPESLLAQ 1489
Cdd:COG1123 482 RIVEDGPTEEVFAN 495
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1265-1488 |
5.34e-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: 102.57 E-value: 5.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYE--NNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1342
Cdd:COG1124 2 LEVRNLSVSYGqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1343 SIILQDPIlfsGSI--RFNLDpeckctdDRLWEALEIAQLKNMVKSLPGGLDAVvteG-GENF--------SVGQRQLFC 1411
Cdd:COG1124 82 QMVFQDPY---ASLhpRHTVD-------RILAEPLRIHGLPDREERIAELLEQV---GlPPSFldryphqlSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1412 LARAFVRKSSILIMDEATASIDMATE----NILQKvvMTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESL 1486
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQaeilNLLKD--LREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADL 226
|
..
gi 530398974 1487 LA 1488
Cdd:COG1124 227 LA 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
688-847 |
7.70e-24 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 100.08 E-value: 7.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKYKAVTDACSLQPDIDLL---PFGDQTEIGER-GI 763
Cdd:cd03247 18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLnqrPYLFDTTLRNNlGR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 764 NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMqEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSV 843
Cdd:cd03247 98 RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLL-SLIFEVLKD--KTLIWITHHLTGIEHMDKILFLENGKI 174
|
....
gi 530398974 844 LREG 847
Cdd:cd03247 175 IMQG 178
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
672-852 |
8.22e-24 |
|
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: 101.64 E-value: 8.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS----KYKAVTDACSL---- 743
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDgkdiTKKNLRELRRKvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 744 --QPDI---------DLLpFG------DQTEIGER--------GI---------NLSGGQRQRICVARALYQNTNIVFLD 789
Cdd:COG1122 81 fqNPDDqlfaptveeDVA-FGpenlglPREEIRERveealelvGLehladrpphELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398974 790 DPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDI 852
Cdd:COG1122 160 EPTAGLDPRGRRELLE--LLKRLNKEGKTVIIVTHDLDLVAeLADRVIVLDDGRIVADGTPREV 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
652-838 |
1.32e-23 |
|
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: 106.99 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 652 LDSYEQSTRRLRPA-ETEDIAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV- 729
Cdd:TIGR02857 301 LDAAPRPLAGKAPVtAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIa 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 730 ------------HWSKY-------------------------------KAVTDACSLQPDIDLLPFGDQTEIGERGINLS 766
Cdd:TIGR02857 381 vngvpladadadSWRDQiawvpqhpflfagtiaenirlarpdasdaeiREALERAGLDEFVAALPQGLDTPIGEGGAGLS 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398974 767 GGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAM 838
Cdd:TIGR02857 461 GGQAQRLALARAFLRDAPLLLLDEPTAHLDAE-TEAEVLEALRALAQG--RTVLLVTHRLALAALADRIVVL 529
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1265-1491 |
1.61e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 101.99 E-value: 1.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1344
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1345 ILQDPI-LFSGS-----IRFNLdpECKCTD-----DRLWEALEIAQLKNMVKSLPggldavvteggENFSVGQRQLFCLA 1413
Cdd:PRK13632 88 IFQNPDnQFIGAtveddIAFGL--ENKKVPpkkmkDIIDDLAKKVGMEDYLDKEP-----------QNLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1414 RAFVRKSSILIMDEATASID-MATENILQKVV-MTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQEN 1491
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDpKGKREIKKIMVdLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
687-855 |
1.68e-23 |
|
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: 106.66 E-value: 1.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 687 TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV--------HWSKYKAVTDACSLQPDIDL--------- 749
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVrldgadlkQWDRETFGKHIGYLPQDVELfpgtvaeni 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 750 ---------------------------LPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDH 802
Cdd:TIGR01842 413 arfgenadpekiieaaklagvhelilrLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQA 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 530398974 803 LMQEgiLKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTK 855
Cdd:TIGR01842 493 LANA--IKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
672-843 |
3.80e-23 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 97.85 E-value: 3.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKYKAVTDACSLQPDIDLLP 751
Cdd:cd03230 1 IEVRNLSKRYGKKTA-LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 752 -----FGDQTeiGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKL 826
Cdd:cd03230 80 eepslYENLT--VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWE--LLRELKKEGKTILLSSHIL 155
|
170
....*....|....*...
gi 530398974 827 QYL-THADWIIAMKDGSV 843
Cdd:cd03230 156 EEAeRLCDRVAILNNGRI 173
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1265-1491 |
7.25e-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: 7.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAffRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1342
Cdd:COG1120 2 LEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLlrALA--GLLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1343 SIILQDPIL-FSGSIR--------------FNLDPEckctDDRL-WEALE---IAQLKN-MVKSLPGGldavvteggenf 1402
Cdd:COG1120 78 AYVPQEPPApFGLTVRelvalgryphlglfGRPSAE----DREAvEEALErtgLEHLADrPVDELSGG------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1403 svgQRQLFCLARAFVRKSSILIMDEATASIDMA----TENILQKvvMTAFADRTVVTIAHRV-HTILTADLVIVMKRGNI 1477
Cdd:COG1120 142 ---ERQRVLIARALAQEPPLLLLDEPTSHLDLAhqleVLELLRR--LARERGRTVVMVLHDLnLAARYADRLVLLKDGRI 216
|
250
....*....|....
gi 530398974 1478 LEYDTPESLLAQEN 1491
Cdd:COG1120 217 VAQGPPEEVLTPEL 230
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
674-846 |
8.45e-23 |
|
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: 98.31 E-value: 8.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 674 VTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH----------------------- 730
Cdd:cd03293 6 VSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvtgpgpdrgyvfqqdall 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 731 -WskyKAVTDACSLQPDIDLLPFGDQTEIGERGIN--------------LSGGQRQRICVARALYQNTNIVFLDDPFSAL 795
Cdd:cd03293 86 pW---LTVLDNVALGLELQGVPKAEARERAEELLElvglsgfenayphqLSGGMRQRVALARALAVDPDVLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 530398974 796 DiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQ---YLthADWIIAM--KDGSVLRE 846
Cdd:cd03293 163 D-ALTREQLQEELLDIWRETGKTVLLVTHDIDeavFL--ADRVVVLsaRPGRIVAE 215
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
682-856 |
1.28e-22 |
|
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: 104.41 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 682 GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLL--------------------------------LAILGEMQTL---- 725
Cdd:TIGR02203 342 GRDRPALDSISLVIEPGETVALVGRSGSGKSTLVnliprfyepdsgqilldghdladytlaslrrqVALVSQDVVLfndt 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 726 ---------EGKVHWSKYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD 796
Cdd:TIGR02203 422 ianniaygrTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALD 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 797 IHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKD 856
Cdd:TIGR02203 502 NE-SERLVQAALERLMQG--RTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARN 558
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
688-873 |
1.76e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 103.77 E-value: 1.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG-------------EMQTLEgKVHWSKYKA------------VTDACS 742
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGflpyqgslkingiELRELD-PESWRKHLSwvgqnpqlphgtLRDNVL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 743 L-QPD------------------IDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHL 803
Cdd:PRK11174 445 LgNPDasdeqlqqalenawvsefLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH-SEQL 523
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 804 MQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEhwktlMNRQDQE 873
Cdd:PRK11174 524 VMQALNAASRR--QTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFAT-----LLAHRQE 586
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
672-848 |
3.20e-22 |
|
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: 96.79 E-value: 3.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSWGSGLAT-LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH-----WSKY----------- 734
Cdd:cd03244 3 IEFKNVSLRYRPNLPPvLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILidgvdISKIglhdlrsrisi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 735 ---------------------------KAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVF 787
Cdd:cd03244 83 ipqdpvlfsgtirsnldpfgeysdeelWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398974 788 LDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 848
Cdd:cd03244 163 LDEATASVDPE-TDALIQKTIREAFKD--CTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
672-852 |
3.69e-22 |
|
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: 97.17 E-value: 3.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSWGS-GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKYK-AVTDACSLQ----- 744
Cdd:cd03252 1 ITFEHVRFRYKPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDlALADPAWLRrqvgv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 745 --------------------PDIDL------------------LPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIV 786
Cdd:cd03252 81 vlqenvlfnrsirdnialadPGMSMervieaaklagahdfiseLPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530398974 787 FLDDPFSALDIHlSDHLMQEGILKFLqdDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDI 852
Cdd:cd03252 161 IFDEATSALDYE-SEHAIMRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
667-852 |
6.99e-22 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 96.70 E-value: 6.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 667 TEDIAIKVTN---GYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWsKYKAVTDAcsl 743
Cdd:COG1116 3 AAAPALELRGvskRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLV-DGKPVTGP--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 744 QPDI-------DLLP---------FG------DQTEIGER--------GI---------NLSGGQRQRICVARALYQNTN 784
Cdd:COG1116 79 GPDRgvvfqepALLPwltvldnvaLGlelrgvPKAERRERarellelvGLagfedayphQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398974 785 IVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQ---YLthADWIIAMKDgsvlREGTLKDI 852
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDE-LLRLWQETGKTVLFVTHDVDeavFL--ADRVVVLSA----RPGRIVEE 222
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
679-839 |
3.85e-21 |
|
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: 93.37 E-value: 3.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 679 FSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH---------------------------- 730
Cdd:cd03235 7 VSYGGHPV-LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkplekerkrigyvpqrrsidrdfpi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 731 ----------------WSKYKAVTDACSLQpdidLLPFGDQTEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFS 793
Cdd:cd03235 86 svrdvvlmglyghkglFRRLSKADKAKVDE----ALERVGLSELADRQIgELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 530398974 794 ALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMK 839
Cdd:cd03235 162 GVDPKTQEDIY--ELLRELRREGMTILVVTHDLGLVLeYFDRVLLLN 206
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
688-848 |
4.66e-21 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 99.40 E-value: 4.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV-------------HWSKYKAVT---------------- 738
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhdipltklqldSWRSRLAVVsqtpflfsdtvannia 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 739 ----DACSLQ-----------PDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHl 803
Cdd:PRK10789 411 lgrpDATQQEiehvarlasvhDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGR-TEH- 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 530398974 804 mqeGILKFLQD--DKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 848
Cdd:PRK10789 489 ---QILHNLRQwgEGRTVIISAHRLSALTEASEILVMQHGHIAQRGN 532
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
688-854 |
7.30e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 93.93 E-value: 7.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH-----WSKY--KAVTDACSLQPDIDLLPFG------- 753
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFlgdkpISMLssRQLARRLALLPQHHLTPEGitvrelv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 754 --------------------------DQTEIGE----RGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHL 803
Cdd:PRK11231 98 aygrspwlslwgrlsaednarvnqamEQTRINHladrRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVEL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 530398974 804 MqeGILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREGTLKDIQT 854
Cdd:PRK11231 178 M--RLMRELNTQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
680-847 |
1.23e-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: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 680 SWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKyKAVTDACSLQPDID-------LLP- 751
Cdd:cd03259 9 TYGSVRA-LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDG-RDVTGVPPERRNIGmvfqdyaLFPh 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 752 --------FG------DQTEIGER--------GIN---------LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 800
Cdd:cd03259 87 ltvaeniaFGlklrgvPKAEIRARvrellelvGLEgllnrypheLSGGQQQRVALARALAREPSLLLLDEPLSALDAKLR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 530398974 801 DHLMQEgILKFLQDDKRTLVLVTHKLQ-YLTHADWIIAMKDGSVLREG 847
Cdd:cd03259 167 EELREE-LKELQRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1265-1481 |
1.42e-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: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHtlRS 1340
Cdd:cd03259 1 LELKGLSKTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTL----LRLIAGLErpdsGEILIDGRDVTGVPPE--RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1341 RLSIILQDPILFS-----GSIRFNLDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCL 1412
Cdd:cd03259 73 NIGMVFQDYALFPhltvaENIAFGLKLRGVPKAEiraRVRELLELVGLEGLLNRYPHEL-----------SGGQQQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398974 1413 ARAFVRKSSILIMDEATASIDMAT-ENILQKVV-MTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYD 1481
Cdd:cd03259 142 ARALAREPSLLLLDEPLSALDAKLrEELREELKeLQRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
672-843 |
1.46e-20 |
|
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: 90.18 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWskykavtdacslqpDIDLLP 751
Cdd:cd03216 1 LELRGITKRFGGVKA-LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV--------------DGKEVS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 752 FGDQTEIGERGIN----LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQ 827
Cdd:cd03216 66 FASPRDARRAGIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK--VIRRLRAQGVAVIFISHRLD 143
|
170
....*....|....*..
gi 530398974 828 -YLTHADWIIAMKDGSV 843
Cdd:cd03216 144 eVFEIADRVTVLRDGRV 160
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
672-841 |
2.55e-20 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 91.01 E-value: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSWGSG---LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTL-EGKVH-------------WSKY 734
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLL-NILGGLDRPtSGEVRvdgtdisklsekeLAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 735 KA---------------------VTDACSLQPD---------IDLLpfgDQTEIGERgIN-----LSGGQRQRICVARAL 779
Cdd:cd03255 80 RRrhigfvfqsfnllpdltalenVELPLLLAGVpkkerreraEELL---ERVGLGDR-LNhypseLSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398974 780 YQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDG 841
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMEL-LRELNKEAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1266-1478 |
2.59e-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: 89.80 E-value: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1266 KIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSII 1345
Cdd:cd03214 1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1346 LQdpILfsgsirfnldpeckctddrlwEALEIAQLKN-MVKSLPGGldavvteggenfsvgQRQLFCLARAFVRKSSILI 1424
Cdd:cd03214 79 PQ--AL---------------------ELLGLAHLADrPFNELSGG---------------ERQRVLLARALAQEPPILL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 530398974 1425 MDEATASIDMATE-NILQKVV-MTAFADRTVVTIAHRV-HTILTADLVIVMKRGNIL 1478
Cdd:cd03214 121 LDEPTSHLDIAHQiELLELLRrLARERGKTVVMVLHDLnLAARYADRVILLKDGRIV 177
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
671-852 |
2.94e-20 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 91.79 E-value: 2.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 671 AIKVTN---GYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAIL-------GEMqTLEGK-VHWSKYKAVTD 739
Cdd:COG1124 1 MLEVRNlsvSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAglerpwsGEV-TFDGRpVTRRRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 740 AC---------SLQP-----DIDLLPFGDQ--TEIGER--------GIN----------LSGGQRQRICVARALYQNTNI 785
Cdd:COG1124 80 RVqmvfqdpyaSLHPrhtvdRILAEPLRIHglPDREERiaelleqvGLPpsfldryphqLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398974 786 VFLDDPFSALDIHlsdhlMQEGILKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 852
Cdd:COG1124 160 LLLDEPTSALDVS-----VQAEILNLLKDLREerglTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADL 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
385-826 |
8.91e-20 |
|
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: 95.12 E-value: 8.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 385 GALLAMIYNKILRLS---TSNLSMGEMtlgqINNLVA-IETNQLMWFLFLCPNLWAMPVQII--MGVILLYNLLGSSALV 458
Cdd:TIGR02868 86 GALRVRVYERLARQAlagRRRLRRGDL----LGRLGAdVDALQDLYVRVIVPAGVALVVGAAavAAIAVLSVPAALILAA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 459 GAAVIVLLAPiqyFIATKLAEAQKSTLDYS-TERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTS 537
Cdd:TIGR02868 162 GLLLAGFVAP---LVSLRAARAAEQALARLrGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 538 LSIFMNAAIPIAAVLATFVTHAYASGNNLKPAEAFASLSLFHILVT-PLFLLSTVVRFAVKAIISVQKLNEFLlsdeigD 616
Cdd:TIGR02868 239 LGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFeAFAALPAAAQQLTRVRAAAERIVEVL------D 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 617 DSWRTGESSLPfesckkhtgvQPKTINRKQPGRyhldsyeqstrrlrpaETEDIAikvtngyFSWGSGLATLSNIDIRIP 696
Cdd:TIGR02868 313 AAGPVAEGSAP----------AAGAVGLGKPTL----------------ELRDLS-------AGYPGAPPVLDGVSLDLP 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 697 TGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKYKA------------------------------------VTD- 739
Cdd:TIGR02868 360 PGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVssldqdevrrrvsvcaqdahlfdttvrenlrlarpdATDe 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 740 -------ACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMqEGILKfl 812
Cdd:TIGR02868 440 elwaaleRVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELL-EDLLA-- 516
|
490
....*....|....
gi 530398974 813 QDDKRTLVLVTHKL 826
Cdd:TIGR02868 517 ALSGRTVVLITHHL 530
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1202-1489 |
9.89e-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: 94.75 E-value: 9.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1202 GLGLLYaltITNYLNwVVRNLAD----LE----VQMGAVKKVnsFLTM---------ESEnyegtmdPSQVPEHWPQEGE 1264
Cdd:COG4172 207 GMALLL---ITHDLG-VVRRFADrvavMRqgeiVEQGPTAEL--FAAPqhpytrkllAAE-------PRGDPRPVPPDAP 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 --IKIHDLCVRYENN---LKPVLKHVKAY------IKPGQKVGICGRTGSGKSSLSLAFFRMVDiFDGKIVIDGIDISKL 1333
Cdd:COG4172 274 plLEARDLKVWFPIKrglFRRTVGHVKAVdgvsltLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGL 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1334 P---LHTLRSRLSIILQDPilFsGSirfnLDPeckctddRL------WEALEI-------AQLKNMVKSLPG--GLDAVV 1395
Cdd:COG4172 353 SrraLRPLRRRMQVVFQDP--F-GS----LSP-------RMtvgqiiAEGLRVhgpglsaAERRARVAEALEevGLDPAA 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1396 -----TEggenFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATenilQKVVMTAFA---------------DRTVV- 1454
Cdd:COG4172 419 rhrypHE----FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV----QAQILDLLRdlqrehglaylfishDLAVVr 490
|
330 340 350
....*....|....*....|....*....|....*
gi 530398974 1455 TIAHRvhtiltadlVIVMKRGNILEYDTPESLLAQ 1489
Cdd:COG4172 491 ALAHR---------VMVMKDGKVVEQGPTEQVFDA 516
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
672-841 |
1.93e-19 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 87.24 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKyKAVTDACSLQPDI---- 747
Cdd:cd03229 1 LELKNVSKRYGQKTV-LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDG-EDLTDLEDELPPLrrri 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 748 -----DLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhlsdhLMQEGILKFLQD----DKRT 818
Cdd:cd03229 79 gmvfqDFALFPHLTVLENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDP-----ITRREVRALLKSlqaqLGIT 153
|
170 180
....*....|....*....|....
gi 530398974 819 LVLVTHKLQYLTH-ADWIIAMKDG 841
Cdd:cd03229 154 VVLVTHDLDEAARlADRVVVLRDG 177
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
377-870 |
2.16e-19 |
|
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: 94.64 E-value: 2.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 377 IETGINlrGALLAMIYNKILRL--------STSNLSMGEMTLGQINNLVAIET-NQLMWFLFLCPNLWAMpvqiimgviL 447
Cdd:TIGR03797 203 LETRMD--ASLQAAVWDRLLRLpvsffrqySTGDLASRAMGISQIRRILSGSTlTTLLSGIFALLNLGLM---------F 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 448 LYNLlgSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLK--------LYAWEHIFCKSVE 519
Cdd:TIGR03797 272 YYSW--KLALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRvagaenraFARWAKLFSRQRK 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 520 ---ETRMKE--LSSLKT-FALYTSLSIFMNAAIPIAAV---LATFVTHAYASGNNLKPAEAFASlSLFHIL-VTPLFlls 589
Cdd:TIGR03797 350 lelSAQRIEnlLTVFNAvLPVLTSAALFAAAISLLGGAglsLGSFLAFNTAFGSFSGAVTQLSN-TLISILaVIPLW--- 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 590 tvvrfavkaiisvqklnefllsdeigddswrtgESSLP-FESckkhtgvQPKT-INRKQPGRYHLdsyeqstrrlrpaet 667
Cdd:TIGR03797 426 ---------------------------------ERAKPiLEA-------LPEVdEAKTDPGKLSG--------------- 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 668 ediAIKVTNGYFSWG-SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHW--------------- 731
Cdd:TIGR03797 451 ---AIEVDRVTFRYRpDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYdgqdlagldvqavrr 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 732 --------------SKYKAVTDACSLQP--------------DIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 783
Cdd:TIGR03797 528 qlgvvlqngrlmsgSIFENIAGGAPLTLdeaweaarmaglaeDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKP 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 784 NIVFLDDPFSALdihlsDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEhw 863
Cdd:TIGR03797 608 RILLFDEATSAL-----DNRTQAIVSESLERLKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQ-- 680
|
....*..
gi 530398974 864 ktLMNRQ 870
Cdd:TIGR03797 681 --LARRQ 685
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
688-852 |
3.24e-19 |
|
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: 94.04 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLE-GKVHWSKYK-AVTDACSLQ--------------------- 744
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLT-KLLQRLYTPQhGQVLVDGVDlAIADPAWLRrqmgvvlqenvlfsrsirdni 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 745 ----PDIDL------------------LPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDH 802
Cdd:TIGR01846 552 alcnPGAPFehvihaaklagahdfiseLPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYE-SEA 630
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 530398974 803 LMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDI 852
Cdd:TIGR01846 631 LIMRNMREICRG--RTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1265-1489 |
4.72e-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: 4.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNLK--PVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLP---L 1335
Cdd:cd03258 2 IELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTL----IRCINGLErptsGSVLVDGTDLTLLSgkeL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1336 HTLRSRLSIILQDPILFS-----GSIRFNLD---PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQR 1407
Cdd:cd03258 78 RKARRRIGMIFQHFNLLSsrtvfENVALPLEiagVPKAEIEERVLELLELVGLEDKADAYPAQL-----------SGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1408 QLFCLARAFVRKSSILIMDEATASIDMA-TENILQ--KVVMTAFaDRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTP 1483
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPEtTQSILAllRDINREL-GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTV 225
|
....*.
gi 530398974 1484 ESLLAQ 1489
Cdd:cd03258 226 EEVFAN 231
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1265-1477 |
4.98e-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: 4.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYEN--NLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHTL 1338
Cdd:cd03255 1 IELKNLSKTYGGggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTL----LNILGGLDrptsGEVRVDGTDISKLSEKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1339 ----RSRLSIILQD---------------PILFSGSIRfnldPECKctdDRLWEALEIAQLKNMVKSLPGGLdavvtegg 1399
Cdd:cd03255 77 aafrRRHIGFVFQSfnllpdltalenvelPLLLAGVPK----KERR---ERAEELLERVGLGDRLNHYPSEL-------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1400 enfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE----NILQKvvMTAFADRTVVTIAHRVHTILTADLVIVMKRG 1475
Cdd:cd03255 142 ---SGGQQQRVAIARALANDPKIILADEPTGNLDSETGkevmELLRE--LNKEAGTTIVVVTHDPELAEYADRIIELRDG 216
|
..
gi 530398974 1476 NI 1477
Cdd:cd03255 217 KI 218
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
668-843 |
5.76e-19 |
|
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: 87.08 E-value: 5.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 668 EDIAIKVTNGYFSWGSGLA-TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS-------KYKAVTD 739
Cdd:cd03369 3 EHGEIEVENLSVRYAPDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDgidistiPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 740 ACSLQPD----------IDLLPFGDQTE--------IGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSD 801
Cdd:cd03369 83 SLTIIPQdptlfsgtirSNLDPFDEYSDeeiygalrVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYA-TD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 530398974 802 HLMQEGILKFLQDDkrTLVLVTHKLQYLTHADWIIAMKDGSV 843
Cdd:cd03369 162 ALIQKTIREEFTNS--TILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
672-852 |
8.62e-19 |
|
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: 87.36 E-value: 8.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV---------------------- 729
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfidgedireqdpvelrrkigyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 730 -----------------------HWSKYKAVTDACSLQPDIDLLPfgdqTEIGER-GINLSGGQRQRICVARALYQNTNI 785
Cdd:cd03295 81 iqqiglfphmtveenialvpkllKWPKEKIRERADELLALVGLDP----AEFADRyPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530398974 786 VFLDDPFSALDIHLSDHLmQEGILKFLQDDKRTLVLVTHKLQ-YLTHADWIIAMKDGSVLREGTLKDI 852
Cdd:cd03295 157 LLMDEPFGALDPITRDQL-QEEFKRLQQELGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
669-846 |
9.01e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 87.02 E-value: 9.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 669 DIAIKVTNGYFSWGSGLAT---LSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTL-EGKVHW------------- 731
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEvtaLRGVSLSIEAGEFVAIVGPSGSGKSTLL-NILGGLDRPtSGEVLIdgqdisslserel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 732 ------------------------------------SKYKAVTDAcslqpdIDLLpfgDQTEIGERgIN-----LSGGQR 770
Cdd:COG1136 81 arlrrrhigfvfqffnllpeltalenvalplllagvSRKERRERA------RELL---ERVGLGDR-LDhrpsqLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398974 771 QRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFL-QDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLRE 846
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLE--LLRELnRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1280-1488 |
1.88e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 87.35 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1280 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGI---DISKLPlhTLRSRLSIILQDP-ILFSG- 1354
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgDFSKLQ--GIRKLVGIVFQNPeTQFVGr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1355 SIRFNL--DPECKCTddrlwEALEIAQLKNMVKSlPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASI 1432
Cdd:PRK13644 94 TVEEDLafGPENLCL-----PPIEIRKRVDRALA-EIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 530398974 1433 DMAT-ENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLA 1488
Cdd:PRK13644 168 DPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
671-862 |
1.94e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 88.59 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 671 AIKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG-EMQTlEGKVHWSKyKAVTDacsLQP---D 746
Cdd:COG3839 3 SLELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGlEDPT-SGEILIGG-RDVTD---LPPkdrN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 747 I-------DLLP---------FG------DQTEIGER--------GI---------NLSGGQRQRICVARALYQNTNIVF 787
Cdd:COG3839 77 IamvfqsyALYPhmtvyeniaFPlklrkvPKAEIDRRvreaaellGLedlldrkpkQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530398974 788 LDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKdiqtkdvELYEH 862
Cdd:COG3839 157 LDEPLSNLDAKLRVEMRAE-IKRLHRRLGTTTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPE-------ELYDR 224
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
747-866 |
1.96e-18 |
|
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: 90.91 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 747 IDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhLSDHLMQEGILKFLQDdkRTLVLVTHKL 826
Cdd:TIGR02204 459 ISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDA-ESEQLVQQALETLMKG--RTTLIIAHRL 535
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 530398974 827 QYLTHADWIIAMKDGSVLREGTLKDIQTKDvELYEHWKTL 866
Cdd:TIGR02204 536 ATVLKADRIVVMDQGRIVAQGTHAELIAKG-GLYARLARL 574
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1265-1479 |
2.56e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.12 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIF-----DGKIVIDGIDISKLPLHTLR 1339
Cdd:PRK14247 4 IEIRDLKVSFGQ--VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1340 SRLSIILQ--DPI----LFSG---SIRFN-LDPECKCTDDRLWEALEIAQLKNMVKSLpggLDAVVTEggenFSVGQRQL 1409
Cdd:PRK14247 82 RRVQMVFQipNPIpnlsIFENvalGLKLNrLVKSKKELQERVRWALEKAQLWDEVKDR---LDAPAGK----LSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530398974 1410 FCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAH------RVhtiltADLVIVMKRGNILE 1479
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVE 225
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
672-860 |
2.63e-18 |
|
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: 86.08 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS-------KYKAVTD----- 739
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgtdinklKGKALRQlrrqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 740 --------------------------------------------ACSLQPDIDLLPFGDQteigeRGINLSGGQRQRICV 775
Cdd:cd03256 81 gmifqqfnlierlsvlenvlsgrlgrrstwrslfglfpkeekqrALAALERVGLLDKAYQ-----RADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 776 ARALYQNTNIVFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQY-LTHADWIIAMKDGSVLREGTLKDIQT 854
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVM-DLLKRINREEGITVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAELTD 234
|
....*..
gi 530398974 855 KDV-ELY 860
Cdd:cd03256 235 EVLdEIY 241
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1265-1475 |
2.72e-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: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYenNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHT--L 1338
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTL----LRCIAGLEepdsGSILIDGEDLTDLEDELppL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1339 RSRLSIILQDPILFSGsirfnldpeckctddrlweaLEIAQlkNMVKSLPGGldavvteggenfsvgQRQLFCLARAFVR 1418
Cdd:cd03229 75 RRRIGMVFQDFALFPH--------------------LTVLE--NIALGLSGG---------------QQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1419 KSSILIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTILT-ADLVIVMKRG 1475
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
672-859 |
5.19e-18 |
|
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: 84.86 E-value: 5.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwskYKAVTDACSLQPDiDLLP 751
Cdd:cd03261 1 IELRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEV----LIDGEDISGLSEA-ELYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 752 --------------FGDQT------------------EIGER--------GI---------NLSGGQRQRICVARALYQN 782
Cdd:cd03261 75 lrrrmgmlfqsgalFDSLTvfenvafplrehtrlseeEIREIvlekleavGLrgaedlypaELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398974 783 TNIVFLDDPFSALDIHLSDhLMQEGILKfLQDDKR-TLVLVTHKLQ-YLTHADWIIAMKDGSVLREGTLKDIQTKDVEL 859
Cdd:cd03261 155 PELLLYDEPTAGLDPIASG-VIDDLIRS-LKKELGlTSIMVTHDLDtAFAIADRIAVLYDGKIVAEGTPEELRASDDPL 231
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1280-1475 |
5.29e-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: 5.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1280 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR----LSIILQDPILFSGS 1355
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1356 IRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDM- 1434
Cdd:cd03290 95 VEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIh 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 530398974 1435 ATENILQKVVMTAFAD--RTVVTIAHRVHTILTADLVIVMKRG 1475
Cdd:cd03290 175 LSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1281-1481 |
6.31e-18 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 90.47 E-value: 6.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1281 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVI-DGIDISKLPLHTLRSRLSIILQDPILFSGSIRFN 1359
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNN 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1360 L--------------------------------DPECKCTDD-----------------RLWEALEIAQLKNM------- 1383
Cdd:PTZ00265 480 IkyslyslkdlealsnyynedgndsqenknkrnSCRAKCAGDlndmsnttdsneliemrKNYQTIKDSEVVDVskkvlih 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1384 --VKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVV--MTAFADRTVVTIAHR 1459
Cdd:PTZ00265 560 dfVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnLKGNENRITIIIAHR 639
|
250 260
....*....|....*....|....*
gi 530398974 1460 VHTILTADLVIVM---KRGNILEYD 1481
Cdd:PTZ00265 640 LSTIRYANTIFVLsnrERGSTVDVD 664
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
657-860 |
6.33e-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: 89.19 E-value: 6.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 657 QSTRRLRPAETEDIAIKVTN---GYFSWGSGLAT-LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS 732
Cdd:COG1123 246 ARGRAAPAAAAAEPLLEVRNlskRYPVRGKGGVRaVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 733 KyKAVTDAC--------------------SLQP-----DI-----DLLPFGDQTEIGER--------GIN---------- 764
Cdd:COG1123 326 G-KDLTKLSrrslrelrrrvqmvfqdpysSLNPrmtvgDIiaeplRLHGLLSRAERRERvaellervGLPpdladryphe 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 765 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKR----TLVLVTHKL---QYLthADWIIA 837
Cdd:COG1123 405 LSGGQRQRVAIARALALEPKLLILDEPTSALDVSV-----QAQILNLLRDLQRelglTYLFISHDLavvRYI--ADRVAV 477
|
250 260
....*....|....*....|...
gi 530398974 838 MKDGSVLREGTLKDIQTKDVELY 860
Cdd:COG1123 478 MYDGRIVEDGPTEEVFANPQHPY 500
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1265-1491 |
8.77e-18 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 84.37 E-value: 8.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidiskLPLHTLRSRLSI 1344
Cdd:COG1121 7 IELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG-----KPPRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1345 ILQD-------PIL--------FSGSIRF--NLDPECKctdDRLWEALE---IAQLKN-MVKSLpggldavvteggenfS 1403
Cdd:COG1121 80 VPQRaevdwdfPITvrdvvlmgRYGRRGLfrRPSRADR---EAVDEALErvgLEDLADrPIGEL---------------S 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1404 VGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMT-AFADRTVVTIAHRVHTILT-ADLVIVMKRGnILEYD 1481
Cdd:COG1121 142 GGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRG-LVAHG 220
|
250
....*....|
gi 530398974 1482 TPESLLAQEN 1491
Cdd:COG1121 221 PPEEVLTPEN 230
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1260-1459 |
1.46e-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: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1260 PQEGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVI-DGIDISKLP 1334
Cdd:COG4178 358 SEDGALALEDLTLRTPDG-RPLLEDLSLSLKPGERLLITGPSGSGKSTL----LRAIaglwPYGSGRIARpAGARVLFLP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1335 lhtlrsrlsiilQDPILFSGSIRFNL---DPECKCTDDRLWEALEIAQLKNmvksLPGGLDaVVTEGGENFSVGQRQLFC 1411
Cdd:COG4178 433 ------------QRPYLPLGTLREALlypATAEAFSDAELREALEAVGLGH----LAERLD-EEADWDQVLSLGEQQRLA 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 530398974 1412 LARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR 1459
Cdd:COG4178 496 FARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
672-856 |
1.49e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 88.15 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSW-GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSL--LLAILGEMQ----TLEG----------------- 727
Cdd:PRK11176 342 IEFRNVTFTYpGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIanLLTRFYDIDegeiLLDGhdlrdytlaslrnqval 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 728 ---KVH-----------------WSKY---KAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTN 784
Cdd:PRK11176 422 vsqNVHlfndtianniayarteqYSREqieEAARMAYAMD-FINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSP 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398974 785 IVFLDDPFSALDIHlSDHLMQEGiLKFLQDDKRTLVlVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKD 856
Cdd:PRK11176 501 ILILDEATSALDTE-SERAIQAA-LDELQKNRTSLV-IAHRLSTIEKADEILVVEDGEIVERGTHAELLAQN 569
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
747-843 |
1.69e-17 |
|
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: 83.29 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 747 IDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKL 826
Cdd:cd03248 133 ISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE-SEQQVQQALYDWPER--RTVLVIAHRL 209
|
90
....*....|....*..
gi 530398974 827 QYLTHADWIIAMKDGSV 843
Cdd:cd03248 210 STVERADQILVLDGGRI 226
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
672-841 |
1.72e-17 |
|
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: 80.57 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSWGSGLaTLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSkykavtdacslqPDIDLLP 751
Cdd:cd03221 1 IELENLSKTYGGKL-LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG------------STVKIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 752 FgDQteigerginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegilkFLQDDKRTLVLVTHKLQYLTH 831
Cdd:cd03221 68 F-EQ---------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEE-----ALKEYPGTVILVSHDRYFLDQ 132
|
170
....*....|.
gi 530398974 832 -ADWIIAMKDG 841
Cdd:cd03221 133 vATKIIELEDG 143
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1265-1479 |
2.57e-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: 2.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYE--NNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAffrMVDIFD-GKIVIDGIDISKLP---LH 1336
Cdd:COG1136 5 LELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLlnILG---GLDRPTsGEVLIDGQDISSLSereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1337 TLRSR-LSIILQDpilfsgsirFNLDPE-----------------CKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteg 1398
Cdd:COG1136 82 RLRRRhIGFVFQF---------FNLLPEltalenvalplllagvsRKERRERARELLERVGLGDRLDHRPSQL------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1399 genfSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT-ENILQkvVMTAFAD---RTVVTIAHRVHTILTADLVIVMKR 1474
Cdd:COG1136 146 ----SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgEEVLE--LLRELNRelgTTIVMVTHDPELAARADRVIRLRD 219
|
....*
gi 530398974 1475 GNILE 1479
Cdd:COG1136 220 GRIVS 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1265-1477 |
3.01e-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: 80.90 E-value: 3.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRM----VDIFDGKIVIDGIDISKLPlHTLRS 1340
Cdd:cd03230 1 IEVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTTL----IKIilglLKPDSGEIKVLGKDIKKEP-EEVKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1341 RLSIILQDPILFSG-SIRFNLDpeckctddrlwealeiaqlknmvkslpggldavvteggenFSVGQRQLFCLARAFVRK 1419
Cdd:cd03230 74 RIGYLPEEPSLYENlTVRENLK----------------------------------------LSGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1420 SSILIMDEATASIDMATENILQKVVMT-AFADRTVVTIAHRVHTILT-ADLVIVMKRGNI 1477
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1265-1491 |
3.14e-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: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYEN-----NLKpvlkhvkayIKPGQKVGICGRTGSGKSSLS--LAFFRMVDifDGKIVIDGIDISKLPLHT 1337
Cdd:COG3840 2 LRLDDLTYRYGDfplrfDLT---------IAAGERVAILGPSGAGKSTLLnlIAGFLPPD--SGRILWNGQDLTALPPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1338 lrsR-LSIILQDPILFSG-SIRFN----LDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQ 1408
Cdd:COG3840 71 ---RpVSMLFQENNLFPHlTVAQNiglgLRPGLKLTAEqraQVEQALERVGLAGLLDRLPGQL-----------SGGQRQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1409 LFCLARAFVRKSSILIMDEATASIDMA-TENILQKVV-MTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPES 1485
Cdd:COG3840 137 RVALARCLVRKRPILLLDEPFSALDPAlRQEMLDLVDeLCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAA 216
|
....*.
gi 530398974 1486 LLAQEN 1491
Cdd:COG3840 217 LLDGEP 222
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
672-843 |
3.77e-17 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 81.92 E-value: 3.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhWSKYKAVTDACSLQPDI---- 747
Cdd:cd03301 1 VELENVTKRFGNVTA-LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRI-YIGGRDVTDLPPKDRDIamvf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 748 ------------DLLPFG------DQTEIGER--------GIN---------LSGGQRQRICVARALYQNTNIVFLDDPF 792
Cdd:cd03301 79 qnyalyphmtvyDNIAFGlklrkvPKDEIDERvrevaellQIEhlldrkpkqLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 530398974 793 SALDIHLSDHLMQEgILKFLQDDKRTLVLVTH-KLQYLTHADWIIAMKDGSV 843
Cdd:cd03301 159 SNLDAKLRVQMRAE-LKRLQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1265-1486 |
4.03e-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: 4.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSR 1341
Cdd:cd03256 1 IEVENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1342 LSIILQDpilfsgsirFNLDPECKCTDDRLWEALeiAQlKNMVKSLPG-----------------GLDAVVTEGGENFSV 1404
Cdd:cd03256 80 IGMIFQQ---------FNLIERLSVLENVLSGRL--GR-RSTWRSLFGlfpkeekqralaalervGLLDKAYQRADQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1405 GQRQLFCLARAFVRKSSILIMDEATASIDMATENIlqkvVMTAFAD------RTVVTIAHRVHTILT-ADLVIVMKRGNI 1477
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQ----VMDLLKRinreegITVIVSLHQVDLAREyADRIVGLKDGRI 223
|
....*....
gi 530398974 1478 LEYDTPESL 1486
Cdd:cd03256 224 VFDGPPAEL 232
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
672-858 |
6.03e-17 |
|
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: 81.83 E-value: 6.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKYKAVTDACSLQPDIDLLP 751
Cdd:COG4555 2 IEVENLSKKYGKVPA-LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 752 ------------------------FGDQ--------------TEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPF 792
Cdd:COG4555 81 derglydrltvreniryfaelyglFDEElkkrieeliellglEEFLDRRVgELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398974 793 SALDIhLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQTKDVE 858
Cdd:COG4555 161 NGLDV-MARRLLRE-ILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
688-843 |
6.52e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 82.42 E-value: 6.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLL--LAIL-----GEMqtLEGKVHWSKykAVTDACSLQPDIDLLPFG---DQTE 757
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLrlLAGLetpsaGEL--LAGTAPLAE--AREDTRLMFQDARLLPWKkviDNVG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 758 IGERG-----------------------INLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhLSDHLMQEGILKFLQD 814
Cdd:PRK11247 104 LGLKGqwrdaalqalaavgladranewpAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA-LTRIEMQDLIESLWQQ 182
|
170 180 190
....*....|....*....|....*....|
gi 530398974 815 DKRTLVLVTHKL-QYLTHADWIIAMKDGSV 843
Cdd:PRK11247 183 HGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
650-852 |
6.60e-17 |
|
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: 86.72 E-value: 6.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 650 YHLDSYEQSTRRLRPAETEDIAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEG-- 727
Cdd:TIGR01193 452 YLVDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGei 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 728 -------------------------------------------KVHWSKYKAVTDACSLQPDIDLLPFGDQTEIGERGIN 764
Cdd:TIGR01193 532 llngfslkdidrhtlrqfinylpqepyifsgsilenlllgakeNVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSS 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 765 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIhLSDHLMQEGILkFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVL 844
Cdd:TIGR01193 612 ISGGQKQRIALARALLTDSKVLILDESTSNLDT-ITEKKIVNNLL-NLQD--KTIIFVAHRLSVAKQSDKIIVLDHGKII 687
|
....*...
gi 530398974 845 REGTLKDI 852
Cdd:TIGR01193 688 EQGSHDEL 695
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1265-1474 |
1.25e-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: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENN--LKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGidiskLPLHTL 1338
Cdd:cd03293 1 LEVRNVSKTYGGGggAVTALEDISLSVEEGEFVALVGPSGCGKSTL----LRIIAGLErptsGEVLVDG-----EPVTGP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1339 RSRLSIILQDPILFS-GSIRFN--LDPECKCTDDRLW-----EALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1410
Cdd:cd03293 72 GPDRGYVFQQDALLPwLTVLDNvaLGLELQGVPKAEAreraeELLELVGLSGFENAYPHQL-----------SGGMRQRV 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398974 1411 CLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVH-TILTADLVIVMKR 1474
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDeAVFLADRVVVLSA 207
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1265-1491 |
1.26e-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: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFR-MVDIF---DGKIVIDGIDISKL---PLHT 1337
Cdd:cd03261 1 IELRGLTKSFGG--RTVLKGVDLDVRRGEILAIIGPSGSGKSTL----LRlIVGLLrpdSGEVLIDGEDISGLseaELYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1338 LRSRLSIILQDPILFSG-----SIRFNLDPECKCTDdrlWEALEIAQLK-NMVkSLPGGLDAVVTEggenFSVGQRQLFC 1411
Cdd:cd03261 75 LRRRMGMLFQSGALFDSltvfeNVAFPLREHTRLSE---EEIREIVLEKlEAV-GLRGAEDLYPAE----LSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1412 LARAFVRKSSILIMDEATASIDMATENILQKVVMT--AFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLA 1488
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFaIADRIAVLYDGKIVAEGTPEELRA 226
|
...
gi 530398974 1489 QEN 1491
Cdd:cd03261 227 SDD 229
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1265-1501 |
1.48e-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: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYeNNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1344
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1345 ILQDPILFSG-SIRFNLD--------PECKcTDDRLWEALEIAQL--KNMVKSLPGGLdavvteggenfSVGQRQLFCLA 1413
Cdd:cd03295 80 VIQQIGLFPHmTVEENIAlvpkllkwPKEK-IRERADELLALVGLdpAEFADRYPHEL-----------SGGQQQRVGVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1414 RAFVRKSSILIMDEATASIDMATENILQKvvmtAFAD------RTVVTIAHRV-HTILTADLVIVMKRGNILEYDTPESL 1486
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQE----EFKRlqqelgKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
250
....*....|....*.
gi 530398974 1487 LA-QENGVFASFVRAD 1501
Cdd:cd03295 224 LRsPANDFVAEFVGAD 239
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1261-1489 |
1.83e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 81.60 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1261 QEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS 1340
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1341 RLSIILQDPI-LFSGS-----IRFNLDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 1411
Cdd:PRK13635 82 QVGMVFQNPDnQFVGAtvqddVAFGLENIGVPREEmveRVDQALRQVGMEDFLNREPHRL-----------SGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1412 LARAFVRKSSILIMDEATASID-MATENILQKV-VMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1489
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDpRGRREVLETVrQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
684-833 |
2.06e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 79.20 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwskykaVTDACSL----Q--PDIDLLPFG--DQ 755
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR------RAGGARVayvpQrsEVPDSLPLTvrDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 756 TEIG---ERGI------------------------------NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDH 802
Cdd:NF040873 78 VAMGrwaRRGLwrrltrddraavddalervgladlagrqlgELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157
|
170 180 190
....*....|....*....|....*....|.
gi 530398974 803 LmqEGILKFLQDDKRTLVLVTHKLQYLTHAD 833
Cdd:NF040873 158 I--IALLAEEHARGATVVVVTHDLELVRRAD 186
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1282-1499 |
2.15e-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: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1282 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRS-RLSIILQDPILFS---- 1353
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRkKISMVFQSFALLPhrtv 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1354 -GSIRFNLDPECKCTDDRL---WEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEAT 1429
Cdd:cd03294 120 lENVAFGLEVQGVPRAEREeraAEALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398974 1430 ASIDMATENILQKVVMTAFAD--RTVVTIAHRV-HTILTADLVIVMKRGNILEYDTPESLLAQ-ENGVFASFVR 1499
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAElqKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILTNpANDYVREFFR 262
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1265-1488 |
2.33e-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: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTlRSRLSI 1344
Cdd:cd03224 1 LEVENLNAGYGKS--QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-RARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1345 IL--QDPILFSG-SIRFNLD-PECKCTDDRLWEALEIA-----QLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARA 1415
Cdd:cd03224 78 GYvpEGRRIFPElTVEENLLlGAYARRRAKRKARLERVyelfpRLKERRKQLAGTL-----------SGGEQQMLAIARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398974 1416 FVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLA 1488
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLApKIVEEIFEAIRELRDEGVTILLVEQNARFALeIADRAYVLERGRVVLEGTAAELLA 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
688-848 |
3.53e-16 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 82.07 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG-EMQTlEGKVHWSKyKAVTDacsLQP----------DIDLLP----- 751
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGfETPD-SGRILLDG-RDVTG---LPPekrnvgmvfqDYALFPhltva 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 752 ----FG------DQTEIGER--------GI---------NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLM 804
Cdd:COG3842 96 envaFGlrmrgvPKAEIRARvaellelvGLegladryphQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMR 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 530398974 805 QEgiLKFLQDD-KRTLVLVTHKlQY--LTHADWIIAMKDGSVLREGT 848
Cdd:COG3842 176 EE--LRRLQRElGITFIYVTHD-QEeaLALADRIAVMNDGRIEQVGT 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
666-841 |
3.81e-16 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 78.70 E-value: 3.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 666 ETEDIAIKVTNGYFswgsglatLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKyKAVTDA----- 740
Cdd:COG4619 2 ELEGLSFRVGGKPI--------LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDG-KPLSAMpppew 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 741 ------CSLQPDI------DLLPFGDQ---------------------TEIGERGI-NLSGGQRQRICVARALYQNTNIV 786
Cdd:COG4619 73 rrqvayVPQEPALwggtvrDNLPFPFQlrerkfdreralellerlglpPDILDKPVeRLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 530398974 787 FLDDPFSALDIHLSDHLmQEGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDG 841
Cdd:COG4619 153 LLDEPTSALDPENTRRV-EELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAG 207
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
688-852 |
3.87e-16 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 79.34 E-value: 3.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKYKAVTDACSLQPDIDLLP---------------- 751
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPqepalypdltvrenlr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 752 -----FG-DQTEIGER--------GI---------NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegI 808
Cdd:COG1131 96 ffarlYGlPRKEARERidellelfGLtdaadrkvgTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWE--L 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 530398974 809 LKFLQDDKRTLVLVTHklqYLTHA----DWIIAMKDGSVLREGTLKDI 852
Cdd:COG1131 174 LRELAAEGKTVLLSTH---YLEEAerlcDRVAIIDKGRIVADGTPDEL 218
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
666-861 |
4.01e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 80.18 E-value: 4.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 666 ETEDIAIKVTNGYFSWGSGLA-TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKyKAVTD----- 739
Cdd:PRK13648 2 EDKNSIIVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNN-QAITDdnfek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 740 -----------------ACSLQPDI------DLLPFGDQTEIGERGIN--------------LSGGQRQRICVARALYQN 782
Cdd:PRK13648 81 lrkhigivfqnpdnqfvGSIVKYDVafglenHAVPYDEMHRRVSEALKqvdmleradyepnaLSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 783 TNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKR-TLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYE 861
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLD--LVRKVKSEHNiTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEELTR 238
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1292-1477 |
4.38e-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: 4.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1292 GQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPlhTLRSRLSIILQDPILFS-----GSIRFNLDP 1362
Cdd:cd03298 24 GEITAIVGPSGSGKSTL----LNLIAGFEtpqsGRVLINGVDVTAAP--PADRPVSMLFQENNLFAhltveQNVGLGLSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1363 ECKCT-DDRlwEALEIAQ----LKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 1437
Cdd:cd03298 98 GLKLTaEDR--QAIEVALarvgLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 530398974 1438 NILQKVVMTAFADR--TVVTIAHRVHTILT-ADLVIVMKRGNI 1477
Cdd:cd03298 165 AEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
688-793 |
4.61e-16 |
|
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: 76.92 E-value: 4.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKyKAVTDAC---------------SLQPD------ 746
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDG-QDLTDDErkslrkeigyvfqdpQLFPRltvren 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398974 747 ----------------------IDLLPFGDQ--TEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 793
Cdd:pfam00005 80 lrlglllkglskrekdaraeeaLEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
688-847 |
4.70e-16 |
|
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: 79.09 E-value: 4.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKyKAVTDAC--------------------SLQPdi 747
Cdd:cd03257 21 LDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDG-KDLLKLSrrlrkirrkeiqmvfqdpmsSLNP-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 748 dLLPFGDQteIGE----------------------RGIN------------LSGGQRQRICVARALYQNTNIVFLDDPFS 793
Cdd:cd03257 98 -RMTIGEQ--IAEplrihgklskkearkeavllllVGVGlpeevlnrypheLSGGQRQRVAIARALALNPKLLIADEPTS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 530398974 794 ALDIHLSDHLMQegILKFLQDDK-RTLVLVTHKL---QYLthADWIIAMKDGSVLREG 847
Cdd:cd03257 175 ALDVSVQAQILD--LLKKLQEELgLTLLFITHDLgvvAKI--ADRVAVMYAGKIVEEG 228
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
688-852 |
6.17e-16 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 80.96 E-value: 6.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGemqtLE----GKVHWSKykavTDACSLQP-----------DIDLLP- 751
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAG----LEtpdsGRIVLNG----RDLFTNLPprerrvgfvfqHYALFPh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 752 --------FG------DQTEIGER-----------GI------NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 800
Cdd:COG1118 90 mtvaeniaFGlrvrppSKAEIRARveellelvqleGLadrypsQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 530398974 801 DHLMQEgILKFLQDDKRTLVLVTHKLQ-YLTHADWIIAMKDGSVLREGTLKDI 852
Cdd:COG1118 170 KELRRW-LRRLHDELGGTTVFVTHDQEeALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1265-1498 |
6.61e-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: 6.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNlkpVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDifDGKIVIDGIDISKLPlhTLRSRL 1342
Cdd:cd03299 1 LKVENLSKDWKEF---KLKNVSLEVERGDYFVILGPTGSGKSVLleTIAGFIKPD--SGKILLNGKDITNLP--PEKRDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1343 SIILQDPILFSG-SIRFNLDPECKctdDRLWEALEI-AQLKNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKS 1420
Cdd:cd03299 74 SYVPQNYALFPHmTVYKNIAYGLK---KRKVDKKEIeRKVLEIAEML--GIDHLLNRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1421 SILIMDEATASIDMATENILQKVVMTAF--ADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQ-ENGVFAS 1496
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRkeFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKpKNEFVAE 228
|
..
gi 530398974 1497 FV 1498
Cdd:cd03299 229 FL 230
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1266-1477 |
6.82e-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: 6.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1266 KIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidiskLPLHTLRSRL--- 1342
Cdd:cd03235 1 EVEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIgyv 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1343 ---SIILQD-PILFSGSIRFNLDPEC------KCTD-DRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 1411
Cdd:cd03235 74 pqrRSIDRDfPISVRDVVLMGLYGHKglfrrlSKADkAKVDEALERVGLSELADRQIGEL-----------SGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530398974 1412 LARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTILT-ADLVIVMKRGNI 1477
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEyFDRVLLLNRTVV 210
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
1297-1498 |
9.19e-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: 9.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1297 ICGRTGSGKSSL--SLAFFRMVDifDGKIVIDGIDISKLPLHtLRSrLSIILQDPILF-----SGSIRFNL--DPECKCT 1367
Cdd:TIGR01187 1 LLGPSGCGKTTLlrLLAGFEQPD--SGSIMLDGEDVTNVPPH-LRH-INMVFQSYALFphmtvEENVAFGLkmRKVPRAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1368 -DDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASID------MATE--N 1438
Cdd:TIGR01187 77 iKPRVLEALRLVQLEEFADRKPHQL-----------SGGQQQRVALARALVFKPKILLLDEPLSALDkklrdqMQLElkT 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398974 1439 ILQKVVMtafadrTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQENGVF-ASFV 1498
Cdd:TIGR01187 146 IQEQLGI------TFVFVTHDQEEAMTmSDRIAIMRKGKIAQIGTPEEIYEEPANLFvARFI 201
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1265-1489 |
1.07e-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: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNLKPVlkhvKA------YIKPGQKVGICGRTGSGKSSLSLAFFRMVD---IFDGKIVIDGIDISKLPL 1335
Cdd:COG0444 2 LEVRNLKVYFPTRRGVV----KAvdgvsfDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1336 HTLRS----RLSIILQDPIlfsGSirfnLDPeCKCTDDRLWEALEI------AQLKNMVKSLpggLDAV-VTEGGE---- 1400
Cdd:COG0444 78 KELRKirgrEIQMIFQDPM---TS----LNP-VMTVGDQIAEPLRIhgglskAEARERAIEL---LERVgLPDPERrldr 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1401 ---NFSVGQRQLFCLARAFVRKSSILIMDEATASIDmATeniLQKVVMTAFADR------TVVTIAHRVHTIL-TADLVI 1470
Cdd:COG0444 147 yphELSGGMRQRVMIARALALEPKLLIADEPTTALD-VT---IQAQILNLLKDLqrelglAILFITHDLGVVAeIADRVA 222
|
250
....*....|....*....
gi 530398974 1471 VMKRGNILEYDTPESLLAQ 1489
Cdd:COG0444 223 VMYAGRIVEEGPVEELFEN 241
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1265-1478 |
1.16e-15 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 77.79 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIF----DGKIVIDGIDISKLPLHTl 1338
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTT----LRMLAGLlepdAGFATVDGFDVVKEPAEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1339 RSRLSIilqdpilFSGSIRFNldpeckctdDRL--WEALEI---------AQLKNMVKSLPGGLD--AVVTEGGENFSVG 1405
Cdd:cd03266 77 RRRLGF-------VSDSTGLY---------DRLtaRENLEYfaglyglkgDELTARLEELADRLGmeELLDRRVGGFSTG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398974 1406 QRQLFCLARAFVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNIL 1478
Cdd:cd03266 141 MRQKVAIARALVHDPPVLLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1265-1463 |
1.72e-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: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNLkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSR 1341
Cdd:cd03292 1 IEFINVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1342 LSIILQDPILFSG-----SIRFNLdpECKCTDDRLW-----EALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 1411
Cdd:cd03292 80 IGVVFQDFRLLPDrnvyeNVAFAL--EVTGVPPREIrkrvpAALELVGLSHKHRALPAEL-----------SGGEQQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398974 1412 LARAFVRKSSILIMDEATASIDMATE----NILQK-------VVMTAFADRTVVTIAHRVHTI 1463
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTweimNLLKKinkagttVVVATHAKELVDTTRHRVIAL 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1265-1433 |
2.70e-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: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIDGIDISKLPLHtLRS 1340
Cdd:COG4133 3 LEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTTL----LRILagllPPSAGEVLWNGEPIRDARED-YRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1341 RLSIILQDPILFSG-SIRFNLD-----PECKCTDDRLWEALEIAqlknmvkslpgGLDAVVTEGGENFSVGQRQLFCLAR 1414
Cdd:COG4133 76 RLAYLGHADGLKPElTVRENLRfwaalYGLRADREAIDEALEAV-----------GLAGLADLPVRQLSAGQKRRVALAR 144
|
170
....*....|....*....
gi 530398974 1415 AFVRKSSILIMDEATASID 1433
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALD 163
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
736-862 |
3.05e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 81.31 E-value: 3.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 736 AVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQEgiLKFLQDd 815
Cdd:TIGR00958 589 AAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE-CEQLLQE--SRSRAS- 664
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 530398974 816 kRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTkDVELYEH 862
Cdd:TIGR00958 665 -RTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLME-DQGCYKH 709
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1265-1479 |
3.48e-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: 3.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSR 1341
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1342 LSIILQD-PILFSGSIRFNL----------DPECKctdDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1410
Cdd:COG2884 81 IGVVFQDfRLLPDRTVYENValplrvtgksRKEIR---RRVREVLDLVGLSDKAKALPHEL-----------SGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398974 1411 CLARAFVRKSSILIMDEATASIDMAT-ENILQkvVMTAFADR--TVVtIA-HRVHTILTADL-VIVMKRGNILE 1479
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETsWEIME--LLEEINRRgtTVL-IAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
765-852 |
4.32e-15 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 77.30 E-value: 4.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 765 LSGGQRQRICVARALYQNTNIVFLDDPFSALD--IHLSdhlMQEGILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMKDG 841
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDplIRRE---MQDELLRLQAELQKTIVFITHDLdEALRLGDRIAIMKDG 237
|
90
....*....|.
gi 530398974 842 SVLREGTLKDI 852
Cdd:cd03294 238 RLVQVGTPEEI 248
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1279-1478 |
4.62e-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: 4.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1279 KPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDIFDGKIVIDGIDISKlplHTLRSRLSIILQDPILFSgsi 1356
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLlnALAGRRTGLGVSGEVLINGRPLDK---RSFRKIIGYVPQDDILHP--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1357 rfnldpeckctDDRLWEALEI-AQLknmvKSLPGgldavvteggenfsvGQRQLFCLARAFVRKSSILIMDEATASIDMA 1435
Cdd:cd03213 96 -----------TLTVRETLMFaAKL----RGLSG---------------GERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 530398974 1436 TENILQKVVMtAFAD--RTVVTIAHRVHTILTA--DLVIVMKRGNIL 1478
Cdd:cd03213 146 SALQVMSLLR-RLADtgRTIICSIHQPSSEIFElfDKLLLLSQGRVI 191
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
672-866 |
5.35e-15 |
|
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: 76.12 E-value: 5.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV------------HWSKYKAVTD 739
Cdd:cd03300 1 IELENVSKFYGGFVA-LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIlldgkditnlppHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 740 ACSLQPDIDL---LPFG------DQTEIGE----------------RGIN-LSGGQRQRICVARALYQNTNIVFLDDPFS 793
Cdd:cd03300 80 NYALFPHLTVfenIAFGlrlkklPKAEIKErvaealdlvqlegyanRKPSqLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398974 794 ALDIHLSDHLMQEgiLKFLQDD-KRTLVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKDIqtkdvelYEHWKTL 866
Cdd:cd03300 160 ALDLKLRKDMQLE--LKRLQKElGITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEI-------YEEPANR 225
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
682-857 |
5.55e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 76.95 E-value: 5.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 682 GSGLATLS-NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV-----HWSKY--KAVTDACSLQPDIDLLPfG 753
Cdd:PRK10253 16 GYGKYTVAeNLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgeHIQHYasKEVARRIGLLAQNATTP-G 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 754 DQT--EIGERGI------------------------------------NLSGGQRQRICVARALYQNTNIVFLDDPFSAL 795
Cdd:PRK10253 95 DITvqELVARGRyphqplftrwrkedeeavtkamqatgithladqsvdTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 796 DIhlsDHlmQEGILKFLQDDKR----TLVLVTHKL----QYLTHadwIIAMKDGSVLREGTLKDIQTKDV 857
Cdd:PRK10253 175 DI---SH--QIDLLELLSELNRekgyTLAAVLHDLnqacRYASH---LIALREGKIVAQGAPKEIVTAEL 236
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
667-859 |
6.68e-15 |
|
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: 75.79 E-value: 6.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 667 TEDIAIKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwskykaV--TDACSLQ 744
Cdd:COG1127 1 MSEPMIEVRNLTKSFG-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEIL------VdgQDITGLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 745 PDiDLLP--------------FGD-------------QTEIGERGIN----------------------LSGGQRQRICV 775
Cdd:COG1127 74 EK-ELYElrrrigmlfqggalFDSltvfenvafplreHTDLSEAEIRelvleklelvglpgaadkmpseLSGGMRKRVAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 776 ARALYQNTNIVFLDDPFSALDIHLS---DHLMQEgilkfLQDD-KRTLVLVTHKLQYL-THADWIIAMKDGSVLREGTLK 850
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPITSaviDELIRE-----LRDElGLTSVVVTHDLDSAfAIADRVAVLADGKIIAEGTPE 227
|
....*....
gi 530398974 851 DIQTKDVEL 859
Cdd:COG1127 228 ELLASDDPW 236
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1265-1491 |
8.84e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 76.31 E-value: 8.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNL-KPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIF----DGKIVIDGIDISKLPLHTLR 1339
Cdd:PRK13650 5 IEVKNLTFKYKEDQeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTT----VRLIDGLleaeSGQIIIDGDLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1340 SRLSIILQDPI-LFSGS-----IRFNLDP---ECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1410
Cdd:PRK13650 81 HKIGMVFQNPDnQFVGAtveddVAFGLENkgiPHEEMKERVNEALELVGMQDFKEREPARL-----------SGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1411 CLARAFVRKSSILIMDEATASID--------MATENILQKVVMTafadrtVVTIAHRVHTILTADLVIVMKRGNILEYDT 1482
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDpegrleliKTIKGIRDDYQMT------VISITHDLDEVALSDRVLVMKNGQVESTST 223
|
....*....
gi 530398974 1483 PESLLAQEN 1491
Cdd:PRK13650 224 PRELFSRGN 232
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
672-852 |
1.27e-14 |
|
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: 74.91 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLL-----LAILGEMQTLEGKVHWskykAVTDACSLQPD 746
Cdd:cd03260 1 IELRDLNVYYGDKHA-LKDISLDIPKGEITALIGPSGCGKSTLLrllnrLNDLIPGAPDEGEVLL----DGKDIYDLDVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 747 IDLL------------PF-----------------GDQTEIGER-------------------GINLSGGQRQRICVARA 778
Cdd:cd03260 76 VLELrrrvgmvfqkpnPFpgsiydnvayglrlhgiKLKEELDERveealrkaalwdevkdrlhALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398974 779 LYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFlqDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 852
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPI-STAKIEELIAEL--KKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
664-827 |
1.81e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 75.20 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 664 PAETEDIAIKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLL-----LAILGEMQTLEGKVHW---SKYK 735
Cdd:PRK14243 3 TLNGTETVLRTENLNVYYGSFLA-VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrLNDLIPGFRVEGKVTFhgkNLYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 736 AVTDACSLQPDIDLL-----PF------------------GDQTEIGER------------------GINLSGGQRQRIC 774
Cdd:PRK14243 82 PDVDPVEVRRRIGMVfqkpnPFpksiydniaygaringykGDMDELVERslrqaalwdevkdklkqsGLSLSGGQQQRLC 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 530398974 775 VARALYQNTNIVFLDDPFSALDiHLSDhLMQEGILKFLQDDkRTLVLVTHKLQ 827
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALD-PIST-LRIEELMHELKEQ-YTIIIVTHNMQ 211
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1265-1489 |
1.82e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.51 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENN----LKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP-LHTLR 1339
Cdd:PRK13633 5 IKCKNVSYKYESNeestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1340 SRLSIILQDP------ILFSGSIRF---NLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1410
Cdd:PRK13633 85 NKAGMVFQNPdnqivaTIVEEDVAFgpeNLGIPPEEIRERVDESLKKVGMYEYRRHAPHLL-----------SGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1411 CLARAFVRKSSILIMDEATASIDmateNILQKVVMTAFADR------TVVTIAHRVHTILTADLVIVMKRGNILEYDTPE 1484
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLD----PSGRREVVNTIKELnkkygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPK 229
|
....*
gi 530398974 1485 SLLAQ 1489
Cdd:PRK13633 230 EIFKE 234
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
678-824 |
1.92e-14 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 74.90 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 678 YFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKyKAVTdacslQPDID--------- 748
Cdd:COG4525 13 YPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG-VPVT-----GPGADrgvvfqkda 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 749 LLPF---GDQTEIGER--GIN---------------------------LSGGQRQRICVARALYQNTNIVFLDDPFSALD 796
Cdd:COG4525 87 LLPWlnvLDNVAFGLRlrGVPkaerraraeellalvgladfarrriwqLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
170 180
....*....|....*....|....*...
gi 530398974 797 IhLSDHLMQEGILKFLQDDKRTLVLVTH 824
Cdd:COG4525 167 A-LTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1265-1490 |
2.08e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 75.27 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG--IDISKLPLHTLRSRL 1342
Cdd:PRK13636 6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1343 SIILQDP--ILFSGSIR-------FNLDPECKCTDDRLWEALE---IAQLKNmvkslpggldavvtEGGENFSVGQRQLF 1410
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYqdvsfgaVNLKLPEDEVRKRVDNALKrtgIEHLKD--------------KPTHCLSFGQKKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1411 CLARAFVRKSSILIMDEATASID-MATENILQKVVMTAFA-DRTVVTIAHRVHTI-LTADLVIVMKRGNILEYDTPESLL 1487
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDpMGVSEIMKLLVEMQKElGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVF 230
|
...
gi 530398974 1488 AQE 1490
Cdd:PRK13636 231 AEK 233
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
688-848 |
2.22e-14 |
|
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: 78.45 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSL--LLAIL-----GEM--------------------------QTLEGKVH---- 730
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIakLVAGLyqpwsGEIlfdgipreeiprevlansvamvdqdiFLFEGTVRdnlt 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 731 -WSK-------YKAVTDACsLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD----IH 798
Cdd:TIGR03796 575 lWDPtipdadlVRACKDAA-IHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDpeteKI 653
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 530398974 799 LSDHLMQEGIlkflqddkrTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 848
Cdd:TIGR03796 654 IDDNLRRRGC---------TCIIVAHRLSTIRDCDEIIVLERGKVVQRGT 694
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
688-842 |
2.35e-14 |
|
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: 72.74 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAIL---GEMQTLEGKVHWSKYKAVTdACSLQPDIDL----LPFGDQTEige 760
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLyasGKARLISFLPKFSRNKLIF-IDQLQFLIDVglgyLTLGQKLS--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 761 rgiNLSGGQRQRICVARALYQNT-NIVF-LDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLTHADWIIAM 838
Cdd:cd03238 87 ---TLSGGELQRVKLASELFSEPpGTLFiLDEPSTGLHQQDINQLLEV--IKGLIDLGNTVILIEHNLDVLSSADWIIDF 161
|
....
gi 530398974 839 KDGS 842
Cdd:cd03238 162 GPGS 165
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1282-1487 |
2.56e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 77.00 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1282 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS----RLSIILQDpilfsgsir 1357
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQS--------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1358 FNLDPECKCTDDRLWeALEIAQLKNMVKSlPGGLDAVVTEGGENF--------SVGQRQLFCLARAFVRKSSILIMDEAT 1429
Cdd:PRK10070 115 FALMPHMTVLDNTAF-GMELAGINAEERR-EKALDALRQVGLENYahsypdelSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398974 1430 ASID--MATENILQKVVMTAFADRTVVTIAHRV-HTILTADLVIVMKRGNILEYDTPESLL 1487
Cdd:PRK10070 193 SALDplIRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1265-1493 |
2.89e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 74.79 E-value: 2.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1344
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1345 ILQDPI-LFSGSI-----RFNLDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARA 1415
Cdd:PRK13648 88 VFQNPDnQFVGSIvkydvAFGLENHAVPYDEmhrRVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1416 FVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQENGV 1493
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1280-1489 |
3.09e-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: 74.89 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1280 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLSIILQDPILFSGSIRFN 1359
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1360 LDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEN- 1438
Cdd:cd03291 118 IIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKe 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 530398974 1439 ILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1489
Cdd:cd03291 198 IFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSL 248
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
703-866 |
3.12e-14 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 75.61 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 703 IVGQVGCGKSSLLLAILGEMQTLEGKVHWSKYKAVTDACSLQP------DIDLLP---------FG------DQTEIGER 761
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHinmvfqSYALFPhmtveenvaFGlkmrkvPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 762 -----------------GINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDD-KRTLVLVT 823
Cdd:TIGR01187 81 vlealrlvqleefadrkPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLE--LKTIQEQlGITFVFVT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 530398974 824 H-KLQYLTHADWIIAMKDGSVLREGTLKdiqtkdvELYEHWKTL 866
Cdd:TIGR01187 159 HdQEEAMTMSDRIAIMRKGKIAQIGTPE-------EIYEEPANL 195
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1265-1490 |
3.12e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 74.84 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSlaffRMV-------DIFDGKIVIDGIDISKLPLHT 1337
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTIS----KLInglllpdDNPNSKITVDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1338 LRSRLSIILQDPI-LFSGS-----IRFNLDpeckctdDRLWEALEIAQLKNMVKSLPGGLDAVVTEGgENFSVGQRQLFC 1411
Cdd:PRK13640 82 IREKVGIVFQNPDnQFVGAtvgddVAFGLE-------NRAVPRPEMIKIVRDVLADVGMLDYIDSEP-ANLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1412 LARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1489
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
.
gi 530398974 1490 E 1490
Cdd:PRK13640 234 V 234
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
688-852 |
3.15e-14 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 73.91 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKykavTDACSLQP---DIDLLP------------- 751
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG----KDITNLPPekrDISYVPqnyalfphmtvyk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 752 ---FG------DQTEIGER--------GIN---------LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQ 805
Cdd:cd03299 91 niaYGlkkrkvDKKEIERKvleiaemlGIDhllnrkpetLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLRE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 530398974 806 EgiLKFLQDDKRTLVL-VTHKL-QYLTHADWIIAMKDGSVLREGTLKDI 852
Cdd:cd03299 171 E--LKKIRKEFGVTVLhVTHDFeEAWALADKVAIMLNGKLIQVGKPEEV 217
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
688-836 |
3.41e-14 |
|
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: 71.80 E-value: 3.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSkykavTDACSL----QP--------DIDLLPFGDq 755
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMP-----EGEDLLflpqRPylplgtlrEQLIYPWDD- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 756 teigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegilkFLQDDKRTLVLVTHKLQYLTHADWI 835
Cdd:cd03223 91 --------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQ-----LLKELGITVISVGHRPSLWKFHDRV 157
|
.
gi 530398974 836 I 836
Cdd:cd03223 158 L 158
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
671-852 |
3.71e-14 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 77.25 E-value: 3.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 671 AIKVTNGYFSWGSG-LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG---EMQTLEGKVHWskykAVTDACSLQPD 746
Cdd:COG1123 4 LLEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLL----DGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 747 I----------------DLLPFGDQ------------TEIGERGIN-----------------LSGGQRQRICVARALYQ 781
Cdd:COG1123 80 LrgrrigmvfqdpmtqlNPVTVGDQiaealenlglsrAEARARVLElleavglerrldryphqLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398974 782 NTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDK-RTLVLVTHKLQY-LTHADWIIAMKDGSVLREGTLKDI 852
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILD--LLRELQRERgTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1260-1475 |
3.88e-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: 3.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1260 PQEGEIKIHDLCVRY--ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIDGidiskL 1333
Cdd:COG1116 3 AAAPALELRGVSKRFptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTL----LRLIagleKPTSGEVLVDG-----K 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1334 PLHTLRSRLSIILQDPILF-----SGSIRFNLD------PECKctdDRLWEALEIAQLKNMVKSLPGGLdavvteggenf 1402
Cdd:COG1116 74 PVTGPGPDRGVVFQEPALLpwltvLDNVALGLElrgvpkAERR---ERARELLELVGLAGFEDAYPHQL----------- 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530398974 1403 SVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVH-TILTADLVIVMKRG 1475
Cdd:COG1116 140 SGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETgkTVLFVTHDVDeAVFLADRVVVLSAR 215
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
664-848 |
4.21e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 77.17 E-value: 4.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 664 PAETEDIAIKVTNGYFSW-GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV--------HWSKy 734
Cdd:PRK11160 331 TAAADQVSLTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIllngqpiaDYSE- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 735 KAVTDACSL-------------------QPDID---------------LLPfGDQ---TEIGERGINLSGGQRQRICVAR 777
Cdd:PRK11160 410 AALRQAISVvsqrvhlfsatlrdnlllaAPNASdealievlqqvglekLLE-DDKglnAWLGEGGRQLSGGEQRRLGIAR 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398974 778 ALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 848
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERQILEL-LAEHAQN--KTVLMITHRLTGLEQFDRICVMDNGQIIEQGT 556
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
688-848 |
4.80e-14 |
|
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: 77.17 E-value: 4.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSL--LL---------AILGEMQTLegkvhwskyKAVTDAcSLQ------------ 744
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLarLLfrfydvtsgRILIDGQDI---------RDVTQA-SLRaaigivpqdtvl 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 745 -------------PD------------------IDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 793
Cdd:COG5265 444 fndtiayniaygrPDaseeeveaaaraaqihdfIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATS 523
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 530398974 794 ALDIHlSDHLMQEGiLKFLQDDKRTLVlVTHKLQYLTHADWIIAMKDGSVLREGT 848
Cdd:COG5265 524 ALDSR-TERAIQAA-LREVARGRTTLV-IAHRLSTIVDADEILVLEAGRIVERGT 575
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
690-856 |
5.84e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 72.87 E-value: 5.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 690 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWsKYKAVTD---------------------------ACS 742
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILW-NGQDLTAlppaerpvsmlfqennlfphltvaqniGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 743 LQPDIDLLPfGDQT---EIGER-GIN---------LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegIL 809
Cdd:COG3840 96 LRPGLKLTA-EQRAqveQALERvGLAglldrlpgqLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLD--LV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 530398974 810 KFLQDD-KRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQTKD 856
Cdd:COG3840 173 DELCRErGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGE 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1265-1485 |
6.21e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 73.93 E-value: 6.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNL---KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIS--KLPLHTLR 1339
Cdd:PRK13637 3 IKIENLTHIYMEGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1340 SRLSIILQDP------------ILFsGSIRFNL-DPECKctdDRLWEALEIAqlknmvkslpgGLDAVVTEGGENF--SV 1404
Cdd:PRK13637 83 KKVGLVFQYPeyqlfeetiekdIAF-GPINLGLsEEEIE---NRVKRAMNIV-----------GLDYEDYKDKSPFelSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1405 GQRQLFCLARAFVRKSSILIMDEATASID-MATENILQKV-VMTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYD 1481
Cdd:PRK13637 148 GQKRRVAIAGVVAMEPKILILDEPTAGLDpKGRDEILNKIkELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQG 227
|
....
gi 530398974 1482 TPES 1485
Cdd:PRK13637 228 TPRE 231
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
684-827 |
6.49e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 73.58 E-value: 6.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKyKAVTD-----ACSLQPDiDLLP------- 751
Cdd:PRK11248 13 GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG-KPVEGpgaerGVVFQNE-GLLPwrnvqdn 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 752 --FG----------------------DQTEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHlMQE 806
Cdd:PRK11248 91 vaFGlqlagvekmqrleiahqmlkkvGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ-MQT 169
|
170 180
....*....|....*....|.
gi 530398974 807 GILKFLQDDKRTLVLVTHKLQ 827
Cdd:PRK11248 170 LLLKLWQETGKQVLLITHDIE 190
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
671-852 |
7.32e-14 |
|
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: 72.76 E-value: 7.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 671 AIKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhWSKYKAVTDACSLQPDI--- 747
Cdd:cd03296 2 SIEVRNVSKRFGDFVA-LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTI-LFGGEDATDVPVQERNVgfv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 748 -------------DLLPFG----------DQTEIGERGINL-----------------SGGQRQRICVARALYQNTNIVF 787
Cdd:cd03296 80 fqhyalfrhmtvfDNVAFGlrvkprserpPEAEIRAKVHELlklvqldwladrypaqlSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398974 788 LDDPFSALDIHLSDHLmqEGILKFLQDDKR-TLVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKDI 852
Cdd:cd03296 160 LDEPFGALDAKVRKEL--RRWLRRLHDELHvTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1265-1490 |
7.46e-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: 72.58 E-value: 7.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslaFFRMVDIF---DGKIVIDGIDISKLPLHTlRSR 1341
Cdd:cd03218 1 LRAENLSKRYGK--RKVVNGVSLSVKQGEIVGLLGPNGAGKTTT---FYMIVGLVkpdSGKILLDGQDITKLPMHK-RAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1342 LSIIL--QDPILFSG-SIRFNL--------DPEcKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1410
Cdd:cd03218 75 LGIGYlpQEASIFRKlTVEENIlavleirgLSK-KEREEKLEELLEEFHITHLRKSKASSL-----------SGGERRRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1411 CLARAFVRKSSILIMDEATASID-MATENIlQKVVMTaFADRTV-VTIA-HRVHTIL-TADLVIVMKRGNILEYDTPESL 1486
Cdd:cd03218 143 EIARALATNPKFLLLDEPFAGVDpIAVQDI-QKIIKI-LKDRGIgVLITdHNVRETLsITDRAYIIYEGKVLAEGTPEEI 220
|
....
gi 530398974 1487 LAQE 1490
Cdd:cd03218 221 AANE 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1265-1477 |
9.33e-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: 71.79 E-value: 9.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDI--SKLPLHTLRSRL 1342
Cdd:cd03262 1 IEIKNLHKSFGDF--HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1343 SIILQDpilfsgsirFNLDPECK----CTDDRLW-------EALEIA-------QLKNMVKSLPGGLdavvteggenfSV 1404
Cdd:cd03262 79 GMVFQQ---------FNLFPHLTvlenITLAPIKvkgmskaEAEERAlellekvGLADKADAYPAQL-----------SG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530398974 1405 GQRQLFCLARAFVRKSSILIMDEATASID--MATEnILQkvVMTAFADR--TVVTIAHRVHTIL-TADLVIVMKRGNI 1477
Cdd:cd03262 139 GQQQRVAIARALAMNPKVMLFDEPTSALDpeLVGE-VLD--VMKDLAEEgmTMVVVTHEMGFAReVADRVIFMDDGRI 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
688-852 |
1.05e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 74.60 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKyKAVTDACSLQPDID-------LLP--------- 751
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDG-QDITHVPAENRHVNtvfqsyaLFPhmtvfenva 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 752 FG------DQTEIGERGI-----------------NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgi 808
Cdd:PRK09452 109 FGlrmqktPAAEITPRVMealrmvqleefaqrkphQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNE-- 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 530398974 809 LKFLQddkRTL----VLVTH-KLQYLTHADWIIAMKDGSVLREGTLKDI 852
Cdd:PRK09452 187 LKALQ---RKLgitfVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
668-847 |
1.17e-13 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 71.04 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 668 EDIAIKVTNGyfSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG--EMQTLEGKV-------HWSKYKAVT 738
Cdd:cd03213 7 RNLTVTVKSS--PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVlingrplDKRSFRKII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 739 DACsLQPDIdLLPFgdQTeIGE--------RGInlSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILK 810
Cdd:cd03213 85 GYV-PQDDI-LHPT--LT-VREtlmfaaklRGL--SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS--LLR 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 530398974 811 FLQDDKRTLVLVTHKLQYLTHA--DWIIAMKDGSVLREG 847
Cdd:cd03213 156 RLADTGRTIICSIHQPSSEIFElfDKLLLLSQGRVIYFG 194
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1263-1498 |
1.49e-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: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1263 GEIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLsLaffRMV----DIFDGKIVIDGIDISKLPlhTL 1338
Cdd:COG3839 2 ASLELENVSKSYGG--VEALKDIDLDIEDGEFLVLLGPSGCGKSTL-L---RMIagleDPTSGEILIGGRDVTDLP--PK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1339 RSRLSIILQDPILF-SGSIRFNL----------DPEckcTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQR 1407
Cdd:COG3839 74 DRNIAMVFQSYALYpHMTVYENIafplklrkvpKAE---IDRRVREAAELLGLEDLLDRKPKQL-----------SGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1408 QLFCLARAFVRKSSILIMDEATASID------MATE--NILQKVVMTafadrTV-VTiaHRVHTILT-ADLVIVMKRGNI 1477
Cdd:COG3839 140 QRVALGRALVREPKVFLLDEPLSNLDaklrveMRAEikRLHRRLGTT-----TIyVT--HDQVEAMTlADRIAVMNDGRI 212
|
250 260
....*....|....*....|..
gi 530398974 1478 LEYDTPESLLAQENGVF-ASFV 1498
Cdd:COG3839 213 QQVGTPEELYDRPANLFvAGFI 234
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
680-845 |
1.71e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 75.53 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 680 SWGSG---LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILG---------------EMQTLEGKV------------ 729
Cdd:PRK10535 13 SYPSGeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLM-NILGcldkptsgtyrvagqDVATLDADAlaqlrrehfgfi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 730 --------HWSK---------YKAVTDACSLQPDIDLLP-FGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 791
Cdd:PRK10535 92 fqryhllsHLTAaqnvevpavYAGLERKQRLLRAQELLQrLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 530398974 792 FSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLR 845
Cdd:PRK10535 172 TGALDSHSGEEVM--AILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
692-847 |
1.72e-13 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 70.98 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 692 DIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV----------------------------HWSKYKAVtdACSL 743
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVlingvdvtaappadrpvsmlfqennlfaHLTVEQNV--GLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 744 QPDIDLLPFgDQTEI----GERGIN---------LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHlMQEGILK 810
Cdd:cd03298 96 SPGLKLTAE-DRQAIevalARVGLAglekrlpgeLSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE-MLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 530398974 811 FLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREG 847
Cdd:cd03298 174 LHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1265-1498 |
2.21e-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: 73.21 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDifDGKIVIDGIDISKLPLHtlRSRL 1342
Cdd:COG3842 6 LELENVSKRYGDV--TALDDVSLSIEPGEFVALLGPSGCGKTTLlrMIAGFETPD--SGRILLDGRDVTGLPPE--KRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1343 SIILQDPILF-----SGSIRFNLD------PECKctdDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 1411
Cdd:COG3842 80 GMVFQDYALFphltvAENVAFGLRmrgvpkAEIR---ARVAELLELVGLEGLADRYPHQL-----------SGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1412 LARAFVRKSSILIMDEATASID------MATE--NILQKVVMTAFadrtVVTiaHRVHTILT-ADLVIVMKRGNILEYDT 1482
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDaklreeMREElrRLQRELGITFI----YVT--HDQEEALAlADRIAVMNDGRIEQVGT 219
|
250
....*....|....*..
gi 530398974 1483 PESLLAQENGVF-ASFV 1498
Cdd:COG3842 220 PEEIYERPATRFvADFI 236
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
672-856 |
2.25e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 73.72 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS--------------KYKAV 737
Cdd:PRK09536 4 IDVSDLSVEFG-DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgddvealsaraasrRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 738 TDACSLQPDID------------LLPFGDQTEIGERGI------------------NLSGGQRQRICVARALYQNTNIVF 787
Cdd:PRK09536 83 PQDTSLSFEFDvrqvvemgrtphRSRFDTWTETDRAAVeramertgvaqfadrpvtSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398974 788 LDDPFSALDIHlsdHLMQE-GILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDIQTKD 856
Cdd:PRK09536 163 LDEPTASLDIN---HQVRTlELVRRLVDDGKTAVAAIHDLDLAArYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1280-1490 |
2.32e-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: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1280 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLSIILQDPILFSGSIRFN 1359
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1360 LDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE-N 1438
Cdd:TIGR01271 507 IIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEkE 586
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 530398974 1439 ILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQE 1490
Cdd:TIGR01271 587 IFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1277-1487 |
2.40e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 71.62 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1277 NLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGI------DISKLPLHTLRSRLSIILQDPI 1350
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1351 LFSG-SIRFNLDPECKCTDDRlwEALEIAQLKNMVKSLPGGLDAV---VTEGGENFSVGQRQLFCLARAFVRKSSILIMD 1426
Cdd:PRK14246 101 PFPHlSIYDNIAYPLKSHGIK--EKREIKKIVEECLRKVGLWKEVydrLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398974 1427 EATASIDMATENILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLL 1487
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVArVADYVAFLYNGELVEWGSSNEIF 240
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1265-1478 |
2.71e-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: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENnlKPVLKHVKAYIKPGQkVGICGRTGSGKSSL--SLA-FFRMVDifdGKIVIDGIDISKLPlHTLRSR 1341
Cdd:cd03264 1 LQLENLTKRYGK--KRALDGVSLTLGPGM-YGLLGPNGAGKTTLmrILAtLTPPSS---GTIRIDGQDVLKQP-QKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1342 LSIILQDpilFSGSIRFnldpeckctddRLWEALE-IAQLKNMVKS-----LPGGLDAVVTEGGEN-----FSVGQRQLF 1410
Cdd:cd03264 74 IGYLPQE---FGVYPNF-----------TVREFLDyIAWLKGIPSKevkarVDEVLELVNLGDRAKkkigsLSGGMRRRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398974 1411 CLARAFVRKSSILIMDEATASID----MATENILQKVVmtafADRTVVTIAHRVHTI-LTADLVIVMKRGNIL 1478
Cdd:cd03264 140 GIAQALVGDPSILIVDEPTAGLDpeerIRFRNLLSELG----EDRIVILSTHIVEDVeSLCNQVAVLNKGKLV 208
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1265-1475 |
3.87e-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: 68.61 E-value: 3.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL-PLHTLRSRLS 1343
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAsPRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1344 IILQdpilfsgsirfnldpeckctddrlwealeiaqlknmvkslpggldavvteggenFSVGQRQLFCLARAFVRKSSIL 1423
Cdd:cd03216 79 MVYQ------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 530398974 1424 IMDEATASIDMA-TENILQkvVMTAFADR--TVVTIAHRVHTIL-TADLVIVMKRG 1475
Cdd:cd03216 105 ILDEPTAALTPAeVERLFK--VIRRLRAQgvAVIFISHRLDEVFeIADRVTVLRDG 158
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
663-827 |
4.04e-13 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 71.22 E-value: 4.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 663 RPAETEDIAIKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI-----LGEMQTLEGKVHwskykaV 737
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDKQA-LKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndLIPGARVEGEIL------L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 738 TDACSLQPDIDLL--------------PF----------G-------DQTEIGER---------------------GINL 765
Cdd:COG1117 76 DGEDIYDPDVDVVelrrrvgmvfqkpnPFpksiydnvayGlrlhgikSKSELDEIveeslrkaalwdevkdrlkksALGL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398974 766 SGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDH---LMQEgiLKflqdDKRTLVLVTHKLQ 827
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKieeLILE--LK----KDYTIVIVTHNMQ 214
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1265-1459 |
6.45e-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: 6.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIdgidisklplhTLRS 1340
Cdd:cd03223 1 IELENLSLATPDG-RVLLKDLSFEIKPGDRLLITGPSGTGKSSL----FRALaglwPWGSGRIGM-----------PEGE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1341 RLSIILQDPILFSGSIRfnldpeckctddrlwealeiaqlknmvkslpgglDAVVTEGGENFSVGQRQLFCLARAFVRKS 1420
Cdd:cd03223 65 DLLFLPQRPYLPLGTLR----------------------------------EQLIYPWDDVLSGGEQQRLAFARLLLHKP 110
|
170 180 190
....*....|....*....|....*....|....*....
gi 530398974 1421 SILIMDEATASIDMATENILQKVVMTAFAdrTVVTIAHR 1459
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
690-847 |
7.52e-13 |
|
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: 69.25 E-value: 7.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 690 NIDIRIPtGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV----------------------------------HWSKYK 735
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfdsrkkinlppqqrkiglvfqqyalfpHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 736 AVT---DACSLQPDID----LLPFGDQTEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEg 807
Cdd:cd03297 95 NLAfglKRKRNREDRIsvdeLLDLLGLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 530398974 808 ILKFLQDDKRTLVLVTHKL---QYLthADWIIAMKDGSVLREG 847
Cdd:cd03297 174 LKQIKKNLNIPVIFVTHDLseaEYL--ADRIVVMEDGRLQYIG 214
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
687-875 |
8.61e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 70.19 E-value: 8.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 687 TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI--LGEMQ---TLEGKVHWSK---YKAVTDACSLQPDIDLL-----PFG 753
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNpevTITGSIVYNGhniYSPRTDTVDLRKEIGMVfqqpnPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 754 ----------------------DQT------------EIGER----GINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 795
Cdd:PRK14239 100 msiyenvvyglrlkgikdkqvlDEAvekslkgasiwdEVKDRlhdsALGLSGGQQQRVCIARVLATSPKIILLDEPTSAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 796 DiHLSDHLMQEGILKFlqDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIqtkdvelyehwktLMNRQDQEL 874
Cdd:PRK14239 180 D-PISAGKIEETLLGL--KDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQM-------------FMNPKHKET 243
|
.
gi 530398974 875 E 875
Cdd:PRK14239 244 E 244
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1202-1479 |
8.74e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.82 E-value: 8.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1202 GLGLLYaltITNYLNwVVRNLADLEVQMGAVKKV--NSFLTMESE----------NYEGTMDPSQVPEHWPQEgeIKIHD 1269
Cdd:PRK15134 207 NMGLLF---ITHNLS-IVRKLADRVAVMQNGRCVeqNRAATLFSApthpytqkllNSEPSGDPVPLPEPASPL--LDVEQ 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1270 LCVRYE---------NNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDGKIVIDGidiskLPLHTL-- 1338
Cdd:PRK15134 281 LQVAFPirkgilkrtVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIWFDG-----QPLHNLnr 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1339 ------RSRLSIILQDPilfSGSIRFNLDPEckctdDRLWEALEI-------AQLKNMVKSLPG--GLDAVV-----TEg 1398
Cdd:PRK15134 355 rqllpvRHRIQVVFQDP---NSSLNPRLNVL-----QIIEEGLRVhqptlsaAQREQQVIAVMEevGLDPETrhrypAE- 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1399 genFSVGQRQLFCLARAFVRKSSILIMDEATASID-------MATENILQKVVMTAFadrtvVTIAHRVHTILT-ADLVI 1470
Cdd:PRK15134 426 ---FSGGQRQRIAIARALILKPSLIILDEPTSSLDktvqaqiLALLKSLQQKHQLAY-----LFISHDLHVVRAlCHQVI 497
|
....*....
gi 530398974 1471 VMKRGNILE 1479
Cdd:PRK15134 498 VLRQGEVVE 506
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
688-848 |
1.31e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 69.42 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV--------HWS-----KYKAV----------------- 737
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVrlngrplaDWSpaelaRRRAVlpqhsslsfpftveevv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 738 -----TDACSLQPD----------IDLLPFGD---QTeigerginLSGGQRQRICVARALYQNTN------IVFLDDPFS 793
Cdd:PRK13548 98 amgraPHGLSRAEDdalvaaalaqVDLAHLAGrdyPQ--------LSGGEQQRVQLARVLAQLWEpdgpprWLLLDEPTS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 794 ALDIHLSDHLMQegILK-FLQDDKRTLVLVTHKL----QYlthADWIIAMKDGSVLREGT 848
Cdd:PRK13548 170 ALDLAHQHHVLR--LARqLAHERGLAVIVVLHDLnlaaRY---ADRIVLLHQGRLVADGT 224
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
671-847 |
1.38e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.91 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 671 AIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGK---------------------- 728
Cdd:PRK15056 6 GIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKisilgqptrqalqknlvayvpq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 729 ---VHWS------------KY--------------KAVTDACSlqpDIDLLPFgDQTEIGErginLSGGQRQRICVARAL 779
Cdd:PRK15056 86 seeVDWSfpvlvedvvmmgRYghmgwlrrakkrdrQIVTAALA---RVDMVEF-RHRQIGE----LSGGQKKRVFLARAI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398974 780 YQNTNIVFLDDPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKdGSVLREG 847
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARII--SLLRELRDEGKTMLVSTHNLGSVTEfCDYTVMVK-GTVLASG 223
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
753-880 |
1.58e-12 |
|
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: 72.23 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 753 GDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHA 832
Cdd:TIGR01192 460 GYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVE-TEARVKNAIDALRKN--RTTFIIAHRLSTVRNA 536
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 530398974 833 DWIIAMKDGSVLREGTLKDIQTKDVELYEHWKTLMNRQDQELEKDMEA 880
Cdd:TIGR01192 537 DLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRRSGLLTNQPATKPLRK 584
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1265-1500 |
2.60e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.99 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1344
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1345 ILQDP--ILFSGSIR-------FNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARA 1415
Cdd:PRK13647 84 VFQDPddQVFSSTVWddvafgpVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1416 FVRKSSILIMDEATASIDMATenilQKVVMTAFAD-----RTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPeSLLAQ 1489
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRG----QETLMEILDRlhnqgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDK-SLLTD 227
|
250
....*....|.
gi 530398974 1490 ENGVFASFVRA 1500
Cdd:PRK13647 228 EDIVEQAGLRL 238
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
697-824 |
2.93e-12 |
|
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: 65.86 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 697 TGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwskykaVTDACSLQPDIDLLpFGDQTEIGERGINLSGGQRQRICVA 776
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV-------IYIDGEDILEEVLD-QLLLIIVGGKKASGSGELRLRLALA 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 530398974 777 RALYQNTNIVFLDDPFSALDIHLSDHLMQEG----ILKFLQDDKRTLVLVTH 824
Cdd:smart00382 73 LARKLKPDVLILDEITSLLDAEQEALLLLLEelrlLLLLKSEKNLTVILTTN 124
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1265-1490 |
3.06e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.07 E-value: 3.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENnlkpvLK-HVKAYIKPGQKVGICGRTGSGKSSL-SL-AFFRMVDifDGKIVIDGIDisklplHTL--- 1338
Cdd:PRK10771 2 LKLTDITWLYHH-----LPmRFDLTVERGERVAILGPSGAGKSTLlNLiAGFLTPA--SGSLTLNGQD------HTTtpp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1339 -RSRLSIILQDPILFSG-SIRFN----LDPECKCTDDRLWEALEIAQ---LKNMVKSLPGGLdavvteggenfSVGQRQL 1409
Cdd:PRK10771 69 sRRPVSMLFQENNLFSHlTVAQNiglgLNPGLKLNAAQREKLHAIARqmgIEDLLARLPGQL-----------SGGQRQR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1410 FCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRV---HTILTADLVIVmkRGNILeYDTP- 1483
Cdd:PRK10771 138 VALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLedaARIAPRSLVVA--DGRIA-WDGPt 214
|
....*..
gi 530398974 1484 ESLLAQE 1490
Cdd:PRK10771 215 DELLSGK 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1265-1490 |
4.54e-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: 4.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLSlaffRMVDIFD----GKIVIDGIDISKLP---L 1335
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLI----RCINLLErptsGSVLVDGVDLTALSereL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1336 HTLRSRLSIILQDpilfsgsirFNLdpeckctddrLWE---------ALEIA-----QLKNMVKSLpggLDAVVTEGGEN 1401
Cdd:COG1135 78 RAARRKIGMIFQH---------FNL----------LSSrtvaenvalPLEIAgvpkaEIRKRVAEL---LELVGLSDKAD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1402 F-----SVGQRQLFCLARAFVRKSSILIMDEATASIDMA-TENIL---QKVvmtafADR---TVVTIAHRVHTILT-ADL 1468
Cdd:COG1135 136 AypsqlSGGQKQRVGIARALANNPKVLLCDEATSALDPEtTRSILdllKDI-----NRElglTIVLITHEMDVVRRiCDR 210
|
250 260
....*....|....*....|....*....
gi 530398974 1469 VIVMKRGNILEYDT-------PESLLAQE 1490
Cdd:COG1135 211 VAVLENGRIVEQGPvldvfanPQSELTRR 239
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
667-852 |
4.54e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 68.09 E-value: 4.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 667 TEDIAIKVTNGYFSWGSG-LATLSNIDIRIPTGQLTMIVGQVGCGKSS---LLLAIL----GEMQT-------------- 724
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTiskILTGLLkpqsGEIKIdgitiskenlkeir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 725 --------------------------LEGK-VHWSKYKAVTDACSLQPDI-DLLPFGDQteigergiNLSGGQRQRICVA 776
Cdd:PRK13632 83 kkigiifqnpdnqfigatveddiafgLENKkVPPKKMKDIIDDLAKKVGMeDYLDKEPQ--------NLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398974 777 RALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDD-KRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDI 852
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKK--IMVDLRKTrKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
691-862 |
4.96e-12 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 69.37 E-value: 4.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 691 IDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV------------------HWSKYKAVTDACSLQPDIDL--- 749
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIvlngrtlfdsrkgiflppEKRRIGYVFQEARLFPHLSVrgn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 750 LPFG------DQTEIG--------------ERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHlmqegI 808
Cdd:TIGR02142 96 LRYGmkrarpSERRISferviellgighllGRLPGrLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE-----I 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 809 LKFLQDDKRTL----VLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQ-TKDVELYEH 862
Cdd:TIGR02142 171 LPYLERLHAEFgipiLYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWaSPDLPWLAR 230
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1265-1477 |
5.54e-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: 5.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIDGIDISKLPlhtLRS 1340
Cdd:cd03301 1 VELENVTKRFGN--VTALDDLNLDIADGEFVVLLGPSGCGKTTT----LRMIagleEPTSGRIYIGGRDVTDLP---PKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1341 R-LSIILQDPILFS-----GSIRFNLD----PEcKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1410
Cdd:cd03301 72 RdIAMVFQNYALYPhmtvyDNIAFGLKlrkvPK-DEIDERVREVAELLQIEHLLDRKPKQL-----------SGGQRQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398974 1411 CLARAFVRKSSILIMDEATASID------MATE-NILQKVVmtafaDRTVVTIAH-RVHTILTADLVIVMKRGNI 1477
Cdd:cd03301 140 ALGRAIVREPKVFLMDEPLSNLDaklrvqMRAElKRLQQRL-----GTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
671-830 |
5.77e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 67.75 E-value: 5.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 671 AIKVTNGYFSWGSGlATLSNIDIRIPTGQLTMIVGQVGCGKSSLL--LAILGEMQT---LEGKVHW---SKYKAVTDACS 742
Cdd:PRK14258 7 AIKVNNLSFYYDTQ-KILEGVSMEIYQSKVTAIIGPSGCGKSTFLkcLNRMNELESevrVEGRVEFfnqNIYERRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 743 LQ-------PDIDLLPFG----------------------------------DQTE--IGERGINLSGGQRQRICVARAL 779
Cdd:PRK14258 86 LRrqvsmvhPKPNLFPMSvydnvaygvkivgwrpkleiddivesalkdadlwDEIKhkIHKSALDLSGGQQQRLCIARAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 530398974 780 YQNTNIVFLDDPFSALDIHLS---DHLMQEGILKflqdDKRTLVLVTHKLQYLT 830
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASmkvESLIQSLRLR----SELTMVIVSHNLHQVS 215
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
688-852 |
5.89e-12 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 67.22 E-value: 5.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG-EMQTlEGKVH-------------------------------WSKYK 735
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGlERPT-SGSVLvdgtdltllsgkelrkarrrigmifqhfnllSSRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 736 AVTDACSLQpdidlLPFGDQTEIGER--------GI---------NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 798
Cdd:cd03258 100 FENVALPLE-----IAGVPKAEIEERvlellelvGLedkadaypaQLSGGQKQRVGIARALANNPKVLLCDEATSALDPE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 530398974 799 LSDhlmqeGILKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 852
Cdd:cd03258 175 TTQ-----SILALLRDINRelglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1265-1491 |
8.73e-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: 8.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSL-SLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLS 1343
Cdd:COG1119 4 LELRNVTVRRGG--KTILDDISWTVKPGEHWAILGPNGAGKSTLlSLITGDLPPTYGNDVRLFGERRGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1344 II---LQDPIL------------FSGSI-RF-NLDPECKCTDDRLWEALEIAQLKNM-VKSLpggldavvteggenfSVG 1405
Cdd:COG1119 82 LVspaLQLRFPrdetvldvvlsgFFDSIgLYrEPTDEQRERARELLELLGLAHLADRpFGTL---------------SQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1406 QRQLFCLARAFVRKSSILIMDEATASIDM-ATENILQkvVMTAFA---DRTVVTIAHRVHTILTA-DLVIVMKRGNILEY 1480
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLgARELLLA--LLDKLAaegAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAA 224
|
250
....*....|.
gi 530398974 1481 DTPESLLAQEN 1491
Cdd:COG1119 225 GPKEEVLTSEN 235
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
760-872 |
9.29e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 67.35 E-value: 9.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 760 ERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDDKRTLVLVTHKLQY-LTHADWIIAM 838
Cdd:PRK09984 148 QRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPE-SARIVMDTLRDINQNDGITVVVTLHQVDYaLRYCERIVAL 226
|
90 100 110
....*....|....*....|....*....|....
gi 530398974 839 KDGSVLREGTlkdIQTKDVELYEHWKTLMNRQDQ 872
Cdd:PRK09984 227 RQGHVFYDGS---SQQFDNERFDHLYRSINRVEE 257
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
690-854 |
9.90e-12 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 68.20 E-value: 9.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 690 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV----------------------------------HWS--- 732
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIrlggevlqdsargiflpphrrrigyvfqearlfpHLSvrg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 733 --KY---KAVTDACSLQPD--IDLLpfgdqtEIG---ERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD 801
Cdd:COG4148 97 nlLYgrkRAPRAERRISFDevVELL------GIGhllDRRPaTLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 530398974 802 HLMQegILKFLQDDKRTLVL-VTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQT 854
Cdd:COG4148 171 EILP--YLERLRDELDIPILyVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLS 223
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
751-848 |
1.06e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 69.60 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 751 PFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLmQEGILKFLQDdkRTLVLVTHKLQYLT 830
Cdd:PRK13657 458 PDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKV-KAALDELMKG--RTTFIIAHRLSTVR 534
|
90
....*....|....*...
gi 530398974 831 HADWIIAMKDGSVLREGT 848
Cdd:PRK13657 535 NADRILVFDNGRVVESGS 552
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
676-860 |
1.31e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 68.13 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 676 NGYFSWGSGLATlSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG--------------EMQTLE------GKVHWSkYk 735
Cdd:PRK11000 8 NVTKAYGDVVIS-KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGleditsgdlfigekRMNDVPpaergvGMVFQS-Y- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 736 avtdacSLQPDIDL---LPFG------DQTEIGERgIN------------------LSGGQRQRICVARALYQNTNIVFL 788
Cdd:PRK11000 85 ------ALYPHLSVaenMSFGlklagaKKEEINQR-VNqvaevlqlahlldrkpkaLSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398974 789 DDPFSALDIHLSDHlMQEGILKFLQDDKRTLVLVTH-KLQYLTHADWIIAMKDGSVLREGtlkdiqtKDVELY 860
Cdd:PRK11000 158 DEPLSNLDAALRVQ-MRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG-------KPLELY 222
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1265-1463 |
1.73e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 66.21 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI-----FDGKIVIDGIDI--SKLPLHT 1337
Cdd:PRK14258 8 IKVNNLSFYYDT--QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELesevrVEGRVEFFNQNIyeRRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1338 LRSRLSIILQDPILFSGSIRFNLDPECKCT--------DDRLWEALEIAQLKNMVKSlpggldaVVTEGGENFSVGQRQL 1409
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNVAYGVKIVgwrpkleiDDIVESALKDADLWDEIKH-------KIHKSALDLSGGQQQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 530398974 1410 FCLARAFVRKSSILIMDEATASID----MATENILQKVVMTafADRTVVTIAHRVHTI 1463
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLR--SELTMVIVSHNLHQV 214
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1265-1479 |
1.75e-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: 64.86 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLS--LAFFRMVDIFDGKIVIDGIDISKLPLHtLRSRL 1342
Cdd:cd03217 1 LEIKDLHVSVGG--KEILKGVNLTIKKGEVHALMGPNGSGKSTLAktIMGHPKYEVTEGEILFKGEDITDLPPE-ERARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1343 SIIL--QDPILFSGsirfnldpeckctddrlwealeiAQLKNMVKSLpggldavvtegGENFSVGQRQLFCLARAFVRKS 1420
Cdd:cd03217 78 GIFLafQYPPEIPG-----------------------VKNADFLRYV-----------NEGFSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398974 1421 SILIMDEATASIDMATENILQKVVMT-AFADRTVVTIAH--RVHTILTADLVIVMKRGNILE 1479
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVK 185
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1265-1498 |
1.80e-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: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHtlRS 1340
Cdd:cd03300 1 IELENVSKFYGG--FVALDGVSLDIKEGEFFTLLGPSGCGKTTL----LRLIAGFEtptsGEILLDGKDITNLPPH--KR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1341 RLSIILQDPILF-----SGSIRFNLD----PEcKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 1411
Cdd:cd03300 73 PVNTVFQNYALFphltvFENIAFGLRlkklPK-AEIKERVAEALDLVQLEGYANRKPSQL-----------SGGQQQRVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1412 LARAFVRKSSILIMDEATASIDMATENILQkVVMTAFADRTVVTIAHRVH----TILTADLVIVMKRGNILEYDTPESLL 1487
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDLKLRKDMQ-LELKRLQKELGITFVFVTHdqeeALTMSDRIAVMNKGKIQQIGTPEEIY 219
|
250
....*....|..
gi 530398974 1488 AQENGVF-ASFV 1498
Cdd:cd03300 220 EEPANRFvADFI 231
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
672-852 |
2.04e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 66.25 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKYKAVTDACSL-------- 743
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLlevrktvg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 744 ----QPDIDL--------LPFG------DQTEIGER--------GI---------NLSGGQRQRICVARALYQNTNIVFL 788
Cdd:PRK13639 82 ivfqNPDDQLfaptveedVAFGplnlglSKEEVEKRvkealkavGMegfenkpphHLSGGQKKRVAIAGILAMKPEIIVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398974 789 DDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYL-THADWIIAMKDGSVLREGTLKDI 852
Cdd:PRK13639 162 DEPTSGLDPMGASQIMK--LLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
688-824 |
2.17e-11 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 64.81 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHW---------SKYKA----VTDACSLQPD-------- 746
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWngepirdarEDYRRrlayLGHADGLKPEltvrenlr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 747 ---------------------IDLLPFGDQtEIGergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDI-------- 797
Cdd:COG4133 98 fwaalyglradreaidealeaVGLAGLADL-PVR----QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAagvallae 172
|
170 180
....*....|....*....|....*..
gi 530398974 798 HLSDHLMQEGIlkflqddkrtLVLVTH 824
Cdd:COG4133 173 LIAAHLARGGA----------VLLTTH 189
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
672-841 |
2.40e-11 |
|
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: 64.86 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI--LGEMQ----TLEG------KVHWSKY----- 734
Cdd:cd03262 1 IEIKNLHKSFG-DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCInlLEEPDsgtiIIDGlkltddKKNINELrqkvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 735 -----------KAVTDACSLQPDIDL-LPFGDQTEIGER-----GI---------NLSGGQRQRICVARALYQNTNIVFL 788
Cdd:cd03262 80 mvfqqfnlfphLTVLENITLAPIKVKgMSKAEAEERALEllekvGLadkadaypaQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 530398974 789 DDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDG 841
Cdd:cd03262 160 DEPTSALDPELVGEVLD--VMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDG 211
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1265-1488 |
2.77e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 65.88 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLS 1343
Cdd:PRK13642 5 LEVENLVFKYEKESDvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1344 IILQDPI-LFSGSIrfnldpeckcTDDRLWEALEIAQL--KNMVKSLPGGLDAV-----VTEGGENFSVGQRQLFCLARA 1415
Cdd:PRK13642 85 MVFQNPDnQFVGAT----------VEDDVAFGMENQGIprEEMIKRVDEALLAVnmldfKTREPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530398974 1416 FVRKSSILIMDEATASIDMATENILQKVVMtAFADR---TVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLA 1488
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIH-EIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1291-1479 |
3.06e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.96 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1291 PGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSRLSIILQDPILfsgsirfNLDPEcKCT 1367
Cdd:PRK10261 349 PGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPYA-------SLDPR-QTV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1368 DDRLWEALEIAQL---KNMVKSLPGGLDAV------VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE- 1437
Cdd:PRK10261 421 GDSIMEPLRVHGLlpgKAAAARVAWLLERVgllpehAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRg 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 530398974 1438 ---NI---LQKVVMTAFA----DRTVVT-IAHRvhtiltadlVIVMKRGNILE 1479
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 ... |
1264-1498 |
3.33e-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: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1264 EIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLhtlRSR-L 1342
Cdd:cd03296 2 SIEVRNVSKRFGD--FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV---QERnV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1343 SIILQDPILF-----SGSIRFNLD-------PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1410
Cdd:cd03296 77 GFVFQHYALFrhmtvFDNVAFGLRvkprserPPEAEIRAKVHELLKLVQLDWLADRYPAQL-----------SGGQRQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1411 CLARAFVRKSSILIMDEATASIDMATENILQKVVmTAFADRTVVTIAHRVH----TILTADLVIVMKRGNILEYDTPESL 1486
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRRWL-RRLHDELHVTTVFVTHdqeeALEVADRVVVMNKGRIEQVGTPDEV 224
|
250
....*....|...
gi 530398974 1487 LAQENGVF-ASFV 1498
Cdd:cd03296 225 YDHPASPFvYSFL 237
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1265-1490 |
3.45e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 65.25 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI-----FDGKIVIDGIDISKLPLHTL- 1338
Cdd:PRK14267 5 IETVNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELneearVEGEVRLFGRNIYSPDVDPIe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1339 -RSRLSIILQDPILF---------SGSIRFN-LDPECKCTDDRLWEALEIAQL----KNMVKSLPGgldavvteggeNFS 1403
Cdd:PRK14267 83 vRREVGMVFQYPNPFphltiydnvAIGVKLNgLVKSKKELDERVEWALKKAALwdevKDRLNDYPS-----------NLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1404 VGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR-VHTILTADLVIVMKRGNILE--- 1479
Cdd:PRK14267 152 GGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEvgp 231
|
250
....*....|....*
gi 530398974 1480 ----YDTPESLLAQE 1490
Cdd:PRK14267 232 trkvFENPEHELTEK 246
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
672-847 |
3.95e-11 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 64.30 E-value: 3.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS-------KYKAVtdacslq 744
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNgqdlsrlKRREI------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 745 P-----------DIDLLPfgDQT-----------------EIGER--------GI---------NLSGGQRQRICVARAL 779
Cdd:COG2884 75 PylrrrigvvfqDFRLLP--DRTvyenvalplrvtgksrkEIRRRvrevldlvGLsdkakalphELSGGEQQRVAIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398974 780 YQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTHADW-IIAMKDGSVLREG 847
Cdd:COG2884 153 VNRPELLLADEPTGNLDPETSWEIME--LLEEINRRGTTVLIATHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
684-862 |
4.21e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 66.78 E-value: 4.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV--------HWSKYK----------AVTDACSLQP 745
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQImldgvdlsHVPPYQrpinmmfqsyALFPHMTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 746 DI------DLLPFGD--------------QTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHlMQ 805
Cdd:PRK11607 111 NIafglkqDKLPKAEiasrvnemlglvhmQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDR-MQ 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 530398974 806 EGILKFLQDDKRTLVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKdiqtkdvELYEH 862
Cdd:PRK11607 190 LEVVDILERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPE-------EIYEH 240
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
672-859 |
4.48e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 65.39 E-value: 4.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV--------HWSKYKAVTDACSL 743
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsgidtgDFSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 744 ---QPDIDL--------LPFGDQ------TEI--------GERGI---------NLSGGQRQRICVARALYQNTNIVFLD 789
Cdd:PRK13644 82 vfqNPETQFvgrtveedLAFGPEnlclppIEIrkrvdralAEIGLekyrhrspkTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398974 790 DPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT----LKDIQTKDVEL 859
Cdd:PRK13644 162 EVTSMLDPDSGIAVLER--IKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEpenvLSDVSLQTLGL 233
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
765-843 |
4.60e-11 |
|
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: 64.11 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 765 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHlMQEGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSV 843
Cdd:TIGR01277 129 LSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREE-MLALVKQLCSERQRTLLMVTHHLSDARAiASQIAVVSQGKI 207
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1281-1490 |
4.97e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.53 E-value: 4.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1281 VLKHVKAYIKPGQKVGICGRTGSGKSSlslAFFRMVDIF---DGKIVIDGIDISKLPLHTlRSRLSI--ILQDPILFSG- 1354
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTT---TFYMVVGIVprdAGNIIIDDEDISLLPLHA-RARRGIgyLPQEASIFRRl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1355 ----------SIRFNLDPECKctDDRLWEALEIAQLKNMVKSLpggldavvtegGENFSVGQRQLFCLARAFVRKSSILI 1424
Cdd:PRK10895 94 svydnlmavlQIRDDLSAEQR--EDRANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398974 1425 MDEATASIDMATENILQKVVmTAFADR--TVVTIAHRV-HTILTADLVIVMKRGNILEYDTPESLLAQE 1490
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRII-EHLRDSglGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
690-852 |
5.23e-11 |
|
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: 67.02 E-value: 5.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 690 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGeMQTLEGKVHWskykavtdacsLQPDIDLL------------------P 751
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRF-----------DGQDLDGLsrralrplrrrmqvvfqdP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 752 FG-----------------------DQTEIGERGINL------------------SGGQRQRICVARALYQNTNIVFLDD 790
Cdd:COG4172 372 FGslsprmtvgqiiaeglrvhgpglSAAERRARVAEAleevgldpaarhryphefSGGQRQRIAIARALILEPKLLVLDE 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398974 791 PFSALDIHLsdhlmQEGILKFLQD--DKRTL--VLVTHKLQ---YLTHadWIIAMKDGSVLREGTLKDI 852
Cdd:COG4172 452 PTSALDVSV-----QAQILDLLRDlqREHGLayLFISHDLAvvrALAH--RVMVMKDGKVVEQGPTEQV 513
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1265-1491 |
6.40e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 64.82 E-value: 6.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1344
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1345 ILQDP--ILFS---------GSIRFNLDPECkcTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLA 1413
Cdd:PRK13652 83 VFQNPddQIFSptveqdiafGPINLGLDEET--VAHRVSSALHMLGLEELRDRVPHHL-----------SGGEKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1414 RAFVRKSSILIMDEATASID-MATENILQkvVMTAFADR---TVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLA 1488
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDpQGVKELID--FLNDLPETygmTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFL 227
|
...
gi 530398974 1489 QEN 1491
Cdd:PRK13652 228 QPD 230
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
669-847 |
7.57e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 64.76 E-value: 7.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 669 DIAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLL-------AILGEMQTLEGKVHWSKYKAVTDAC 741
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLhlngiylPQRGRVKVMGREVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 742 SL---QPD--------IDLLPFG------DQTEIGERG-----------------INLSGGQRQRICVARALYQNTNIVF 787
Cdd:PRK13647 82 GLvfqDPDdqvfsstvWDDVAFGpvnmglDKDEVERRVeealkavrmwdfrdkppYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398974 788 LDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQY-LTHADWIIAMKDGSVLREG 847
Cdd:PRK13647 162 LDEPMAYLDPRGQETLME--ILDRLHNQGKTVIVATHDVDLaAEWADQVIVLKEGRVLAEG 220
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
765-850 |
9.43e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 64.00 E-value: 9.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 765 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSV 843
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLN--TIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRI 222
|
....*..
gi 530398974 844 LREGTLK 850
Cdd:PRK11264 223 VEQGPAK 229
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
754-847 |
9.79e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.83 E-value: 9.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 754 DQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTH-A 832
Cdd:PRK10619 142 DERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR--IMQQLAEEGKTMVVVTHEMGFARHvS 219
|
90
....*....|....*
gi 530398974 833 DWIIAMKDGSVLREG 847
Cdd:PRK10619 220 SHVIFLHQGKIEEEG 234
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
688-852 |
1.11e-10 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 63.22 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWskykAVTDACSLQPD------IDLLP-----FGDQT 756
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRF----DGRDITGLPPHeraragIGYVPegrriFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 757 -----EIGE----------------------------RGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHL 803
Cdd:cd03224 92 veenlLLGAyarrrakrkarlervyelfprlkerrkqLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 530398974 804 MQegILKFLQDDKRTLVLVTHKLQY-LTHADWIIAMKDGSVLREGTLKDI 852
Cdd:cd03224 172 FE--AIRELRDEGVTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAEL 219
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
688-852 |
1.29e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 64.72 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV----------------------HWSKYKAVT--DACSL 743
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIrfhgtdvsrlhardrkvgfvfqHYALFRHMTvfDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 744 ---------QPDID--------LLPFGDQTEIGER-GINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLmQ 805
Cdd:PRK10851 98 gltvlprreRPNAAaikakvtqLLEMVQLAHLADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKEL-R 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 530398974 806 EGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 852
Cdd:PRK10851 177 RWLRQLHEELKFTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQV 224
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
677-846 |
1.97e-10 |
|
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: 63.29 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 677 GYFSWGSG-LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHW-----SKYKAvTDACSLQPDIDLL 750
Cdd:TIGR02769 15 GGLFGAKQrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFrgqdlYQLDR-KQRRAFRRDVQLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 751 pFGD-----------QTEIGE---------------------------------RGINLSGGQRQRICVARALYQNTNIV 786
Cdd:TIGR02769 94 -FQDspsavnprmtvRQIIGEplrhltsldeseqkariaelldmvglrsedadkLPRQLSGGQLQRINIARALAVKPKLI 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398974 787 FLDDPFSALDIHLsdhlmQEGILKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAMKDGSVLRE 846
Cdd:TIGR02769 173 VLDEAVSNLDMVL-----QAVILELLRKLQQafgtAYLFITHDLRLVQSfCQRVAVMDKGQIVEE 232
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
989-1158 |
2.17e-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: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 989 VAGFSILCGAGIFLclvTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLT 1068
Cdd:cd18552 45 IIGLFLLRGLASYL---QTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1069 RSTLLCLSAIGMISYA----TPVFLVALLPLGVAFYFIQKYFRVASKDLQE-LDDSTQlpllcHFSETAEGLTTIRAFRH 1143
Cdd:cd18552 122 RDPLTVIGLLGVLFYLdwklTLIALVVLPLAALPIRRIGKRLRKISRRSQEsMGDLTS-----VLQETLSGIRVVKAFGA 196
|
170
....*....|....*
gi 530398974 1144 ETRFKQRMLELTDTN 1158
Cdd:cd18552 197 EDYEIKRFRKANERL 211
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
672-877 |
2.21e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.96 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFsW--GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHW----------SKYKAVTD 739
Cdd:PRK15079 20 IKDGKQWF-WqpPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWlgkdllgmkdDEWRAVRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 740 A---------CSLQP-----DIDLLPFG------DQTEIGER--------G-----IN-----LSGGQRQRICVARALYQ 781
Cdd:PRK15079 99 DiqmifqdplASLNPrmtigEIIAEPLRtyhpklSRQEVKDRvkammlkvGllpnlINrypheFSGGQCQRIGIARALIL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 782 NTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTlkdiqtkD 856
Cdd:PRK15079 179 EPKLIICDEPVSALDVSI-----QAQVVNLLQQLQRemglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGT-------Y 246
|
250 260
....*....|....*....|....*....
gi 530398974 857 VELYEH-----WKTLMNR---QDQELEKD 877
Cdd:PRK15079 247 DEVYHNplhpyTKALMSAvpiPDPDLERN 275
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
688-824 |
2.28e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 62.11 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ---TLEGKV----------------------------HWS---- 732
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVllngrrltalpaeqrrigilfqddllfpHLSvgen 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 733 -------------KYKAVTDAcsLQpDIDLLPFGDQTeIGErginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 799
Cdd:COG4136 97 lafalpptigraqRRARVEQA--LE-EAGLAGFADRD-PAT----LSGGQRARVALLRALLAEPRALLLDEPFSKLDAAL 168
|
170 180
....*....|....*....|....*..
gi 530398974 800 SDHLMQegiLKFLQDDKRTL--VLVTH 824
Cdd:COG4136 169 RAQFRE---FVFEQIRQRGIpaLLVTH 192
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1277-1486 |
2.48e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.96 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1277 NLKPVlKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL---PLHTLRSRLSIILQDPiLFS 1353
Cdd:PRK15079 33 TLKAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMkddEWRAVRSDIQMIFQDP-LAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1354 GSIRFNLdpeckctDDRLWEALEI-------AQLKNMVKSL---PGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSIL 1423
Cdd:PRK15079 111 LNPRMTI-------GEIIAEPLRTyhpklsrQEVKDRVKAMmlkVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1424 IMDEATASIDMATE----NILQKvvMTAFADRTVVTIAHR---VHTIltADLVIVMKRGNILEYDTPESL 1486
Cdd:PRK15079 184 ICDEPVSALDVSIQaqvvNLLQQ--LQREMGLSLIFIAHDlavVKHI--SDRVLVMYLGHAVELGTYDEV 249
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1269-1488 |
2.61e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 63.10 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1269 DLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG--IDISKLPLHTLRSRLSIIL 1346
Cdd:PRK13638 6 DLWFRYQD--EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1347 QDP---ILFS---GSIRFNLD----PECKCTDdRLWEALEIAQLKNMVKslpggldavvtEGGENFSVGQRQLFCLARAF 1416
Cdd:PRK13638 84 QDPeqqIFYTdidSDIAFSLRnlgvPEAEITR-RVDEALTLVDAQHFRH-----------QPIQCLSHGQKKRVAIAGAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398974 1417 VRKSSILIMDEATASIDMATEN----ILQKVVMTAfadRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLA 1488
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTqmiaIIRRIVAQG---NHVIISSHDIDLIYeISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1297-1483 |
3.62e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 63.33 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1297 ICGRTGSGKSSLSLAF----------FRMVDIFDG-KIVIDGIDISKLP-----LHTLRSRLSIILQDP--ILFSGSIRf 1358
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFnglikskygtIQVGDIYIGdKKNNHELITNPYSkkiknFKELRRRVSMVFQFPeyQLFKDTIE- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1359 nldpeckctDDRLWEALEIAQLKNMVKSLPG------GLDAVVTEGGE-NFSVGQRQLFCLARAFVRKSSILIMDEATAS 1431
Cdd:PRK13631 136 ---------KDIMFGPVALGVKKSEAKKLAKfylnkmGLDDSYLERSPfGLSGGQKRRVAIAGILAIQPEILIFDEPTAG 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 530398974 1432 IDMATENILQKVVMTAFAD-RTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTP 1483
Cdd:PRK13631 207 LDPKGEHEMMQLILDAKANnKTVFVITHTMEHVLeVADEVIVMDKGKILKTGTP 260
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
641-842 |
3.85e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 64.44 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 641 TINRkqpgryhLDSYEQSTRRLRPAETEDIAIKVTNGyfswgSGLAT-------------LSNIDIRIPTGQLTMIVGQV 707
Cdd:COG4178 331 TVDR-------LAGFEEALEAADALPEAASRIETSED-----GALALedltlrtpdgrplLEDLSLSLKPGERLLITGPS 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 708 GCGKSSLLLAILGemqtL----EGKVH---------------------------------WS--KYKAVTDACSLQPDID 748
Cdd:COG4178 399 GSGKSTLLRAIAG----LwpygSGRIArpagarvlflpqrpylplgtlreallypataeaFSdaELREALEAVGLGHLAE 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 749 LLpfgDQTEIGERGinLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDdkRTLVLVTHKLQY 828
Cdd:COG4178 475 RL---DEEADWDQV--LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-LREELPG--TTVISVGHRSTL 546
|
250
....*....|....
gi 530398974 829 LTHADWIIAMKDGS 842
Cdd:COG4178 547 AAFHDRVLELTGDG 560
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1282-1488 |
3.92e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.50 E-value: 3.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1282 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPI----------- 1350
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPStslnprqrisq 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1351 LFSGSIRFNLDPECKCTDDRLWEAL-EIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEAT 1429
Cdd:PRK15112 109 ILDFPLRLNTDLEPEQREKQIIETLrQVGLLPDHASYYPHML-----------APGQKQRLGLARALILRPKVIIADEAL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398974 1430 ASIDMATENILQKVVMTAFADRTVVTIAHRVHTILT---ADLVIVMKRGNILEYDTPESLLA 1488
Cdd:PRK15112 178 ASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMkhiSDQVLVMHQGEVVERGSTADVLA 239
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
765-852 |
4.33e-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: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 765 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD---HLMQEgilkfLQDDKR-TLVLVTHKLQYLTH-ADWIIAMK 839
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSqiiNLMLE-----LQEKLGiSYIYVSQHLGIVKHiSDKVLVMH 224
|
90
....*....|...
gi 530398974 840 DGSVLREGTLKDI 852
Cdd:COG4167 225 QGEVVEYGKTAEV 237
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
1018-1146 |
4.68e-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: 4.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1018 AKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATP-VFLVALL--- 1093
Cdd:cd18573 73 VARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPkLTLVMLLvvp 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 530398974 1094 PLGVAFYFIQKYFRVASKDLQE-LDDSTQLpllchfsetAE----GLTTIRAFRHETR 1146
Cdd:cd18573 153 PIAVGAVFYGRYVRKLSKQVQDaLADATKV---------AEerlsNIRTVRAFAAERK 201
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
690-852 |
4.69e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 63.20 E-value: 4.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 690 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhWSKYKAVTDACSLQPDI-------DLLP---FGD----- 754
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQI-FIDGEDVTHRSIQQRDIcmvfqsyALFPhmsLGEnvgyg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 755 -------QTEIGER-----------GI------NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHlMQEGILK 810
Cdd:PRK11432 103 lkmlgvpKEERKQRvkealelvdlaGFedryvdQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRS-MREKIRE 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 530398974 811 FLQDDKRTLVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKDI 852
Cdd:PRK11432 182 LQQQFNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
721-866 |
4.89e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.67 E-value: 4.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 721 EMQTLEGKVHWSKYKAVTDAcslqpdIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlS 800
Cdd:PTZ00265 1321 EDATREDVKRACKFAAIDEF------IESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-S 1393
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398974 801 DHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAM----KDGS-VLREGTLKDIQTKDVELYEHWKTL 866
Cdd:PTZ00265 1394 EKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSfVQAHGTHEELLSVQDGVYKKYVKL 1464
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
688-852 |
5.92e-10 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 61.16 E-value: 5.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLL--LAILGEMQ----TLEG---------------------------------- 727
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLrcINLLEEPDsgtiTVDGedltdskkdinklrrkvgmvfqqfnlfphltvle 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 728 -------KVH-WSKYKAVTDAcslqpdIDLLpfgDQTEIGERG----INLSGGQRQRICVARALYQNTNIVFLDDPFSAL 795
Cdd:COG1126 97 nvtlapiKVKkMSKAEAEERA------MELL---ERVGLADKAdaypAQLSGGQQQRVAIARALAMEPKVMLFDEPTSAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 796 DIHLSdhlmQE--GILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 852
Cdd:COG1126 168 DPELV----GEvlDVMRDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1266-1436 |
6.44e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 60.57 E-value: 6.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1266 KIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLsLAF--------FRmvdiFDGKIVIDGIDISKLPlhT 1337
Cdd:COG4136 3 SLENLTITLGG--RPLLAPLSLTVAPGEILTLMGPSGSGKSTL-LAAiagtlspaFS----ASGEVLLNGRRLTALP--A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1338 LRSRLSIILQDPILFS-----GSIRFNLDPECKCTD--DRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1410
Cdd:COG4136 74 EQRRIGILFQDDLLFPhlsvgENLAFALPPTIGRAQrrARVEQALEEAGLAGFADRDPATL-----------SGGQRARV 142
|
170 180
....*....|....*....|....*.
gi 530398974 1411 CLARAFVRKSSILIMDEATASIDMAT 1436
Cdd:COG4136 143 ALLRALLAEPRALLLDEPFSKLDAAL 168
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1265-1490 |
6.81e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 62.94 E-value: 6.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1344
Cdd:PRK09536 4 IDVSDLSVEFGD--TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1345 ILQDPilfsgSIRFNLDPE----------------CKCTDDRLWE-ALEiaqlknmvkslPGGLDAVVTEGGENFSVGQR 1407
Cdd:PRK09536 82 VPQDT-----SLSFEFDVRqvvemgrtphrsrfdtWTETDRAAVErAME-----------RTGVAQFADRPVTSLSGGER 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1408 QLFCLARAFVRKSSILIMDEATASIDMATE-NILQKVVMTAFADRTVVTIAHRVHtiLTA---DLVIVMKRGNILEYDTP 1483
Cdd:PRK09536 146 QRVLLARALAQATPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLD--LAArycDELVLLADGRVRAAGPP 223
|
....*..
gi 530398974 1484 ESLLAQE 1490
Cdd:PRK09536 224 ADVLTAD 230
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
688-844 |
7.81e-10 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 61.46 E-value: 7.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV-----------------------------------HWS 732
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIvidgidisklplhtlrsrlsiilqdpilfsgsirfNLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 733 KYKAVTDA--------CSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhLSDHLM 804
Cdd:cd03288 117 PECKCTDDrlwealeiAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDM-ATENIL 195
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 530398974 805 QEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVL 844
Cdd:cd03288 196 QKVVMTAFAD--RTVVTIAHRVSTILDADLVLVLSRGILV 233
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1231-1493 |
8.95e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.07 E-value: 8.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1231 AVKKVNSFltmESENYEGTMDPSQVPEHWPQegeIKIHDLCVRYENN---LKPVlkhvKAYIKPGQKVGICGRTGSGKSS 1307
Cdd:PRK10522 295 AFNKLNKL---ALAPYKAEFPRPQAFPDWQT---LELRNVTFAYQDNgfsVGPI----NLTIKRGELLFLIGGNGSGKST 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1308 LSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSirfnLDPECKCTDDRLWEA-LEIAQLKNMVKs 1386
Cdd:PRK10522 365 LAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALVEKwLERLKMAHKLE- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1387 lpggldavvTEGGE----NFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRV 1460
Cdd:PRK10522 440 ---------LEDGRisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEmgKTIFAISHDD 510
|
250 260 270
....*....|....*....|....*....|...
gi 530398974 1461 HTILTADLVIVMKRGNILEYDTPESLLAQENGV 1493
Cdd:PRK10522 511 HYFIHADRLLEMRNGQLSELTGEERDAASRDAV 543
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
688-862 |
1.03e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 59.85 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEmqtlegkvhwSKYKaVTDACSLQPDIDLLpfgdQTEIGER---GI- 763
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH----------PKYE-VTEGEILFKGEDIT----DLPPEERarlGIf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 764 -----------------------NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhlsDHL-MQEGILKFLQDDKRTL 819
Cdd:cd03217 81 lafqyppeipgvknadflryvneGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI---DALrLVAEVINKLREEGKSV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 530398974 820 VLVTHKLQYLTH--ADWIIAMKDGSVLREGtlkdiqtkDVELYEH 862
Cdd:cd03217 158 LIITHYQRLLDYikPDRVHVLYDGRIVKSG--------DKELALE 194
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
688-848 |
1.12e-09 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 60.21 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKYKAVTDACSLQPDI------DLL----------- 750
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLgycpqfDALfdeltvrehlr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 751 --------PFGDQTEIGERGI--------------NLSGGQRQRICVARALYQNTNIVFLDDPFSALdihlsDHLMQEGI 808
Cdd:cd03263 98 fyarlkglPKSEIKEEVELLLrvlgltdkankrarTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGL-----DPASRRAI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 530398974 809 LKFLQDDK--RTLVLVTHKLQ---YLthADWIIAMKDGSVLREGT 848
Cdd:cd03263 173 WDLILEVRkgRSIILTTHSMDeaeAL--CDRIAIMSDGKLRCIGS 215
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
663-848 |
1.26e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 62.81 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 663 RPAETEDIAIKvtNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHW----------- 731
Cdd:PRK10790 334 RPLQSGRIDID--NVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLdgrplsslshs 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 732 ------------------SKYKAVT--------------DACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARAL 779
Cdd:PRK10790 412 vlrqgvamvqqdpvvladTFLANVTlgrdiseeqvwqalETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398974 780 YQNTNIVFLDDPFSALDIHlsdhlMQEGILKFLQ--DDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 848
Cdd:PRK10790 492 VQTPQILILDEATANIDSG-----TEQAIQQALAavREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGT 557
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1264-1458 |
1.39e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 60.57 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1264 EIKIHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIF-----DGKIVIDGIDI--SKLPLH 1336
Cdd:PRK14243 10 VLRTENLNVYYGSFL--AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIpgfrvEGKVTFHGKNLyaPDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1337 TLRSRLSIILQDPILFSGSIRFNLDPECKCT------DDRLWEALEIAQLKNMVKSlpggldaVVTEGGENFSVGQRQLF 1410
Cdd:PRK14243 88 EVRRRIGMVFQKPNPFPKSIYDNIAYGARINgykgdmDELVERSLRQAALWDEVKD-------KLKQSGLSLSGGQQQRL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 530398974 1411 CLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAH 1458
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTH 208
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
765-852 |
1.40e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 61.97 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 765 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHlMQEGILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMKDGSV 843
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE-MQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEV 243
|
....*....
gi 530398974 844 LREGTLKDI 852
Cdd:PRK10070 244 VQVGTPDEI 252
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1279-1498 |
1.51e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 61.78 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1279 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHtlRSRLSIILQDPILF-- 1352
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTL----LRMLAGFEqptaGQIMLDGVDLSHVPPY--QRPINMMFQSYALFph 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1353 ---SGSIRFNLD----PECKCTDdRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIM 1425
Cdd:PRK11607 106 mtvEQNIAFGLKqdklPKAEIAS-RVNEMLGLVHMQEFAKRKPHQL-----------SGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1426 DEATASID------MATE--NILQKVVMTAfadrtvVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQENGVF-A 1495
Cdd:PRK11607 174 DEPMGALDkklrdrMQLEvvDILERVGVTC------VMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEIYEHPTTRYsA 247
|
...
gi 530398974 1496 SFV 1498
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 ... |
1208-1489 |
1.78e-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: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1208 ALTITNYLNWVVRNLADLEVQM--GAVKKVNSFLTMESENYEGTMDPSQVPEHWPQEGEIKIHDLCVRYENNLKPVLKHV 1285
Cdd:TIGR03269 221 SMVLTSHWPEVIEDLSDKAIWLenGEIKEEGTPDEVVAVFMEGVSEVEKECEVEVGEPIIKVRNVSKRYISVDRGVVKAV 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1286 KAY---IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVI----DGIDISKlPLHTLRSR----LSIILQDPILFSG 1354
Cdd:TIGR03269 301 DNVsleVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTK-PGPDGRGRakryIGILHQEYDLYPH 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1355 SIRFnldpeckctdDRLWEAL------EIAQLKNMVKSLPGGLD-----AVVTEGGENFSVGQRQLFCLARAFVRKSSIL 1423
Cdd:TIGR03269 380 RTVL----------DNLTEAIglelpdELARMKAVITLKMVGFDeekaeEILDKYPDELSEGERHRVALAQVLIKEPRIV 449
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398974 1424 IMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLAQ 1489
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSILKAREEmeQTFIIVSHDMDFVLdVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
688-852 |
1.87e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 60.56 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV--------HWSKYKAV-------------------TDa 740
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVtvddititHKTKDKYIrpvrkrigmvfqfpesqlfED- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 741 cSLQPDIDLLP--FG-DQTEIGERGINL------------------SGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 799
Cdd:PRK13646 102 -TVEREIIFGPknFKmNLDEVKNYAHRLlmdlgfsrdvmsqspfqmSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQS 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 530398974 800 SDHLMQegILKFLQ-DDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDI 852
Cdd:PRK13646 181 KRQVMR--LLKSLQtDENKTIILVSHDMNEVArYADEVIVMKEGSIVSQTSPKEL 233
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1282-1493 |
2.23e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 60.18 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1282 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP----LHTLRSRLSIILQDP-------- 1349
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRPVRKRIGMVFQFPesqlfedt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1350 ----ILFsGSIRFNLDPEcKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIM 1425
Cdd:PRK13646 103 vereIIF-GPKNFKMNLD-EVKNYAHRLLMDLGFSRDVMSQSPFQM-----------SGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398974 1426 DEATASIDMATenilQKVVMTAFA------DRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQENGV 1493
Cdd:PRK13646 170 DEPTAGLDPQS----KRQVMRLLKslqtdeNKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKDKKKL 240
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1264-1490 |
2.29e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 60.03 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1264 EIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLS 1343
Cdd:PRK11231 2 TLRTENLTVGYGT--KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1344 IILQDPILFSG-SIR----------FNLDPECKCTDDRLWE-ALEIAQLKNMVkslpgglDAVVTEggenFSVGQRQLFC 1411
Cdd:PRK11231 80 LLPQHHLTPEGiTVRelvaygrspwLSLWGRLSAEDNARVNqAMEQTRINHLA-------DRRLTD----LSGGQRQRAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1412 LARAFVRKSSILIMDEATASIDMATENILQKVV-MTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQ 1489
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMrELNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMTP 228
|
.
gi 530398974 1490 E 1490
Cdd:PRK11231 229 G 229
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1265-1458 |
2.36e-09 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 57.46 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslaffrmvdifdgkividgidisklplhtlrsrLSI 1344
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTL---------------------------------LKL 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1345 ILQDPILFSGSIRFNldpeckctddrlwEALEIAQLknmvkslpggldavvteggENFSVGQRQLFCLARAFVRKSSILI 1424
Cdd:cd03221 46 IAGELEPDEGIVTWG-------------STVKIGYF-------------------EQLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190
....*....|....*....|....*....|....*...
gi 530398974 1425 MDEATASIDMAT----ENILQKvvmtaFaDRTVVTIAH 1458
Cdd:cd03221 94 LDEPTNHLDLESiealEEALKE-----Y-PGTVILVSH 125
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
942-1158 |
2.43e-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: 60.26 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 942 GGFFLLILMIFSKLLKHSVIVAIDYWLATWtseysinntgkadqtyYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNL 1021
Cdd:cd07346 11 ATALGLALPLLTKLLIDDVIPAGDLSLLLW----------------IALLLLLLALLRALLSYLRRYLAARLGQRVVFDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1022 HHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIG-MISYATPVFLVALLPL---GV 1097
Cdd:cd07346 75 RRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALViLFYLNWKLTLVALLLLplyVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398974 1098 AFYFIQKYFRVASKDLQE-LDDSTQlpllcHFSETAEGLTTIRAFRHETRFKQRMLELTDTN 1158
Cdd:cd07346 155 ILRYFRRRIRKASREVREsLAELSA-----FLQESLSGIRVVKAFAAEEREIERFREANRDL 211
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1280-1477 |
2.47e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.61 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1280 PVLKHVKAYIKPGQKVGICGRTGSGKSSLS--LAFFRMVDIfdGKIVIDGIDISKL-PLHTLRSRLSIILQDPILFSG-- 1354
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMkiIAGIVPPDS--GTLEIGGNPCARLtPAKAHQLGIYLVPQEPLLFPNls 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1355 ---SIRFNLdPEckctddrlwEALEIAQLKNMVKSLPGGLDAVVTEGgeNFSVGQRQLFCLARAFVRKSSILIMDEATAS 1431
Cdd:PRK15439 103 vkeNILFGL-PK---------RQASMQKMKQLLAALGCQLDLDSSAG--SLEVADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 530398974 1432 IDMA-TENILQKVVMTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNI 1477
Cdd:PRK15439 171 LTPAeTERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTI 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
688-838 |
2.60e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 59.34 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS----------KYKAVTDACSLQPDI---------- 747
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEgedistlkpeIYRQQVSYCAQTPTLfgdtvydnli 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 748 -----------------DLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQEGIL 809
Cdd:PRK10247 103 fpwqirnqqpdpaifldDLERFALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDES-NKHNVNEIIH 181
|
170 180
....*....|....*....|....*....
gi 530398974 810 KFLQDDKRTLVLVTHKLQYLTHADWIIAM 838
Cdd:PRK10247 182 RYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
669-843 |
2.62e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 61.62 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 669 DIAIKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSK------YKAVTDAcs 742
Cdd:COG0488 313 KKVLELEGLSKSYG-DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGEtvkigyFDQHQEE-- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 743 LQPD-------IDLLPFGDQTEIgeRGI----------------NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHl 799
Cdd:COG0488 390 LDPDktvldelRDGAPGGTEQEV--RGYlgrflfsgddafkpvgVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIE- 466
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 530398974 800 sdhlMQEGILKFLQDDKRTLVLVTHKLQYL-THADWIIAMKDGSV 843
Cdd:COG0488 467 ----TLEALEEALDDFPGTVLLVSHDRYFLdRVATRILEFEDGGV 507
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
688-862 |
2.80e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 60.03 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKY--KAVTDACSLQP-------------------- 745
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERviTAGKKNKKLKPlrkkvgivfqfpehqlfeet 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 746 ---DIDLLP--FGDQTEIGER---------GIN----------LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD 801
Cdd:PRK13634 103 vekDICFGPmnFGVSEEDAKQkaremielvGLPeellarspfeLSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398974 802 HLMqEGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQTKDVELYEH 862
Cdd:PRK13634 183 EMM-EMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFADPDELEAI 243
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
944-1156 |
2.82e-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: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 944 FFLLILMIFSKLLkhsvIVAIDYWLATWTSEYSINNTGKADQTY-YVAGFSILCGAGIFLCLVTSLTVEWMGLTAA---- 1018
Cdd:cd18547 2 ILVIILAIISTLL----SVLGPYLLGKAIDLIIEGLGGGGGVDFsGLLRILLLLLGLYLLSALFSYLQNRLMARVSqrtv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1019 KNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIG-MISYATPVFLVALLPLGV 1097
Cdd:cd18547 78 YDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLImMLYISPLLTLIVLVTVPL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530398974 1098 AFYFI-------QKYFRVASKDLQELDDSTQlpllchfsETAEGLTTIRAFRHETRFKQRMLELTD 1156
Cdd:cd18547 158 SLLVTkfiakrsQKYFRKQQKALGELNGYIE--------EMISGQKVVKAFNREEEAIEEFDEINE 215
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1280-1487 |
2.83e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 59.34 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1280 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDI--SKLPLHTLRSRLSIILQdpilfsgsiR 1357
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEAGMVFQ---------Q 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1358 FNLDPECKCTDDRLWEALEI-----AQLKNMVKSLPG--GLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA 1430
Cdd:PRK09493 86 FYLFPHLTALENVMFGPLRVrgaskEEAEKQARELLAkvGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398974 1431 SIDmatENILQKV--VMTAFADR----TVVT----IAHRVHTILtadlvIVMKRGNILEYDTPESLL 1487
Cdd:PRK09493 166 ALD---PELRHEVlkVMQDLAEEgmtmVIVTheigFAEKVASRL-----IFIDKGRIAEDGDPQVLI 224
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
675-854 |
2.88e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 59.70 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 675 TNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHW-----SKYKAvTDACSLQPDIDL 749
Cdd:PRK10419 15 HGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWrgeplAKLNR-AQRKAFRRDIQM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 750 LpFGD-------QTEIGE-------------------------------------RGINLSGGQRQRICVARALYQNTNI 785
Cdd:PRK10419 94 V-FQDsisavnpRKTVREiireplrhllsldkaerlarasemlravdlddsvldkRPPQLSGGQLQRVCLARALAVEPKL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530398974 786 VFLDDPFSALDIHLsdhlmQEGILKFLQDDKRTL----VLVTHKL---QYLTHAdwIIAMKDGSVLREGTLKDIQT 854
Cdd:PRK10419 173 LILDEAVSNLDLVL-----QAGVIRLLKKLQQQFgtacLFITHDLrlvERFCQR--VMVMDNGQIVETQPVGDKLT 241
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
668-852 |
3.34e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 59.86 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 668 EDIAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS------------KYK 735
Cdd:PRK13636 2 EDYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDgkpidysrkglmKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 736 AVTDACSLQPDIDL--------LPFG------DQTEIGER--------GIN---------LSGGQRQRICVARALYQNTN 784
Cdd:PRK13636 82 ESVGMVFQDPDNQLfsasvyqdVSFGavnlklPEDEVRKRvdnalkrtGIEhlkdkpthcLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398974 785 IVFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDI 852
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIM-KLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEV 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
672-843 |
4.00e-09 |
|
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: 58.57 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYfswGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKykavTDACSLQ------- 744
Cdd:cd03292 4 INVTKTY---PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNG----QDVSDLRgraipyl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 745 --------PDIDLLP---------FG-DQTEIGERGIN----------------------LSGGQRQRICVARALYQNTN 784
Cdd:cd03292 77 rrkigvvfQDFRLLPdrnvyenvaFAlEVTGVPPREIRkrvpaalelvglshkhralpaeLSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 785 IVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTH-KLQYLTHADWIIAMKDGSV 843
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMN--LLKKINKAGTTVVVATHaKELVDTTRHRVIALERGKL 214
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1265-1436 |
4.42e-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: 4.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVDIFD-GKIVIDGIDISKL---PLHTL 1338
Cdd:COG4181 9 IELRGLTKTVGTGAGELtiLKGISLEVEAGESVAIVGASGSGKSTL-LGLLAGLDRPTsGTVRLAGQDLFALdedARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1339 RSR-LSIILQD---------------PILFSGsirfnlDPECKctdDRLWEALEIAQLKNMVKSLPGGLdavvtEGGEnf 1402
Cdd:COG4181 88 RARhVGFVFQSfqllptltalenvmlPLELAG------RRDAR---ARARALLERVGLGHRLDHYPAQL-----SGGE-- 151
|
170 180 190
....*....|....*....|....*....|....
gi 530398974 1403 svgqRQLFCLARAFVRKSSILIMDEATASIDMAT 1436
Cdd:COG4181 152 ----QQRVALARAFATEPAILFADEPTGNLDAAT 181
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
680-862 |
4.64e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 59.86 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 680 SWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKyKAVTDacsLQP---DI--------- 747
Cdd:PRK11650 12 SYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGG-RVVNE---LEPadrDIamvfqnyal 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 748 -------DLLPFG------DQTEIGER-----GI------------NLSGGQRQRICVARALYQNTNiVFL-DDPFSALD 796
Cdd:PRK11650 88 yphmsvrENMAYGlkirgmPKAEIEERvaeaaRIleleplldrkprELSGGQRQRVAMGRAIVREPA-VFLfDEPLSNLD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 797 IHLSDHLMQEgiLKFLQddKR---TLVLVTH-KLQYLTHADWIIAMKDGSVLREGTlkdiqtkDVELYEH 862
Cdd:PRK11650 167 AKLRVQMRLE--IQRLH--RRlktTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGT-------PVEVYEK 225
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
671-865 |
4.84e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 58.70 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 671 AIKVTNGYFSWGSGlATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI-----LGEMQTLEGKVHW---SKYKAVTDACS 742
Cdd:PRK14267 4 AIETVNLRVYYGSN-HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLfgrNIYSPDVDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 743 LQPDIDLL-----PF-------------------GDQTEIGER---------------------GINLSGGQRQRICVAR 777
Cdd:PRK14267 83 VRREVGMVfqypnPFphltiydnvaigvklnglvKSKKELDERvewalkkaalwdevkdrlndyPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 778 ALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDdkRTLVLVTHK-LQYLTHADWIIAMKDGSVLREG-TLKDIQTK 855
Cdd:PRK14267 163 ALAMKPKILLMDEPTANID-PVGTAKIEELLFELKKE--YTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGpTRKVFENP 239
|
250
....*....|
gi 530398974 856 DVELYEHWKT 865
Cdd:PRK14267 240 EHELTEKYVT 249
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
764-861 |
5.06e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 59.04 E-value: 5.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 764 NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKR-TLVLVTHKLQYLTHADWIIAMKDGS 842
Cdd:PRK13640 143 NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILK--LIRKLKKKNNlTVISITHDIDEANMADQVLVLDDGK 220
|
90
....*....|....*....
gi 530398974 843 VLREGTLKDIQTKDVELYE 861
Cdd:PRK13640 221 LLAQGSPVEIFSKVEMLKE 239
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1281-1493 |
5.56e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 58.94 E-value: 5.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1281 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG--IDISKLPLHTLRSRLSIILQDP--ILFSGSI 1356
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTVGIVFQNPddQLFAPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1357 R-------FNLdpeckctddrlweALEIAQLKNMVKSlpgGLDAVVTEGGEN-----FSVGQRQLFCLARAFVRKSSILI 1424
Cdd:PRK13639 97 EedvafgpLNL-------------GLSKEEVEKRVKE---ALKAVGMEGFENkpphhLSGGQKKRVAIAGILAMKPEIIV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398974 1425 MDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTI-LTADLVIVMKRGNILEYDTPESLLAQENGV 1493
Cdd:PRK13639 161 LDEPTSGLDpMGASQIMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDIETI 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1265-1484 |
5.91e-09 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 58.22 E-value: 5.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYeNNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIF----DGKIVIDGIDISKLPLHtLRS 1340
Cdd:cd03219 1 LEVRGLTKRF-GGLV-ALDDVSFSVRPGEIHGLIGPNGAGKTTL----FNLISGFlrptSGSVLFDGEDITGLPPH-EIA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1341 RLSII--LQDPILFSG-SIRFNLD-----------------PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvtegge 1400
Cdd:cd03219 74 RLGIGrtFQIPRLFPElTVLENVMvaaqartgsglllararREEREARERAEELLERVGLADLADRPAGEL--------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1401 nfSVGQRQLFCLARAFVRKSSILIMDEATASIDMA-TENILQKVVMTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNIL 1478
Cdd:cd03219 145 --SYGQQRRLEIARALATDPKLLLLDEPAAGLNPEeTEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVI 222
|
....*.
gi 530398974 1479 EYDTPE 1484
Cdd:cd03219 223 AEGTPD 228
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
671-848 |
6.40e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 58.10 E-value: 6.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 671 AIKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLL-------------LAILG------------EMQTL 725
Cdd:PRK11124 2 SIQLNGINCFYGAHQA-LFDITLDCPQGETLVLLGPSGAGKSSLLrvlnllemprsgtLNIAGnhfdfsktpsdkAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 726 EGKVH--------W-------------------SKYKAVTDACSLQPDIDLLPFGDQTEIgergiNLSGGQRQRICVARA 778
Cdd:PRK11124 81 RRNVGmvfqqynlWphltvqqnlieapcrvlglSKDQALARAEKLLERLRLKPYADRFPL-----HLSGGQQQRVAIARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398974 779 LYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGT 848
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDPEITAQIVS--IIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGD 224
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
766-852 |
7.67e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 59.21 E-value: 7.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 766 SGGQRQRICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKRTL----VLVTHKLQYLTH-ADWIIAMKD 840
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSV-----QAQVLNLMMDLQQELglsyVFISHDLSVVEHiADEVMVMYL 230
|
90
....*....|..
gi 530398974 841 GSVLREGTLKDI 852
Cdd:PRK11308 231 GRCVEKGTKEQI 242
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
684-854 |
1.20e-08 |
|
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: 57.45 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwskYKAvTDACSLQPD----------------- 746
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVL---FDG-EDITGLPPHeiarlgigrtfqiprlf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 747 ---------------------IDLLPFGDQTEIGER--------GI---------NLSGGQRQRICVARALYQNTNIVFL 788
Cdd:cd03219 88 peltvlenvmvaaqartgsglLLARARREEREARERaeellervGLadladrpagELSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398974 789 DDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDIQT 854
Cdd:cd03219 168 DEPAAGLNPEETEELAE--LIRELRERGITVLLVEHDMDVVMsLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
765-826 |
1.25e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 57.28 E-value: 1.25e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530398974 765 LSGGQRQRICVARALYQNTNIVFLDDPFSALDihlsDHLMQEgILKFLQD--DKR--TLVLVTHKL 826
Cdd:PRK10771 130 LSGGQRQRVALARCLVREQPILLLDEPFSALD----PALRQE-MLTLVSQvcQERqlTLLMVSHSL 190
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
765-859 |
1.78e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 57.40 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 765 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSVL 844
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNT-IKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVV 223
|
90
....*....|....*
gi 530398974 845 REGTLKDIqTKDVEL 859
Cdd:PRK13633 224 MEGTPKEI-FKEVEM 237
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
673-900 |
1.85e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.03 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 673 KVTNGYfswGSGLaTLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSK-----YKAV-------TDA 740
Cdd:PRK10636 317 KVSAGY---GDRI-ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKgiklgYFAQhqleflrADE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 741 CSLQPDIDLLP-------------FGDQ----TEIGERginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHL 803
Cdd:PRK10636 393 SPLQHLARLAPqeleqklrdylggFGFQgdkvTEETRR---FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQAL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 804 MQ-----EGILKFLQDDKRTLVLVTHKLqYLTHadwiiamkDGSVlregtlkDIQTKDVELYEHWktLMNRQDQELEKDM 878
Cdd:PRK10636 470 TEalidfEGALVVVSHDRHLLRSTTDDL-YLVH--------DGKV-------EPFDGDLEDYQQW--LSDVQKQENQTDE 531
|
250 260
....*....|....*....|..
gi 530398974 879 EADQTTLERKTLRRAMYSREAK 900
Cdd:PRK10636 532 APKENNANSAQARKDQKRREAE 553
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
681-825 |
2.05e-08 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 56.51 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 681 WGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ---TLEGKVHW----SKYKAVTDACS--LQPDIdLLP 751
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFngqpRKPDQFQKCVAyvRQDDI-LLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 752 F------------------------------------GDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 795
Cdd:cd03234 95 GltvretltytailrlprkssdairkkrvedvllrdlALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190
....*....|....*....|....*....|
gi 530398974 796 DIHLSDHLMQegILKFLQDDKRTLVLVTHK 825
Cdd:cd03234 175 DSFTALNLVS--TLSQLARRNRIVILTIHQ 202
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1289-1497 |
2.14e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 57.81 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1289 IKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIDGIDISKlplHTLRSR-LSIILQDPILFSG-SIRFNL-- 1360
Cdd:PRK11432 29 IKQGTMVTLLGPSGCGKTTV----LRLVagleKPTEGQIFIDGEDVTH---RSIQQRdICMVFQSYALFPHmSLGENVgy 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1361 --------DPECKctdDRLWEALEIAQLKnmvkslpGGLDAVVteggENFSVGQRQLFCLARAFVRKSSILIMDEATASI 1432
Cdd:PRK11432 102 glkmlgvpKEERK---QRVKEALELVDLA-------GFEDRYV----DQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398974 1433 D------MaTENI--LQKVVmtafaDRTVVTIAH-RVHTILTADLVIVMKRGNILEYDTPESLLAQENGVF-ASF 1497
Cdd:PRK11432 168 DanlrrsM-REKIreLQQQF-----NITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFmASF 236
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
688-828 |
2.18e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 56.64 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLL------------------LAILG-----------------------EMQTLE 726
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLrcinkleeitsgdlivdgLKVNDpkvderlirqeagmvfqqfylfpHLTALE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 727 ----GKVH---WSKYKAVTDAcslqpdIDLLpfgDQTEIGERG----INLSGGQRQRICVARALYQNTNIVFLDDPFSAL 795
Cdd:PRK09493 97 nvmfGPLRvrgASKEEAEKQA------RELL---AKVGLAERAhhypSELSGGQQQRVAIARALAVKPKLMLFDEPTSAL 167
|
170 180 190
....*....|....*....|....*....|...
gi 530398974 796 DIHLSDHLMQegILKFLQDDKRTLVLVTHKLQY 828
Cdd:PRK09493 168 DPELRHEVLK--VMQDLAEEGMTMVIVTHEIGF 198
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1265-1491 |
2.22e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 56.70 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1344
Cdd:PRK13548 3 LEARNLSVRLGG--RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1345 ILQDPIL-FSGS----IRFNLDP--ECKCTDDRLWEA----LEIAQLKNmvKSLPggldavVTEGGENfsvgQR-QlfcL 1412
Cdd:PRK13548 81 LPQHSSLsFPFTveevVAMGRAPhgLSRAEDDALVAAalaqVDLAHLAG--RDYP------QLSGGEQ----QRvQ---L 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1413 ARAFVR------KSSILIMDEATASIDMATenilQKVVMTA---FADR---TVVTIAHRVH-TILTADLVIVMKRGNILE 1479
Cdd:PRK13548 146 ARVLAQlwepdgPPRWLLLDEPTSALDLAH----QHHVLRLarqLAHErglAVIVVLHDLNlAARYADRIVLLHQGRLVA 221
|
250
....*....|..
gi 530398974 1480 YDTPESLLAQEN 1491
Cdd:PRK13548 222 DGTPAEVLTPET 233
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
688-852 |
2.41e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.05 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH--------WSKYKAVTDAC-----------------S 742
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTvgdivvssTSKQKEIKPVRkkvgvvfqfpesqlfeeT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 743 LQPDIDLLP--FGDQTEIGER---------GIN----------LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD 801
Cdd:PRK13643 102 VLKDVAFGPqnFGIPKEKAEKiaaeklemvGLAdefwekspfeLSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 530398974 802 HLMQegILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDI 852
Cdd:PRK13643 182 EMMQ--LFESIHQSGQTVVLVTHLMDDVAdYADYVYLLEKGHIISCGTPSDV 231
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1265-1481 |
2.42e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 56.71 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYenNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI-----FDGKIVIDGIDISKLPLHT-- 1337
Cdd:PRK14239 6 LQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNIYSPRTDTvd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1338 LRSRLSIILQDPILFSGSI--------RFNLDPECKCTDDRLWEALEIAQLKNMVKSlpggldaVVTEGGENFSVGQRQL 1409
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIyenvvyglRLKGIKDKQVLDEAVEKSLKGASIWDEVKD-------RLHDSALGLSGGQQQR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398974 1410 FCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTI-LTADLVIVMKRGNILEYD 1481
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYN 229
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
688-861 |
2.47e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 57.06 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV--------HWSKYKAVTD-----------------ACS 742
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVrvddtlitSTSKNKDIKQirkkvglvfqfpesqlfEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 743 LQPDIDLLP--FGDQTEIGER---------GIN----------LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD 801
Cdd:PRK13649 103 VLKDVAFGPqnFGVSQEEAEAlareklalvGISeslfeknpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRK 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398974 802 HLMQegILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDIqTKDVELYE 861
Cdd:PRK13649 183 ELMT--LFKKLHQSGMTIVLVTHLMDDVAnYADFVYVLEKGKLVLSGKPKDI-FQDVDFLE 240
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
765-865 |
2.52e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 56.84 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 765 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLmqEGILKFLQDDKrTLVLVTH-KLQYLTHADWIIAMKDGSV 843
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKI--ESLFLELKKDM-TIVLVTHfPQQAARISDYVAFLYKGQI 223
|
90 100
....*....|....*....|...
gi 530398974 844 LREGTLKDIQTKDV-ELYEHWKT 865
Cdd:PRK14247 224 VEWGPTREVFTNPRhELTEKYVT 246
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
764-853 |
3.13e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 57.02 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 764 NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQY-LTHADWIIAMKDGS 842
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKQGKTIILVTHDLDNvLEWTKRTIFFKDGK 242
|
90
....*....|....*
gi 530398974 843 VLREG----TLKDIQ 853
Cdd:PRK13651 243 IIKDGdtydILSDNK 257
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
684-808 |
3.63e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 55.27 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHW-------SKYKAVT------DAC--------- 741
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLdggdiddPDVAEAChylghrNAMkpaltvaen 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 742 ----------------------SLQPDIDLlPFGdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH- 798
Cdd:PRK13539 94 lefwaaflggeeldiaaaleavGLAPLAHL-PFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAa 162
|
170
....*....|....*..
gi 530398974 799 -------LSDHLMQEGI 808
Cdd:PRK13539 163 valfaelIRAHLAQGGI 179
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1280-1484 |
3.98e-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: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1280 PVLKHVKAYIKPGQKVGICGRTGSGKSSLS--LA-FFRMvDifDGKIVIDGIDISKL-PLHTLRSRLSIILQDPILFSG- 1354
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMkiLSgVYQP-D--SGEILLDGEPVRFRsPRDAQAAGIAIIHQELNLVPNl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1355 SIRFNL------------DpeckctddrlWEALeIAQLKNMVKSLpgGLD----AVVteggENFSVGQRQLFCLARAFVR 1418
Cdd:COG1129 95 SVAENIflgreprrggliD----------WRAM-RRRARELLARL--GLDidpdTPV----GDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398974 1419 KSSILIMDEATASIDMA-TENILQkvVMTAFADR--TVVTIAHRVHTILT-ADLVIVMKRG-NILEYDTPE 1484
Cdd:COG1129 158 DARVLILDEPTASLTEReVERLFR--IIRRLKAQgvAIIYISHRLDEVFEiADRVTVLRDGrLVGTGPVAE 226
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1292-1489 |
3.99e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 57.04 E-value: 3.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1292 GQKVGICGRTGSGKSSLSLAFFRMV---DIFDGKIVIDGIDISKLP---LHTLRS-RLSIILQDPILfsgsirfNLDPEC 1364
Cdd:PRK09473 42 GETLGIVGESGSGKSQTAFALMGLLaanGRIGGSATFNGREILNLPekeLNKLRAeQISMIFQDPMT-------SLNPYM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1365 KCTDdrlwEALEIAQL-KNMVKSLP-----GGLDAV--------VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA 1430
Cdd:PRK09473 115 RVGE----QLMEVLMLhKGMSKAEAfeesvRMLDAVkmpearkrMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTT 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398974 1431 SID-------MATENILQKVVMTAfadrtVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLAQ 1489
Cdd:PRK09473 191 ALDvtvqaqiMTLLNELKREFNTA-----IIMITHDLGVVAgICDKVLVMYAGRTMEYGNARDVFYQ 252
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
672-861 |
4.49e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 56.21 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSW--GSGLAT--LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH------WSKYKAVTD-- 739
Cdd:PRK13637 3 IKIENLTHIYmeGTPFEKkaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIidgvdiTDKKVKLSDir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 740 ---ACSLQ-PDIDL--------LPFG------DQTEIGER--------GIN-----------LSGGQRQRICVARALYQN 782
Cdd:PRK13637 83 kkvGLVFQyPEYQLfeetiekdIAFGpinlglSEEEIENRvkramnivGLDyedykdkspfeLSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 783 TNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDD-KRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIqTKDVELY 860
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEILNK--IKELHKEyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREV-FKEVETL 239
|
.
gi 530398974 861 E 861
Cdd:PRK13637 240 E 240
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
672-847 |
5.56e-08 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 54.89 E-value: 5.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSWGSGLAtLSNIDIRIPTGqLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKYKAVTDACSLQPDIDLLP 751
Cdd:cd03264 1 LQLENLTKRYGKKRA-LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 752 --FG------------------------------------DQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPF 792
Cdd:cd03264 79 qeFGvypnftvrefldyiawlkgipskevkarvdevlelvNLGDRAKKKIGsLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 793 SALD----IHLSDHLMQEGilkflqdDKRTLVLVTHKLQ-YLTHADWIIAMKDGSVLREG 847
Cdd:cd03264 159 AGLDpeerIRFRNLLSELG-------EDRIVILSTHIVEdVESLCNQVAVLNKGKLVFEG 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1265-1488 |
5.66e-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: 5.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVDIFD---GKIV----------------- 1324
Cdd:TIGR03269 1 IEVKNLTKKFDG--KEVLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMDQYEptsGRIIyhvalcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1325 ----------------IDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFnLDPECKCTDDRLWEALE----IAQLKNMV 1384
Cdd:TIGR03269 78 vgepcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTV-LDNVLEALEEIGYEGKEavgrAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1385 KslpggLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHT 1462
Cdd:TIGR03269 157 Q-----LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEV 231
|
250 260
....*....|....*....|....*..
gi 530398974 1463 IL-TADLVIVMKRGNILEYDTPESLLA 1488
Cdd:TIGR03269 232 IEdLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1269-1481 |
5.78e-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: 5.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1269 DLCVRYENNLKPVlkHVK-AYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIDG---IDISK---LPLHt 1337
Cdd:cd03297 1 MLCVDIEKRLPDF--TLKiDFDLNEEVTGIFGASGAGKSTL----LRCIagleKPDGGTIVLNGtvlFDSRKkinLPPQ- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1338 lRSRLSIILQDPILFSG-SIRFNLD---PECKCTDDRLW--EALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 1411
Cdd:cd03297 74 -QRKIGLVFQQYALFPHlNVRENLAfglKRKRNREDRISvdELLDLLGLDHLLNRYPAQL-----------SGGEKQRVA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398974 1412 LARAFVRKSSILIMDEATASIDMATENILQKVV--MTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYD 1481
Cdd:cd03297 142 LARALAAQPELLLLDEPFSALDRALRLQLLPELkqIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
689-824 |
6.04e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.81 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 689 SNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHW--SKYKAVTDA--CSL-----QPDI--DLLPF----- 752
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWqgEPIRRQRDEyhQDLlylghQPGIktELTALenlrf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 753 -----GDQTE---------IGERGI------NLSGGQRQRICVARALYQNTNIVFLDDPFSALDI--------HLSDHLM 804
Cdd:PRK13538 98 yqrlhGPGDDealwealaqVGLAGFedvpvrQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKqgvarleaLLAQHAE 177
|
170 180
....*....|....*....|
gi 530398974 805 QEGIlkflqddkrtLVLVTH 824
Cdd:PRK13538 178 QGGM----------VILTTH 187
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1281-1484 |
6.28e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 56.63 E-value: 6.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1281 VLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLplHTLRSRLSIILQDPILF---- 1352
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTL----LRIIAGLEhqtsGHIRFHGTDVSRL--HARDRKVGFVFQHYALFrhmt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1353 -SGSIRFNLD-------PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILI 1424
Cdd:PRK10851 91 vFDNIAFGLTvlprrerPNAAAIKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398974 1425 MDEATASIDMATENILQKVVMTAFADR--TVVTIAH-RVHTILTADLVIVMKRGNILEYDTPE 1484
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
765-862 |
6.80e-08 |
|
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: 55.48 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 765 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlsdhlMQEGILKFL----QDDKRTLVLVTHKLQYL----THAdwiI 836
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLG-----ARELLLALLdklaAEGAPTLVLVTHHVEEIppgiTHV---L 214
|
90 100
....*....|....*....|....*...
gi 530398974 837 AMKDGSVLREGTLKDIQTKDV--ELYEH 862
Cdd:COG1119 215 LLKDGRVVAAGPKEEVLTSENlsEAFGL 242
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
688-847 |
7.12e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.96 E-value: 7.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGK-------VHWSKYKAVTDACSLQPDIDllpfgDQTEIGE 760
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAgcvdvpdNQFGREASLIDAIGRKGDFK-----DAVELLN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 761 R-GIN-----------LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSdHLMQEGILKFLQDDKRTLVLVTHklqy 828
Cdd:COG2401 121 AvGLSdavlwlrrfkeLSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA-KRVARNLQKLARRAGITLVVATH---- 195
|
170
....*....|....*....
gi 530398974 829 ltHADWIIAMKDGSVLREG 847
Cdd:COG2401 196 --HYDVIDDLQPDLLIFVG 212
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
688-878 |
7.15e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 55.78 E-value: 7.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKY------KAVTDACSLQPDIDL------------ 749
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYaipanlKKIKEVKRLRKEIGLvfqfpeyqlfqe 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 750 -----LPFG------DQTEIGER------------------GINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 800
Cdd:PRK13645 107 tiekdIAFGpvnlgeNKQEAYKKvpellklvqlpedyvkrsPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 801 DHLMQEgILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREGT----------LKDIQTKDVELYEHWKTLMNR 869
Cdd:PRK13645 187 EDFINL-FERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSpfeifsnqelLTKIEIDPPKLYQLMYKLKNK 265
|
....*....
gi 530398974 870 QDQELEKDM 878
Cdd:PRK13645 266 GIDLLNKNI 274
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1272-1472 |
7.87e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 54.72 E-value: 7.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1272 VRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPIL 1351
Cdd:PRK10247 13 VGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1352 FSGSIRFNLD-PeckctddrlWEALEIA-QLKNMVKSLP--GGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDE 1427
Cdd:PRK10247 93 FGDTVYDNLIfP---------WQIRNQQpDPAIFLDDLErfALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 530398974 1428 ATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILTADLVIVM 1472
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVITL 210
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1265-1490 |
9.18e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.03 E-value: 9.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLS--LAFFRMVDIFDGKIVIDGIDISKLPlHTLRSRL 1342
Cdd:CHL00131 8 LEIKNLHASVNEN--EILKGLNLSINKGEIHAIMGPNGSGKSTLSkvIAGHPAYKILEGDILFKGESILDLE-PEERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1343 SIIL--QDPILFSGS-----IRFNLDPECKCTDDRLWEALE----IAQLKNMVKSLPGGLDAVVTEGgenFSVGQRQLFC 1411
Cdd:CHL00131 85 GIFLafQYPIEIPGVsnadfLRLAYNSKRKFQGLPELDPLEfleiINEKLKLVGMDPSFLSRNVNEG---FSGGEKKRNE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1412 LARAFVRKSSILIMDEATASIDM-ATENILQKVVMTAFADRTVVTIAH--RVHTILTADLVIVMKRGNILEydTPESLLA 1488
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDIdALKIIAEGINKLMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIK--TGDAELA 239
|
..
gi 530398974 1489 QE 1490
Cdd:CHL00131 240 KE 241
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
691-847 |
9.63e-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: 54.30 E-value: 9.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 691 IDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKYKAVTDACSLQPDIDLLP-----------------FG 753
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFVSdstglydrltarenleyFA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 754 ------------------DQTEIGE----RGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKF 811
Cdd:cd03266 104 glyglkgdeltarleelaDRLGMEElldrRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALRE--FIRQ 181
|
170 180 190
....*....|....*....|....*....|....*..
gi 530398974 812 LQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREG 847
Cdd:cd03266 182 LRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
688-852 |
9.83e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.57 E-value: 9.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLlAIL--------GEMqTLEGKVHwsKYKAVTDACSL------QpDIDLLP-- 751
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLM-KILsgvyqpdsGEI-LLDGEPV--RFRSPRDAQAAgiaiihQ-ELNLVPnl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 752 -------FGDqtEIGERGI----------------------------NLSGGQRQRICVARALYQNTNIVFLDDPFSALD 796
Cdd:COG1129 95 svaenifLGR--EPRRGGLidwramrrrarellarlgldidpdtpvgDLSVAQQQLVEIARALSRDARVLILDEPTASLT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 530398974 797 IHLSDHLMqeGILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREGTLKDI 852
Cdd:COG1129 173 EREVERLF--RIIRRLKAQGVAIIYISHRLdEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
761-849 |
1.01e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 54.44 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 761 RGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVL-VTHKLQYLTHADWIIAMK 839
Cdd:PRK11629 142 RPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQ--LLGELNRLQGTAFLvVTHDLQLAKRMSRQLEMR 219
|
90
....*....|
gi 530398974 840 DGSVLREGTL 849
Cdd:PRK11629 220 DGRLTAELSL 229
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
688-847 |
1.15e-07 |
|
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: 53.82 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWsKYKAVTDAcsLQPDIDLLP----------FGDQT- 756
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF-DGKPLDIA--ARNRIGYLPeerglypkmkVIDQLv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 757 ------------------------EIGE----RGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgi 808
Cdd:cd03269 93 ylaqlkglkkeearrridewlerlELSEyankRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDV-- 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 530398974 809 LKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREG 847
Cdd:cd03269 171 IRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
1021-1235 |
1.23e-07 |
|
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: 54.87 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1021 LHHNLLNKiilgPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGM---ISYA-TPVFLVALLPLG 1096
Cdd:cd18557 75 LFSSLLRQ----EIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIIlfiLSWKlTLVLLLVIPLLL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1097 VAFYFIQKYFRVASKDLQE-LDDSTQlpllcHFSETAEGLTTIRAF----RHETRFKQRMLELTDTNN---IAYLFLSAA 1168
Cdd:cd18557 151 IASKIYGRYIRKLSKEVQDaLAKAGQ-----VAEESLSNIRTVRSFsaeeKEIRRYSEALDRSYRLARkkaLANALFQGI 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398974 1169 NRWLEvrtdYLGACIVLtasiasisgSSNSGLVGLG----------LLYALTITNYLNWVVRNLADLEVQMGAVKKV 1235
Cdd:cd18557 226 TSLLI----YLSLLLVL---------WYGGYLVLSGqltvgeltsfILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
695-836 |
1.29e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 53.34 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 695 IPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKYKAvtdacSLQPdidllpfgdqteigeRGINLSGGQRQRIC 774
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP-----VYKP---------------QYIDLSGGELQRVA 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398974 775 VARALYQNTNIVFLDDPFSALDIHLSDHLMQeGILKFLQDDKRTLVLVTHKLQYLTH-ADWII 836
Cdd:cd03222 82 IAAALLRNATFYLFDEPSAYLDIEQRLNAAR-AIRRLSEEGKKTALVVEHDLAVLDYlSDRIH 143
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
765-852 |
1.31e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 55.02 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 765 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMqeGILKFLQDDKRTLVL-VTHKLQYLTHADWIIAMKDGSV 843
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVL--ETVRQLKEQKGITVLsITHDLDEAAQADRVIVMNKGEI 218
|
....*....
gi 530398974 844 LREGTLKDI 852
Cdd:PRK13635 219 LEEGTPEEI 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
683-843 |
1.68e-07 |
|
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: 52.82 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 683 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS----KYKAVTDAcsLQPDIDLLP------- 751
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDgkpvTRRSPRDA--IRAGIAYVPedrkreg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 752 -FGDQTeIGER---GINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQ 827
Cdd:cd03215 89 lVLDLS-VAENialSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYR--LIRELADAGKAVLLISSELD 165
|
170
....*....|....*..
gi 530398974 828 YLTH-ADWIIAMKDGSV 843
Cdd:cd03215 166 ELLGlCDRILVMYEGRI 182
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
367-605 |
1.68e-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: 54.48 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 367 TFLQASYYVTIETGI--NLRGALlamiYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFLF-LCPNLWAMPVQIIM 443
Cdd:cd07346 56 SYLRRYLAARLGQRVvfDLRRDL----FRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSsGLLQLLSDVLTLIG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 444 GVILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWE----HIFCKSVE 519
Cdd:cd07346 130 ALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEereiERFREANR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 520 ETRMKELSSLKTFALYTSLSIFMNAAIPIAAVL--ATFVthayaSGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVK 597
Cdd:cd07346 210 DLRDANLRAARLSALFSPLIGLLTALGTALVLLygGYLV-----LQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQ 284
|
....*...
gi 530398974 598 AIISVQKL 605
Cdd:cd07346 285 ALASLERI 292
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
686-854 |
1.70e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 54.28 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 686 ATLSNIDIRIPTGQLTMIVGQVGCGKSSLL------LAILGEMQTLEGKV-HWSKYKAVTDACSLQPDIDLL-----PF- 752
Cdd:PRK14246 24 AILKDITIKIPNNSIFGIMGPSGSGKSTLLkvlnrlIEIYDSKIKVDGKVlYFGKDIFQIDAIKLRKEVGMVfqqpnPFp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 753 ----------------------------------GDQTEIGER----GINLSGGQRQRICVARALYQNTNIVFLDDPFSA 794
Cdd:PRK14246 104 hlsiydniayplkshgikekreikkiveeclrkvGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398974 795 LDIhlsdhLMQEGILKFLQDDKR--TLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQT 854
Cdd:PRK14246 184 IDI-----VNSQAIEKLITELKNeiAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFT 241
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1267-1458 |
1.82e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 55.46 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1267 IHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVID-GIDISKLPlhtlrsr 1341
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTL----LKILagelEPDSGEVSIPkGLRIGYLP------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1342 lsiilQDPILFSG-SIRFNL----------------------DPECKCTD-DRLWEALEIA---QLKNMVKSLPGGL--- 1391
Cdd:COG0488 68 -----QEPPLDDDlTVLDTVldgdaelraleaeleeleaklaEPDEDLERlAELQEEFEALggwEAEARAEEILSGLgfp 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1392 ----DAVVTEggenFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT----ENILQK----VVMT----AFADRTVVT 1455
Cdd:COG0488 143 eedlDRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFLKNypgtVLVVshdrYFLDRVATR 218
|
...
gi 530398974 1456 IAH 1458
Cdd:COG0488 219 ILE 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
688-824 |
2.11e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 55.46 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSK-----------------------YKAVTDACSLQ 744
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglrigylpqeppldddltvldtvLDGDAELRALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 745 PDIDLL--PFGDQTEIGER---------------------------GI----------NLSGGQRQRICVARALYQNTNI 785
Cdd:COG0488 94 AELEELeaKLAEPDEDLERlaelqeefealggweaearaeeilsglGFpeedldrpvsELSGGWRRRVALARALLSEPDL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 530398974 786 VFLDDPFSALDIhlsdhlmqEGIL---KFLQDDKRTLVLVTH 824
Cdd:COG0488 174 LLLDEPTNHLDL--------ESIEwleEFLKNYPGTVLVVSH 207
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1267-1486 |
2.11e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.63 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1267 IHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKI-------------VIDGIDIS 1331
Cdd:PRK10261 15 VENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1332 KLPLHTLR-SRLSIILQDPIL-----------FSGSIRFNLD---PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvt 1396
Cdd:PRK10261 95 AAQMRHVRgADMAMIFQEPMTslnpvftvgeqIAESIRLHQGasrEEAMVEAKRMLDQVRIPEAQTILSRYPHQL----- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1397 eggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE-NILQKV-VMTAFADRTVVTIAHRVHTIL-TADLVIVMK 1473
Cdd:PRK10261 170 ------SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQaQILQLIkVLQKEMSMGVIFITHDMGVVAeIADRVLVMY 243
|
250
....*....|...
gi 530398974 1474 RGNILEYDTPESL 1486
Cdd:PRK10261 244 QGEAVETGSVEQI 256
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
765-841 |
2.18e-07 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 53.59 E-value: 2.18e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398974 765 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegiLKF-LQDDKR-TLVLVTHKLQYLTHADWIIAMKDG 841
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIID---LLFeLNRERGtTLVLVTHDPALAARCDRVLRLRAG 222
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
688-838 |
2.22e-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: 53.42 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSL---LLAILGEMQTLEG-------KVHWSKYKAVTDACSLQPDIDLlpfgDQ-- 755
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdTIYAEGQRRYVESlsayarqFLGQMDKPDVDSIEGLSPAIAI----DQkt 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 756 ------------TEIG-----------------------------ERGIN-LSGGQRQRICVARALYQN-TNIVF-LDDP 791
Cdd:cd03270 87 tsrnprstvgtvTEIYdylrllfarvgirerlgflvdvglgyltlSRSAPtLSGGEAQRIRLATQIGSGlTGVLYvLDEP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 530398974 792 FSALdiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAM 838
Cdd:cd03270 167 SIGL--HPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDI 211
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1282-1465 |
2.35e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 53.34 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1282 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL---PLHTLRSRLSIILQD---------- 1348
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrEVPFLRRQIGMIFQDhhllmdrtvy 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1349 -----PILFSGSirfnldpeckCTDD---RLWEALEIAQLKNMVKSLPggldaVVTEGGENFSVGqrqlfcLARAFVRKS 1420
Cdd:PRK10908 98 dnvaiPLIIAGA----------SGDDirrRVSAALDKVGLLDKAKNFP-----IQLSGGEQQRVG------IARAVVNKP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 530398974 1421 SILIMDEATASIDMA-TENILQ------KVVMTAF-ADRTVVTIAHRVHTILT 1465
Cdd:PRK10908 157 AVLLADEPTGNLDDAlSEGILRlfeefnRVGVTVLmATHDIGLISRRSYRMLT 209
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
703-826 |
2.40e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 54.35 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 703 IVGQVGCGKSSLLLAILGEMQTLEGKVHWsKYKAVTDA--------------------CSLQP-----DIDLLPF----- 752
Cdd:COG4608 49 LVGESGCGKSTLGRLLLRLEEPTSGEILF-DGQDITGLsgrelrplrrrmqmvfqdpyASLNPrmtvgDIIAEPLrihgl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 753 GDQTEIGER--------GIN----------LSGGQRQRICVARALYQNTNIVFLDDPFSALDihLSdhlMQEGILKFLQD 814
Cdd:COG4608 128 ASKAERRERvaellelvGLRpehadrypheFSGGQRQRIGIARALALNPKLIVCDEPVSALD--VS---IQAQVLNLLED 202
|
170
....*....|....*.
gi 530398974 815 DKR----TLVLVTHKL 826
Cdd:COG4608 203 LQDelglTYLFISHDL 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
683-857 |
2.52e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.18 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 683 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLL----------------------------------------LAILGEM 722
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMkvlsgiheptkgtitinninynkldhklaaqlgigiiyqeLSVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 723 QTLE----GK-----------VHWSKYKAVTDacslqpdIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVF 787
Cdd:PRK09700 96 TVLEnlyiGRhltkkvcgvniIDWREMRVRAA-------MMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVII 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398974 788 LDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQTKDV 857
Cdd:PRK09700 169 MDEPTSSLTNKEVDYLFL--IMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDVSNDDI 237
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
987-1235 |
2.99e-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: 53.70 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 987 YYVAGFSILCG------AGIFLcLVTSLTVEWMGLTaaknLHHNLLNKiilgPIRFFDTTPLGLILNRFSADTNIIDQHI 1060
Cdd:cd18572 40 LLLLLLSVLSGlfsglrGGCFS-YAGTRLVRRLRRD----LFRSLLRQ----DIAFFDATKTGELTSRLTSDCQKVSDPL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1061 PPTLESLTRSTLLCLSAIGMISYATP----VFLVALLPLGVAFYFIQKYFRVASKDLQElddstqlpLLCHFSETAE--- 1133
Cdd:cd18572 111 STNLNVFLRNLVQLVGGLAFMFSLSWrltlLAFITVPVIALITKVYGRYYRKLSKEIQD--------ALAEANQVAEeal 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1134 -GLTTIRAFRHET----RFKQRMLELTDTN---NIAYLFLSAANRWLevrtDYLGACIVLtasiasisgssnsgLVGLGL 1205
Cdd:cd18572 183 sNIRTVRSFATEErearRYERALDKALKLSvrqALAYAGYVAVNTLL----QNGTQVLVL--------------FYGGHL 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 530398974 1206 ---------------LYALTITNYLNWVVRNLADLEVQMGAVKKV 1235
Cdd:cd18572 245 vlsgrmsagqlvtfmLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1265-1349 |
3.07e-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: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRY--ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVD----IFDGKIVIDGIDISKLPLHTL 1338
Cdd:COG4172 7 LSVEDLSVAFgqGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPdpaaHPSGSILFDGQDLLGLSEREL 86
|
90
....*....|....*
gi 530398974 1339 R----SRLSIILQDP 1349
Cdd:COG4172 87 RrirgNRIAMIFQEP 101
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
688-852 |
4.21e-07 |
|
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: 53.52 E-value: 4.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG---EMQTLEGKVHW----------SKYKAV-------------Tdac 741
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFdgedllklseKELRKIrgreiqmifqdpmT--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 742 SLQPdidLLPFGDQ-------------TEIGER--------GIN------------LSGGQRQRICVARALYQNTNIVFL 788
Cdd:COG0444 98 SLNP---VMTVGDQiaeplrihgglskAEARERaiellervGLPdperrldrypheLSGGMRQRVMIARALALEPKLLIA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398974 789 DDPFSALDIhlsdhLMQEGILKFLQDDKR----TLVLVTHKL---QYLthADWIIAMKDGSVLREGTLKDI 852
Cdd:COG0444 175 DEPTTALDV-----TIQAQILNLLKDLQRelglAILFITHDLgvvAEI--ADRVAVMYAGRIVEEGPVEEL 238
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
742-875 |
4.41e-07 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 54.42 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 742 SLQPDIDLLpfgDQTEIGER----GINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDhLMQEGILKFLQDDKR 817
Cdd:TIGR03269 145 AVGRAVDLI---EMVQLSHRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAK-LVHNALEEAVKASGI 220
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 530398974 818 TLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQTKDVELYEhwktlMNRQDQELE 875
Cdd:TIGR03269 221 SMVLTSHWPEVIEDlSDKAIWLENGEIKEEGTPDEVVAVFMEGVS-----EVEKECEVE 274
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1281-1488 |
5.36e-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: 5.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1281 VLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVD---IFDGKIVIDG---IDISKLPLHTLRSRLSIILQDpilf 1352
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLlrCINLLEQPEagtIRVGDITIDTarsLSQQKGLIRQLRQHVGFVFQN---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1353 sgsirFNLDPEckctddrlWEALE-IAQLKNMVKSLPGG---------LDAVVTEGGEN-----FSVGQRQLFCLARAFV 1417
Cdd:PRK11264 94 -----FNLFPH--------RTVLEnIIEGPVIVKGEPKEeatararelLAKVGLAGKETsyprrLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398974 1418 RKSSILIMDEATASID--MATEnILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLA 1488
Cdd:PRK11264 161 MRPEVILFDEPTSALDpeLVGE-VLNTIRQLAQEKRTMVIVTHEMSFARdVADRAIFMDQGRIVEQGPAKALFA 233
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1279-1488 |
6.51e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 52.79 E-value: 6.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1279 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI-----FDGKIVIDGIDI-SKLPLHTLRSRLSIILQDPILF 1352
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1353 SGSIRFNLDPECKCtdDRLWEALEIAQLKNMVKSLPGGLDAV---VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEAT 1429
Cdd:PRK14271 114 PMSIMDNVLAGVRA--HKLVPRKEFRGVAQARLTEVGLWDAVkdrLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530398974 1430 ASIDMATENILQKVVMTaFADR-TVVTIAHRV-HTILTADLVIVMKRGNILEYDTPESLLA 1488
Cdd:PRK14271 192 SALDPTTTEKIEEFIRS-LADRlTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
765-869 |
8.79e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 52.55 E-value: 8.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 765 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMKDGSV 843
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQ--LILDAKANNKTVFVITHTMeHVLEVADEVIVMDKGKI 254
|
90 100
....*....|....*....|....*.
gi 530398974 844 LREGTLKDIQTkDVELYEHWKTLMNR 869
Cdd:PRK13631 255 LKTGTPYEIFT-DQHIINSTSIQVPR 279
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
765-852 |
1.11e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 52.44 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 765 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSV 843
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQII-ELLLELQQKENMALVLITHDLALVAEaAHKIIVMYAGQV 232
|
....*....
gi 530398974 844 LREGTLKDI 852
Cdd:PRK11022 233 VETGKAHDI 241
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
684-824 |
1.11e-06 |
|
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: 50.95 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKYKAVTDACSLQPDIDLL------------- 750
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLghapgikttlsvl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 751 -------PFGDQT-------EIGERGI------NLSGGQRQRICVARALYQNTNIVFLDDPFSALDI--------HLSDH 802
Cdd:cd03231 92 enlrfwhADHSDEqveealaRVGLNGFedrpvaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKagvarfaeAMAGH 171
|
170 180
....*....|....*....|..
gi 530398974 803 LMQEGIlkflqddkrtLVLVTH 824
Cdd:cd03231 172 CARGGM----------VVLTTH 183
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
764-857 |
1.46e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 51.33 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 764 NLSGGQRQRICVARALYQNTNIVFLDDPFSALDI-HLSDHLMQegILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDG 841
Cdd:PRK10575 147 SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIaHQVDVLAL--VHRLSQERGLTVIAVLHDINMAArYCDYLVALRGG 224
|
90
....*....|....*.
gi 530398974 842 SVLREGTLKDIQTKDV 857
Cdd:PRK10575 225 EMIAQGTPAELMRGET 240
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
765-847 |
1.51e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 51.64 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 765 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSdhlmqEGILKFLQD--DKRTLVLVTHKL-QYLTHADWIIAMKDG 841
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTT-----EKIEEFIRSlaDRLTVIIVTHNLaQAARISDRAALFFDG 238
|
....*.
gi 530398974 842 SVLREG 847
Cdd:PRK14271 239 RLVEEG 244
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1265-1480 |
1.63e-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: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV-DIF---DGKIVIDGIDISKLPLHT--- 1337
Cdd:cd03269 1 LEVENVTKRFGR--VTALDDISFSVEKGEIFGLLGPNGAGKTTT----IRMIlGIIlpdSGEVLFDGKPLDIAARNRigy 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1338 ------LRSRLSIilQDPILFSGSIRfNLDP-ECKCTDDRLWEALEIAQLKNmvKSLpggldavvteggENFSVGQRQLF 1410
Cdd:cd03269 75 lpeergLYPKMKV--IDQLVYLAQLK-GLKKeEARRRIDEWLERLELSEYAN--KRV------------EELSKGNQQKV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398974 1411 CLARAFVRKSSILIMDEATASIDMATENILQKVVMT-AFADRTVVTIAHRVHTI-LTADLVIVMKRGNILEY 1480
Cdd:cd03269 138 QFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLY 209
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
766-847 |
1.79e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.40 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 766 SGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKR-TLVLVTHKLQY---LTHAdwIIAMKDG 841
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILA--LLKSLQQKHQlAYLFISHDLHVvraLCHQ--VIVLRQG 502
|
....*.
gi 530398974 842 SVLREG 847
Cdd:PRK15134 503 EVVEQG 508
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
748-848 |
1.84e-06 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 50.45 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 748 DLLPFGDQTEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHkl 826
Cdd:cd03265 114 ELLDFVGLLEAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVW-EYIEKLKEEFGMTILLTTH-- 190
|
90 100
....*....|....*....|....*.
gi 530398974 827 qYLTHA----DWIIAMKDGSVLREGT 848
Cdd:cd03265 191 -YMEEAeqlcDRVAIIDHGRIIAEGT 215
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1279-1498 |
1.86e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 51.87 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1279 KPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDifDGKIVIDGIDISKLP-----LHTlrsrlsiILQDPIL 1351
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVlrLIAGFETPD--SGRIMLDGQDITHVPaenrhVNT-------VFQSYAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1352 FSG-SIRFNLDPECKC-------TDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSIL 1423
Cdd:PRK09452 98 FPHmTVFENVAFGLRMqktpaaeITPRVMEALRMVQLEEFAQRKPHQL-----------SGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1424 IMDEATASID------MATE-NILQKVVMTAFadrtvVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQENGVF- 1494
Cdd:PRK09452 167 LLDESLSALDyklrkqMQNElKALQRKLGITF-----VFVTHDQEEALTmSDRIVVMRDGRIEQDGTPREIYEEPKNLFv 241
|
....
gi 530398974 1495 ASFV 1498
Cdd:PRK09452 242 ARFI 245
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1291-1489 |
2.41e-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: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1291 PGQKV-GICGRTGSGKSSLslafFRMV------DifDGKIVIDG---IDISK---LPLHtlRSRLSIILQDPILFSG-SI 1356
Cdd:COG4148 23 PGRGVtALFGPSGSGKTTL----LRAIaglerpD--SGRIRLGGevlQDSARgifLPPH--RRRIGYVFQEARLFPHlSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1357 RFNLD--------PECKCTDDRLWEALEIAQLknmVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEA 1428
Cdd:COG4148 95 RGNLLygrkraprAERRISFDEVVELLGIGHL---LDRRPATL-----------SGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398974 1429 TASIDMATEN----ILQKVvmtafADRT---VVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQ 1489
Cdd:COG4148 161 LAALDLARKAeilpYLERL-----RDELdipILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1272-1481 |
2.49e-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: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1272 VRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslaffrmVDIFDGKIVIDGIDISKLPL------HTLRSRLSII 1345
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTT-------LKILSGLLQPTSGEVRVAGLvpwkrrKKFLRRIGVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1346 L------------QDPILFSGSIrFNLDP-ECKCTDDRLWEALEIAQLknmvkslpggLDAVVteggENFSVGQRQLFCL 1412
Cdd:cd03267 100 FgqktqlwwdlpvIDSFYLLAAI-YDLPPaRFKKRLDELSELLDLEEL----------LDTPV----RQLSLGQRMRAEI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398974 1413 ARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILT-ADLVIVMKRGNILeYD 1481
Cdd:cd03267 165 AAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLL-YD 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
764-847 |
2.66e-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: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 764 NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQ-YLTHADWIiamkdgS 842
Cdd:COG3845 141 DLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFE--ILRRLAAEGKSIIFITHKLReVMAIADRV------T 212
|
....*
gi 530398974 843 VLREG 847
Cdd:COG3845 213 VLRRG 217
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
765-843 |
5.53e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 49.73 E-value: 5.53e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398974 765 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSV 843
Cdd:PRK13650 141 LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKT-IKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
688-839 |
5.73e-06 |
|
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: 48.12 E-value: 5.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLL----LAILGEMQtlegkvHWSKYKAVTDAC-SLQPDIDLLPFGDQteigerg 762
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILdaigLALGGAQS------ATRRRSGVKAGCiVAAVSAELIFTRLQ------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 763 inLSGGQRQRICVARAL----YQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLqDDKRTLVLVTHKLQYLTHADWIIAM 838
Cdd:cd03227 78 --LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPR-DGQALAEAILEHL-VKGAQVIVITHLPELAELADKLIHI 153
|
.
gi 530398974 839 K 839
Cdd:cd03227 154 K 154
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
765-852 |
5.90e-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: 5.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 765 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKRT----LVLVTHKLQYLTH-ADWIIAMK 839
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTV-----QAQILDLLKDLQRElgmaLLLITHDLGVVRRfADRVAVMR 231
|
90
....*....|...
gi 530398974 840 DGSVLREGTLKDI 852
Cdd:COG4172 232 QGEIVEQGPTAEL 244
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1275-1483 |
6.66e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.00 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1275 ENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLslaffrmVDIFDGKIV---IDG-IDISKLP-LHTLRSRLS------ 1343
Cdd:PLN03140 890 EDRLQ-LLREVTGAFRPGVLTALMGVSGAGKTTL-------MDVLAGRKTggyIEGdIRISGFPkKQETFARISgyceqn 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1344 ------IILQDPILFSGSIRfnLDPECKCTD-----DRLWEALEIAQLKNMVKSLPGgldavVTeggeNFSVGQRQLFCL 1412
Cdd:PLN03140 962 dihspqVTVRESLIYSAFLR--LPKEVSKEEkmmfvDEVMELVELDNLKDAIVGLPG-----VT----GLSTEQRKRLTI 1030
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398974 1413 ARAFVRKSSILIMDEATASIDMATENILQKVVM-TAFADRTVVTIAHRVHT-ILTA-DLVIVMKRGNILEYDTP 1483
Cdd:PLN03140 1031 AVELVANPSIIFMDEPTSGLDARAAAIVMRTVRnTVDTGRTVVCTIHQPSIdIFEAfDELLLMKRGGQVIYSGP 1104
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1289-1444 |
6.75e-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: 6.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1289 IKPGQKVGICGRTGSGKSSLS--LAFFRMVDIFDGKIVIDGIDISKLPLH-TLRSRLSIILQDPILFSG-SIRFN--LDP 1362
Cdd:TIGR02633 24 VRPGECVGLCGENGAGKSTLMkiLSGVYPHGTWDGEIYWSGSPLKASNIRdTERAGIVIIHQELTLVPElSVAENifLGN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1363 ECKCTDDRLWEALEIAQLKNMVKSLPggLDAV-VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQ 1441
Cdd:TIGR02633 104 EITLPGGRMAYNAMYLRAKNLLRELQ--LDADnVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILL 181
|
...
gi 530398974 1442 KVV 1444
Cdd:TIGR02633 182 DII 184
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
684-847 |
7.00e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.29 E-value: 7.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS----KYKAVTDACS-----------LQPDID 748
Cdd:PRK11288 16 GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDgqemRFASTTAALAagvaiiyqelhLVPEMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 749 L--------LP--FG--DQTEIGER--------GIN---------LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 799
Cdd:PRK11288 96 VaenlylgqLPhkGGivNRRLLNYEareqlehlGVDidpdtplkyLSIGQRQMVEIAKALARNARVIAFDEPTSSLSARE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 530398974 800 SDHLMQegILKFLQDDKRTLVLVTHKLqylthaDWIIAMKDG-SVLREG 847
Cdd:PRK11288 176 IEQLFR--VIRELRAEGRVILYVSHRM------EEIFALCDAiTVFKDG 216
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
685-846 |
7.17e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 49.01 E-value: 7.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 685 LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHW-------------SKYKA--------------- 736
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvgqplhqmdeearAKLRAkhvgfvfqsfmlipt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 737 ---------------VTDACSLQPDIDLLpfgDQTEIGER----GINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 797
Cdd:PRK10584 103 lnalenvelpallrgESSRQSRNGAKALL---EQLGLGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 530398974 798 HLSDHLMqEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSvLRE 846
Cdd:PRK10584 180 QTGDKIA-DLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQ-LQE 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
764-852 |
7.18e-06 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 50.08 E-value: 7.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 764 NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDhlmqeGILKFLQDDKR----TLVLVTH------KLqylthAD 833
Cdd:COG1135 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTR-----SILDLLKDINRelglTIVLITHemdvvrRI-----CD 209
|
90
....*....|....*....
gi 530398974 834 WIIAMKDGSVLREGTLKDI 852
Cdd:COG1135 210 RVAVLENGRIVEQGPVLDV 228
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
694-835 |
8.53e-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: 48.90 E-value: 8.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 694 RIPT---GQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV--------------------HWSKYKAVTDACSLQPD-IDL 749
Cdd:cd03236 19 RLPVpreGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildefrgselqnYFTKLLEGDVKVIVKPQyVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 750 LP----------------------FGDQTEIG---ERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlsDHL 803
Cdd:cd03236 99 IPkavkgkvgellkkkdergkldeLVDQLELRhvlDRNIdQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK--QRL 176
|
170 180 190
....*....|....*....|....*....|...
gi 530398974 804 MQEGILKFLQDDKRTLVLVTHKLQYLTH-ADWI 835
Cdd:cd03236 177 NAARLIRELAEDDNYVLVVEHDLAVLDYlSDYI 209
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
647-797 |
1.11e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.85 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 647 PGRYHLDSYEQSTRRLRPAETEDIA-----IKVTN--GYFSWGSGL--------ATLSNIDIRIPTGQLTMIVGQVGCGK 711
Cdd:PRK10261 284 PRRFPLISLEHPAKQEPPIEQDTVVdgepiLQVRNlvTRFPLRSGLlnrvtrevHAVEKVSFDLWPGETLSLVGESGSGK 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 712 SSLLLAILGEMQTLEGKVHWSKYKAVT-DACSLQP---DIDLLpFGD--------QT----------------------- 756
Cdd:PRK10261 364 STTGRALLRLVESQGGEIIFNGQRIDTlSPGKLQAlrrDIQFI-FQDpyasldprQTvgdsimeplrvhgllpgkaaaar 442
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 530398974 757 --EIGER-GI----------NLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 797
Cdd:PRK10261 443 vaWLLERvGLlpehawryphEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
964-1175 |
1.11e-05 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 49.02 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 964 IDYWLATwtseysiNNTGKADQTyyvagFSILCGAGIFLCLVTSL---TVEWMGLTAAKNLHHNLLNKIILGPIRFFDTT 1040
Cdd:cd18575 23 IDQGFAA-------GNTALLNRA-----FLLLLAVALVLALASALrfyLVSWLGERVVADLRKAVFAHLLRLSPSFFETT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1041 PLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATP---VFLVALLPLGVA-FYFIQKYFRVASKDLQE- 1115
Cdd:cd18575 91 RTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPkltLLVLLVIPLVVLpIILFGRRVRRLSRASQDr 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1116 LDDSTQlpllcHFSETAEGLTTIRAFRHETRFKQRMLELTDTNniaylfLSAANRWLEVR 1175
Cdd:cd18575 171 LADLSA-----FAEETLSAIKTVQAFTREDAERQRFATAVEAA------FAAALRRIRAR 219
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
666-843 |
1.17e-05 |
|
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: 48.70 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 666 ETEDIAIKVTNGyfswgsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAIL------GEMQtLEGkVHWSKY----- 734
Cdd:cd03289 4 TVKDLTAKYTEG------GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLrllnteGDIQ-IDG-VSWNSVplqkw 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 735 -KA--------------------------------VTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQ 781
Cdd:cd03289 76 rKAfgvipqkvfifsgtfrknldpygkwsdeeiwkVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398974 782 NTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSV 843
Cdd:cd03289 156 KAKILLLDEPSAHLD-PITYQVIRKTLKQAFAD--CTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
763-852 |
1.35e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.10 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 763 INLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVL-VTHKLQYLTH-ADWIIAMKD 840
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP--YLERLAREINIPILyVSHSLDEILRlADRVVVLEQ 204
|
90
....*....|..
gi 530398974 841 GSVLREGTLKDI 852
Cdd:PRK11144 205 GKVKAFGPLEEV 216
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
715-852 |
1.62e-05 |
|
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: 47.92 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 715 LLAILgEMQTLEGKVHWSKYKAVTDACSLQPDIDllpfgdqteigERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 794
Cdd:cd03218 96 ILAVL-EIRGLSKKEREEKLEELLEEFHITHLRK-----------SKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398974 795 LD-IHLSDhlMQEgILKFLQdDKRTLVLVT----HKLQYLTHADWIIamKDGSVLREGTLKDI 852
Cdd:cd03218 164 VDpIAVQD--IQK-IIKILK-DRGIGVLITdhnvRETLSITDRAYII--YEGKVLAEGTPEEI 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
639-824 |
1.87e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 48.67 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 639 PKTINRKQPGRYHLDSYEQSTRRlrPAETEDIAIKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI 718
Cdd:PRK13536 11 PRRLELSPIERKHQGISEAKASI--PGSMSTVAIDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 719 LGEMQTLEGKVHW------SKYKAVTDACSLQPDID-----------LLPFGDQTEIGERGI------------------ 763
Cdd:PRK13536 88 LGMTSPDAGKITVlgvpvpARARLARARIGVVPQFDnldleftvrenLLVFGRYFGMSTREIeavipsllefarleskad 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398974 764 ----NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDDKrTLVLVTH 824
Cdd:PRK13536 168 arvsDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-ARHLIWERLRSLLARGK-TILLTTH 230
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
765-863 |
2.12e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 48.29 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 765 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDGSV 843
Cdd:PRK13641 146 LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQ--LFKDYQKAGHTVILVTHNMDDVAeYADDVLVLEHGKL 223
|
90 100
....*....|....*....|
gi 530398974 844 LREGTLKDIQTKDVELYEHW 863
Cdd:PRK13641 224 IKHASPKEIFSDKEWLKKHY 243
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
760-852 |
2.52e-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: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 760 ERGIN-LSGGQRQRICVARAL-YQNTNIVF-LDDPfsALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWII 836
Cdd:TIGR00630 483 SRAAGtLSGGEAQRIRLATQIgSGLTGVLYvLDEP--SIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVI 560
|
90 100
....*....|....*....|..
gi 530398974 837 AM------KDGSVLREGTLKDI 852
Cdd:TIGR00630 561 DIgpgageHGGEVVASGTPEEI 582
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
660-852 |
2.56e-05 |
|
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: 48.65 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 660 RRLRPAETEDIAIKVTN---GYFSWGSGLA-TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV------ 729
Cdd:TIGR03269 268 EKECEVEVGEPIIKVRNvskRYISVDRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgd 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 730 -------------------------------HWSKYKAVTDACSLQ-PD--------IDLLPFGDQTEIGERGIN----- 764
Cdd:TIGR03269 348 ewvdmtkpgpdgrgrakryigilhqeydlypHRTVLDNLTEAIGLElPDelarmkavITLKMVGFDEEKAEEILDkypde 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 765 LSGGQRQRICVARALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQY-LTHADWIIAMKDGSV 843
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMD-PITKVDVTHSILKAREEMEQTFIIVSHDMDFvLDVCDRAALMRDGKI 506
|
....*....
gi 530398974 844 LREGTLKDI 852
Cdd:TIGR03269 507 VKIGDPEEI 515
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
688-827 |
2.74e-05 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 47.33 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH------WSKYKA--------------------VTDAC 741
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvaglvpWKRRKKflrrigvvfgqktqlwwdlpVIDSF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 742 SLQPDI----------------DLLPFGDQTEIGERgiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlsdhlMQ 805
Cdd:cd03267 117 YLLAAIydlpparfkkrldelsELLDLEELLDTPVR--QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV-----AQ 189
|
170 180
....*....|....*....|....*.
gi 530398974 806 EGILKFLQDDKR----TLVLVTHKLQ 827
Cdd:cd03267 190 ENIRNFLKEYNRergtTVLLTSHYMK 215
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
764-900 |
2.85e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 48.78 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 764 NLSGGQRQRICVARALYQNTNIVFLDDPfsaldihlSDHLMQEGIL---KFLQDDKRTLVLVTHKLQYLTH-ADWIIAMK 839
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEP--------TNHLDAESVAwleRHLQEYPGTVVAVTHDRYFLDNvAGWILELD 232
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398974 840 DG-SVLREGTlkdiqtkdvelYEHW---KTlmNRQDQElEKDMEADQTTLERKT--LRRAMYSREAK 900
Cdd:TIGR03719 233 RGrGIPWEGN-----------YSSWleqKQ--KRLEQE-EKEESARQKTLKRELewVRQSPKGRQAK 285
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1263-1478 |
2.92e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 48.72 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1263 GEIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDIFDGKIVIDGIDISKlplHTLRs 1340
Cdd:PLN03211 67 HKPKISDETRQIQE--RTILNGVTGMASPGEILAVLGPSGSGKSTLlnALAGRIQGNNFTGTILANNRKPTK---QILK- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1341 RLSIILQDPILFSG-SIRFNLdpeCKCTDDRLWEALEiAQLKNMVKslpgglDAVVTEGG----EN----------FSVG 1405
Cdd:PLN03211 141 RTGFVTQDDILYPHlTVRETL---VFCSLLRLPKSLT-KQEKILVA------ESVISELGltkcENtiignsfirgISGG 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530398974 1406 QRQLFCLARAFVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIAH----RVHTILtaDLVIVMKRGNIL 1478
Cdd:PLN03211 211 ERKRVSIAHEMLINPSLLILDEPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHqpssRVYQMF--DSVLVLSEGRCL 286
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1289-1484 |
3.03e-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: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1289 IKPGQKVGICGRTGSGKSSLslafFRMV------DifDGKIVIDGIDISKLPLHtLRSRLSII--LQDPILFSG------ 1354
Cdd:COG0411 27 VERGEIVGLIGPNGAGKTTL----FNLItgfyrpT--SGRILFDGRDITGLPPH-RIARLGIArtFQNPRLFPEltvlen 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1355 --------------SIRFNLDP---ECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFV 1417
Cdd:COG0411 100 vlvaaharlgrgllAALLRLPRarrEEREARERAEELLERVGLADRADEPAGNL-----------SYGQQRRLEIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1418 RKSSILIMDEATASIDMA-TENILQKVV-MTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPE 1484
Cdd:COG0411 169 TEPKLLLLDEPAAGLNPEeTEELAELIRrLRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPA 238
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
761-852 |
3.37e-05 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 46.95 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 761 RGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD-IHLSDhlMQEgILKFLQDdkRTL-VLVT-HK----LQ-----Y 828
Cdd:COG1137 133 KAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDpIAVAD--IQK-IIRHLKE--RGIgVLITdHNvretLGicdraY 207
|
90 100
....*....|....*....|....
gi 530398974 829 LthadwiiaMKDGSVLREGTLKDI 852
Cdd:COG1137 208 I--------ISEGKVLAEGTPEEI 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
765-852 |
3.41e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.31 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 765 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRT-LVLVTHKLQYLTH-ADWIIAMKDGS 842
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQ--LIKVLQKEMSMgVIFITHDMGVVAEiADRVLVMYQGE 246
|
90
....*....|
gi 530398974 843 VLREGTLKDI 852
Cdd:PRK10261 247 AVETGSVEQI 256
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1241-1459 |
3.54e-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: 48.59 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1241 MESENYEGTMDP--------SQVPEHWPQEGEIKIHDLCVRYEN------NLKPVLKHVKAYIKPGQKVGICGRTGSGKS 1306
Cdd:TIGR00954 413 VKSGNFKRPRVEeiesgregGRNSNLVPGRGIVEYQDNGIKFENiplvtpNGDVLIESLSFEVPSGNNLLICGPNGCGKS 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1307 SLslafFRMVD----IFDGKIVIDG----IDISKLPLHTLRSrlsiiLQDPILFSGSIrfnLDPECK-CTDDRLWEALEI 1377
Cdd:TIGR00954 493 SL----FRILGelwpVYGGRLTKPAkgklFYVPQRPYMTLGT-----LRDQIIYPDSS---EDMKRRgLSDKDLEQILDN 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1378 AQLKNMVKSlPGGLDAVvTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA--SIDM--ATENILQKVVMTAFadrtv 1453
Cdd:TIGR00954 561 VQLTHILER-EGGWSAV-QDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSavSVDVegYMYRLCREFGITLF----- 633
|
....*.
gi 530398974 1454 vTIAHR 1459
Cdd:TIGR00954 634 -SVSHR 638
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
764-852 |
3.74e-05 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 47.49 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 764 NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDhlmqeGILKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAM 838
Cdd:PRK11153 140 QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTR-----SILELLKDINRelglTIVLITHEMDVVKRiCDRVAVI 214
|
90
....*....|....
gi 530398974 839 KDGSVLREGTLKDI 852
Cdd:PRK11153 215 DAGRLVEQGTVSEV 228
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1270-1435 |
4.46e-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: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1270 LCVRYEnnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDP 1349
Cdd:TIGR01189 7 ACSRGE---RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1350 ILFSGSIRFNLD---PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMD 1426
Cdd:TIGR01189 84 LKPELSALENLHfwaAIHGGAQRTIEDALAAVGLTGFEDLPAAQL-----------SAGQQRRLALARLWLSRRPLWILD 152
|
....*....
gi 530398974 1427 EATASIDMA 1435
Cdd:TIGR01189 153 EPTTALDKA 161
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
688-846 |
4.63e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 47.00 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV--------HWSKYK------------------------ 735
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIlidgkdvtKLPEYKrakyigrvfqdpmmgtapsmtiee 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 736 ----------------AVTDAcslqpDIDLlpFGDQTEIGERGI---------NLSGGQRQRICVARALYQNTNIVFLDD 790
Cdd:COG1101 102 nlalayrrgkrrglrrGLTKK-----RREL--FRELLATLGLGLenrldtkvgLLSGGQRQALSLLMATLTKPKLLLLDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 530398974 791 PFSALDIHLSDHLMQegiL--KFLQDDKRTLVLVTHKLQY-LTHADWIIAMKDGSVLRE 846
Cdd:COG1101 175 HTAALDPKTAALVLE---LteKIVEENNLTTLMVTHNMEQaLDYGNRLIMMHEGRIILD 230
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
943-1163 |
5.20e-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: 5.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 943 GFFLLILMIFSKLLKHSVI-VAIDywlatwtsEYSINNTGKADQTYYVAGFSILCGAGIFLCL-VTSLTVEWMGLTAAKN 1020
Cdd:cd18544 4 ALLLLLLATALELLGPLLIkRAID--------DYIVPGQGDLQGLLLLALLYLGLLLLSFLLQyLQTYLLQKLGQRIIYD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1021 LHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISY----ATPVFLVALLPLG 1096
Cdd:cd18544 76 LRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLlnwrLALISLLVLPLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398974 1097 VAFYFIQKYFRVASKDLQEL--DDSTQLpllchfSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYL 1163
Cdd:cd18544 156 LATYLFRKKSRKAYREVREKlsRLNAFL------QESISGMSVIQLFNREKREFEEFDEINQEYRKANL 218
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
672-861 |
6.02e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 46.62 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 672 IKVTNGYFSWG--SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH-----------WSKYKAVT 738
Cdd:PRK13642 5 LEVENLVFKYEkeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKidgelltaenvWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 739 DACSlQPDI--------DLLPFGDQTEIGER------------GIN-----------LSGGQRQRICVARALYQNTNIVF 787
Cdd:PRK13642 85 MVFQ-NPDNqfvgatveDDVAFGMENQGIPReemikrvdeallAVNmldfktreparLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398974 788 LDDPFSALDIHLSDHLMQegILKFLQDDKRTLVL-VTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYE 861
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMR--VIHEIKEKYQLTVLsITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMVE 236
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
766-847 |
6.81e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 46.46 E-value: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 766 SGGQRQRICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLqddkRTLV--------LVTHKL---QYLTHAdw 834
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSV-----QARLLDLL----RGLVrelglavvIVTHDLavaRLLAHR-- 221
|
90
....*....|...
gi 530398974 835 IIAMKDGSVLREG 847
Cdd:PRK11701 222 LLVMKQGRVVESG 234
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
688-848 |
7.57e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 46.07 E-value: 7.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAIL---------------GEMQTLEGKVHWSK------------------- 733
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLypalarrlhlkkeqpGNHDRIEGLEHIDKvividqspigrtprsnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 734 -----------------------------YKAVTDACSLQPDID------------------LLPFG-DQTEIGERGINL 765
Cdd:cd03271 91 ytgvfdeirelfcevckgkrynretlevrYKGKSIADVLDMTVEealeffenipkiarklqtLCDVGlGYIKLGQPATTL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 766 SGGQRQRICVARALYQNTN---IVFLDDPFSALdiHLSD--HLMQegILKFLQDDKRTLVLVTHKLQYLTHADWIIAM-- 838
Cdd:cd03271 171 SGGEAQRIKLAKELSKRSTgktLYILDEPTTGL--HFHDvkKLLE--VLQRLVDKGNTVVVIEHNLDVIKCADWIIDLgp 246
|
250
....*....|....
gi 530398974 839 ----KDGSVLREGT 848
Cdd:cd03271 247 eggdGGGQVVASGT 260
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1012-1154 |
8.91e-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: 8.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1012 WMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATP---VF 1088
Cdd:cd18576 62 RVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWkltLL 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398974 1089 LVALLP-LGVAFYFIQKYFRVASKDLQ-ELDDSTQlpllcHFSETAEGLTTIRAFRHE----TRFKQRMLEL 1154
Cdd:cd18576 142 MLATVPvVVLVAVLFGRRIRKLSKKVQdELAEANT-----IVEETLQGIRVVKAFTREdyeiERYRKALERV 208
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1289-1490 |
9.56e-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: 46.74 E-value: 9.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1289 IKPGQKVGICGRTGSGKSSLSLAFFRMVD-IFDGKIVIDG--IDIsKLPLHTLRSRLSIILQD-------PIL------- 1351
Cdd:TIGR02633 283 LRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGkpVDI-RNPAQAIRAGIAMVPEDrkrhgivPILgvgknit 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1352 ------FSGSIRFNLDPECKCTDdrlwEALEIAQLKNMVKSLP-GGLdavvteggenfSVGQRQLFCLARAFVRKSSILI 1424
Cdd:TIGR02633 362 lsvlksFCFKMRIDAAAELQIIG----SAIQRLKVKTASPFLPiGRL-----------SGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530398974 1425 MDEATASIDM-ATENILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNiLEYDTPESLLAQE 1490
Cdd:TIGR02633 427 LDEPTRGVDVgAKYEIYKLINQLAQEGVAIIVVSSELAEVLgLSDRVLVIGEGK-LKGDFVNHALTQE 493
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1265-1481 |
1.02e-04 |
|
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: 45.22 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNLKP--------------------VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIV 1324
Cdd:cd03220 1 IELENVSKSYPTYKGGssslkklgilgrkgevgefwALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1325 IDGIDISKLPLHT-LRSRLSIIlqDPILFSGSIrFNLDPecKCTDDRLWEALEIAQLKNMvkslpggLDAVVteggENFS 1403
Cdd:cd03220 81 VRGRVSSLLGLGGgFNPELTGR--ENIYLNGRL-LGLSR--KEIDEKIDEIIEFSELGDF-------IDLPV----KTYS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1404 VGQ--RQLFCLARAFvrKSSILIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTIL-TADLVIVMKRGNILE 1479
Cdd:cd03220 145 SGMkaRLAFAIATAL--EPDILLIDEVLAVGDAAFQEKCQRRLRELLKQgKTVILVSHDPSSIKrLCDRALVLEKGKIRF 222
|
..
gi 530398974 1480 YD 1481
Cdd:cd03220 223 DG 224
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1289-1479 |
1.09e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 46.27 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1289 IKPGQKVGICGRTGSGKSSLSLAFFRMVDiFDGKIV-----IDGIDISKLPLHTLR----SRLSIILQDPILfsgsirfN 1359
Cdd:PRK11022 30 VKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMaekleFNGQDLQRISEKERRnlvgAEVAMIFQDPMT-------S 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1360 LDPeCKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEG-----------GENFSVGQRQLFCLARAFVRKSSILIMDEA 1428
Cdd:PRK11022 102 LNP-CYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGipdpasrldvyPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1429 TASIDMATE--------NILQKVVMtafadrTVVTIAHRVHTIL-TADLVIVMKRGNILE 1479
Cdd:PRK11022 181 TTALDVTIQaqiielllELQQKENM------ALVLITHDLALVAeAAHKIIVMYAGQVVE 234
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
683-857 |
1.16e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.58 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 683 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEG--KVHWSKYKAVTDACSLQPDIDLLP-----FGDQ 755
Cdd:PRK15439 22 SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGtlEIGGNPCARLTPAKAHQLGIYLVPqepllFPNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 756 T---------------------EIGERGINL----SGG-----QRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQ 805
Cdd:PRK15439 102 SvkenilfglpkrqasmqkmkqLLAALGCQLdldsSAGslevaDRQIVEILRGLMRDSRILILDEPTASLTPAETERLFS 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 530398974 806 EgiLKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQTKDV 857
Cdd:PRK15439 182 R--IRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLSTDDI 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1265-1481 |
1.16e-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: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRM----VDIFDGKIVI-DGIDISKLPlhtlr 1339
Cdd:COG0488 316 LELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTL----LKLlageLEPDSGTVKLgETVKIGYFD----- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1340 srlsiilQDpilfsgsiRFNLDPeckctDDRLWEAL-------EIAQLKNMVKSL--PGglDAVVTEGGeNFSVGQRQLF 1410
Cdd:COG0488 385 -------QH--------QEELDP-----DKTVLDELrdgapggTEQEVRGYLGRFlfSG--DDAFKPVG-VLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398974 1411 CLARAFVRKSSILIMDEATASIDMATENILQKVVMTaFaDRTVVTIAH------RVhtiltADLVIVMKRGNILEYD 1481
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDD-F-PGTVLLVSHdryfldRV-----ATRILEFEDGGVREYP 511
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
765-824 |
1.16e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 45.95 E-value: 1.16e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 765 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQEGiLKFLQDDKRTLVLVTH 824
Cdd:PRK13537 139 LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ-ARHLMWER-LRSLLARGKTILLTTH 196
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1279-1433 |
1.26e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 45.98 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1279 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKlPLHTLRSRLSIILQdpilFSgsirf 1358
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQ----FD----- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1359 NLDPECKCTDD------------RLWEA-----LEIAQLKNMVkslpgglDAVVTEggenFSVGQRQLFCLARAFVRKSS 1421
Cdd:PRK13536 124 NLDLEFTVRENllvfgryfgmstREIEAvipslLEFARLESKA-------DARVSD----LSGGMKRRLTLARALINDPQ 192
|
170
....*....|..
gi 530398974 1422 ILIMDEATASID 1433
Cdd:PRK13536 193 LLILDEPTTGLD 204
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
763-841 |
1.41e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 44.87 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 763 INLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSdhlmqEGILKFLQDDKR---TLVLVTHKLQYLTHADW-IIAM 838
Cdd:PRK10908 136 IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS-----EGILRLFEEFNRvgvTVLMATHDIGLISRRSYrMLTL 210
|
...
gi 530398974 839 KDG 841
Cdd:PRK10908 211 SDG 213
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1291-1470 |
1.53e-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: 43.52 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1291 PGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIdgIDISKLPLHTLRSRLSIILQDPILFSGSIRfnldpeckctddr 1370
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--IDGEDILEEVLDQLLLIIVGGKKASGSGEL------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1371 lwealeiaqlknmvkslpggldavvteggenfsvGQRQLFclARAFVRKSSILIMDEATASIDMATENILQKVVMTAF-- 1448
Cdd:smart00382 66 ----------------------------------RLRLAL--ALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLll 109
|
170 180
....*....|....*....|....*..
gi 530398974 1449 -----ADRTVVTIAHRVHTILTADLVI 1470
Cdd:smart00382 110 llkseKNLTVILTTNDEKDLGPALLRR 136
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
765-841 |
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 530398974 765 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAMK 839
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSV-----QAQILQLLRELQQelnmGLLFITHNLSIVRKlADRVAVMQ 231
|
..
gi 530398974 840 DG 841
Cdd:PRK15134 232 NG 233
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
1021-1150 |
1.65e-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: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1021 LHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIG---MISYA-TPVFLVALLPLG 1096
Cdd:cd18780 77 LRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVfmfTTSWKlTLVMLSVVPPLS 156
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 530398974 1097 VAFYFIQKYFRVASKDLQ-ELDDStqlpllchfSETAE----GLTTIRAFRHETRFKQR 1150
Cdd:cd18780 157 IGAVIYGKYVRKLSKKFQdALAAA---------STVAEesisNIRTVRSFAKETKEVSR 206
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
762-864 |
1.74e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 44.88 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 762 GINLSGGQRQRICVARALYQNTNIVFLDDPFSALD-IHLSDhlmQEGILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMK 839
Cdd:PRK10895 135 GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDpISVID---IKRIIEHLRDSGLGVLITDHNVrETLAVCERAYIVS 211
|
90 100
....*....|....*....|....*....
gi 530398974 840 DGSVLREGT----LKDIQTKDVELYEHWK 864
Cdd:PRK10895 212 QGHLIAHGTpteiLQDEHVKRVYLGEDFR 240
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
700-836 |
1.76e-04 |
|
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: 44.52 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 700 LTMIVGQVGCGKSSLLLAIL----GEM-QTLEGKVHWSKYKAVTDAcSLQPDIDL-LPFGDQTEI--------------- 758
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALKyaltGELpPNSKGGAHDPKLIREGEV-RAQVKLAFeNANGKKYTItrslailenvifchq 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 759 GE--------RGiNLSGGQRQ------RICVARALYQNTNIVFLDDPFSALDihlSDHLMQ--EGILKFLQDDK-RTLVL 821
Cdd:cd03240 103 GEsnwplldmRG-RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD---EENIEEslAEIIEERKSQKnFQLIV 178
|
170
....*....|....*
gi 530398974 822 VTHKLQYLTHADWII 836
Cdd:cd03240 179 ITHDEELVDAADHIY 193
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
1013-1156 |
2.07e-04 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 45.12 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1013 MGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADT----NIIDQHIPptlESLTRSTLLCLSAIGMISYATPVF 1088
Cdd:cd18551 63 TGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTtllrELITSGLP---QLVTGVLTVVGAVVLMFLLDWVLT 139
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398974 1089 LVALLPLGVAF---YFIQKYFRVASKDLQE-LDDSTQlpllcHFSETAEGLTTIRAFRHETRFKQRMLELTD 1156
Cdd:cd18551 140 LVTLAVVPLAFliiLPLGRRIRKASKRAQDaLGELSA-----ALERALSAIRTVKASNAEERETKRGGEAAE 206
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
698-824 |
2.26e-04 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 44.71 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 698 GQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSKYKAVTDACSLQPDI-----DLLP-----FGD----QTEIG---- 759
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYegtvrDLLSsitkdFYThpyfKTEIAkplq 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398974 760 -----ERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlsDHLMQEGILK-FLQDDKRTLVLVTH 824
Cdd:cd03237 105 ieqilDREVPeLSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE--QRLMASKVIRrFAENNEKTAFVVEH 174
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1391-1475 |
2.26e-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: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1391 LDAVVteggENFSVGQRQLFCLARAFVRKSSILIMDEATASI-DMATENILQkvVMTAFAD--RTVVTIAHRVHTILT-A 1466
Cdd:COG3845 135 PDAKV----EDLSVGEQQRVEILKALYRGARILILDEPTAVLtPQEADELFE--ILRRLAAegKSIIFITHKLREVMAiA 208
|
....*....
gi 530398974 1467 DLVIVMKRG 1475
Cdd:COG3845 209 DRVTVLRRG 217
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
758-848 |
2.52e-04 |
|
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: 45.77 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 758 IGERGINLSGGQRQRICVARALYQNTN---IVFLDDPFSALdiHLSD--HLMQegILKFLQDDKRTLVLVTHKLQYLTHA 832
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGL--HFDDikKLLE--VLQRLVDKGNTVVVIEHNLDVIKTA 898
|
90 100
....*....|....*....|..
gi 530398974 833 DWII------AMKDGSVLREGT 848
Cdd:TIGR00630 899 DYIIdlgpegGDGGGTVVASGT 920
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
703-833 |
4.72e-04 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 42.44 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 703 IVGQVGCGKSSLLLAILGEMQTLEGKVHwskykAVT---DACSLQPDIDLLPFgdqTEIGERGINLSGGQRQRICVARAL 779
Cdd:cd00882 2 VVGRGGVGKSSLLNALLGGEVGEVSDVP-----GTTrdpDVYVKELDKGKVKL---VLVDTPGLDEFGGLGREELARLLL 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 530398974 780 YQNTNIVFLDDpfsaLDIHLSDHLMQEGILKFLQDDKRTLVLVthklqyLTHAD 833
Cdd:cd00882 74 RGADLILLVVD----STDRESEEDAKLLILRRLRKEGIPIILV------GNKID 117
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
764-856 |
4.91e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 43.64 E-value: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 764 NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLmqegiLKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAM 838
Cdd:PRK13652 137 HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKEL-----IDFLNDLPEtygmTVIFSTHQLDLVPEmADYIYVM 211
|
90
....*....|....*...
gi 530398974 839 KDGSVLREGTLKDIQTKD 856
Cdd:PRK13652 212 DKGRIVAYGTVEEIFLQP 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1270-1483 |
5.51e-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: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1270 LCVR-----YENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIsKLPLHTLRSRLSI 1344
Cdd:TIGR01257 929 VCVKnlvkiFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGM 1007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1345 ILQDPILF-----SGSIRFNLDpeckcTDDRLWEALEIaQLKNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLARAFVRK 1419
Cdd:TIGR01257 1008 CPQHNILFhhltvAEHILFYAQ-----LKGRSWEEAQL-EMEAMLEDT--GLHHKRNEEAQDLSGGMQRKLSVAIAFVGD 1079
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530398974 1420 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRV-HTILTADLVIVMKRGNILEYDTP 1483
Cdd:TIGR01257 1080 AKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMdEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1291-1434 |
7.90e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 43.32 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1291 PGQKV-GICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG---IDISK---LPLHtlRSRLSIILQDPILFSG-SIRFNLDP 1362
Cdd:PRK11144 22 PAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgicLPPE--KRRIGYVFQDARLFPHyKVRGNLRY 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530398974 1363 ECKCTD----DRLWEALEIAQLknmVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDM 1434
Cdd:PRK11144 100 GMAKSMvaqfDKIVALLGIEPL---LDRYPGSL-----------SGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1265-1433 |
9.06e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 43.26 E-value: 9.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1265 IKIHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTlRSRLSI 1344
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1345 ILQdpilFSgsirfNLDPECKCTDDRL----WEALEIAQLKNMVKSL------PGGLDAVVTEggenFSVGQRQLFCLAR 1414
Cdd:PRK13537 85 VPQ----FD-----NLDPDFTVRENLLvfgrYFGLSAAAARALVPPLlefaklENKADAKVGE----LSGGMKRRLTLAR 151
|
170
....*....|....*....
gi 530398974 1415 AFVRKSSILIMDEATASID 1433
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLD 170
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
683-858 |
9.53e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.76 E-value: 9.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 683 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLL------------------------------------------LAILG 720
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMkvlsgvyphgtyegeiifegeelqasnirdteragiaiihqeLALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 721 EMQTLE-----------GKVHWSKYKAVTDACSLQPDIDLLPfgdQTEIGergiNLSGGQRQRICVARALYQNTNIVFLD 789
Cdd:PRK13549 96 ELSVLEniflgneitpgGIMDYDAMYLRAQKLLAQLKLDINP---ATPVG----NLGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 790 DPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLqylthaDWIIAMKDG-SVLREGtlKDIQTKDVE 858
Cdd:PRK13549 169 EPTASLTESETAVLLD--IIRDLKAHGIACIYISHKL------NEVKAISDTiCVIRDG--RHIGTRPAA 228
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
1033-1168 |
1.07e-03 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 42.78 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1033 PIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIG-MISYATPVFLVALLPL---GVAFYFIQKYFRV 1108
Cdd:cd18541 87 SPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVmMFTISPKLTLIALLPLpllALLVYRLGKKIHK 166
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530398974 1109 ASKDLQE----LDDSTQlpllchfsETAEGLTTIRAFRHETRFKQRMLELTDTN---NIAYLFLSAA 1168
Cdd:cd18541 167 RFRKVQEafsdLSDRVQ--------ESFSGIRVIKAFVQEEAEIERFDKLNEEYvekNLRLARVDAL 225
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
766-852 |
1.16e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 42.79 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 766 SGGQRQRICVARALYQNTNIVFLDDPFSALDIhlsdhLMQEGILKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAMKD 840
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDV-----TVQAQIMTLLNELKRefntAIIMITHDLGVVAGiCDKVLVMYA 237
|
90
....*....|..
gi 530398974 841 GSVLREGTLKDI 852
Cdd:PRK09473 238 GRTMEYGNARDV 249
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
978-1170 |
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 530398974 978 NNTGKADQTYYVAGFSILCGAGIFLCL------VTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSA 1051
Cdd:cd18554 32 GSSLTLDEKVYKLFTIIGIMFFIFLILrppveyYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVIN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1052 DTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVA---LLPL-GVAFYFIQKYFRVASKDL-QELDDstqlpLLC 1126
Cdd:cd18554 112 DVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVslvIFPFyILAVKYFFGRLRKLTKERsQALAE-----VQG 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 530398974 1127 HFSETAEGLTTIRAFRHETRFKQrmlELTDTNNiayLFLSAANR 1170
Cdd:cd18554 187 FLHERIQGMSVIKSFALEKHEQK---QFDKRNG---HFLTRALK 224
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
764-835 |
1.32e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.18 E-value: 1.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530398974 764 NLSGGQRQRICVARALYQNTNIVFLDDPfsaldihlSDHLMQEGIL---KFLQDDKRTLVLVTHKLQYLTH-ADWI 835
Cdd:PRK11819 163 KLSGGERRRVALCRLLLEKPDMLLLDEP--------TNHLDAESVAwleQFLHDYPGTVVAVTHDRYFLDNvAGWI 230
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1292-1449 |
1.66e-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: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1292 GQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECK-CTDDR 1370
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHAdHSDEQ 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398974 1371 LWEALEIAQLkNMVKSLPGGldavvteggeNFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILqkvvMTAFA 1449
Cdd:cd03231 106 VEEALARVGL-NGFEDRPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF----AEAMA 169
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
688-811 |
1.68e-03 |
|
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: 43.00 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGK------VHWSKYKAVTDAcsLQPD----------IDLLP 751
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTieigetVKLAYVDQSRDA--LDPNktvweeisggLDIIK 415
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530398974 752 FGD-------------------QTEIGErginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLmQEGILKF 811
Cdd:TIGR03719 416 LGKreipsrayvgrfnfkgsdqQKKVGQ----LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRAL-EEALLNF 489
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
765-852 |
1.77e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 42.08 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 765 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD---HLMQEgilkfLQDDKR-TLVLVTHKLQYLTH-ADWIIAMK 839
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSqliNLMLE-----LQEKQGiSYIYVTQHLGMMKHiSDQVLVMH 224
|
90
....*....|...
gi 530398974 840 DGSVLREGTLKDI 852
Cdd:PRK15112 225 QGEVVERGSTADV 237
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
688-719 |
2.19e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.69 E-value: 2.19e-03
10 20 30
....*....|....*....|....*....|..
gi 530398974 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAIL 719
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINDTL 655
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
766-829 |
2.69e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 2.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530398974 766 SGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLmQEGILKFlqddKRTLVLVTHKLQYL 829
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWL-ETYLLKW----PKTFIVVSHAREFL 404
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
1024-1186 |
2.93e-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: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1024 NLLNK-IILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTllcLSAIGMI------SYATPVFLVALLPL- 1095
Cdd:cd18784 73 NLLFRsIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSL---VKAIGVIvfmfklSWQLSLVTLIGLPLi 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1096 -GVAFYFiQKYFRVASKDLQeldDStqlplLCHFSETAE----GLTTIRAFRHET----RFK---QRMLELTDTNNIAYL 1163
Cdd:cd18784 150 aIVSKVY-GDYYKKLSKAVQ---DS-----LAKANEVAEetisSIRTVRSFANEDgeanRYSeklKDTYKLKIKEALAYG 220
|
170 180
....*....|....*....|....*..
gi 530398974 1164 FLSAANRWLE----VRTDYLGACIVLT 1186
Cdd:cd18784 221 GYVWSNELTElaltVSTLYYGGHLVIT 247
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
703-797 |
2.93e-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: 42.08 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 703 IVGQVGCGKSSL--LLAilGEMQTLEGKVHWSK---YKAVTdacsLQPDIDLL-----------PFGD---QTEIGER-G 762
Cdd:COG1245 371 IVGPNGIGKTTFakILA--GVLKPDEGEVDEDLkisYKPQY----ISPDYDGTveeflrsantdDFGSsyyKTEIIKPlG 444
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 530398974 763 I---------NLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 797
Cdd:COG1245 445 LeklldknvkDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
764-826 |
3.63e-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: 3.63e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398974 764 NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhlSDHLMQEGILKFLQDDKRTLVLVTHKL 826
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI--YQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
760-893 |
3.69e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 760 ERGIN-LSGGQRQRICVARAL-YQNTNIVF-LDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTHADWII 836
Cdd:PRK00635 471 ERALAtLSGGEQERTALAKHLgAELIGITYiLDEPSIGLHPQDTHKLIN--VIKKLRDQGNTVLLVEHDEQMISLADRII 548
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530398974 837 ------AMKDGSVLREGTLKDIQTKDVELYEHWKtlmnRQDQELEKDmEADQTTLERKTLRRA 893
Cdd:PRK00635 549 digpgaGIFGGEVLFNGSPREFLAKSDSLTAKYL----RQELTIPIP-EKRTNSLGTLTLSKA 606
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
755-824 |
3.70e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 41.96 E-value: 3.70e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530398974 755 QTEIGERGI--NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTH 824
Cdd:TIGR00955 155 NTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQ--VLKGLAQKGKTIICTIH 224
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
698-857 |
3.89e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 40.69 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 698 GQLTMIVGQVGCGKSSLLLAILGeMQTLEGKVHW-----SKYKAVTDA------CSLQPDIDLLPF--------GDQTEI 758
Cdd:PRK03695 22 GEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFagqplEAWSAAELArhraylSQQQTPPFAMPVfqyltlhqPDKTRT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 759 G-------------------ERGIN-LSGGQRQRICVARALYQ-------NTNIVFLDDPFSALDI-------HLSDHLM 804
Cdd:PRK03695 101 EavasalnevaealglddklGRSVNqLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVaqqaaldRLLSELC 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 530398974 805 QEGIlkflqddkrTLVLVTHKLQY-LTHADWIIAMKDGSVLREGTLKDIQTKDV 857
Cdd:PRK03695 181 QQGI---------AVVMSSHDLNHtLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
758-861 |
4.59e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 41.76 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 758 IGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHK--LQYLTHADW 834
Cdd:PLN03140 1012 VGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRT--VRNTVDTGRTVVCTIHQpsIDIFEAFDE 1089
|
90 100
....*....|....*....|....*...
gi 530398974 835 IIAMK-DGSVLREGTLKDIQTKDVELYE 861
Cdd:PLN03140 1090 LLLMKrGGQVIYSGPLGRNSHKIIEYFE 1117
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
691-857 |
4.74e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.50 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 691 IDIRIPTGQLTMIVGQVGCGKSSL--LLAIL-----------GEMQTLEGKVHWSK-YKAV-----------------TD 739
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLamLLTGLyqpqsgeilldGKPVTAEQPEDYRKlFSAVftdfhlfdqllgpegkpAN 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 740 ACSLQPDIDLLPFGDQTEIGE---RGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDK 816
Cdd:PRK10522 422 PALVEKWLERLKMAHKLELEDgriSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQV-LLPLLQEMG 500
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 530398974 817 RTLVLVTHKLQYLTHADWIIAMKDGsVLRE--GTLKDIQTKDV 857
Cdd:PRK10522 501 KTIFAISHDDHYFIHADRLLEMRNG-QLSEltGEERDAASRDA 542
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
746-841 |
5.03e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.25 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 746 DIDLLPfgdqteiGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHK 825
Cdd:PRK10982 123 DIDIDP-------RAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFT--IIRKLKERGCGIVYISHK 193
|
90
....*....|....*..
gi 530398974 826 LQYLTH-ADWIIAMKDG 841
Cdd:PRK10982 194 MEEIFQlCDEITILRDG 210
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1289-1477 |
5.10e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.05 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1289 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG--IDISKlPLHTLRSrlSIIL------QDPILFSGSIRFNL 1360
Cdd:PRK11288 276 VRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRS-PRDAIRA--GIMLcpedrkAEGIIPVHSVADNI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1361 DPECK-------CTDDRLWEA----LEIAQLKnmVKSlPGGLDAVVteggeNFSVGQRQLFCLARAFVRKSSILIMDEAT 1429
Cdd:PRK11288 353 NISARrhhlragCLINNRWEAenadRFIRSLN--IKT-PSREQLIM-----NLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 530398974 1430 ASIDM-ATENILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNI 1477
Cdd:PRK11288 425 RGIDVgAKHEIYNVIYELAAQGVAVLFVSSDLPEVLgVADRIVVMREGRI 474
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
756-797 |
6.48e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.95 E-value: 6.48e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 530398974 756 TEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 797
Cdd:PRK13409 203 ENILDRDIsELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
758-869 |
7.12e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 758 IGERGINLSGGQRQRICVARALY---QNTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLTHADW 834
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQ--LRTLVSLGHSVIYIDHDPALLKQADY 1770
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 530398974 835 IIAM------KDGSVLREGTLKDIQ-TKDVELyehwKTLMNR 869
Cdd:PRK00635 1771 LIEMgpgsgkTGGKILFSGPPKDISaSKDSLL----KTYMCN 1808
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1297-1458 |
7.43e-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: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1297 ICGRTGSGKSSLslaffrmvdifdgkivIDGIDISKLPLHTLRSRLSIILQDPIlFSGSIRFNLDPECKCTDDRLWEAL- 1375
Cdd:cd03240 27 IVGQNGAGKTTI----------------IEALKYALTGELPPNSKGGAHDPKLI-REGEVRAQVKLAFENANGKKYTITr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1376 EIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFC------LARAFVRKSSILIMDEATASIDmaTENILQKVV----- 1444
Cdd:cd03240 90 SLAILENVIFCHQGESNWPLLDMRGRCSGGEKVLASliirlaLAETFGSNCGILALDEPTTNLD--EENIEESLAeiiee 167
|
170
....*....|....
gi 530398974 1445 MTAFADRTVVTIAH 1458
Cdd:cd03240 168 RKSQKNFQLIVITH 181
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
996-1162 |
8.42e-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: 8.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 996 CGAGIFLCLVTSLTvewmgltaaKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCL 1075
Cdd:cd18590 55 LRGGLFMCTLSRLN---------LRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1076 SAIG-MISYATPVFLVALL--PLGVAfyfIQK----YFRVASKDLQE-LDDSTQLPllchfSETAEGLTTIRAFRHET-- 1145
Cdd:cd18590 126 GMLGfMLSLSWQLTLLTLIemPLTAI---AQKvyntYHQKLSQAVQDsIAKAGELA-----REAVSSIRTVRSFKAEEee 197
|
170 180
....*....|....*....|..
gi 530398974 1146 --RFKQ---RMLELTDTNNIAY 1162
Cdd:cd18590 198 acRYSEaleRTYNLKDRRDTVR 219
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
1026-1150 |
8.56e-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: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530398974 1026 LNKIILGPIRFFDTTPLGLILNRFSaDTNIIDQHIPPTLESLTRSTLLCL-SAIGMISYATPVFLVALLPL---GVAFYF 1101
Cdd:cd18570 82 FKHLLKLPLSFFETRKTGEIISRFN-DANKIREAISSTTISLFLDLLMVIiSGIILFFYNWKLFLITLLIIplyILIILL 160
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 530398974 1102 IQKYFRVASKDLQELDDSTQlpllCHFSETAEGLTTIRAFRHETRFKQR 1150
Cdd:cd18570 161 FNKPFKKKNREVMESNAELN----SYLIESLKGIETIKSLNAEEQFLKK 205
|
|
| |
