|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1-748 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 625.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 1 MTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQII 80
Cdd:PLN03130 731 LTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRII 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 81 LLENGKICENGTHSELMqKKGKyaqLIQK-MHKEATSDMLQDTAKIAEKPKVESQALATSLEESLNGNAVPEHQ------ 153
Cdd:PLN03130 811 LVHEGMIKEEGTYEELS-NNGP---LFQKlMENAGKMEEYVEENGEEEDDQTSSKPVANGNANNLKKDSSSKKKskegks 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 154 -LTQEEEMEEGSLSWRVYHHYIQAAGGYMVSCIIFFFVVLIVFLTIFSFWWLSYWLEQGSGtnssrESNGTMadlgniad 232
Cdd:PLN03130 887 vLIKQEERETGVVSWKVLERYKNALGGAWVVMILFLCYVLTEVFRVSSSTWLSEWTDQGTP-----KTHGPL-------- 953
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 233 npqlsFYQLVYGLNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLP 312
Cdd:PLN03130 954 -----FYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVA 1028
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 313 IFSEQFL--VLSLMVIAVLL-IVSVLSPYILLMGAIIMVICFIYYMMFKKAIgvfKRLENYSRSPLFSHILNSLQGLSSI 389
Cdd:PLN03130 1029 VFVNMFLgqIFQLLSTFVLIgIVSTISLWAIMPLLVLFYGAYLYYQSTAREV---KRLDSITRSPVYAQFGEALNGLSTI 1105
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 390 HVYgKTEDFISQFK-RLTDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGIS--STPYSFKV---MAVNIVLQ 463
Cdd:PLN03130 1106 RAY-KAYDRMAEINgRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMQNGraENQAAFAStmgLLLSYALN 1184
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 464 LASSFQATARIGLETEAQFTAVERILQYMKMcVSEAPLHMEGTSCPQGWPQHGEIIFQDYHMKYRDNTPTVLHGINLTIR 543
Cdd:PLN03130 1185 ITSLLTAVLRLASLAENSLNAVERVGTYIDL-PSEAPLVIENNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEIS 1263
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 544 GHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRHTDQQ 623
Cdd:PLN03130 1264 PSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDAD 1343
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 624 IWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQG 703
Cdd:PLN03130 1344 LWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKS 1423
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 767990724 704 CTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGSLFA 748
Cdd:PLN03130 1424 CTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFS 1468
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-748 |
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: 580.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECI--KKTLRGKTVVLVTHQLQYLEFCGQI 79
Cdd:TIGR00957 752 TEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVI 831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 80 ILLENGKICENGTHSELMQKKGKYAQLI-------QKMHKEATSDMLQdTAKIAEKPKVESQALAT-----------SLE 141
Cdd:TIGR00957 832 IVMSGGKISEMGSYQELLQRDGAFAEFLrtyapdeQQGHLEDSWTALV-SGEGKEAKLIENGMLVTdvvgkqlqrqlSAS 910
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 142 ESLNGNAVPEH----------------QLTQEEEMEEGSLSWRVYHHYIQAAGGYMVSCIIFFFVVLIVfLTIFSFWWLS 205
Cdd:TIGR00957 911 SSDSGDQSRHHgssaelqkaeakeetwKLMEADKAQTGQVELSVYWDYMKAIGLFITFLSIFLFVCNHV-SALASNYWLS 989
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 206 YWleqgsgtnssreSNGTMADLGNIADNPQLSFYQLVYGLN--ALLLICVGVCSSGIFtkvtrkASTALHNKLFNKVFRC 283
Cdd:TIGR00957 990 LW------------TDDPMVNGTQNNTSLRLSVYGALGILQgfAVFGYSMAVSIGGIQ------ASRVLHQDLLHNKLRS 1051
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 284 PMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPyilLMGAIIMVICFIYYMMFKKAIGV 363
Cdd:TIGR00957 1052 PMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATP---IAAVIIPPLGLLYFFVQRFYVAS 1128
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 364 ---FKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVAL 440
Cdd:TIGR00957 1129 srqLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAAL 1208
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 441 FVAFGISSTPYSFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYMKMcVSEAPLHMEGTSCPQGWPQHGEIIF 520
Cdd:TIGR00957 1209 FAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSET-EKEAPWQIQETAPPSGWPPRGRVEF 1287
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 521 QDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQ 600
Cdd:TIGR00957 1288 RNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQ 1367
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 601 DPVLLSGTIRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDE 680
Cdd:TIGR00957 1368 DPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDE 1447
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 681 ATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGSLFA 748
Cdd:TIGR00957 1448 ATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYS 1515
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-751 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 566.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 1 MTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQII 80
Cdd:PLN03232 731 LTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRII 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 81 LLENGKICENGTHSELMQKKGKYAQLIQKMHK-EATSDMLQDTAKIAEK-PKVE---SQALATSLEESLNGNAVpehqLT 155
Cdd:PLN03232 811 LVSEGMIKEEGTFAELSKSGSLFKKLMENAGKmDATQEVNTNDENILKLgPTVTidvSERNLGSTKQGKRGRSV----LV 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 156 QEEEMEEGSLSWRVYHHYIQAAGGYMVSCIIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSResngtmadlgniadnpq 235
Cdd:PLN03232 887 KQEERETGIISWNVLMRYNKAVGGLWVVMILLVCYLTTEVLRVSSSTWLSIWTDQSTPKSYSP----------------- 949
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 236 lSFYQLVYGLNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQ----LL 311
Cdd:PLN03232 950 -GFYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRnvanLM 1028
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 312 PIFSEQFLVLsLMVIAVLLIVSVLSPYILLMGAIIMVICFIYYMMFKKAIgvfKRLENYSRSPLFSHILNSLQGLSSIHV 391
Cdd:PLN03232 1029 NMFMNQLWQL-LSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREV---RRLDSVTRSPIYAQFGEALNGLSSIRA 1104
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 392 YgKTEDFISQFK-RLTDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGISSTP-----YSFKVMAVNIVLQLA 465
Cdd:PLN03232 1105 Y-KAYDRMAKINgKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLRNGNAEnqagfASTMGLLLSYTLNIT 1183
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 466 SSFQATARIGLETEAQFTAVERILQYMKMcVSEAPLHMEGTSCPQGWPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGH 545
Cdd:PLN03232 1184 TLLSGVLRQASKAENSLNSVERVGNYIDL-PSEATAIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPS 1262
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 546 EVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRHTDQQIW 625
Cdd:PLN03232 1263 EKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLW 1342
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 626 DALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCT 705
Cdd:PLN03232 1343 EALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCT 1422
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 767990724 706 VLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGSLFAALM 751
Cdd:PLN03232 1423 MLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMV 1468
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
2-751 |
6.40e-154 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 486.59 E-value: 6.40e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIIL 81
Cdd:PTZ00243 774 TEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVA 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 82 LENGKICENGTHSELMQK---KGKYAQLIQKMH-KEATSDMLQDTAKIAE------KPKVESQALATSLEESLNGNAVpE 151
Cdd:PTZ00243 854 LGDGRVEFSGSSADFMRTslyATLAAELKENKDsKEGDADAEVAEVDAAPggavdhEPPVAKQEGNAEGGDGAALDAA-A 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 152 HQLTQEEEMEEGSLSWRVYHHYIQAAGGYMVSCIIFFFVVLIVFLTIFSFWWLSYWleqgsGTNSSRESNGTmadlgnia 231
Cdd:PTZ00243 933 GRLMTREEKASGSVPWSTYVAYLRFCGGLHAAGFVLATFAVTELVTVSSGVWLSMW-----STRSFKLSAAT-------- 999
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 232 dnpqlsfYQLVYglnaLLLICVGVCSSGIFTKVT----RKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQL 307
Cdd:PTZ00243 1000 -------YLYVY----LGIVLLGTFSVPLRFFLSyeamRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDIL 1068
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 308 DQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLmgAIIMViCFIYY--MMFKKAIG-VFKRLENYSRSPLFSHILNSLQ 384
Cdd:PTZ00243 1069 DNTLPMSYLYLLQCLFSICSSILVTSASQPFVLV--ALVPC-GYLYYrlMQFYNSANrEIRRIKSVAKSPVFTLLEEALQ 1145
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 385 GLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGISSTPYSFKVMAVNIVLQL 464
Cdd:PTZ00243 1146 GSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIGVIGTMLRATSQEIGLVSLSLTM 1225
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 465 ASSFQAT----ARIGLETEAQFTAVERILQYMKMCVSEAPLHM----------EGT-------------SCPQGWP---Q 514
Cdd:PTZ00243 1226 AMQTTATlnwlVRQVATVEADMNSVERLLYYTDEVPHEDMPELdeevdalerrTGMaadvtgtvviepaSPTSAAPhpvQ 1305
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 515 HGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSK 594
Cdd:PTZ00243 1306 AGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQ 1385
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 595 LSVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVL-RNS 673
Cdd:PTZ00243 1386 FSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGS 1465
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 674 KIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGSLFAALM 751
Cdd:PTZ00243 1466 GFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMV 1543
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
179-492 |
1.06e-136 |
|
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: 405.79 E-value: 1.06e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 179 GYMVSCIIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSRESNgTMADLGNIADNPQLSFYQLVYGLNALLLICVGVCSS 258
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGSGNTTNNVDN-STVDSGNISDNPDLNFYQLVYGGSILVILLLSLIRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 259 GIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPY 338
Cdd:cd18599 80 FVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 339 ILLMGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLS 418
Cdd:cd18599 160 FLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNC 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767990724 419 STRWMALRLEIMTNLVTLAVALFVAFGISSTPYSFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 492
Cdd:cd18599 240 AMRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
516-736 |
7.98e-127 |
|
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: 376.83 E-value: 7.98e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 516 GEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKL 595
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 596 SVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKI 675
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767990724 676 ILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRP 736
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
166-750 |
7.60e-112 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 351.39 E-value: 7.60e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 166 SWRVYHHYIQAAGGYMVSCII-FFFVVLIVFLTIFSFWWLSYWLEQGSgtnssreSNGTMADLGNIAdnpqlsfyqLVYG 244
Cdd:COG1132 5 PRKLLRRLLRYLRPYRGLLILaLLLLLLSALLELLLPLLLGRIIDALL-------AGGDLSALLLLL---------LLLL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 245 LNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLM 324
Cdd:COG1132 69 GLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 325 VIAVLLIVSVLSPYILLMGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKR 404
Cdd:COG1132 149 LIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFRE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 405 LTDaqnNYLLLFLSSTRWMAL---RLEIMTNLVTLAVALFVAFGISS---TPYSFkVMAVNIVLQLASSFQATARIGLET 478
Cdd:COG1132 229 ANE---ELRRANLRAARLSALffpLMELLGNLGLALVLLVGGLLVLSgslTVGDL-VAFILYLLRLFGPLRQLANVLNQL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 479 EAQFTAVERILQYMkmcvSEAPLHMEGTSCPQGWPQHGEIIFQDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGK 558
Cdd:COG1132 305 QRALASAERIFELL----DEPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRP-VLKDISLTIPPGETVALVGPSGSGK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 559 SSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRH-TDQQIWDALERTFLTKAI 637
Cdd:COG1132 380 STLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDaTDEEVEEAAKAAQAHEFI 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 638 SKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVL 717
Cdd:COG1132 460 EALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIR 539
|
570 580 590
....*....|....*....|....*....|...
gi 767990724 718 NCDHILVMGNGKVVEFDRPEVLRKKPGsLFAAL 750
Cdd:COG1132 540 NADRILVLDDGRIVEQGTHEELLARGG-LYARL 571
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-734 |
1.03e-104 |
|
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: 351.13 E-value: 1.03e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIIL 81
Cdd:TIGR01271 540 TVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILL 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 82 LENGKICENGTHSELMQKKGKYAQLI------QKMHKEATSDMLQDT---------------------------AKIAEK 128
Cdd:TIGR01271 620 LHEGVCYFYGTFSELQAKRPDFSSLLlgleafDNFSAERRNSILTETlrrvsidgdstvfsgpetikqsfkqppPEFAEK 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 129 PK-------------------VESQALATSLEESLNG------NAVPE-------------------------------- 151
Cdd:TIGR01271 700 RKqsiilnpiasarkfsfvqmGPQKAQATTIEDAVREpserkfSLVPEdeqgeeslprgnqyhhglqhqaqrrqsvlqlm 779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 152 ----------HQLT--------------------------------------QEEEMEE----------GSLSWRVYHHY 173
Cdd:TIGR01271 780 thsnrgenrrEQLQtsfrkkssitqqnelaseldiysrrlskdsvyeiseeiNEEDLKEcfaderenvfETTTWNTYLRY 859
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 174 IQAAGGyMVSCIIFFFVVlivFLTIFSFWWLSYWLEQGSGTNSSRESNGTMADLGNIADNPQL----SFYQLVYglnall 249
Cdd:TIGR01271 860 ITTNRN-LVFVLIFCLVI---FLAEVAASLLGLWLITDNPSAPNYVDQQHANASSPDVQKPVIitptSAYYIFY------ 929
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 250 lICVGVCSS----GIF-------TKVTrkASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQF 318
Cdd:TIGR01271 930 -IYVGTADSvlalGFFrglplvhTLLT--VSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDF 1006
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 319 LVLSLMVIAVLLIVSVLSPYILLMGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDF 398
Cdd:TIGR01271 1007 IQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYF 1086
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 399 ISQFKRLTDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVAlFVAFGISSTpysfKVMAVNIVLQLA----SSFQATARI 474
Cdd:TIGR01271 1087 ETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVT-FIAIGTNQD----GEGEVGIILTLAmnilSTLQWAVNS 1161
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 475 GLETEAQFTAVERILQYMKMCVSEAP-------------LHMEGTSCPQGWPQHGEIIFQDYHMKYRDNTPTVLHGINLT 541
Cdd:TIGR01271 1162 SIDVDGLMRSVSRVFKFIDLPQEEPRpsggggkyqlstvLVIENPHAQKCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFS 1241
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 542 IRGHEVVGIVGRTGSGKSSLGMALFRLVEpMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRHTD 621
Cdd:TIGR01271 1242 VEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSD 1320
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 622 QQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAF 701
Cdd:TIGR01271 1321 EEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSF 1400
|
890 900 910
....*....|....*....|....*....|...
gi 767990724 702 QGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFD 734
Cdd:TIGR01271 1401 SNCTVILSEHRVEALLECQQFLVIEGSSVKQYD 1433
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
512-736 |
2.67e-100 |
|
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: 307.80 E-value: 2.67e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 512 WPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDL 591
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 592 RSKLSVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALErtfltkaiskfpkklhtdVVENGGNFSVGERQLLCIARAVLR 671
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767990724 672 NSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRP 736
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
260-752 |
2.30e-94 |
|
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: 309.07 E-value: 2.30e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 260 IFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFaGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYI 339
Cdd:COG2274 219 LLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 340 LLMGAIIMVICFIYYMMFKKAIG--VFKRLENYSRspLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLlfl 417
Cdd:COG2274 298 ALVVLLLIPLYVLLGLLFQPRLRrlSREESEASAK--RQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARF--- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 418 sSTRWMALRLEIMTNLVT-LAVALFVAFGisstpySFKVM----------AVNIVL-QLASSFQATARIGLETEAQFTAV 485
Cdd:COG2274 373 -KLRRLSNLLSTLSGLLQqLATVALLWLG------AYLVIdgqltlgqliAFNILSgRFLAPVAQLIGLLQRFQDAKIAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 486 ERILQYMKMcVSEAPLHMEGTSCPQGwpqHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMAL 565
Cdd:COG2274 446 ERLDDILDL-PPEREEGRSKLSLPRL---KGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 566 FRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRH-TDQQIWDALERTFLTKAISKFPKKL 644
Cdd:COG2274 522 LGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDaTDEEIIEAARLAGLHDFIEALPMGY 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 645 HTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILV 724
Cdd:COG2274 602 DTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIV 681
|
490 500
....*....|....*....|....*...
gi 767990724 725 MGNGKVVEFDRPEVLRKKPGsLFAALMA 752
Cdd:COG2274 682 LDKGRIVEDGTHEELLARKG-LYAELVQ 708
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
516-753 |
1.29e-76 |
|
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: 247.90 E-value: 1.29e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 516 GEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKL 595
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 596 SVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKI 675
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 676 ILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGSLFAALMAT 753
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVRT 255
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
294-744 |
1.23e-75 |
|
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: 255.08 E-value: 1.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 294 GRLLNCFAGDLEQLDQL-----LPIfseqfLVLSLMVIAVLLIVSVLSPYI-LLMGAIIMVICFIY-YMMFKKAIGVFKR 366
Cdd:COG4987 112 GDLLNRLVADVDALDNLylrvlLPL-----LVALLVILAAVAFLAFFSPALaLVLALGLLLAGLLLpLLAARLGRRAGRR 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 367 LENySRSPLFSHILNSLQGLSSIHVYGKTEDFIsqfKRLTDAQNNYLLLFLSSTRWMALR---LEIMTNLVTLAVALFVA 443
Cdd:COG4987 187 LAA-ARAALRARLTDLLQGAAELAAYGALDRAL---ARLDAAEARLAAAQRRLARLSALAqalLQLAAGLAVVAVLWLAA 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 444 FGISSTPYSFKVMAVnIVLQLASSFQATARIGL---ETEAQFTAVERILQymkmcVSEAPLHMEGTSCPQGWPQHGEIIF 520
Cdd:COG4987 263 PLVAAGALSGPLLAL-LVLAALALFEALAPLPAaaqHLGRVRAAARRLNE-----LLDAPPAVTEPAEPAPAPGGPSLEL 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 521 QDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQ 600
Cdd:COG4987 337 EDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQ 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 601 DPVLLSGTIRFNL---DPfdRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIIL 677
Cdd:COG4987 417 RPHLFDTTLRENLrlaRP--DATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILL 494
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767990724 678 IDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPG 744
Cdd:COG4987 495 LDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNG 561
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
183-492 |
9.44e-74 |
|
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: 241.25 E-value: 9.44e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 183 SCIIFFFVVLIVFLTIFSFWWLSYWLEQGSGTnssresngtmadlgniaDNPQLSFYQLVY-GLNALLLICVGVCSSGIF 261
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSS-----------------PNSSSGYYLGVYaALLVLASVLLVLLRWLLF 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 262 TKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILL 341
Cdd:cd18580 64 VLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 342 MGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLSSTR 421
Cdd:cd18580 144 VLPPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQR 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767990724 422 WMALRLEIMTNLVTLAVALFVAFGISSTPYSFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 492
Cdd:cd18580 224 WLGLRLDLLGALLALVVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
516-744 |
3.23e-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: 234.81 E-value: 3.23e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 516 GEIIFQDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKL 595
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 596 SVIPQDPVLLSGTIRFNLDPFD-RHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSK 674
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRpNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 675 IILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPG 744
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
518-729 |
1.03e-66 |
|
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: 218.02 E-value: 1.03e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 518 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSV 597
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 598 IPQDPVLLSGTIRFNLdpfdrhtdqqiwdalertfltkaiskfpkklhtdvvenggnFSVGERQLLCIARAVLRNSKIIL 677
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767990724 678 IDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGK 729
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
248-732 |
5.74e-65 |
|
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: 226.52 E-value: 5.74e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 248 LLLICVGVC---SSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLpifSEQFLVL--- 321
Cdd:TIGR02203 62 GLAVLRGICsfvSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAA---TDAFIVLvre 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 322 SLMVIA---VLLIVS-VLSPYILLMGAIIMVICFIYYmmfkkaigvfKRLENYSRsplfsHILNS-----------LQGL 386
Cdd:TIGR02203 139 TLTVIGlfiVLLYYSwQLTLIVVVMLPVLSILMRRVS----------KRLRRISK-----EIQNSmgqvttvaeetLQGY 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 387 SSIHVYGKTEdfiSQFKRLtDAQNNYLLLFlsstrwmALRLEIMTNL--------------VTLAVALFVAFGISSTPYS 452
Cdd:TIGR02203 204 RVVKLFGGQA---YETRRF-DAVSNRNRRL-------AMKMTSAGSIsspitqliaslalaVVLFIALFQAQAGSLTAGD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 453 FKVMAVNIvLQLASSFQATARIGLETEAQFTAVERILQYmkmcVSEAPLHMEGTSCPQgwPQHGEIIFQDYHMKYRDNTP 532
Cdd:TIGR02203 273 FTAFITAM-IALIRPLKSLTNVNAPMQRGLAAAESLFTL----LDSPPEKDTGTRAIE--RARGDVEFRNVTFRYPGRDR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFN 612
Cdd:TIGR02203 346 PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANN 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 613 LDPFDRHT--DQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETD 690
Cdd:TIGR02203 426 IAYGRTEQadRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESE 505
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 767990724 691 TLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 732
Cdd:TIGR02203 506 RLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVE 547
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
518-750 |
1.00e-63 |
|
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: 212.48 E-value: 1.00e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 518 IIFQDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSV 597
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 598 IPQDPVLLSGTIRFNLdpfdRH-----TDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRN 672
Cdd:cd03253 80 VPQDTVLFNDTIGYNI----RYgrpdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 673 SKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKpGSLFAAL 750
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAK-GGLYAEM 232
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
183-491 |
5.74e-63 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 213.34 E-value: 5.74e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 183 SCIIFFFVVLIVFLT----IFSFWWLSYWLEQGSGTNSSRESNGTMADLGNIADNPQLSFYQLVYGLNALLLICVGVCSS 258
Cdd:cd18601 1 GVFVFILLVLLNIAAqvlyVLSDWWLSYWANLEEKLNDTTDRVQGENSTNVDIEDLDRDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 259 GIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPY 338
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 339 ILLmGAIIMVICFI----YYMMFKKAIgvfKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLL 414
Cdd:cd18601 161 VLI-PVIPLVILFLflrrYYLKTSREV---KRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWF 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 415 LFLSSTRWMALRLEIMTnLVTLAVALFVAFGISSTPYSFKV-MAVNIVLQLASSFQATARIGLETEAQFTAVERILQY 491
Cdd:cd18601 237 LFLATSRWLAVRLDALC-ALFVTVVAFGSLFLAESLDAGLVgLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEY 313
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
185-492 |
2.03e-61 |
|
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: 208.49 E-value: 2.03e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 185 IIFFFVVLIVFLTIFSFWWLSYWLEQgsgtnssresngtmADLGNIADNPQLSFYQLVYGLNALLLICVGVCSSGIFTKV 264
Cdd:cd18603 3 LILLLYLLSQAFSVGSNIWLSEWSDD--------------PALNGTQDTEQRDYRLGVYGALGLGQAIFVFLGSLALALG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 265 TRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILlmgA 344
Cdd:cd18603 69 CVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFL---V 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 345 IIMVICFIYYMMFKKAIGV---FKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLSSTR 421
Cdd:cd18603 146 VIIPLAILYFFIQRFYVATsrqLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNR 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767990724 422 WMALRLEIMTNLVTLAVALFVAFGISSTPYSFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 492
Cdd:cd18603 226 WLAVRLEFLGNLIVLFAALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEYS 296
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
518-732 |
2.19e-61 |
|
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: 206.31 E-value: 2.19e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 518 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSV 597
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 598 IPQDPVLLSGTIRFNLdPFDRH--TDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKI 675
Cdd:cd03251 81 VSQDVFLFNDTVAENI-AYGRPgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767990724 676 ILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 732
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVE 216
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
185-492 |
3.61e-61 |
|
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: 207.71 E-value: 3.61e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 185 IIFFFVVLIVFLTIFSFWWLSYWLEqgsgtNSSRESNGtmadlgniadnpqlsFYQLVY-GLNALLLICVgVCSSGIFTK 263
Cdd:cd18606 3 LLLLLLILSQFAQVFTNLWLSFWTE-----DFFGLSQG---------------FYIGIYaGLGVLQAIFL-FLFGLLLAY 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 264 VTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMg 343
Cdd:cd18606 62 LGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIA- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 344 AIIMVICFIYYMMFKKAIGV-FKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLSSTRW 422
Cdd:cd18606 141 LPPLLVLYYFIANYYRASSReLKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRW 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767990724 423 MALRLEIMTNLVTLAVALFVAFGISS-TPYSFKVmAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 492
Cdd:cd18606 221 LAIRLDLLGSLLVLIVALLCVTRRFSiSPSSTGL-VLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
185-492 |
8.75e-59 |
|
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: 201.16 E-value: 8.75e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 185 IIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSRESNGTmadlgniadnpqLSFYQLVYGLNALLLICVGVCSSGIFTKV 264
Cdd:cd18604 3 LLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEVS------------VLYYLGIYALISLLSVLLGTLRYLLFFFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 265 TRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGA 344
Cdd:cd18604 71 SLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 345 IIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLSSTRWMA 424
Cdd:cd18604 151 VLAALYVYIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLS 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 425 LRLEIMTNLVTLAVALFVAFGISSTPySFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 492
Cdd:cd18604 231 VRIDLLGALFSFATAALLVYGPGIDA-GLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
518-751 |
2.96e-58 |
|
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: 197.76 E-value: 2.96e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 518 IIFQDYHMKY--RDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKL 595
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 596 SVIPQDPVLLSGTIRFN--LDPFDRhTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNS 673
Cdd:cd03249 80 GLVSQEPVLFDGTIAENirYGKPDA-TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 674 KIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGsLFAALM 751
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKG-VYAKLV 235
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
515-732 |
9.35e-55 |
|
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: 198.89 E-value: 9.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 515 HGEIIFQDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSK 594
Cdd:COG5265 355 GGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 595 LSVIPQDPVLLSGTIRFNLdPFDRH--TDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRN 672
Cdd:COG5265 434 IGIVPQDTVLFNDTIAYNI-AYGRPdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKN 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 673 SKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 732
Cdd:COG5265 513 PPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVE 572
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
518-752 |
1.59e-53 |
|
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: 185.00 E-value: 1.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 518 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSV 597
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 598 IPQDPVLLSGTIRFNLDPFDRHTD-QQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKII 676
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSmERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767990724 677 LIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKpGSLFAALMA 752
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE-NGLYAYLYQ 235
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
516-734 |
7.26e-53 |
|
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: 184.67 E-value: 7.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 516 GEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEpMAGRILIDGVDICSIGLEDLRSKL 595
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 596 SVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKI 675
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767990724 676 ILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFD 734
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYD 218
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
294-712 |
5.32e-51 |
|
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: 186.80 E-value: 5.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 294 GRLLNCFAGDLEQLDQLLP--IFSeqfLVLSLMV--IAVLLIVSVLSPYILLMGAIIMVICFIYYMMFKKAIGVFKRLEN 369
Cdd:TIGR02868 110 GDLLGRLGADVDALQDLYVrvIVP---AGVALVVgaAAVAAIAVLSVPAALILAAGLLLAGFVAPLVSLRAARAAEQALA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 370 YSRSPLFSHILNSLQGLSSIHVYGKTEDFIsqfKRLTDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGI--- 446
Cdd:TIGR02868 187 RLRGELAAQLTDALDGAAELVASGALPAAL---AQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGpav 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 447 SSTPYSFKVMAVNIVLQLASsFQATARIGLE----TEAQfTAVERILQYM--KMCVSEAPLHMEGTSCPQGWPqhgeIIF 520
Cdd:TIGR02868 264 ADGRLAPVTLAVLVLLPLAA-FEAFAALPAAaqqlTRVR-AAAERIVEVLdaAGPVAEGSAPAAGAVGLGKPT----LEL 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 521 QDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQ 600
Cdd:TIGR02868 338 RDLSAGYPGAPP-VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQ 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 601 DPVLLSGTIRFNLDpFDRH--TDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILI 678
Cdd:TIGR02868 417 DAHLFDTTVRENLR-LARPdaTDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLL 495
|
410 420 430
....*....|....*....|....*....|....
gi 767990724 679 DEATASIDMETDTLIQRTIREAFQGCTVLVIAHR 712
Cdd:TIGR02868 496 DEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
277-750 |
7.41e-51 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 187.48 E-value: 7.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 277 FNKVFRCPMSFFDTIPIGRLLNCFagdLEQLDQL----LPIFSEQFLvlSLMVIAVLLIVSVlspYI-LLMGAIIMVICF 351
Cdd:PRK13657 96 FERIIQLPLAWHSQRGSGRALHTL---LRGTDALfglwLEFMREHLA--TLVALVVLLPLAL---FMnWRLSLVLVVLGI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 352 IYYMM----FKKAIGVFKRLENYsRSPLFSHILNSLQGLSSIHVYGKTEDFISQFK----RLTDAQNNYL--------LL 415
Cdd:PRK13657 168 VYTLIttlvMRKTKDGQAAVEEH-YHDLFAHVSDAIGNVSVVQSYNRIEAETQALRdiadNLLAAQMPVLswwalasvLN 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 416 FLSSTRWMALRLEIMTNLVT---LAVALFVAFgisstpYSFKVMAVNIVLQLAS----SFQATARIgleteAQFTAVERI 488
Cdd:PRK13657 247 RAASTITMLAILVLGAALVQkgqLRVGEVVAF------VGFATLLIGRLDQVVAfinqVFMAAPKL-----EEFFEVEDA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 489 LQYmkmcVSEAPlhmeGTSCPQGWpqHGEIIFQDYHMKYrDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRL 568
Cdd:PRK13657 316 VPD----VRDPP----GAIDLGRV--KGAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRV 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 569 VEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNL-----DPfdrhTDQQIWDALERTFLTKAISKFPKK 643
Cdd:PRK13657 385 FDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIrvgrpDA----TDEEMRAAAERAQAHDFIERKPDG 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 644 LHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHIL 723
Cdd:PRK13657 461 YDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRIL 540
|
490 500 510
....*....|....*....|....*....|
gi 767990724 724 VMGNGKVVE---FDrpEVLRKkpGSLFAAL 750
Cdd:PRK13657 541 VFDNGRVVEsgsFD--ELVAR--GGRFAAL 566
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
265-725 |
3.62e-50 |
|
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: 184.41 E-value: 3.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 265 TRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFagdLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPyILLMGA 344
Cdd:TIGR02857 72 AAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLA---LEGVEALDGYFARYLPQLVLAVIVPLAILAAVFP-QDWISG 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 345 IIMVICFIYYMMFKKAIGVF------KRLENYSRspLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAqnnylllFLS 418
Cdd:TIGR02857 148 LILLLTAPLIPIFMILIGWAaqaaarKQWAALSR--LSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEE-------YRE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 419 STrwMA-LRLEIMTNLV-----TLAVALfVAFGISstpysFKVMAVNIVL------------------QLASSFQATAri 474
Cdd:TIGR02857 219 RT--MRvLRIAFLSSAVlelfaTLSVAL-VAVYIG-----FRLLAGDLDLatglfvlllapefylplrQLGAQYHARA-- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 475 glETEAQFTAVERILQymkmcVSEAPLHMEGtscPQGWPQHGEIIFQDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRT 554
Cdd:TIGR02857 289 --DGVAAAEALFAVLD-----AAPRPLAGKA---PVTAAPASSLEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPS 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 555 GSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRH-TDQQIWDALERTFL 633
Cdd:TIGR02857 358 GAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDaSDAEIREALERAGL 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 634 TKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRV 713
Cdd:TIGR02857 438 DEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRL 517
|
490
....*....|..
gi 767990724 714 TTVLNCDHILVM 725
Cdd:TIGR02857 518 ALAALADRIVVL 529
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1-86 |
6.49e-50 |
|
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: 173.81 E-value: 6.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 1 MTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLR-GKTVVLVTHQLQYLEFCGQI 79
Cdd:cd03250 118 LTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLnNKTRILVTHQLQLLPHADQI 197
|
....*..
gi 767990724 80 ILLENGK 86
Cdd:cd03250 198 VVLDNGR 204
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
184-492 |
1.20e-49 |
|
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: 176.64 E-value: 1.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 184 CIIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSRESNGTMADlgniaDNPQLSFYQLVYGLNALLLICVGVCSSGIFTK 263
Cdd:cd18602 2 ALVLALALLKQGLRVATDFWLADWTEANHDVASVVFNITSSSL-----EDDEVSYYISVYAGLSLGAVILSLVTNLAGEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 264 VTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMG 343
Cdd:cd18602 77 AGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 344 AIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAqNNYLLLFLSST-RW 422
Cdd:cd18602 157 IPIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDR-NNTAFLFLNTAnRW 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767990724 423 MALRLEIMTNLVTLA---VALFVAFGISSTPySFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 492
Cdd:cd18602 236 LGIRLDYLGAVIVFLaalSSLTAALAGYISP-SLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
516-731 |
4.43e-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: 172.00 E-value: 4.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 516 GEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKL 595
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 596 SVIPQDPVLLSGTIRFNL---DPFdrHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRN 672
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNItlgAPL--ADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 673 SKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRvTTVLN-CDHILVMGNGKVV 731
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHR-PSLLDlVDRIIVMDSGRIV 217
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
185-492 |
4.53e-47 |
|
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: 169.25 E-value: 4.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 185 IIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSRESNgtmadlgniadnpQLSFYQLVYGLNALLLICVGVCSSGIFTKV 264
Cdd:cd18605 3 LILLSLILMQASRNLIDFWLSYWVSHSNNSFFNFIND-------------SFNFFLTVYGFLAGLNSLFTLLRAFLFAYG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 265 TRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLmga 344
Cdd:cd18605 70 GLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLL--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 345 IIMVICFIYYMM---FKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQF-KRLTDAQNNYLLLfLSST 420
Cdd:cd18605 147 LLLPLAFIYYRIqryYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYlEKLENNQRAQLAS-QAAS 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767990724 421 RWMALRLEIMTNLVTLAVALFVAFGIS---STPYSFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 492
Cdd:cd18605 226 QWLSIRLQLLGVLIVTFVALTAVVQHFfglSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
276-752 |
5.30e-47 |
|
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: 177.84 E-value: 5.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 276 LFNKVFRCPMSFFDTIPIGRLLNCFAGdLEQLDQLLP----------IFSEQFLVLSLMVIAVLLIVSVLspyILLmgAI 345
Cdd:TIGR03797 215 VWDRLLRLPVSFFRQYSTGDLASRAMG-ISQIRRILSgstlttllsgIFALLNLGLMFYYSWKLALVAVA---LAL--VA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 346 IMVICFIYYMMFKKaigVFKRLENYSRspLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQnnylllflsstRWMAL 425
Cdd:TIGR03797 289 IAVTLVLGLLQVRK---ERRLLELSGK--ISGLTVQLINGISKLRVAGAENRAFARWAKLFSRQ-----------RKLEL 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 426 RLEIMTNLVT------LAVALFVAFGISSTPYSFKVMAVNIVLQLASSF-QATARIGLETEAQFTAVERILQYMKMC-VS 497
Cdd:TIGR03797 353 SAQRIENLLTvfnavlPVLTSAALFAAAISLLGGAGLSLGSFLAFNTAFgSFSGAVTQLSNTLISILAVIPLWERAKpIL 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 498 EAPLHMEGTSCPQGwPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLgmalFRLV----EPMA 573
Cdd:TIGR03797 433 EALPEVDEAKTDPG-KLSGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTL----LRLLlgfeTPES 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 574 GRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGG 653
Cdd:TIGR03797 508 GSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGG 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 654 NFSVGERQLLCIARAVLRNSKIILIDEATASIDMETdtliQRTIREAF--QGCTVLVIAHRVTTVLNCDHILVMGNGKVV 731
Cdd:TIGR03797 588 TLSGGQRQRLLIARALVRKPRILLFDEATSALDNRT----QAIVSESLerLKVTRIVIAHRLSTIRNADRIYVLDAGRVV 663
|
490 500
....*....|....*....|.
gi 767990724 732 EFDRPEVLRKKPGsLFAALMA 752
Cdd:TIGR03797 664 QQGTYDELMAREG-LFAQLAR 683
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
278-732 |
7.99e-47 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 176.06 E-value: 7.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 278 NKVFRCPMSFFDTIPIGRLLNCFAGDLEQL-DQLLPIFSEQFLVLSL---MVIAVLLI---VSVLSPYILLMGAIIMVIc 350
Cdd:PRK10790 106 DAALRQPLSAFDTQPVGQLISRVTNDTEVIrDLYVTVVATVLRSAALigaMLVAMFSLdwrMALVAIMIFPAVLVVMVI- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 351 fiyYMMFKKAIgvFKRLenysRSPL------FSHILNslqGLSSIHVYGKTEDFisqFKRLTDAQNNYLLlflssTRWMA 424
Cdd:PRK10790 185 ---YQRYSTPI--VRRV----RAYLadindgFNEVIN---GMSVIQQFRQQARF---GERMGEASRSHYM-----ARMQT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 425 LRLE--IMTNLVTLAVA-----LFVAFGISSTP-------YSFkvmaVNIVLQLASSF-QATARIGLETEAqFTAVERIL 489
Cdd:PRK10790 245 LRLDgfLLRPLLSLFSAlilcgLLMLFGFSASGtievgvlYAF----ISYLGRLNEPLiELTTQQSMLQQA-VVAGERVF 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 490 QYMkmcvsEAPLHMEGTScpqGWP-QHGEIIFQDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRL 568
Cdd:PRK10790 320 ELM-----DGPRQQYGND---DRPlQSGRIDIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGY 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 569 VEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLdPFDRH-TDQQIWDALERTFLTKAISKFPKKLHTD 647
Cdd:PRK10790 391 YPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANV-TLGRDiSEEQVWQALETVQLAELARSLPDGLYTP 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 648 VVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGN 727
Cdd:PRK10790 470 LGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHR 549
|
....*
gi 767990724 728 GKVVE 732
Cdd:PRK10790 550 GQAVE 554
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
256-744 |
4.14e-45 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 172.98 E-value: 4.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 256 CSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVL 335
Cdd:TIGR00958 220 LRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 336 SPYILLMGAIIMVICFIYYMMFKKAI-GVFKRLENySRSPLFSHILNSLQGLSSIHVYG-------KTEDFISQFKRLTD 407
Cdd:TIGR00958 300 SPRLTMVTLINLPLVFLAEKVFGKRYqLLSEELQE-AVAKANQVAEEALSGMRTVRSFAaeegeasRFKEALEETLQLNK 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 408 AQNNYLLLFLSSTRWMALRLE----------IMTNLVTlaVALFVAFGIsstpYSFKV-MAVNIVLQLASSFQATArigl 476
Cdd:TIGR00958 379 RKALAYAGYLWTTSVLGMLIQvlvlyyggqlVLTGKVS--SGNLVSFLL----YQEQLgEAVRVLSYVYSGMMQAV---- 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 477 eteaqfTAVERILQYM--KMCVSE----APLHMEGTscpqgwpqhgeIIFQDYHMKY--RDNTPtVLHGINLTIRGHEVV 548
Cdd:TIGR00958 449 ------GASEKVFEYLdrKPNIPLtgtlAPLNLEGL-----------IEFQDVSFSYpnRPDVP-VLKGLTFTLHPGEVV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 549 GIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLD-PFDRHTDQQIWDA 627
Cdd:TIGR00958 511 ALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDTPDEEIMAA 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 628 LERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTirEAFQGCTVL 707
Cdd:TIGR00958 591 AKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVL 668
|
490 500 510
....*....|....*....|....*....|....*..
gi 767990724 708 VIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPG 744
Cdd:TIGR00958 669 LIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
262-752 |
1.09e-44 |
|
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: 171.67 E-value: 1.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 262 TKVTRKASTALHNKLFNKVFRCPMSFFDTipigRllncFAGDLE---QL-DQLLPIFSEQFL--VLSLMVIAVLLIVSVL 335
Cdd:TIGR03796 219 RRLEIKLAVGMSARFLWHILRLPVRFFAQ----R----HAGDIAsrvQLnDQVAEFLSGQLAttALDAVMLVFYALLMLL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 336 spYILLMGAIIMVICFIYYMMFKKaigVFKRLENYSRS------PLFSHILNSLQGLSSIHVYGKTEDFisqFKRLTDAQ 409
Cdd:TIGR03796 291 --YDPVLTLIGIAFAAINVLALQL---VSRRRVDANRRlqqdagKLTGVAISGLQSIETLKASGLESDF---FSRWAGYQ 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 410 NNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGisstpySFKVMAVNIVL-------QLASSFQA--TARIGL---- 476
Cdd:TIGR03796 363 AKLLNAQQELGVLTQILGVLPTLLTSLNSALILVVG------GLRVMEGQLTIgmlvafqSLMSSFLEpvNNLVGFggtl 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 477 -ETEAQFTAVERILQYMKMCVSEAPLHMEGTSCPQgWPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTG 555
Cdd:TIGR03796 437 qELEGDLNRLDDVLRNPVDPLLEEPEGSAATSEPP-RRLSGYVELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSG 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 556 SGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRH-TDQQIWDALERTFLT 634
Cdd:TIGR03796 516 SGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTiPDADLVRACKDAAIH 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 635 KAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREafQGCTVLVIAHRVT 714
Cdd:TIGR03796 596 DVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLS 673
|
490 500 510
....*....|....*....|....*....|....*...
gi 767990724 715 TVLNCDHILVMGNGKVVEFDRPEVLRKKPGsLFAALMA 752
Cdd:TIGR03796 674 TIRDCDEIIVLERGKVVQRGTHEELWAVGG-AYARLIR 710
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
294-732 |
2.27e-42 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 162.69 E-value: 2.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 294 GRLLNCFAGDLEQLDQL-LPIFSEqfLVLSLMVIAVLLI-VSVLSPYI-LLMGAIIMVICFIYYMMFKKAIGVFKRLENY 370
Cdd:PRK11160 117 GDLLNRLVADVDTLDHLyLRLISP--LVAALVVILVLTIgLSFFDLTLaLTLGGILLLLLLLLPLLFYRLGKKPGQDLTH 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 371 SRSPLFSHILNSLQGLSSIHVYGKTEDFIsqfKRLTDAQnnylllflssTRWMAlRLEIMTNLVTLAVALFVAFGisstp 450
Cdd:PRK11160 195 LRAQYRVQLTEWLQGQAELTLFGAEDRYR---QQLEQTE----------QQWLA-AQRRQANLTGLSQALMILAN----- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 451 ysfkVMAVNIVLQLASS-----FQATARIGLETEAQFTAVERIL------QYMKMCVS-----------EAPLHMEGTSC 508
Cdd:PRK11160 256 ----GLTVVLMLWLAAGgvggnAQPGALIALFVFAALAAFEALMpvagafQHLGQVIAsarrineiteqKPEVTFPTTST 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 509 PQgwPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGL 588
Cdd:PRK11160 332 AA--ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 589 EDLRSKLSVIPQDPVLLSGTIRFNL---DPfdRHTDQQIWDALERTFLTKAISKfPKKLHTDVVENGGNFSVGERQLLCI 665
Cdd:PRK11160 410 AALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGI 486
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767990724 666 ARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 732
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIE 553
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
513-730 |
1.94e-41 |
|
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: 151.08 E-value: 1.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 513 PQH--GEIIFQDYHMKYRDNTPT-VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLE 589
Cdd:cd03248 5 PDHlkGIVKFQNVTFAYPTRPDTlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 590 DLRSKLSVIPQDPVLLSGTIRFNLD------PFDRHTDQQIwDALERTFltkaISKFPKKLHTDVVENGGNFSVGERQLL 663
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAyglqscSFECVKEAAQ-KAHAHSF----ISELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767990724 664 CIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKV 730
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
538-758 |
3.28e-41 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 159.63 E-value: 3.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 538 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVePMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFD 617
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 618 RH-TDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRT 696
Cdd:PRK11174 448 PDaSDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA 527
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767990724 697 IREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGsLFAALMATATSSL 758
Cdd:PRK11174 528 LNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGG-LFATLLAHRQEEI 588
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
516-744 |
1.52e-40 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 157.49 E-value: 1.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 516 GEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKL 595
Cdd:PRK11176 340 GDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 596 SVIPQDPVLLSGTIRFNLD--PFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNS 673
Cdd:PRK11176 420 ALVSQNVHLFNDTIANNIAyaRTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767990724 674 KIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPG 744
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNG 570
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
526-730 |
8.18e-38 |
|
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: 138.89 E-value: 8.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 526 KYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLL 605
Cdd:cd03246 9 RYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDELF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 606 SGTIRFNLdpfdrhtdqqiwdalertfltkaiskfpkklhtdvvenggnFSVGERQLLCIARAVLRNSKIILIDEATASI 685
Cdd:cd03246 89 SGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767990724 686 DMETDTLIQRTIREA-FQGCTVLVIAHRVTTVLNCDHILVMGNGKV 730
Cdd:cd03246 128 DVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
534-741 |
8.61e-38 |
|
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: 149.13 E-value: 8.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 534 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNL 613
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 614 DPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLI 693
Cdd:COG4618 427 ARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAAL 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767990724 694 QRTIREA-FQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEF-DRPEVLRK 741
Cdd:COG4618 507 AAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFgPRDEVLAR 556
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
528-733 |
3.12e-35 |
|
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: 133.40 E-value: 3.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 528 RDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG---LEDLRSKLSVIPQDPVL 604
Cdd:cd03257 14 GGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMVFQDPMS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 605 lsgtirfNLDPfdRHT-DQQIWDALERTFLTKAISKFPKKLHTDVVENGGN----------FSVGERQLLCIARAVLRNS 673
Cdd:cd03257 94 -------SLNP--RMTiGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPeevlnrypheLSGGQRQRVAIARALALNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767990724 674 KIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEF 733
Cdd:cd03257 165 KLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEE 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
535-683 |
3.41e-35 |
|
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: 130.46 E-value: 3.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 535 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSG-TIRFNL 613
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767990724 614 -------DPFDRHTDQQIWDALERTfltkaisKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATA 683
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKL-------GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
527-729 |
3.67e-34 |
|
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: 127.75 E-value: 3.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 527 YRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQdpvlLS 606
Cdd:cd00267 7 FRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ----LS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 607 GtirfnldpfdrhtdqqiwdalertfltkaiskfpkklhtdvvenggnfsvGERQLLCIARAVLRNSKIILIDEATASID 686
Cdd:cd00267 83 G--------------------------------------------------GQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767990724 687 METDTLIQRTIREAFQ-GCTVLVIAHRVTTVLN-CDHILVMGNGK 729
Cdd:cd00267 113 PASRERLLELLRELAEeGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
518-732 |
9.27e-34 |
|
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: 127.43 E-value: 9.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 518 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGlEDLRSKLSV 597
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 598 IPQDPVLLSGTIRFNLdpfdrhtdqqiwdalertfltkaiskfpkklhtdvvenGGNFSVGERQLLCIARAVLRNSKIIL 677
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767990724 678 IDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 732
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
528-737 |
3.36e-33 |
|
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: 134.65 E-value: 3.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 528 RDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG---LEDLRSKLSVIPQDPVL 604
Cdd:COG1123 274 GKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRVQMVFQDPYS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 605 -------LSGTIRFNLDPFDRHTDQQIWD----ALERTFL-TKAISKFPkklHTdvvenggnFSVGERQLLCIARAVLRN 672
Cdd:COG1123 354 slnprmtVGDIIAEPLRLHGLLSRAERRErvaeLLERVGLpPDLADRYP---HE--------LSGGQRQRVAIARALALE 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767990724 673 SKIILIDEATASIDMetdtLIQRTIREAFQ------GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPE 737
Cdd:COG1123 423 PKLLILDEPTSALDV----SVQAQILNLLRdlqrelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTE 490
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-108 |
7.31e-33 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 134.52 E-value: 7.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLRGKTVVLVTHQLQYLEFCGQIIL 81
Cdd:COG1132 468 TVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEA-LERLMKGRTTIVIAHRLSTIRNADRILV 546
|
90 100
....*....|....*....|....*..
gi 767990724 82 LENGKICENGTHSELMQKKGKYAQLIQ 108
Cdd:COG1132 547 LDDGRIVEQGTHEELLARGGLYARLYR 573
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-727 |
1.39e-32 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 135.93 E-value: 1.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDaHVGKHIFEECIKkTLRG---KTVVLVTHQLQYLEFCGQ 78
Cdd:PTZ00265 571 TLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTIN-NLKGnenRITIIIAHRLSTIRYANT 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 79 IILLENGK-----------------------------------------------ICENGTHSELMQKK-GKYAQLI--Q 108
Cdd:PTZ00265 649 IFVLSNRErgstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnagsyIIEQGTHDALMKNKnGIYYTMInnQ 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 109 KMHKEAT--------SDMLQDTAKIAEKPKVESQALATSLEESLNGNAVPEHQLTQEEEME---EGSLSW--RVYHHYIQ 175
Cdd:PTZ00265 729 KVSSKKSsnndndkdSDMKSSAYKDSERGYDPDEMNGNSKHENESASNKKSCKMSDENASEnnaGGKLPFlrNLFKRKPK 808
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 176 AAGGY-MVSCIIFFFV--VLIVFLTI---------FSFWWLSYWleqgsgtnssresnGTMADLGNI-ADNPQLSFYQLV 242
Cdd:PTZ00265 809 APNNLrIVYREIFSYKkdVTIIALSIlvagglypvFALLYAKYV--------------STLFDFANLeANSNKYSLYILV 874
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 243 YglnALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDT---IPiGRLLNCFAGDLEQLDQLLP----IFS 315
Cdd:PTZ00265 875 I---AIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHINRDVHLLKTGLVnnivIFT 950
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 316 eQFLVLslmviavLLIVSVLSPYIL-LMGAIIMVICFIYYMMF-------------KKAIG------VFKRLENYSRSPL 375
Cdd:PTZ00265 951 -HFIVL-------FLVSMVMSFYFCpIVAAVLTGTYFIFMRVFairarltankdveKKEINqpgtvfAYNSDDEIFKDPS 1022
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 376 FShILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNylllflsstrwmALRLEIMTNLVTLAVALFVAFGISSTPYSFK- 454
Cdd:PTZ00265 1023 FL-IQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNK------------GQKRKTLVNSMLWGFSQSAQLFINSFAYWFGs 1089
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 455 ------VMAVNIVLQLASSFQATAR-----IGLETEAQfTAVERILQYMKMCVSEAPLHME---GTSCPQGWPQHGEIIF 520
Cdd:PTZ00265 1090 flirrgTILVDDFMKSLFTFLFTGSyagklMSLKGDSE-NAKLSFEKYYPLIIRKSNIDVRdngGIRIKNKNDIKGKIEI 1168
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 521 QDYHMKY--RDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRL------------------------------ 568
Cdd:PTZ00265 1169 MDVNFRYisRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneqdyqgdee 1247
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 569 ------------------------VEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDpFDRH--TDQ 622
Cdd:PTZ00265 1248 qnvgmknvnefsltkeggsgedstVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FGKEdaTRE 1326
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 623 QIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ 702
Cdd:PTZ00265 1327 DVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKD 1406
|
890 900
....*....|....*....|....*..
gi 767990724 703 GC--TVLVIAHRVTTVLNCDHILVMGN 727
Cdd:PTZ00265 1407 KAdkTIITIAHRIASIKRSDKIVVFNN 1433
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
518-749 |
1.64e-32 |
|
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: 132.33 E-value: 1.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 518 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEP---MAGRILIDGVDICSIGLEDLRSK 594
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 595 LSVIPQDP--VLLSGTIRF-------NLDPFDRHTDQQIWDALERTFLTKAISKFPkklHTdvvenggnFSVGERQLLCI 665
Cdd:COG1123 85 IGMVFQDPmtQLNPVTVGDqiaealeNLGLSRAEARARVLELLEAVGLERRLDRYP---HQ--------LSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 666 ARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKK 742
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
....*..
gi 767990724 743 PGSLFAA 749
Cdd:COG1123 234 PQALAAV 240
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-108 |
1.61e-31 |
|
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: 131.49 E-value: 1.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFeECIKKTLRGKTVVLVTHQLQYLEFCGQIIL 81
Cdd:COG2274 603 TVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIIL-ENLRRLLKGRTVIIIAHRLSTIRLADRIIV 681
|
90 100
....*....|....*....|....*..
gi 767990724 82 LENGKICENGTHSELMQKKGKYAQLIQ 108
Cdd:COG2274 682 LDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
533-739 |
4.02e-31 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 122.46 E-value: 4.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDP---------- 602
Cdd:COG1120 15 PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPpapfgltvre 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 603 -VLLSgtiRFN-LDPFDRHTD---QQIWDALERTfltkAISKFpkkLHTDVVEnggnFSVGERQLLCIARAVLRNSKIIL 677
Cdd:COG1120 95 lVALG---RYPhLGLFGRPSAedrEAVEEALERT----GLEHL---ADRPVDE----LSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 678 IDEATASIDM----ETDTLIQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRP-EVL 739
Cdd:COG1120 161 LDEPTSHLDLahqlEVLELLRRLARE--RGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPeEVL 226
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
166-492 |
5.03e-31 |
|
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: 124.14 E-value: 5.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 166 SWRVYHHYIQAAGGYMVSCIIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSRESNGTMAdlgnIADNPQLSFYQL-VYG 244
Cdd:cd18600 2 TWNTYLRYITSHKSLIFVLILCLVIFAIEVAASLVGLWLLRSQADRVNTTRPESSSNTYA----VIVTFTSSYYVFyIYV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 245 LNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLM 324
Cdd:cd18600 78 GVADSLLAMGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 325 VIAVLLIVSVLSPYILLMGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKR 404
Cdd:cd18600 158 VIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 405 LTDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVAlFVAFGISstpySFKVMAVNIVLQLA----SSFQATARIGLETEA 480
Cdd:cd18600 238 ALNLHTANWFLYLSTLRWFQMRIEMIFVIFFTAVT-FISIGTT----GDGEGRVGIILTLAmnimSTLQWAVNTSIDVDS 312
|
330
....*....|..
gi 767990724 481 QFTAVERILQYM 492
Cdd:cd18600 313 LMRSVSRIFKFI 324
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-101 |
1.65e-30 |
|
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: 127.18 E-value: 1.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLRGKTVVLVTHQLQYLEFCGQIIL 81
Cdd:COG4988 465 TPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQA-LRRLAKGRTVILITHRLALLAQADRILV 543
|
90 100
....*....|....*....|
gi 767990724 82 LENGKICENGTHSELMQKKG 101
Cdd:COG4988 544 LDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
184-464 |
3.18e-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: 120.44 E-value: 3.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 184 CIIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSRESngtmadlgniadnpQLSFYQLVYGLNALLLICVGVCSSGIFTK 263
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQ--------------ALNVYSLALLLLGLAQFILSFLQSYLLNH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 264 VTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMG 343
Cdd:pfam00664 68 TGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 344 AIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLSSTRWM 423
Cdd:pfam00664 148 LAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLS 227
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 767990724 424 ALRLEIMTNLVTLAVALFVAFGISSTPYSFKVMAVNIVLQL 464
Cdd:pfam00664 228 FGITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFA 268
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-109 |
3.34e-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: 119.26 E-value: 3.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFeECIKKTLRGKTVVLVTHQLQYLEFCGQIIL 81
Cdd:cd03253 129 TIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQ-AALRDVSKGRTTIVIAHRLSTIVNADKIIV 207
|
90 100
....*....|....*....|....*...
gi 767990724 82 LENGKICENGTHSELMQKKGKYAQLIQK 109
Cdd:cd03253 208 LKDGRIVERGTHEELLAKGGLYAEMWKA 235
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
518-729 |
3.74e-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: 117.96 E-value: 3.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 518 IIFQDYHMKYRDN---TPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGvdicsigledlrsK 594
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 595 LSVIPQDPVLLSGTIRFNL---DPFDrhtDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLR 671
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENIlfgKPFD---EERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 672 NSKIILIDEATASIDMET-DTLIQRTIREAFQGC-TVLVIAHRVTTVLNCDHILVMGNGK 729
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVgRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-108 |
4.68e-30 |
|
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: 125.65 E-value: 4.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLRGKTVVLVTHQLQYLEFCGQIIL 81
Cdd:COG4987 463 TWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLAD-LLEALAGRTVLLITHRLAGLERMDRILV 541
|
90 100
....*....|....*....|....*..
gi 767990724 82 LENGKICENGTHSELMQKKGKYAQLIQ 108
Cdd:COG4987 542 LEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
497-744 |
4.11e-29 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 122.90 E-value: 4.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 497 SEAPLHMEGT-SCPQGwpqHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGR 575
Cdd:PRK10789 295 AEAPVVKDGSePVPEG---RGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGD 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 576 ILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNL---DPfdRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENG 652
Cdd:PRK10789 372 IRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIalgRP--DATQQEIEHVARLASVHDDILRLPQGYDTEVGERG 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 653 GNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 732
Cdd:PRK10789 450 VMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQ 529
|
250
....*....|..
gi 767990724 733 FDRPEVLRKKPG 744
Cdd:PRK10789 530 RGNHDQLAQQSG 541
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
526-729 |
9.50e-29 |
|
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: 114.10 E-value: 9.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 526 KYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDP--V 603
Cdd:cd03225 8 SYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPddQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 604 LLSGTIR---------FNLDPFDRhtDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSK 674
Cdd:cd03225 88 FFGPTVEeevafglenLGLPEEEI--EERVEEALELVGLEGLRDRSPFTL-----------SGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767990724 675 IILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGK 729
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
524-731 |
2.67e-28 |
|
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: 111.76 E-value: 2.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 524 HMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQdpV 603
Cdd:cd03214 6 SVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ--A 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 604 LlsgtIRFNLDPFdrhtdqqiwdaLERTFLTkaiskfpkklhtdvvenggnFSVGERQLLCIARAVLRNSKIILIDEATA 683
Cdd:cd03214 82 L----ELLGLAHL-----------ADRPFNE--------------------LSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767990724 684 SIDM----ETDTLIQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV 731
Cdd:cd03214 127 HLDIahqiELLELLRRLARE--RGKTVVMVLHDLNLAARyADRVILLKDGRIV 177
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
533-736 |
2.35e-27 |
|
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: 113.22 E-value: 2.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMA---GRILIDGVDICSIGLEDLRS----KLSVIPQD---- 601
Cdd:COG0444 19 KAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKELRKirgrEIQMIFQDpmts 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 602 --PVLlsgTIRFNL-DPFDRHTD-------QQIWDALERTFLTKA---ISKFPkklHtdvvenggNFSVGERQLLCIARA 668
Cdd:COG0444 99 lnPVM---TVGDQIaEPLRIHGGlskaearERAIELLERVGLPDPerrLDRYP---H--------ELSGGMRQRVMIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 669 VLRNSKIILIDEATASIDMetdtLIQRTI-------REAFqGCTVLVIAHRVTTVLN-CDHILVMGNGKVVE-------F 733
Cdd:COG0444 165 LALEPKLLIADEPTTALDV----TIQAQIlnllkdlQREL-GLAILFITHDLGVVAEiADRVAVMYAGRIVEegpveelF 239
|
...
gi 767990724 734 DRP 736
Cdd:COG0444 240 ENP 242
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
518-732 |
4.26e-27 |
|
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: 110.36 E-value: 4.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 518 IIFQDYHMKYRDNTP--TVLHGINLTIRGHEVVGIVGRTGSGKSSLgMALFRLVE-PMAGRILIDGVDICSI---GLEDL 591
Cdd:cd03258 2 IELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTL-IRCINGLErPTSGSVLVDGTDLTLLsgkELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 592 RSKLSVIPQDPVLLSG-TIRFNLD-PF------DRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLL 663
Cdd:cd03258 81 RRRIGMIFQHFNLLSSrTVFENVAlPLeiagvpKAEIEERVLELLELVGLEDKADAYPAQL-----------SGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767990724 664 CIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVE 732
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVE 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
533-741 |
4.63e-27 |
|
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: 110.28 E-value: 4.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICS---IGLEDLRSKLSVIPQDPVLLSG-T 608
Cdd:cd03261 14 TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseAELYRLRRRMGMLFQSGALFDSlT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 609 IRFNLD-PFDRHT-------DQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDE 680
Cdd:cd03261 94 VFENVAfPLREHTrlseeeiREIVLEKLEAVGLRGAEDLYPAEL-----------SGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767990724 681 ATASIDMETDTLIQRTIRE--AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRK 741
Cdd:cd03261 163 PTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-109 |
5.19e-27 |
|
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: 109.94 E-value: 5.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIfEECIKKTLRGKTVVLVTHQLQYLEFCGQIIL 81
Cdd:cd03249 131 TLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLV-QEALDRAMKGRTTIVIAHRLSTIRNADLIAV 209
|
90 100
....*....|....*....|....*...
gi 767990724 82 LENGKICENGTHSELMQKKGKYAQLIQK 109
Cdd:cd03249 210 LQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-106 |
8.65e-27 |
|
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: 109.24 E-value: 8.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIIL 81
Cdd:cd03251 130 TVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDT-ESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVV 208
|
90 100
....*....|....*....|....*
gi 767990724 82 LENGKICENGTHSELMQKKGKYAQL 106
Cdd:cd03251 209 LEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
534-739 |
1.20e-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: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 534 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVE-----PMAGRILIDGVDICSIG--LEDLRSKLSVIPQDPVLLS 606
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDvdVLELRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 607 GTIRFNLDPFDRHT---DQQIWDALERTFLTKAiskfpkKLHTDVVE--NGGNFSVGERQLLCIARAVLRNSKIILIDEA 681
Cdd:cd03260 95 GSIYDNVAYGLRLHgikLKEELDERVEEALRKA------ALWDEVKDrlHALGLSGGQQQRLCLARALANEPEVLLLDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767990724 682 TASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNC-DHILVMGNGKVVEFDRPEVL 739
Cdd:cd03260 169 TSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
527-736 |
1.51e-26 |
|
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: 108.81 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 527 YRDNTpTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG---LEDLRSKLSVIPQDPV 603
Cdd:cd03256 10 YPNGK-KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQIGMIFQQFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 604 L----------LSG------TIRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIAR 667
Cdd:cd03256 89 LierlsvlenvLSGrlgrrsTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQL-----------SGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767990724 668 AVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVL-NCDHILVMGNGKVVeFDRP 736
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAReYADRIVGLKDGRIV-FDGP 228
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
2-85 |
7.65e-26 |
|
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: 106.26 E-value: 7.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRG--KTVVLVTHQLQYLEFCGQI 79
Cdd:cd03290 132 TEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWI 211
|
....*.
gi 767990724 80 ILLENG 85
Cdd:cd03290 212 IAMKDG 217
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
533-729 |
7.99e-26 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 104.96 E-value: 7.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG--LEDLRSKLSVIPQDPVLLSgtir 610
Cdd:cd03229 14 TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFALFP---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 611 fnldpfdrhtdqqiwdalertfltkaiskfpkklHTDVVENGG-NFSVGERQLLCIARAVLRNSKIILIDEATASIDMET 689
Cdd:cd03229 90 ----------------------------------HLTVLENIAlGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPIT 135
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767990724 690 DTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGK 729
Cdd:cd03229 136 RREVRALLKSLQAqlGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
534-740 |
8.87e-26 |
|
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: 105.98 E-value: 8.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 534 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLED-LRSKLSVIPQDPVLLSG-TIRF 611
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 612 NLD-PFDRHTDQQIWDALERTFltkaiSKFPK---KLHTDvvenGGNFSVGERQLLCIARAVLRNSKIILIDEATA---- 683
Cdd:cd03224 95 NLLlGAYARRRAKRKARLERVY-----ELFPRlkeRRKQL----AGTLSGGEQQMLAIARALMSRPKLLLLDEPSEglap 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 684 SIDMETDTLIqRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLR 740
Cdd:cd03224 166 KIVEEIFEAI-RELRD--EGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
535-737 |
9.20e-26 |
|
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: 112.09 E-value: 9.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 535 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVePMAGRILIDGVDICSIG---LEDLRSKLSVIPQDPvllsgtirF 611
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--------F 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 612 N-LDPfdRHT---------------------DQQIWDALERTFLTKA-ISKFPkklHtdvvEnggnFSVGERQLLCIARA 668
Cdd:COG4172 373 GsLSP--RMTvgqiiaeglrvhgpglsaaerRARVAEALEEVGLDPAaRHRYP---H----E----FSGGQRQRIAIARA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 669 VLRNSKIILIDEATASIDMetdtLIQRTIREAFQ------GCTVLVIAH--RVTTVLnCDHILVMGNGKVVE-------F 733
Cdd:COG4172 440 LILEPKLLVLDEPTSALDV----SVQAQILDLLRdlqrehGLAYLFISHdlAVVRAL-AHRVMVMKDGKVVEqgpteqvF 514
|
....
gi 767990724 734 DRPE 737
Cdd:COG4172 515 DAPQ 518
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
533-731 |
1.31e-25 |
|
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: 105.31 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcsiglEDLRSKLSVIPQ------------ 600
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-----EKERKRIGYVPQrrsidrdfpisv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 601 -DPVLLSGTIRFNLDPFDRHTDQQIWD-ALERTfltkAISKFPKKlhtdvveNGGNFSVGERQLLCIARAVLRNSKIILI 678
Cdd:cd03235 88 rDVVLMGLYGHKGLFRRLSKADKAKVDeALERV----GLSELADR-------QIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767990724 679 DEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMgNGKVV 731
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVV 210
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-101 |
2.63e-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: 101.92 E-value: 2.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIfEECIKKTLRGKTVVLVTHQLQYLEFCGQIIL 81
Cdd:cd03254 131 TVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLI-QEALEKLMKGRTSIIIAHRLSTIKNADKILV 209
|
90 100
....*....|....*....|
gi 767990724 82 LENGKICENGTHSELMQKKG 101
Cdd:cd03254 210 LDDGKIIEEGTHDELLAKKG 229
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
533-731 |
4.41e-24 |
|
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: 99.43 E-value: 4.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLED-LRSKLSVIPQdpvllsgtirf 611
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ----------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 612 nldpfdrhtdqqiwdalertfltkaiskfpkklhtdvvenggnFSVGERQLLCIARAVLRNSKIILIDEATASI-DMETD 690
Cdd:cd03216 83 -------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALtPAEVE 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767990724 691 TLIQ--RTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV 731
Cdd:cd03216 120 RLFKviRRLRA--QGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
2-108 |
4.96e-24 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 107.91 E-value: 4.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIIL 81
Cdd:TIGR01846 585 TEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYE-SEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIV 663
|
90 100
....*....|....*....|....*..
gi 767990724 82 LENGKICENGTHSELMQKKGKYAQLIQ 108
Cdd:TIGR01846 664 LEKGQIAESGRHEELLALQGLYARLWQ 690
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
529-730 |
6.08e-24 |
|
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: 100.64 E-value: 6.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 529 DNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLgMALFRLVE-PMAGRILIDGVDICSIGLEDL----RSKLSVIPQDPV 603
Cdd:cd03255 14 GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTL-LNILGGLDrPTSGEVRVDGTDISKLSEKELaafrRRHIGFVFQSFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 604 LLSG-TIRFNLD-------PFDRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKI 675
Cdd:cd03255 93 LLPDlTALENVElplllagVPKKERRERAEELLERVGLGDRLNHYPSEL-----------SGGQQQRVAIARALANDPKI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767990724 676 ILIDEATASIDMETDTLIQRTIRE--AFQGCTVLVIAHRVTTVLNCDHILVMGNGKV 730
Cdd:cd03255 162 ILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
518-730 |
6.20e-24 |
|
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: 100.56 E-value: 6.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 518 IIFQDYHMKYRDNTPTvLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSI---GLEDLRSK 594
Cdd:cd03292 1 IEFINVTKTYPNGTAA-LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 595 LSVIPQDPVLLSgtirfNLDPFD-------------RHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQ 661
Cdd:cd03292 80 IGVVFQDFRLLP-----DRNVYEnvafalevtgvppREIRKRVPAALELVGLSHKHRALPAEL-----------SGGEQQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767990724 662 LLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ-GCTVLVIAHRVTTVLNCDH-ILVMGNGKV 730
Cdd:cd03292 144 RVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKaGTTVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
518-732 |
8.83e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 100.13 E-value: 8.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 518 IIFQDYHMKYRDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSI---GLEDLRSK 594
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 595 LSVIPQDPVLLsgtirFNLDPFD-------------RHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQ 661
Cdd:COG2884 81 IGVVFQDFRLL-----PDRTVYEnvalplrvtgksrKEIRRRVREVLDLVGLSDKAKALPHEL-----------SGGEQQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767990724 662 LLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ-GCTVLVIAHRVTTVLNCDH-ILVMGNGKVVE 732
Cdd:COG2884 145 RVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRrGTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-109 |
8.90e-24 |
|
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: 100.64 E-value: 8.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIIL 81
Cdd:cd03252 130 TIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE-SEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIV 208
|
90 100
....*....|....*....|....*...
gi 767990724 82 LENGKICENGTHSELMQKKGKYAQLIQK 109
Cdd:cd03252 209 MEKGRIVEQGSHDELLAENGLYAYLYQL 236
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
11-86 |
2.16e-23 |
|
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: 97.45 E-value: 2.16e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFeECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGK 86
Cdd:cd03228 97 LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALIL-EALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
518-742 |
1.78e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 97.75 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 518 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSV 597
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 598 IPQDP------VLLSGTIRFNLD--PFDRH-TDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARA 668
Cdd:PRK13632 88 IFQNPdnqfigATVEDDIAFGLEnkKVPPKkMKDIIDDLAKKVGMEDYLDKEPQNL-----------SGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767990724 669 VLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRP-EVLRKK 742
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPkEILNNK 233
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-109 |
2.00e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 102.21 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 4 IGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEeCIKKTLRGKTVVLVTHQLQYLEFCGQIILLE 83
Cdd:PRK11160 469 LGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILE-LLAEHAQNKTVLMITHRLTGLEQFDRICVMD 547
|
90 100
....*....|....*....|....*.
gi 767990724 84 NGKICENGTHSELMQKKGKYAQLIQK 109
Cdd:PRK11160 548 NGQIIEQGTHQELLAQQGRYYQLKQR 573
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
2-107 |
2.90e-22 |
|
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: 97.62 E-value: 2.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIIL 81
Cdd:cd03291 151 TVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILI 230
|
90 100
....*....|....*....|....*.
gi 767990724 82 LENGKICENGTHSELMQKKGKYAQLI 107
Cdd:cd03291 231 LHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
2-106 |
3.45e-22 |
|
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: 101.32 E-value: 3.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIIL 81
Cdd:TIGR02204 468 TYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAE-SEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVV 546
|
90 100
....*....|....*....|....*
gi 767990724 82 LENGKICENGTHSELMQKKGKYAQL 106
Cdd:TIGR02204 547 MDQGRIVAQGTHAELIAKGGLYARL 571
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
518-732 |
3.61e-22 |
|
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: 95.62 E-value: 3.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 518 IIFQDYHMKYRDNTP--TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGledlrSKL 595
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 596 SVIPQDPVLL-----SGTIRFNLD---PFDRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIAR 667
Cdd:cd03293 76 GYVFQQDALLpwltvLDNVALGLElqgVPKAEARERAEELLELVGLSGFENAYPHQL-----------SGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 668 AVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVT-TVLNCDHILVMGN--GKVVE 732
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-108 |
4.69e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 101.07 E-value: 4.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFeECIKKTLRGKTVVLVTHQLQYLEFCGQIIL 81
Cdd:PRK11174 477 TPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM-QALNAASRRQTTLMVTHQLEDLAQWDQIWV 555
|
90 100
....*....|....*....|....*..
gi 767990724 82 LENGKICENGTHSELMQKKGKYAQLIQ 108
Cdd:PRK11174 556 MQDGQIVQQGDYAELSQAGGLFATLLA 582
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-106 |
6.51e-22 |
|
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: 100.66 E-value: 6.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIfEECIKKTLRGKTVVLVTHQLQYLEFCGQIIL 81
Cdd:COG5265 486 TRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAI-QAALREVARGRTTLVIAHRLSTIVDADEILV 564
|
90 100
....*....|....*....|....*
gi 767990724 82 LENGKICENGTHSELMQKKGKYAQL 106
Cdd:COG5265 565 LEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
533-732 |
6.53e-22 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 97.84 E-value: 6.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSI---GLEDLRSKLSVIPQDPVLLS--- 606
Cdd:COG1135 19 TALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALserELRAARRKIGMIFQHFNLLSsrt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 607 --GTIRFNL-----DPFDRhtDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILID 679
Cdd:COG1135 99 vaENVALPLeiagvPKAEI--RKRVAELLELVGLSDKADAYPSQL-----------SGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767990724 680 EATASIDMETdT-----LIQRtIREAFqGCTVLVIAH------RVttvlnCDHILVMGNGKVVE 732
Cdd:COG1135 166 EATSALDPET-TrsildLLKD-INREL-GLTIVLITHemdvvrRI-----CDRVAVLENGRIVE 221
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
538-727 |
8.87e-22 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 101.64 E-value: 8.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 538 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILI-DGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNL--- 613
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkys 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 614 ----------------DPFDRHT---------------------------------------DQQIWDALERTFLTKAIS 638
Cdd:PTZ00265 484 lyslkdlealsnyyneDGNDSQEnknkrnscrakcagdlndmsnttdsneliemrknyqtikDSEVVDVSKKVLIHDFVS 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 639 KFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIR--EAFQGCTVLVIAHRVTTV 716
Cdd:PTZ00265 564 ALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTI 643
|
250
....*....|.
gi 767990724 717 LNCDHILVMGN 727
Cdd:PTZ00265 644 RYANTIFVLSN 654
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-91 |
1.48e-21 |
|
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: 93.81 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLRGKTVVLVTHQLQYLEFCGQIIL 81
Cdd:cd03245 132 LQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKER-LRQLLGDKTLIIITHRPSLLDLVDRIIV 210
|
90
....*....|
gi 767990724 82 LENGKICENG 91
Cdd:cd03245 211 MDSGRIVADG 220
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-107 |
1.64e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 99.80 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcikKTLRGKTVVLVTHQLQYLEFCGQIIL 81
Cdd:TIGR00958 609 TEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES---RSRASRTVLLIAHRLSTVERADQILV 685
|
90 100
....*....|....*....|....*.
gi 767990724 82 LENGKICENGTHSELMQKKGKYAQLI 107
Cdd:TIGR00958 686 LKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
533-741 |
1.66e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.55 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--VDICSIgLEDLRSKLSVIPQDPVL---LS- 606
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSP-RDAQAAGIAIIHQELNLvpnLSv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 607 -------------GTIRfnldpfdrhtdqqiWDALERTFlTKAISKFpkKLHTDVVENGGNFSVGERQLLCIARAVLRNS 673
Cdd:COG1129 97 aeniflgreprrgGLID--------------WRAMRRRA-RELLARL--GLDIDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 674 KIILIDEATASI-DMETDTLIQ--RTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV------EFDRPEVLRK 741
Cdd:COG1129 160 RVLILDEPTASLtEREVERLFRiiRRLKA--QGVAIIYISHRLDEVFEiADRVTVLRDGRLVgtgpvaELTEDELVRL 235
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
531-730 |
2.76e-21 |
|
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: 91.72 E-value: 2.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 531 TPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLED-LRSKLSVIPQDP----VLL 605
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPEDRkregLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 606 SGTIRFNLdpfdrhtdqqiwdalertFLTKAISkfpkklhtdvvenGGNfsvgeRQLLCIARAVLRNSKIILIDEATASI 685
Cdd:cd03215 92 DLSVAENI------------------ALSSLLS-------------GGN-----QQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767990724 686 DMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKV 730
Cdd:cd03215 136 DVGAKAEIYRLIRElADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
518-731 |
4.25e-21 |
|
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: 92.43 E-value: 4.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 518 IIFQDYHMKYRDNTPTV--LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEdLRSKL 595
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE-ARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 596 SVIPQDPVLLSG-TIRFNLDPFDR-HtdqqiwdALERTFLTKAISKFPKKLHTDVVEN--GGNFSVGERQLLCIARAVLR 671
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYFAGlY-------GLKGDELTARLEELADRLGMEELLDrrVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767990724 672 NSKIILIDEATASID-METDTLIQ--RTIREAfqGCTVLVIAHRVTTVLN-CDHILVMGNGKVV 731
Cdd:cd03266 154 DPPVLLLDEPTTGLDvMATRALREfiRQLRAL--GKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
2-117 |
6.06e-21 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 97.48 E-value: 6.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLRGKTVVLVTHQLQYLEFCGQIIL 81
Cdd:PRK10789 443 TEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHN-LRQWGEGRTVIISAHRLSALTEASEILV 521
|
90 100 110
....*....|....*....|....*....|....*.
gi 767990724 82 LENGKICENGTHSELMQKKGKYAQLIQKMHKEATSD 117
Cdd:PRK10789 522 MQHGHIAQRGNHDQLAQQSGWYRDMYRYQQLEAALD 557
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
533-734 |
6.60e-21 |
|
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: 6.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEdlRSKLSVIPQDPVL---LS--G 607
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALfphLTvaE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 608 TIRFNLDPF---DRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEATAS 684
Cdd:cd03259 92 NIAFGLKLRgvpKAEIRARVRELLELVGLEGLLNRYPHEL-----------SGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767990724 685 IDMETDTLIQRTIREAF--QGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFD 734
Cdd:cd03259 161 LDAKLREELREELKELQreLGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
518-730 |
7.01e-21 |
|
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: 91.82 E-value: 7.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 518 IIFQDYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIC--SIGLEDLRSKL 595
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 596 SVIPQDpvllsgtirFNLDP----FDRHTDQQIW--------------DALERTFLTKAISKFPKKLhtdvvenggnfSV 657
Cdd:cd03262 79 GMVFQQ---------FNLFPhltvLENITLAPIKvkgmskaeaeeralELLEKVGLADKADAYPAQL-----------SG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767990724 658 GERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKV 730
Cdd:cd03262 139 GQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
527-737 |
7.50e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 93.13 E-value: 7.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 527 YRDNTPTvLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG-LEDLRSKLSVIPQDPV-- 603
Cdd:PRK13644 11 YPDGTPA-LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVFQNPEtq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 604 ---------LLSGTIRFNLDPFDrhTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSK 674
Cdd:PRK13644 90 fvgrtveedLAFGPENLCLPPIE--IRKRVDRALAEIGLEKYRHRSPKTL-----------SGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767990724 675 IILIDEATASIDMET-DTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPE 737
Cdd:PRK13644 157 CLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPE 220
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-106 |
8.25e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 97.01 E-value: 8.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVgkhifEECIKKTL----RGKTVVLVTHQLQYLEFCG 77
Cdd:PRK11176 472 TVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES-----ERAIQAALdelqKNRTSLVIAHRLSTIEKAD 546
|
90 100
....*....|....*....|....*....
gi 767990724 78 QIILLENGKICENGTHSELMQKKGKYAQL 106
Cdd:PRK11176 547 EILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
518-749 |
1.03e-20 |
|
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: 91.98 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 518 IIFQDYHMKYRDNTPTVlHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLS- 596
Cdd:cd03295 1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 597 VIPQDPVLLSGTIRFN------LDPFDRHT-DQQIWDALERTFLTKA--ISKFPKKLhtdvvenggnfSVGERQLLCIAR 667
Cdd:cd03295 80 VIQQIGLFPHMTVEENialvpkLLKWPKEKiRERADELLALVGLDPAefADRYPHEL-----------SGGQQQRVGVAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 668 AVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKPG 744
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEILRSPA 228
|
....*
gi 767990724 745 SLFAA 749
Cdd:cd03295 229 NDFVA 233
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
530-728 |
3.94e-20 |
|
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: 89.70 E-value: 3.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 530 NTPTvLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSK----LSVIPQDPVLL 605
Cdd:cd03290 13 GLAT-LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 606 SGTIRFNL---DPFDRHTDQQIWDALErtfLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEAT 682
Cdd:cd03290 92 NATVEENItfgSPFNKQRYKAVTDACS---LQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767990724 683 ASIDME-TDTLIQRTIREAFQG--CTVLVIAHRVTTVLNCDHILVMGNG 728
Cdd:cd03290 169 SALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
185-492 |
4.91e-20 |
|
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: 91.12 E-value: 4.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 185 IIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSsresngtmadlgniadnpQLSFYQLVYGLNALLLICVGVCSSGIFTKV 264
Cdd:cd18559 4 LIKLVLCNHVFSGPSNLWLLLWFDDPVNGPQE------------------HGQVYLSVLGALAILQGITVFQYSMAVSIG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 265 TRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPyILLMGA 344
Cdd:cd18559 66 GIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGP-MAAVGI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 345 IIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLfLSSTRWMA 424
Cdd:cd18559 145 PLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPS-IVYLRALA 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 425 LRLEIMTNLVTLAVALFVAFGISSTPySFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYM 492
Cdd:cd18559 224 VRLWCVGPCIVLFASFFAYVSRHSLA-GLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
533-743 |
6.92e-20 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 89.42 E-value: 6.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLgmalFRLV----EPMAGRILIDGVDICSIGlEDLRSKLSV-----IPQ--- 600
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTL----FNLIsgflRPTSGSVLFDGEDITGLP-PHEIARLGIgrtfqIPRlfp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 601 -----DPVLLSGTIR----FNLDPFDRH---TDQQIWDALERTFLTKaiskfpkKLHTDVvengGNFSVGERQLLCIARA 668
Cdd:cd03219 89 eltvlENVMVAAQARtgsgLLLARARREereARERAEELLERVGLAD-------LADRPA----GELSYGQQRRLEIARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767990724 669 VLRNSKIILIDEATASI-DMETDTLIQ--RTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKP 743
Cdd:cd03219 158 LATDPKLLLLDEPAAGLnPEETEELAEliRELRE--RGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNNP 234
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
530-738 |
9.09e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.16 E-value: 9.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 530 NTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--VDICSIGlEDLRSKLSVIPQD----PV 603
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPR-DAIRAGIAYVPEDrkgeGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 604 LLSGTIRFN-----LDPFDRHtdQQIWDALERTFLTKAISKF---PKKLHTDVvengGNFSVGERQLLCIARAVLRNSKI 675
Cdd:COG1129 342 VLDLSIRENitlasLDRLSRG--GLLDRRRERALAEEYIKRLrikTPSPEQPV----GNLSGGNQQKVVLAKWLATDPKV 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767990724 676 ILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVL-NCDHILVMGNGKVV-EFDRPEV 738
Cdd:COG1129 416 LILDEPTRGIDVGAKAEIYRLIRElAAEGKAVIVISSELPELLgLSDRILVMREGRIVgELDREEA 481
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
533-725 |
2.15e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 92.56 E-value: 2.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLgmalFR------------LVEPMAGRILidgvdicsigledlrsklsVIPQ 600
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTL----LRaiaglwpygsgrIARPAGARVL-------------------FLPQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 601 DPVLLSGTIRFNL---DPFDRHTDQQIWDALERTFLTKAISKFpkklhtDVVENGGN-FSVGERQLLCIARAVLRNSKII 676
Cdd:COG4178 434 RPYLPLGTLREALlypATAEAFSDAELREALEAVGLGHLAERL------DEEADWDQvLSLGEQQRLAFARLLLHKPDWL 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767990724 677 LIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVM 725
Cdd:COG4178 508 FLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLEL 556
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
518-732 |
2.19e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 90.25 E-value: 2.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 518 IIFQDYHMKYRDNTPTV--LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRS-- 593
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 594 -KLSVIPQDPVLLSG-TIRFN------LDPFDR-HTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLC 664
Cdd:PRK11153 82 rQIGMIFQHFNLLSSrTVFDNvalpleLAGTPKaEIKARVTELLELVGLSDKADRYPAQL-----------SGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767990724 665 IARAVLRNSKIILIDEATASIDMET-----DTL--IQRTIreafqGCTVLVIAHRVTTVLN-CDHILVMGNGKVVE 732
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATtrsilELLkdINREL-----GLTIVLITHEMDVVKRiCDRVAVIDAGRLVE 221
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
533-738 |
2.24e-19 |
|
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: 87.87 E-value: 2.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGlEDLRSKL---SV---------IPQ 600
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD-EDARARLrarHVgfvfqsfqlLPT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 601 ----DPVLLSGTIRFNLDPFDRHTdqqiwDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKII 676
Cdd:COG4181 105 ltalENVMLPLELAGRRDARARAR-----ALLERVGLGHRLDHYPAQL-----------SGGEQQRVALARAFATEPAIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767990724 677 LIDEATASIDMETDTLIQRTIRE--AFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEV 738
Cdd:COG4181 169 FADEPTGNLDAATGEQIIDLLFElnRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
528-729 |
2.47e-19 |
|
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: 86.76 E-value: 2.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 528 RDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcSIGLEDLRSKLSVIPQDPVLLSG 607
Cdd:COG4133 12 RGERL-LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-RDAREDYRRRLAYLGHADGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 608 -TIRFNLDpF------DRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDE 680
Cdd:COG4133 90 lTVRENLR-FwaalygLRADREAIDEALEAVGLAGLADLPVRQL-----------SAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767990724 681 ATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRvTTVLNCDHILVMGNGK 729
Cdd:COG4133 158 PFTALDAAGVALLAELIAAhLARGGAVLLTTHQ-PLELAAARVLDLGDFK 206
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
534-749 |
9.66e-19 |
|
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: 86.24 E-value: 9.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 534 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEdlRSKLSVIPQDPVLLSG-TIRFN 612
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHmTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 613 LDPFDRHtdqQIWDALERTFLTKAISKFpkkLHTDVVEN--GGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMET- 689
Cdd:cd03299 92 IAYGLKK---RKVDKKEIERKVLEIAEM---LGIDHLLNrkPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTk 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767990724 690 DTLIQ--RTIREAFqGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKPGSLFAA 749
Cdd:cd03299 166 EKLREelKKIRKEF-GVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKPKNEFVA 227
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
242-754 |
1.08e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 91.58 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 242 VYGLNALLLICVGV-CSSGIFTKVTR---KASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGD---LEQLDQLL-PI 313
Cdd:PLN03232 342 VYAFLIFFGVTFGVlCESQYFQNVGRvgfRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDanaLQQIAEQLhGL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 314 FSEQFLVLSLMVIAV--LLIVSVLSPYILLMgaIIMVICFIYYMMFKKAIGVFKRLENysRSPLFSHILNSLqglSSIHV 391
Cdd:PLN03232 422 WSAPFRIIVSMVLLYqqLGVASLFGSLILFL--LIPLQTLIVRKMRKLTKEGLQWTDK--RVGIINEILASM---DTVKC 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 392 YGKTEDFISqfkRLTDAQNNYLLLFLSSTRWMALRLEIMTNL---VTL-AVALFVAFGISSTP----YSFKVMAV----- 458
Cdd:PLN03232 495 YAWEKSFES---RIQGIRNEELSWFRKAQLLSAFNSFILNSIpvvVTLvSFGVFVLLGGDLTParafTSLSLFAVlrspl 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 459 ----NIVLQLASSFQATARIgletEAQFTAVERILqymkmcVSEAPLHmegtscpqgwPQHGEIIFQDYHMKYRDNT--P 532
Cdd:PLN03232 572 nmlpNLLSQVVNANVSLQRI----EELLLSEERIL------AQNPPLQ----------PGAPAISIKNGYFSWDSKTskP 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TvLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAgrilidgvDICSigleDLRSKLSVIPQDPVLLSGTIRFN 612
Cdd:PLN03232 632 T-LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE--------TSSV----VIRGSVAYVPQVSWIFNATVREN 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 613 LDPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDME-TDT 691
Cdd:PLN03232 699 ILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQ 778
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767990724 692 LIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKpGSLFAALMATA 754
Cdd:PLN03232 779 VFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKS-GSLFKKLMENA 840
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
534-733 |
1.28e-18 |
|
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: 84.94 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 534 VLHGINLTIrGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcSIGLEDLRSKLSVIPQDPVLLSG-TIRFN 612
Cdd:cd03264 15 ALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV-LKQPQKLRRRIGYLPQEFGVYPNfTVREF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 613 LDPF-------DRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEATASI 685
Cdd:cd03264 93 LDYIawlkgipSKEVKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGIAQALVGDPSILIVDEPTAGL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767990724 686 DMETDTLIQRTIREAFQGCTVLVIAHRVTTV-LNCDHILVMGNGKVVEF 733
Cdd:cd03264 162 DPEERIRFRNLLSELGEDRIVILSTHIVEDVeSLCNQVAVLNKGKLVFE 210
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
533-749 |
1.75e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 88.36 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPvllsgTIRFN 612
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDT-----SLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 613 LD----------P----FDRHTD---QQIWDALERTfltkAISKFPKKLHTDVvenggnfSVGERQLLCIARAVLRNSKI 675
Cdd:PRK09536 92 FDvrqvvemgrtPhrsrFDTWTEtdrAAVERAMERT----GVAQFADRPVTSL-------SGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 676 ILIDEATASIDM----ETDTLIQRTIREafqGCTVLVIAHRvttvLN-----CDHILVMGNGKVVEFDRPE-VLrkKPGS 745
Cdd:PRK09536 161 LLLDEPTASLDInhqvRTLELVRRLVDD---GKTAVAAIHD----LDlaaryCDELVLLADGRVRAAGPPAdVL--TADT 231
|
....
gi 767990724 746 LFAA 749
Cdd:PRK09536 232 LRAA 235
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-107 |
2.02e-18 |
|
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: 89.80 E-value: 2.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKktLRGKTVVLVTHQLQYLEFCGQIIL 81
Cdd:TIGR01193 603 TELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN--LQDKTIIFVAHRLSVAKQSDKIIV 680
|
90 100
....*....|....*....|....*.
gi 767990724 82 LENGKICENGTHSELMQKKGKYAQLI 107
Cdd:TIGR01193 681 LDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
534-739 |
4.46e-18 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 84.70 E-value: 4.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 534 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVE--P---MAGRILIDGVDI--CSIGLEDLRSKLSVIPQDPVLLS 606
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVVELRRRVGMVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 607 GTIRFN----------LDPfdRHTDQQIWDALERTFL---TKAiskfpkKLHtdvvENGGNFSVGERQLLCIARAVLRNS 673
Cdd:COG1117 106 KSIYDNvayglrlhgiKSK--SELDEIVEESLRKAALwdeVKD------RLK----KSALGLSGGQQQRLCIARALAVEP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767990724 674 KIILIDEATASID-METDTlIQRTIREAFQGCTVLVIAH------RVTtvlncDHILVMGNGKVVEFDRPEVL 739
Cdd:COG1117 174 EVLLMDEPTSALDpISTAK-IEELILELKKDYTIVIVTHnmqqaaRVS-----DYTAFFYLGELVEFGPTEQI 240
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
533-740 |
4.87e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 84.44 E-value: 4.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVL-----LSG 607
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsfpftVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 608 TIRFNLDPF--DRHTDQQIWD-ALERtfltkaiskfpkklhTDVVENGGNF----SVGERQLLCIARaVL-------RNS 673
Cdd:PRK13548 96 VVAMGRAPHglSRAEDDALVAaALAQ---------------VDLAHLAGRDypqlSGGEQQRVQLAR-VLaqlwepdGPP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767990724 674 KIILIDEATASIDM--ETDTLiqRTIRE--AFQGCTVLVIAHRvttvLN-----CDHILVMGNGKVVEFDRP-EVLR 740
Cdd:PRK13548 160 RWLLLDEPTSALDLahQHHVL--RLARQlaHERGLAVIVVLHD----LNlaaryADRIVLLHQGRLVADGTPaEVLT 230
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
533-737 |
1.12e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 83.52 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSG-TIR- 610
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 611 ---FNLDPFDRH------TDQQIWD-ALERTfltkAISKFPKKLHTDVvenggnfSVGERQLLCIARAVLRNSKIILIDE 680
Cdd:PRK11231 96 lvaYGRSPWLSLwgrlsaEDNARVNqAMEQT----RINHLADRRLTDL-------SGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767990724 681 ATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRvttvLN-----CDHILVMGNGKVVEFDRPE 737
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRElNTQGKTVVTVLHD----LNqasryCDHLVVLANGHVMAQGTPE 223
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
241-740 |
1.62e-17 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 86.39 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 241 LVYGLNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEqFLV 320
Cdd:COG4615 52 LLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVRLPE-LLQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 321 LSLMVIAVLLIVSVLSPYILLMGAIIMVIC-FIYYMMFKKAIGVFKRL-ENYSRspLFSHILNSLQG-----LSSihvyG 393
Cdd:COG4615 131 SVALVLGCLAYLAWLSPPLFLLTLVLLGLGvAGYRLLVRRARRHLRRArEAEDR--LFKHFRALLEGfkelkLNR----R 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 394 KTEDFISQfkRLTDAQNNYLLLFLSSTRWMALrLEIMTN---LVTLAVALFVAFGISSTPYS----------FKVMAVNI 460
Cdd:COG4615 205 RRRAFFDE--DLQPTAERYRDLRIRADTIFAL-ANNWGNllfFALIGLILFLLPALGWADPAvlsgfvlvllFLRGPLSQ 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 461 VLQLASSFqATARIgleteaqftAVERILQyMKMCVSEAPLHMEGTSCPQGWPQHGEIIFQDYHMKYR---DNTPTVLHG 537
Cdd:COG4615 282 LVGALPTL-SRANV---------ALRKIEE-LELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPgedGDEGFTLGP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 538 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLlsgtirFN--LDP 615
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHL------FDrlLGL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 616 FDRHTDQQIWDALERtfLtkaiskfpkKLHTDV-VENGG----NFSVGERQLLCIARAVLRNSKIILIDEATASIDMEtd 690
Cdd:COG4615 425 DGEADPARARELLER--L---------ELDHKVsVEDGRfsttDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPE-- 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767990724 691 tliqrtIREAF----------QGCTVLVIAH--RVTTVlnCDHILVMGNGKVVEFDRPEVLR 740
Cdd:COG4615 492 ------FRRVFytellpelkaRGKTVIAISHddRYFDL--ADRVLKMDYGKLVELTGPAALA 545
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
521-741 |
1.63e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 83.74 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 521 QDYHMKYRDNTpTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--VDICSIGLEDLRSKLSVI 598
Cdd:PRK13636 9 EELNYNYSDGT-HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 599 PQDP--VLLSGTIR-------FNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAV 669
Cdd:PRK13636 88 FQDPdnQLFSASVYqdvsfgaVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCL-----------SFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 670 LRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTV-LNCDHILVMGNGKVV-------EFDRPEVL 739
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVpLYCDNVFVMKEGRVIlqgnpkeVFAEKEML 236
|
..
gi 767990724 740 RK 741
Cdd:PRK13636 237 RK 238
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
11-86 |
1.79e-17 |
|
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: 79.98 E-value: 1.79e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKTL-RGKTVVLVTHQLQYLE-FCGQIILLENGK 86
Cdd:cd00267 81 LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA-SRERLLELLRELAeEGRTVIIVTHDPELAElAADRVIVLKDGK 157
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
533-731 |
2.62e-17 |
|
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: 80.67 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMAL--FRLVEPMAGRILIDGVdicSIGLEDLRSKLSVIPQDPVLlsgtir 610
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGR---PLDKRSFRKIIGYVPQDDIL------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 611 fnldpfdrHTDQQIWDALERTFLTKAISKfpkklhtdvvenggnfsvGERQLLCIARAVLRNSKIILIDEATASIDMETD 690
Cdd:cd03213 94 --------HPTLTVRETLMFAAKLRGLSG------------------GERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767990724 691 TLIQRTIRE-AFQGCTVLVIAHRVTTVL--NCDHILVMGNGKVV 731
Cdd:cd03213 148 LQVMSLLRRlADTGRTIICSIHQPSSEIfeLFDKLLLLSQGRVI 191
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1-88 |
5.16e-17 |
|
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: 80.27 E-value: 5.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 1 MTEIGERGL-NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEecIKKTLR--GKTVVLVTHQL-QYLEFC 76
Cdd:cd03235 122 LSELADRQIgELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYE--LLRELRreGMTILVVTHDLgLVLEYF 199
|
90
....*....|..
gi 767990724 77 GQIILLENGKIC 88
Cdd:cd03235 200 DRVLLLNRTVVA 211
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-135 |
6.51e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 84.63 E-value: 6.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVgkhifEECIKKTL----RGKTVVLVTHQLQYLEFCG 77
Cdd:PRK13657 463 TVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVET-----EAKVKAALdelmKGRTTFIIAHRLSTVRNAD 537
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 78 QIILLENGKICENGTHSELMQKKGKYAQLIQkmhkeaTSDMLQDTAKiAEKPKVESQA 135
Cdd:PRK13657 538 RILVFDNGRVVESGSFDELVARGGRFAALLR------AQGMLQEDER-RKQPAAEGAN 588
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
10-96 |
7.94e-17 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 82.50 E-value: 7.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVgkhifeeciKKTLR----------GKTVVLVTH-QLQYLEFCGQ 78
Cdd:COG1118 133 QLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKV---------RKELRrwlrrlhdelGGTTVFVTHdQEEALELADR 203
|
90
....*....|....*...
gi 767990724 79 IILLENGKICENGTHSEL 96
Cdd:COG1118 204 VVVMNQGRIEQVGTPDEV 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-82 |
8.95e-17 |
|
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: 84.26 E-value: 8.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLRGKTVVLVTHQLQYLEFCGQIIL 81
Cdd:TIGR02857 450 TPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEA-LRALAQGRTVLLVTHRLALAALADRIVV 528
|
.
gi 767990724 82 L 82
Cdd:TIGR02857 529 L 529
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-87 |
9.80e-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: 79.82 E-value: 9.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIIL 81
Cdd:cd03248 142 TEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE-SEQQVQQALYDWPERRTVLVIAHRLSTVERADQILV 220
|
....*.
gi 767990724 82 LENGKI 87
Cdd:cd03248 221 LDGGRI 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-99 |
1.03e-16 |
|
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: 84.03 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECI---KKtlRGKTVVLVTHQLQYLEFCGQ 78
Cdd:COG4618 459 TRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD-EGEAALAAAIralKA--RGATVVVITHRPSLLAAVDK 535
|
90 100
....*....|....*....|.
gi 767990724 79 IILLENGKICENGTHSELMQK 99
Cdd:COG4618 536 LLVLRDGRVQAFGPRDEVLAR 556
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
533-752 |
1.03e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.92 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLR-SKLSVIPQDP----VLLSG 607
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRrLGVAYIPEDRlgrgLVPDM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 608 TIRFNLDpFDRHTDQQI-------WDALeRTFLTKAISKF---PKKLHTDVvengGNFSVGERQLLCIARAVLRNSKIIL 677
Cdd:COG3845 352 SVAENLI-LGRYRRPPFsrggfldRKAI-RAFAEELIEEFdvrTPGPDTPA----RSLSGGNQQKVILARELSRDPKLLI 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 678 IDEATASIDMETDTLIQRTIREAF-QGCTVLVIAHRVTTVLN-CDHILVMGNGKVV-EFDRPEVLRKKPGslfaALMA 752
Cdd:COG3845 426 AAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEGRIVgEVPAAEATREEIG----LLMA 499
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
523-737 |
1.61e-16 |
|
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: 79.51 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 523 YHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLeDLRSKLSVI--PQ 600
Cdd:cd03218 4 ENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIGylPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 601 DPVLLSG-TIRFNLDPfdrhtdqqiwdALERTFLTKAISKfpKKL-------HTDVVEN--GGNFSVGERQLLCIARAVL 670
Cdd:cd03218 83 EASIFRKlTVEENILA-----------VLEIRGLSKKERE--EKLeelleefHITHLRKskASSLSGGERRRVEIARALA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767990724 671 RNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPE 737
Cdd:cd03218 150 TNPKFLLLDEPFAGVDPIAVQDIQKIIKIlKDRGIGVLITDHNVRETLSiTDRAYIIYEGKVLAEGTPE 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-102 |
1.66e-16 |
|
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: 79.52 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 1 MTEIGERGL-NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIKKtLR--GKTVVLVTHQLQYLE-FC 76
Cdd:COG4555 122 LEEFLDRRVgELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV-MARRLLREILRA-LKkeGKTVLFSSHIMQEVEaLC 199
|
90 100
....*....|....*....|....*.
gi 767990724 77 GQIILLENGKICENGTHSELMQKKGK 102
Cdd:COG4555 200 DRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1-87 |
2.70e-16 |
|
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: 77.48 E-value: 2.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 1 MTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVD----AHVGKHIFEECIKktlRGKTVVLVTHQL-QYLE 74
Cdd:cd03214 87 LAHLADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDiahqIELLELLRRLARE---RGKTVVMVLHDLnLAAR 163
|
90
....*....|...
gi 767990724 75 FCGQIILLENGKI 87
Cdd:cd03214 164 YADRVILLKDGRI 176
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-99 |
5.29e-16 |
|
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: 81.63 E-value: 5.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIKKT-LRGKTVVLVTHQLQYLEFCGQII 80
Cdd:TIGR01842 446 TVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDE-EGEQALANAIKALkARGITVVVITHRPSLLGCVDKIL 524
|
90
....*....|....*....
gi 767990724 81 LLENGKICENGTHSELMQK 99
Cdd:TIGR01842 525 VLQDGRIARFGERDEVLAK 543
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-98 |
5.47e-16 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 78.21 E-value: 5.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 4 IGErglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKtLR--GKTVVLVTHQLQYL-EFCGQII 80
Cdd:COG1121 137 IGE----LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAA-TEEALYELLRE-LRreGKTILVVTHDLGAVrEYFDRVL 210
|
90
....*....|....*...
gi 767990724 81 LLENGKICEnGTHSELMQ 98
Cdd:COG1121 211 LLNRGLVAH-GPPEEVLT 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
10-99 |
5.87e-16 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 77.80 E-value: 5.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIKK-TLRGKTVVLVTHQLQYLE-FCGQIILLENGKI 87
Cdd:COG1131 131 TLSGGMKQRLGLALALLHDPELLILDEPTSGLDP-EARRELWELLRElAAEGKTVLLSTHYLEEAErLCDRVAIIDKGRI 209
|
90
....*....|..
gi 767990724 88 CENGTHSELMQK 99
Cdd:COG1131 210 VADGTPDELKAR 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
8-91 |
6.29e-16 |
|
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: 76.20 E-value: 6.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 8 GLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFeECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKI 87
Cdd:cd03247 96 GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLL-SLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKI 174
|
....
gi 767990724 88 CENG 91
Cdd:cd03247 175 IMQG 178
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
535-743 |
6.61e-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: 78.45 E-value: 6.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 535 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRS----KLSVIPQDPVLLSG-TI 609
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLPHrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 610 RFN---------LDPFDRHtdQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDE 680
Cdd:cd03294 120 LENvafglevqgVPRAERE--ERAAEALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 681 ATASIdmetDTLIQRTIREAF------QGCTVLVIAHRVTTVLNC-DHILVMGNGKVVEFDRPEVLRKKP 743
Cdd:cd03294 187 AFSAL----DPLIRREMQDELlrlqaeLQKTIVFITHDLDEALRLgDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
534-732 |
7.37e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 78.03 E-value: 7.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 534 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVE-----PMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSgt 608
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIP-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 609 irfNLDPFD---------------RHTDQQIWDALERTFLTKAISkfpKKLHTDvvenGGNFSVGERQLLCIARAVLRNS 673
Cdd:PRK14247 96 ---NLSIFEnvalglklnrlvkskKELQERVRWALEKAQLWDEVK---DRLDAP----AGKLSGGQQQRLCIARALAFQP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767990724 674 KIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAH------RVTtvlncDHILVMGNGKVVE 732
Cdd:PRK14247 166 EVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVE 225
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
527-731 |
8.60e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 78.55 E-value: 8.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 527 YRDNTP---TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIC--SIGLEDLRSKLSVIPQD 601
Cdd:PRK13637 12 YMEGTPfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 602 P--VLLSGT----IRF---NLDPFDRHTDQQIWDALERTFLT----KAISKFpkklhtdvvenggNFSVGERQLLCIARA 668
Cdd:PRK13637 92 PeyQLFEETiekdIAFgpiNLGLSEEEIENRVKRAMNIVGLDyedyKDKSPF-------------ELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767990724 669 VLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVV 731
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCE 224
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
293-757 |
9.03e-16 |
|
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: 81.92 E-value: 9.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 293 IGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGA--IIMVICFIYYMMFKKAIGVFKRLENY 370
Cdd:TIGR00957 414 VGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAvmVLMVPLNAVMAMKTKTYQVAHMKSKD 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 371 SRSPLFSHILNslqGLSSIHVYGKTEDFISQFKRLTDAQNNYL--LLFLSST---RWMALrlEIMTNLVTLAVALFV--- 442
Cdd:TIGR00957 494 NRIKLMNEILN---GIKVLKLYAWELAFLDKVEGIRQEELKVLkkSAYLHAVgtfTWVCT--PFLVALITFAVYVTVden 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 443 -------AFgISSTPYSFKVMAVNIVLQLASSFqATARIGLETEAQFTAVERIlqymkmcvseAPLHMEGTSCPQGwpQH 515
Cdd:TIGR00957 569 nildaekAF-VSLALFNILRFPLNILPMVISSI-VQASVSLKRLRIFLSHEEL----------EPDSIERRTIKPG--EG 634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 516 GEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGvdicsigledlrsKL 595
Cdd:TIGR00957 635 NSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SV 701
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 596 SVIPQDPVLLSGTIRFNL---DPFDRHTDQQIwdaLERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRN 672
Cdd:TIGR00957 702 AYVPQQAWIQNDSLRENIlfgKALNEKYYQQV---LEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSN 778
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 673 SKIILIDEATASIDMETDTLIQRTI---REAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGSlFAA 749
Cdd:TIGR00957 779 ADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGA-FAE 857
|
....*...
gi 767990724 750 LMATATSS 757
Cdd:TIGR00957 858 FLRTYAPD 865
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
9-87 |
1.08e-15 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 75.51 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 9 LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIKK-TLRGKTVVLVTHQLQYLE-FCGQIILLENGK 86
Cdd:cd03230 94 LKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP-ESRREFWELLRElKKEGKTILLSSHILEEAErLCDRVAILNNGR 172
|
.
gi 767990724 87 I 87
Cdd:cd03230 173 I 173
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
539-745 |
1.17e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 79.69 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 539 NLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRS----KLSVIPQDPVLLSGTIRFNLD 614
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 615 PFD--------RHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEATASID 686
Cdd:PRK10070 128 AFGmelaginaEERREKALDALRQVGLENYAHSYPDEL-----------SGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767990724 687 METDTLIQRTI--REAFQGCTVLVIAHRVTTVLNC-DHILVMGNGKVVEFDRPEVLRKKPGS 745
Cdd:PRK10070 197 PLIRTEMQDELvkLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNNPAN 258
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
533-731 |
1.41e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.21 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDI--------CSIGLEDLRSKLSVIPQDPVL 604
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnkldhklaAQLGIGIIYQELSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 605 LSGTIrfnldpfDRHTDQQIW--DALERTFLTKAISKFPKK--LHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDE 680
Cdd:PRK09700 99 ENLYI-------GRHLTKKVCgvNIIDWREMRVRAAMMLLRvgLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767990724 681 ATASI-DMETDTL--IQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV 731
Cdd:PRK09700 172 PTSSLtNKEVDYLflIMNQLRK--EGTAIVYISHKLAEIRRiCDRYTVMKDGSSV 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
11-87 |
2.44e-15 |
|
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: 75.63 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLR--GKTVVLVTH-QLQYLEFCGQIILLENGKI 87
Cdd:cd03259 131 LSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREE-LKELQRelGITTIYVTHdQEEALALADRIAVMNEGRI 209
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
521-737 |
2.46e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 76.98 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 521 QDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQ 600
Cdd:PRK13635 9 EHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 601 DP--VLLSGTIR----FNLD----PFDRHTdQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVL 670
Cdd:PRK13635 89 NPdnQFVGATVQddvaFGLEnigvPREEMV-ERVDQALRQVGMEDFLNREPHRL-----------SGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767990724 671 RNSKIILIDEATASIDMETDTLIQRTIRE--AFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPE 737
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
535-738 |
2.53e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.30 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 535 LHGINLTIRGHEVVGIVGRTGSGKSSLgM-ALFRLVEPMAGRILIDG--VDICS--------IGLedlrsklsvIPQDPV 603
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTL-MkILYGLYQPDSGEILIDGkpVRIRSprdaialgIGM---------VHQHFM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 604 L-------------LSGTIRFNLDpfdrhtdqqiWDALERtfLTKAISK---FPKKLHTDVvengGNFSVGERQLLCIAR 667
Cdd:COG3845 91 LvpnltvaenivlgLEPTKGGRLD----------RKAARA--RIRELSErygLDVDPDAKV----EDLSVGEQQRVEILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767990724 668 AVLRNSKIILIDEATASI-DMETDTLIqRTIRE-AFQGCTVLVIAHR---VTTVlnCDHILVMGNGKVV-EFDRPEV 738
Cdd:COG3845 155 ALYRGARILILDEPTAVLtPQEADELF-EILRRlAAEGKSIIFITHKlreVMAI--ADRVTVLRRGKVVgTVDTAET 228
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
524-735 |
3.24e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 75.52 E-value: 3.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 524 HMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPV 603
Cdd:PRK10247 12 NVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 604 LLSGTIRFNLD-PF----DRHTDQQIWDALER-----TFLTKAISKfpkklhtdvvenggnFSVGERQLLCIARAVLRNS 673
Cdd:PRK10247 92 LFGDTVYDNLIfPWqirnQQPDPAIFLDDLERfalpdTILTKNIAE---------------LSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 674 KIILIDEATASIDMETDT----LIQRTIREafQGCTVLVIAHRVTTVLNCDHILV----MGNGKVVEFDR 735
Cdd:PRK10247 157 KVLLLDEITSALDESNKHnvneIIHRYVRE--QNIAVLWVTHDKDEINHADKVITlqphAGEMQEARYEL 224
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
534-728 |
4.72e-15 |
|
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: 76.43 E-value: 4.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 534 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGvdicsigledlrsKLSVIPQDPVLLSGTIRFNL 613
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 614 ---DPFDRHTDQQIWDALErtfLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETD 690
Cdd:cd03291 119 ifgVSYDEYRYKSVVKACQ---LEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767990724 691 tliqrtiREAFQGC--------TVLVIAHRVTTVLNCDHILVMGNG 728
Cdd:cd03291 196 -------KEIFESCvcklmankTRILVTSKMEHLKKADKILILHEG 234
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
11-87 |
4.78e-15 |
|
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: 73.79 E-value: 4.78e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDaHVGKHIFEECIKKT-LRGKTVVLVTHQLQYLEFCGQIILLENGKI 87
Cdd:cd03246 97 LSGGQRQRLGLARALYGNPRILVLDEPNSHLD-VEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1-86 |
4.78e-15 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 73.76 E-value: 4.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 1 MTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECikKTLR---GKTVVLVTHQLQYLE-FC 76
Cdd:cd03229 91 LTVLENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALL--KSLQaqlGITVVLVTHDLDEAArLA 168
|
90
....*....|
gi 767990724 77 GQIILLENGK 86
Cdd:cd03229 169 DRVVVLRDGK 178
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
510-741 |
1.04e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.82 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 510 QGWPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLE 589
Cdd:PRK10575 2 QEYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 590 DLRSKLSVIPQD-PVLLSGTIRfNLDPFDR---HTDQQIWDALERTFLTKAISKFP-KKLHTDVVENggnFSVGERQLLC 664
Cdd:PRK10575 82 AFARKVAYLPQQlPAAEGMTVR-ELVAIGRypwHGALGRFGAADREKVEEAISLVGlKPLAHRLVDS---LSGGERQRAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 665 IARAVLRNSKIILIDEATASIDM----ETDTLIQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV------EF 733
Cdd:PRK10575 158 IAMLVAQDSRCLLLDEPTSALDIahqvDVLALVHRLSQE--RGLTVIAVLHDINMAARyCDYLVALRGGEMIaqgtpaEL 235
|
....*...
gi 767990724 734 DRPEVLRK 741
Cdd:PRK10575 236 MRGETLEQ 243
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
534-728 |
1.13e-14 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 74.01 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 534 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILID----GVDICSIG---LEDLRSK--------LSVI 598
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASpreILALRRRtigyvsqfLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 599 PQ--------DPVLLSGT-------------IRFNLDpfdrhtdQQIWDALERTFltkaiskfpkklhtdvvenggnfSV 657
Cdd:COG4778 106 PRvsaldvvaEPLLERGVdreearararellARLNLP-------ERLWDLPPATF-----------------------SG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767990724 658 GERQLLCIARAVLRNSKIILIDEATASIDMET-DTLIQRtIREA-FQGCTVLVIAH------RVttvlnCDHILVMGNG 728
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANrAVVVEL-IEEAkARGTAIIGIFHdeevreAV-----ADRVVDVTPF 228
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
540-731 |
1.23e-14 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 73.68 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 540 LTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSigLEDLRSKLSVIPQDPVL-----------LSGT 608
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA--APPADRPVSMLFQENNLfahltveqnvgLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 609 IRFNLDPFDRhtdQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEATASID-- 686
Cdd:cd03298 97 PGLKLTAEDR---QAIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVLLLDEPFAALDpa 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767990724 687 --METDTLIQRTIREafQGCTVLVIAHRVTTVLNC-DHILVMGNGKVV 731
Cdd:cd03298 163 lrAEMLDLVLDLHAE--TKMTVLMVTHQPEDAKRLaQRVVFLDNGRIA 208
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
533-736 |
1.26e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 74.72 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSI---GLEDLRSKLSVIPQDP---VLLS 606
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSisaVNPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 607 GTIRFNLDPFDRH------TDQQ--IWDALERTFLTKAI-SKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIIL 677
Cdd:PRK10419 106 KTVREIIREPLRHllsldkAERLarASEMLRAVDLDDSVlDKRPPQL-----------SGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767990724 678 IDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEfDRP 736
Cdd:PRK10419 175 LDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERfCQRVMVMDNGQIVE-TQP 235
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
518-731 |
1.27e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 74.74 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 518 IIFQDYHMKYRDNT----PTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG-LEDLR 592
Cdd:PRK13633 5 IKCKNVSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 593 SKLSVIPQDP------VLLSGTIRF---NLDPFDRHTDQQIWDALERTFLTKaISKFPKKLhtdvvenggnFSVGERQLL 663
Cdd:PRK13633 85 NKAGMVFQNPdnqivaTIVEEDVAFgpeNLGIPPEEIRERVDESLKKVGMYE-YRRHAPHL----------LSGGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 664 CIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLNCDHILVMGNGKVV 731
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVV 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
11-87 |
1.31e-14 |
|
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: 73.68 E-value: 1.31e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKT--LRGKTVVLVTHQLQYLEFCGQIILLENGKI 87
Cdd:cd03255 141 LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMEL-LRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
530-732 |
1.66e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 74.31 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 530 NTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVE------PMAGRILIDGVDICSIGLEDLRSKLSVIPQDP- 602
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 603 ----VLLSGTIRFNLDPFDRHTDQQIWDALERTFLTKAISKfpkKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILI 678
Cdd:PRK14246 101 pfphLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWK---EVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767990724 679 DEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVE 732
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVE 232
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
226-445 |
2.06e-14 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 74.51 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 226 DLGNIADNPQLSFYQLVYGLNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLE 305
Cdd:cd07346 28 DVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 306 QLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQG 385
Cdd:cd07346 108 AVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSG 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 386 LSSIHVYGKTEDFISQFKRLTDAqnnYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFG 445
Cdd:cd07346 188 IRVVKAFAAEEREIERFREANRD---LRDANLRAARLSALFSPLIGLLTALGTALVLLYG 244
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
524-741 |
2.06e-14 |
|
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: 72.56 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 524 HMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMAL--FRLVEPMAGRILIDGVDICSIGLEDlRSKLSVI--P 599
Cdd:cd03217 5 DLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEE-RARLGIFlaF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 600 QDPVLLSGtIRFNldpfdrhtdqqiwdalerTFLtkaiskfpkklhTDVVEnggNFSVGERQLLCIARAVLRNSKIILID 679
Cdd:cd03217 84 QYPPEIPG-VKNA------------------DFL------------RYVNE---GFSGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767990724 680 EATASIDMETDTLIQRTIRE-AFQGCTVLVIAH--RVTTVLNCDHILVMGNGKVVEFDRPEVLRK 741
Cdd:cd03217 130 EPDSGLDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKELALE 194
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
271-728 |
2.37e-14 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 77.26 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 271 ALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILL-MGAIIMVI 349
Cdd:TIGR01271 156 ALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCgLGFLILLA 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 350 CF---IYYMMFK---KAIGVFKRlenysRSPLFSHILNSLQglsSIHVYGKTE------DFISQFKRLTDAQNNYLLLFL 417
Cdd:TIGR01271 236 LFqacLGQKMMPyrdKRAGKISE-----RLAITSEIIENIQ---SVKAYCWEEamekiiKNIRQDELKLTRKIAYLRYFY 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 418 SSTRWMAlrleimtnlvtlavALFVAFgISSTPYS----------FKVMAVNIVLQLASSFQATARIGL--ETEAQFTAV 485
Cdd:TIGR01271 308 SSAFFFS--------------GFFVVF-LSVVPYAlikgiilrriFTTISYCIVLRMTVTRQFPGAIQTwyDSLGAITKI 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 486 E--------RILQYmKMCVSEAPLHMEGTSCPQGWPQHGEIIFQDYHMKYRDN--------------TPtVLHGINLTIR 543
Cdd:TIGR01271 373 QdflckeeyKTLEY-NLTTTEVEMVNVTASWDEGIGELFEKIKQNNKARKQPNgddglffsnfslyvTP-VLKNISFKLE 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 544 GHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGvdicsigledlrsKLSVIPQDPVLLSGTIRFNLD---PFDRHT 620
Cdd:TIGR01271 451 KGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNIIfglSYDEYR 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 621 DQQIWDALErtfLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDtliqrtiREA 700
Cdd:TIGR01271 518 YTSVIKACQ---LEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE-------KEI 587
|
490 500 510
....*....|....*....|....*....|....*.
gi 767990724 701 FQGC--------TVLVIAHRVTTVLNCDHILVMGNG 728
Cdd:TIGR01271 588 FESClcklmsnkTRILVTSKLEHLKKADKILLLHEG 623
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
532-754 |
2.67e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 77.09 E-value: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 532 PTvLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIdgvdicsigledLRSKLSVIPQDPVLLSGTIRF 611
Cdd:PLN03130 631 PT-LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYVPQVSWIFNATVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 612 NL---DPFDRhtdQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDME 688
Cdd:PLN03130 698 NIlfgSPFDP---ERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAH 774
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767990724 689 T-DTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKpGSLFAALMATA 754
Cdd:PLN03130 775 VgRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNN-GPLFQKLMENA 840
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
11-96 |
2.95e-14 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 74.75 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLR--GKTVVLVTH-QLQYLEFCGQIILLENGKI 87
Cdd:COG3842 136 LSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREE-LRRLQRelGITFIYVTHdQEEALALADRIAVMNDGRI 214
|
....*....
gi 767990724 88 CENGTHSEL 96
Cdd:COG3842 215 EQVGTPEEI 223
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
534-731 |
3.83e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.86 E-value: 3.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 534 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVdicsigledLRSKLS----------VIPQDPV 603
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN---------PCARLTpakahqlgiyLVPQEPL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 604 LLSG-TIRFN-LDPFDRHTDqqiwdALERtfLTKAISKFPKKLHTDVveNGGNFSVGERQLLCIARAVLRNSKIILIDEA 681
Cdd:PRK15439 97 LFPNlSVKENiLFGLPKRQA-----SMQK--MKQLLAALGCQLDLDS--SAGSLEVADRQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767990724 682 TASID-METDTLIQRtIREAF-QGCTVLVIAHRVTTVLN-CDHILVMGNGKVV 731
Cdd:PRK15439 168 TASLTpAETERLFSR-IRELLaQGVGIVFISHKLPEIRQlADRISVMRDGTIA 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
10-87 |
3.87e-14 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 71.77 E-value: 3.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKTLR--GKTVVLVTHQLQYLE-FCGQIILLENGK 86
Cdd:COG4619 130 RLSGGERQRLALIRALLLQPDVLLLDEPTSALDPE-NTRRVEELLREYLAeeGRAVLWVSHDPEQIErVADRVLTLEAGR 208
|
.
gi 767990724 87 I 87
Cdd:COG4619 209 L 209
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-108 |
4.15e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.91 E-value: 4.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVgkhifEECIKKTLRG----KTVVLVTHQLQYLEFCG 77
Cdd:PRK10790 468 TPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGT-----EQAIQQALAAvrehTTLVVIAHRLSTIVEAD 542
|
90 100 110
....*....|....*....|....*....|.
gi 767990724 78 QIILLENGKICENGTHSELMQKKGKYAQLIQ 108
Cdd:PRK10790 543 TILVLHRGQAVEQGTHQQLLAAQGRYWQMYQ 573
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
538-732 |
4.41e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 72.90 E-value: 4.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 538 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICsIGLEDLRS-KLSVIPQDPV-----------LL 605
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDYSYRSqRIRMIFQDPStslnprqrisqIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 606 SGTIRFN--LDPFDRhtDQQIWDALERT-FLTKAISKFPKKLHTdvvenggnfsvGERQLLCIARAVLRNSKIILIDEAT 682
Cdd:PRK15112 111 DFPLRLNtdLEPEQR--EKQIIETLRQVgLLPDHASYYPHMLAP-----------GQKQRLGLARALILRPKVIIADEAL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767990724 683 ASIDMETDTLIQRTIRE--AFQGCT-VLVIAHRVTTVLNCDHILVMGNGKVVE 732
Cdd:PRK15112 178 ASLDMSMRSQLINLMLElqEKQGISyIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
11-97 |
4.43e-14 |
|
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: 72.72 E-value: 4.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIK-KTLRGKTVVLVTHQLQ-YLEFCGQIILLENGKIC 88
Cdd:cd03295 136 LSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRlQQELGKTIVFVTHDIDeAFRLADRIAIMKNGEIV 215
|
....*....
gi 767990724 89 ENGTHSELM 97
Cdd:cd03295 216 QVGTPDEIL 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
10-86 |
5.20e-14 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 71.36 E-value: 5.20e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKTL-RGKTVVLVTHQLQYLEFCgQIILLENGK 86
Cdd:COG4133 131 QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA-GVALLAELIAAHLaRGGAVLLTTHQPLELAAA-RVLDLGDFK 206
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
10-96 |
5.90e-14 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 71.84 E-value: 5.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFE--ECIKKTLrGKTVVLVTHQLQYL-EFCGQIILLENGK 86
Cdd:cd03258 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILAllRDINREL-GLTIVLITHEMEVVkRICDRVAVMEKGE 218
|
90
....*....|
gi 767990724 87 ICENGTHSEL 96
Cdd:cd03258 219 VVEEGTVEEV 228
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
533-745 |
5.94e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 72.05 E-value: 5.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcsiglEDLRSKLSVIPQDpvllSGTI--R 610
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV-----NDPKVDERLIRQE----AGMVfqQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 611 FNLDP---------FD----RHTDQQIWDALERTFLTKA-----ISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRN 672
Cdd:PRK09493 86 FYLFPhltalenvmFGplrvRGASKEEAEKQARELLAKVglaerAHHYPSEL-----------SGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 673 SKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAH------RVTTVLncdhiLVMGNGKVVEFDRPEVLRKKPGS 745
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDlAEEGMTMVIVTHeigfaeKVASRL-----IFIDKGRIAEDGDPQVLIKNPPS 229
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
524-740 |
6.05e-14 |
|
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: 71.63 E-value: 6.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 524 HMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEdLRSKLSVIPQDPV 603
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIGIVFQDLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 604 L---LSGtiRFNLDPFDR-------HTDQQIWDALERTFLTKAISKFPKklhtdvvenggNFSVGERQLLCIARAVLRNS 673
Cdd:cd03265 84 VddeLTG--WENLYIHARlygvpgaERRERIDELLDFVGLLEAADRLVK-----------TYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 674 KIILIDEATASIDMETDTLIQRTIRE--AFQGCTVLVIAHRVTTV-LNCDHILVMGNGKVVEFDRPEVLR 740
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
11-98 |
8.17e-14 |
|
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: 71.76 E-value: 8.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECI---KKTLrGKTVVLVTHQLQ-YLEFCGQIILLENGK 86
Cdd:cd03261 137 LSGGMKKRVALARALALDPELLLYDEPTAGLDP-IASGVIDDLIrslKKEL-GLTSIMVTHDLDtAFAIADRIAVLYDGK 214
|
90
....*....|..
gi 767990724 87 ICENGTHSELMQ 98
Cdd:cd03261 215 IVAEGTPEELRA 226
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-92 |
9.72e-14 |
|
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: 70.99 E-value: 9.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDahvgkHIFEECIKKTLR----GKTVVLVTHQLQYLEFCG 77
Cdd:cd03244 131 TVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVD-----PETDALIQKTIReafkDCTVLTIAHRLDTIIDSD 205
|
90
....*....|....*
gi 767990724 78 QIILLENGKICENGT 92
Cdd:cd03244 206 RILVLDKGRVVEFDS 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
518-746 |
1.03e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 72.09 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 518 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSV 597
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 598 IPQDP--VLLSGTIRF--------NLDPFDRhTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIAR 667
Cdd:PRK13648 88 VFQNPdnQFVGSIVKYdvafglenHAVPYDE-MHRRVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 668 AVLRNSKIILIDEATASIDMETDTLIQRTIRE--AFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGS 745
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKvkSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
.
gi 767990724 746 L 746
Cdd:PRK13648 236 L 236
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-70 |
1.10e-13 |
|
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: 74.32 E-value: 1.10e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLRGKTVVLVTHQL 70
Cdd:TIGR02868 463 TVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLED-LLAALSGRTVVLITHHL 530
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
11-87 |
1.20e-13 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 70.84 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFE---ECIKKtlRGKTVVLVTHQLQYLEFCGQIILLENGKI 87
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLEllrELNRE--LGTTIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
526-739 |
1.21e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 72.07 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 526 KYRDNT--PTvLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDP- 602
Cdd:PRK13650 13 KYKEDQekYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPd 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 603 -----VLLSGTIRFNLD----PFDRhTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNS 673
Cdd:PRK13650 92 nqfvgATVEDDVAFGLEnkgiPHEE-MKERVNEALELVGMQDFKEREPARL-----------SGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767990724 674 KIILIDEATASIDMETD-TLIQ--RTIREAFQgCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVL 739
Cdd:PRK13650 160 KIIILDEATSMLDPEGRlELIKtiKGIRDDYQ-MTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
10-86 |
1.27e-13 |
|
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: 70.57 E-value: 1.27e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYL-EFCGQIILLENGK 86
Cdd:cd03225 134 TLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
546-732 |
1.54e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.12 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 546 EVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--VDICSIG-LEDLRSKLSVIPQDPVLlsgtirfNLDPfdRHT-- 620
Cdd:PRK10261 351 ETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTLSPGkLQALRRDIQFIFQDPYA-------SLDP--RQTvg 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 621 ------------------DQQIWDALERTFLTKAIS-KFPKKlhtdvvenggnFSVGERQLLCIARAVLRNSKIILIDEA 681
Cdd:PRK10261 422 dsimeplrvhgllpgkaaAARVAWLLERVGLLPEHAwRYPHE-----------FSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767990724 682 TASIDMETDTLI-------QRTIREAFqgctvLVIAHRVTTVLNCDH-ILVMGNGKVVE 732
Cdd:PRK10261 491 VSALDVSIRGQIinllldlQRDFGIAY-----LFISHDMAVVERISHrVAVMYLGQIVE 544
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-98 |
1.67e-13 |
|
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: 70.99 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHI---FEEcIKKTlRGKTVVLVTHQLQYLEF-CGQIILLENGK 86
Cdd:COG1124 139 LSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEIlnlLKD-LREE-RGLTYLFVSHDLAVVAHlCDRVAVMQNGR 216
|
90
....*....|..
gi 767990724 87 ICENGTHSELMQ 98
Cdd:COG1124 217 IVEELTVADLLA 228
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
522-748 |
1.70e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.58 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 522 DYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--VDICSIGLEDLRSKLSVIP 599
Cdd:PRK13638 6 DLWFRYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 600 QDP------VLLSGTIRFNL-------DPFDRHTDQQIWDALERTFLTKAISkfpkklhtdvvenggNFSVGERQLLCIA 666
Cdd:PRK13638 84 QDPeqqifyTDIDSDIAFSLrnlgvpeAEITRRVDEALTLVDAQHFRHQPIQ---------------CLSHGQKKRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 667 RAVLRNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDrpevlrkKPG 744
Cdd:PRK13638 149 GALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHG-------APG 221
|
....
gi 767990724 745 SLFA 748
Cdd:PRK13638 222 EVFA 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
533-734 |
2.12e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.56 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSlgmaLFRL----VEPMAGRILIdGVDIcSIG-----LEDLRSKLSVIPqdpv 603
Cdd:COG0488 329 TLLDDLSLRIDRGDRIGLIGPNGAGKST----LLKLlageLEPDSGTVKL-GETV-KIGyfdqhQEELDPDKTVLD---- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 604 llsgTIRfnlDPFDRHTDQQIWDALERtFLtkaiskF-PKKLHTDVvengGNFSVGERQLLCIARAVLRNSKIILIDEAT 682
Cdd:COG0488 399 ----ELR---DGAPGGTEQEVRGYLGR-FL------FsGDDAFKPV----GVLSGGEKARLALAKLLLSPPNVLLLDEPT 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 683 ASIDMETDTLIQRTIREaFQGcTVLVIAH------RVttvlnCDHILVMGNGKVVEFD 734
Cdd:COG0488 461 NHLDIETLEALEEALDD-FPG-TVLLVSHdryfldRV-----ATRILEFEDGGVREYP 511
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
534-733 |
2.61e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 74.04 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 534 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDgvdicsigledlRSkLSVIPQDPVLLSGTIRFNL 613
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE------------RS-IAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 614 DPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDtli 693
Cdd:PTZ00243 742 LFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVG--- 818
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767990724 694 QRTIREAFQG---CTVLVIA-HRVTTVLNCDHILVMGNGKvVEF 733
Cdd:PTZ00243 819 ERVVEECFLGalaGKTRVLAtHQVHVVPRADYVVALGDGR-VEF 861
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-97 |
2.61e-13 |
|
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: 70.46 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 1 MTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvgkHIFE--ECIKK--TLRGKTVVLVTHQL-QYLE 74
Cdd:COG1120 127 LEHLADRPVDeLSGGERQRVLIARALAQEPPLLLLDEPTSHLDLA---HQLEvlELLRRlaRERGRTVVMVLHDLnLAAR 203
|
90 100
....*....|....*....|...
gi 767990724 75 FCGQIILLENGKICENGTHSELM 97
Cdd:COG1120 204 YADRLVLLKDGRIVAQGPPEEVL 226
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
533-749 |
2.89e-13 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 72.03 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSL-----GmalfrLVEPMAGRILIDGVDIcsIGLEDLRSKLSVIPQDPVL--- 604
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLlrmiaG-----LEDPTSGEILIGGRDV--TDLPPKDRNIAMVFQSYALyph 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 605 LS--GTIRFNL-----DPFDRhtDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIIL 677
Cdd:COG3839 90 MTvyENIAFPLklrkvPKAEI--DRRVREAAELLGLEDLLDRKPKQL-----------SGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 678 IDEATASID----METDTLIQRTIREafQGCTVLViahrVT-------TVlnCDHILVMGNGKVVEFDRPEVLRKKPGSL 746
Cdd:COG3839 157 LDEPLSNLDaklrVEMRAEIKRLHRR--LGTTTIY----VThdqveamTL--ADRIAVMNDGRIQQVGTPEELYDRPANL 228
|
...
gi 767990724 747 FAA 749
Cdd:COG3839 229 FVA 231
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
533-749 |
3.20e-13 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 69.96 E-value: 3.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcsIGLEDLRSKLSVIPQDPVLLSgtirfN 612
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFP-----H 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 613 LDPFD-------------RHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILID 679
Cdd:cd03300 87 LTVFEniafglrlkklpkAEIKERVAEALDLVQLEGYANRKPSQL-----------SGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767990724 680 EATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKPGSLFAA 749
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEIYEEPANRFVA 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
522-741 |
3.30e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 70.49 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 522 DYHMKYRDNTpTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--VDICSIGLEDLRSKLSVIP 599
Cdd:PRK13639 6 DLKYSYPDGT-EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 600 QDP--VLLSGTIR-------FNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVL 670
Cdd:PRK13639 85 QNPddQLFAPTVEedvafgpLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHL-----------SGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 671 RNSKIILIDEATASIDMETDTLIQRTIREAF-QGCTVLVIAHRVTTV-LNCDHILVMGNGKVVE-------FDRPEVLRK 741
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNkEGITIIISTHDVDLVpVYADKVYVMSDGKIIKegtpkevFSDIETIRK 233
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-87 |
3.72e-13 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 68.82 E-value: 3.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 9 LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH----VGKhIFEECikkTLRGKTVVLVTHQLQYL-EFCGQIILLE 83
Cdd:cd03226 125 LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKnmerVGE-LIREL---AAQGKAVIVITHDYEFLaKVCDRVLLLA 200
|
....
gi 767990724 84 NGKI 87
Cdd:cd03226 201 NGAI 204
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
11-96 |
5.71e-13 |
|
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: 69.29 E-value: 5.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHifeecIKKTLR------GKTVVLVTH-QLQYLEFCGQIILLE 83
Cdd:cd03296 137 LSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKE-----LRRWLRrlhdelHVTTVFVTHdQEEALEVADRVVVMN 211
|
90
....*....|...
gi 767990724 84 NGKICENGTHSEL 96
Cdd:cd03296 212 KGRIEQVGTPDEV 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
533-737 |
6.53e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.15 E-value: 6.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGL-EDLRSKLSVIPQDPvllsgTIRF 611
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEA-----SIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 612 NLDPFDR-HTDQQIWDALERTFLTKAISKFPKKLHTDVVEN--GGNFSVGERQLLCIARAVLRNSKIILIDEATASIDME 688
Cdd:PRK10895 92 RLSVYDNlMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDsmGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767990724 689 TDTLIQRTIREAF-QGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPE 737
Cdd:PRK10895 172 SVIDIKRIIEHLRdSGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPT 222
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
10-100 |
6.65e-13 |
|
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: 68.90 E-value: 6.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKK-TLRGKTVVLVTHQLQYL-EFCGQIILLENGKI 87
Cdd:COG1122 134 ELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPR-GRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRI 212
|
90
....*....|...
gi 767990724 88 CENGTHSELMQKK 100
Cdd:COG1122 213 VADGTPREVFSDY 225
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
11-87 |
7.80e-13 |
|
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: 68.44 E-value: 7.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLR--GKTVVLVTH-QLQYLEFCGQIILLENGKI 87
Cdd:cd03301 131 LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAE-LKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
533-732 |
1.33e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 68.24 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDI------------------------CSIGL 588
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqqkglirqlrqhvgfvfQNFNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 589 EDLRSKLSVIPQDPVLLSGTIRFNLDPFDRhtdqqiwDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARA 668
Cdd:PRK11264 97 FPHRTVLENIIEGPVIVKGEPKEEATARAR-------ELLAKVGLAGKETSYPRRL-----------SGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767990724 669 VLRNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVE 732
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVE 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
11-98 |
1.34e-12 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 67.86 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVD-------AHVGKHIFEEcikktlRGKTVVLVTHQLQ-YLEFCGQIILL 82
Cdd:COG3840 130 LSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrqemLDLVDELCRE------RGLTVLMVTHDPEdAARIADRVLLV 203
|
90
....*....|....*.
gi 767990724 83 ENGKICENGTHSELMQ 98
Cdd:COG3840 204 ADGRIAADGPTAALLD 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
533-732 |
1.36e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.89 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVePMAGRILIDGVDICSIG---LEDLRSKLSVIPQDPVlLSGTI 609
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDPN-SSLNP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 610 RFN---------------LDPFDRhtDQQIWDALERTFLTKAI-SKFPkklhtdvvengGNFSVGERQLLCIARAVLRNS 673
Cdd:PRK15134 378 RLNvlqiieeglrvhqptLSAAQR--EQQVIAVMEEVGLDPETrHRYP-----------AEFSGGQRQRIAIARALILKP 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767990724 674 KIILIDEATASIDMETDTLI-------QRTIREAFqgctvLVIAHRVTTVLN-CDHILVMGNGKVVE 732
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQIlallkslQQKHQLAY-----LFISHDLHVVRAlCHQVIVLRQGEVVE 506
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
529-731 |
1.52e-12 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 67.68 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 529 DNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMA---GRILIDGVDIcSIGLedLRSKLSVIPQDPVLL 605
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPR-KPDQ--FQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 606 SG-----TIRF-NLDPFDRHTDQQIWDALERTFLTKAISkfpkklHTDVvenGGNF----SVGERQLLCIARAVLRNSKI 675
Cdd:cd03234 94 PGltvreTLTYtAILRLPRKSSDAIRKKRVEDVLLRDLA------LTRI---GGNLvkgiSGGERRRVSIAVQLLWDPKV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767990724 676 ILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVL--NCDHILVMGNGKVV 731
Cdd:cd03234 165 LILDEPTSGLDSFTALNLVSTLSQlARRNRIVILTIHQPRSDLfrLFDRILLLSSGEIV 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
10-87 |
1.70e-12 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 69.33 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVgKHIFEECIKKTLR--GKTVVLVTH-QLQYLEFCGQIILLENGK 86
Cdd:COG3839 133 QLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKL-RVEMRAEIKRLHRrlGTTTIYVTHdQVEAMTLADRIAVMNDGR 211
|
.
gi 767990724 87 I 87
Cdd:COG3839 212 I 212
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
11-70 |
1.85e-12 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 67.11 E-value: 1.85e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLR--GKTVVLVTHQL 70
Cdd:cd03293 132 LSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEE-LLDIWRetGKTVLLVTHDI 192
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
535-731 |
2.06e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.14 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 535 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDI-CSIGLEDLRSKLSVIPQD-PVLLSGTIRFN 612
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdFKSSKEALENGISMVHQElNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 613 L--------DPFDRHtdqqiwDALERTflTKAISKfpkKLHTDV--VENGGNFSVGERQLLCIARAVLRNSKIILIDEAT 682
Cdd:PRK10982 94 MwlgryptkGMFVDQ------DKMYRD--TKAIFD---ELDIDIdpRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767990724 683 ASI-DMETDTL--IQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV 731
Cdd:PRK10982 163 SSLtEKEVNHLftIIRKLKE--RGCGIVYISHKMEEIFQlCDEITILRDGQWI 213
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
518-743 |
2.39e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 68.29 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 518 IIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMA---GRILIDGVDICSIGLEDLRSK 594
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 595 LSVIPQDP------VLLSGTIRFNLDpfDRHTDQQ-----IWDALERTFLTKAISKFPKklhtdvvenggNFSVGERQLL 663
Cdd:PRK13640 86 VGIVFQNPdnqfvgATVGDDVAFGLE--NRAVPRPemikiVRDVLADVGMLDYIDSEPA-----------NLSGGQKQRV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 664 CIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRK 741
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
..
gi 767990724 742 KP 743
Cdd:PRK13640 233 KV 234
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
537-732 |
2.46e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 68.96 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 537 GINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDL---RSKLSVIPQDPvLLSGTIRFNL 613
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravRSDIQMIFQDP-LASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 614 -----DPFDRH----TDQQIWDALeRTFLTKA------ISKFPKKlhtdvvenggnFSVGERQLLCIARAVLRNSKIILI 678
Cdd:PRK15079 118 geiiaEPLRTYhpklSRQEVKDRV-KAMMLKVgllpnlINRYPHE-----------FSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767990724 679 DEATA----SIDMETDTLIQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVE 732
Cdd:PRK15079 186 DEPVSaldvSIQAQVVNLLQQLQRE--MGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVE 242
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-92 |
2.99e-12 |
|
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: 66.28 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 3 EIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVgKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILL 82
Cdd:cd03369 118 RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT-DALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVM 196
|
90
....*....|
gi 767990724 83 ENGKICENGT 92
Cdd:cd03369 197 DAGEVKEYDH 206
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-93 |
3.14e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 68.70 E-value: 3.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKTL-RGKTVVLVTHQLQYLE-FCGQIILLENG-KI 87
Cdd:PRK13536 173 LSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-ARHLIWERLRSLLaRGKTILLTTHFMEEAErLCDRLCVLEAGrKI 251
|
....*.
gi 767990724 88 CENGTH 93
Cdd:PRK13536 252 AEGRPH 257
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
8-96 |
4.92e-12 |
|
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: 66.05 E-value: 4.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 8 GLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCG-QIILLENGK 86
Cdd:cd03260 139 ALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDP-ISTAKIEELIAELKKEYTIVIVTHNMQQAARVAdRTAFLLNGR 217
|
90
....*....|
gi 767990724 87 ICENGTHSEL 96
Cdd:cd03260 218 LVEFGPTEQI 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
11-96 |
5.69e-12 |
|
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: 66.11 E-value: 5.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEC--IKKTLrGKTVVLVTH-QLQYLEFCGQIILLENGKI 87
Cdd:cd03300 131 LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELkrLQKEL-GITFVFVTHdQEEALTMSDRIAVMNKGKI 209
|
....*....
gi 767990724 88 CENGTHSEL 96
Cdd:cd03300 210 QQIGTPEEI 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
10-100 |
6.30e-12 |
|
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: 66.05 E-value: 6.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD---AHVGKHIFEEcIKKTlRGKTVVLVTHQLQY-LEFCGQIILLENG 85
Cdd:cd03256 144 QLSGGQQQRVAIARALMQQPKLILADEPVASLDpasSRQVMDLLKR-INRE-EGITVIVSLHQVDLaREYADRIVGLKDG 221
|
90
....*....|....*
gi 767990724 86 KICENGTHSELMQKK 100
Cdd:cd03256 222 RIVFDGPPAELTDEV 236
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
529-733 |
6.48e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.44 E-value: 6.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 529 DNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEP---MAGRILIDGVDICSI---GLEDLRS-KLSVIPQD 601
Cdd:PRK09473 26 DGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLpekELNKLRAeQISMIFQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 602 PVLlsgtirfNLDPFDRHTDQ---------------------QIWDALERTFLTKAISKFPKKlhtdvvenggnFSVGER 660
Cdd:PRK09473 106 PMT-------SLNPYMRVGEQlmevlmlhkgmskaeafeesvRMLDAVKMPEARKRMKMYPHE-----------FSGGMR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 661 QLLCIARAVLRNSKIILIDEATASIDMETD----TLIQRTIREaFqGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEF 733
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQaqimTLLNELKRE-F-NTAIIMITHDLGVVAGiCDKVLVMYAGRTMEY 243
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
537-737 |
6.53e-12 |
|
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: 68.68 E-value: 6.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 537 GINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAG----RILIDGVDICSIGLED----------LRSKLSVIPQDP 602
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevnvRVGDEWVDMTKPGPDGrgrakryigiLHQEYDLYPHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 603 VLLSGTIRFNLD-PFDRhtdqqiwdALERTFLTKAISKFPKKLHTDVVEN-GGNFSVGERQLLCIARAVLRNSKIILIDE 680
Cdd:TIGR03269 382 VLDNLTEAIGLElPDEL--------ARMKAVITLKMVGFDEEKAEEILDKyPDELSEGERHRVALAQVLIKEPRIVILDE 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 681 ATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPE 737
Cdd:TIGR03269 454 PTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPE 513
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
535-730 |
7.51e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 66.19 E-value: 7.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 535 LHGINLTIRGHEVVGIVGRTGSGKSSLgmalfrlVEPMAGRILIDGVDICSIGL------------EDLR---------- 592
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTL-------LRHLSGLITGDKSAGSHIELlgrtvqregrlaRDIRksrantgyif 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 593 ------SKLSVIPQdpvLLSGTI------RFNLDPFDRHTDQQIWDALERTfltkAISKFPkklHTDVvengGNFSVGER 660
Cdd:PRK09984 93 qqfnlvNRLSVLEN---VLIGALgstpfwRTCFSWFTREQKQRALQALTRV----GMVHFA---HQRV----STLSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767990724 661 QLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKV 730
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDYALRyCERIVALRQGHV 231
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
533-714 |
7.56e-12 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 64.10 E-value: 7.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGvdicsigledlRSKLSVIPQDPVLLSGTIRfn 612
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLFLPQRPYLPLGTLR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 613 ldpfdrhtdQQI---WDalertfltkaiskfpkklhtDVvenggnFSVGERQLLCIARAVLRNSKIILIDEATASIDMET 689
Cdd:cd03223 82 ---------EQLiypWD--------------------DV------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES 126
|
170 180
....*....|....*....|....*
gi 767990724 690 DTLIQRTIREAfqGCTVLVIAHRVT 714
Cdd:cd03223 127 EDRLYQLLKEL--GITVISVGHRPS 149
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
10-96 |
8.67e-12 |
|
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: 65.22 E-value: 8.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDaHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEF-CGQIILLENGKIC 88
Cdd:cd03263 133 TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD-PASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
....*...
gi 767990724 89 ENGTHSEL 96
Cdd:cd03263 212 CIGSPQEL 219
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
535-748 |
9.31e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 66.27 E-value: 9.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 535 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDP------VLLSGT 608
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdnqfvgATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 609 IRFNLD----PFDRHTdQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEATAS 684
Cdd:PRK13642 103 VAFGMEnqgiPREEMI-KRVDEALLAVNMLDFKTREPARL-----------SGGQKQRVAVAGIIALRPEIIILDESTSM 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767990724 685 IDMETDTLIQRTIREAFQG--CTVLVIAHRVTTVLNCDHILVMGNGKVVEfdrpevlRKKPGSLFA 748
Cdd:PRK13642 171 LDPTGRQEIMRVIHEIKEKyqLTVLSITHDLDEAASSDRILVMKAGEIIK-------EAAPSELFA 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-98 |
1.23e-11 |
|
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: 67.62 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLR--GKTVVLVTHQLQY-LEFCGQIILLENGKI 87
Cdd:COG1123 143 LSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDL-LRELQRerGTTVLLITHDLGVvAEIADRVVVMDDGRI 221
|
90
....*....|.
gi 767990724 88 CENGTHSELMQ 98
Cdd:COG1123 222 VEDGPPEEILA 232
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
518-739 |
1.44e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 65.53 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 518 IIFQDYHMKYRDNTpTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSV 597
Cdd:PRK13647 5 IEVEDLHFRYKDGT-KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 598 IPQDP--VLLSGTIR-------FNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARA 668
Cdd:PRK13647 84 VFQDPddQVFSSTVWddvafgpVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767990724 669 VLRNSKIILIDEATASIDMETdtliQRTIREAF-----QGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVL 739
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRG----QETLMEILdrlhnQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLL 225
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
11-96 |
1.68e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 66.65 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHifeecIKKTLRGK------TVVLVTH-QLQYLEFCGQIILLE 83
Cdd:PRK10851 137 LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKE-----LRRWLRQLheelkfTSVFVTHdQEEAMEVADRVVVMS 211
|
90
....*....|...
gi 767990724 84 NGKICENGTHSEL 96
Cdd:PRK10851 212 QGNIEQAGTPDQV 224
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
185-441 |
1.94e-11 |
|
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: 65.50 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 185 IIFFFVVLIVFLTIFSFWWLsywleqGSGTN--SSRESNGTMADLGNIAdnPQLSFYQLVYGLNALLLICVGVcssgIFT 262
Cdd:cd18547 3 LVIILAIISTLLSVLGPYLL------GKAIDliIEGLGGGGGVDFSGLL--RILLLLLGLYLLSALFSYLQNR----LMA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 263 KVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQ-LLPIFSeQFLVLSLMVIAVLLIVSVLSPYILL 341
Cdd:cd18547 71 RVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQaLSQSLT-QLISSILTIVGTLIMMLYISPLLTL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 342 MGAIIMVICFIYYMMF-KKAIGVFKRLENySRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDA--QNNYLLLFLS 418
Cdd:cd18547 150 IVLVTVPLSLLVTKFIaKRSQKYFRKQQK-ALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEElyKASFKAQFYS 228
|
250 260
....*....|....*....|...
gi 767990724 419 STRWMALRLeiMTNLVTLAVALF 441
Cdd:cd18547 229 GLLMPIMNF--INNLGYVLVAVV 249
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
518-739 |
2.88e-11 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 64.34 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 518 IIFQDYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAG---RIL---IDGVDIC----SIG 587
Cdd:COG1119 4 LELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFgerRGGEDVWelrkRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 588 L------EDLRSKLSVIpqDpVLLSGtiRFN-LDPFDRHTDQQ------------IWDALERTFLTkaiskfpkklhtdv 648
Cdd:COG1119 82 LvspalqLRFPRDETVL--D-VVLSG--FFDsIGLYREPTDEQrerarellellgLAHLADRPFGT-------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 649 venggnFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLV-IAHRVTTVLNC-DHILVM 725
Cdd:COG1119 143 ------LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVEEIPPGiTHVLLL 216
|
250
....*....|....*
gi 767990724 726 GNGKVVEF-DRPEVL 739
Cdd:COG1119 217 KDGRVVAAgPKEEVL 231
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
11-68 |
2.88e-11 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 64.34 E-value: 2.88e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIK-KTLRGKTVVLVTH 68
Cdd:COG1116 139 LSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRlWQETGKTVLFVTH 197
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
529-743 |
3.04e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 66.65 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 529 DNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRL-----VEPMAGRILIDGVDICSIGLEDLR----SKLSVIP 599
Cdd:PRK15134 19 QTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHASEQTLRgvrgNKIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 600 QDPVLlsgtirfNLDPFdrHTDQ--------------------QIWDALERTFLTKA---ISKFPKKLhtdvvenggnfS 656
Cdd:PRK15134 99 QEPMV-------SLNPL--HTLEkqlyevlslhrgmrreaargEILNCLDRVGIRQAakrLTDYPHQL-----------S 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 657 VGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEF 733
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQ 238
|
250
....*....|
gi 767990724 734 DRPEVLRKKP 743
Cdd:PRK15134 239 NRAATLFSAP 248
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
522-737 |
3.48e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 64.09 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 522 DYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVE-----PMAGRILIDGVDICSIGLE--DLRSK 594
Cdd:PRK14267 9 NLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDpiEVRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 595 LSVIPQDPvllsgtirfnlDPFDRHTdqqIWD----ALERTFLTKAISKFPKKLHT--------DVVEN-----GGNFSV 657
Cdd:PRK14267 87 VGMVFQYP-----------NPFPHLT---IYDnvaiGVKLNGLVKSKKELDERVEWalkkaalwDEVKDrlndyPSNLSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 658 GERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAH------RVTtvlncDHILVMGNGKVV 731
Cdd:PRK14267 153 GQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHspaqaaRVS-----DYVAFLYLGKLI 227
|
250
....*....|...
gi 767990724 732 E-------FDRPE 737
Cdd:PRK14267 228 EvgptrkvFENPE 240
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-97 |
3.86e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 64.22 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 5 GERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLE-FCGQIILLE 83
Cdd:PRK10619 147 GKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARhVSSHVIFLH 226
|
90
....*....|....
gi 767990724 84 NGKICENGTHSELM 97
Cdd:PRK10619 227 QGKIEEEGAPEQLF 240
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-98 |
4.39e-11 |
|
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: 66.08 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHI---FEEcIKKTLrGKTVVLVTHQLQY-LEFCGQIILLENGK 86
Cdd:COG1123 405 LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQIlnlLRD-LQREL-GLTYLFISHDLAVvRYIADRVAVMYDGR 482
|
90
....*....|..
gi 767990724 87 ICENGTHSELMQ 98
Cdd:COG1123 483 IVEDGPTEEVFA 494
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
10-92 |
4.60e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 65.35 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLR--GKTVVLVTH-QLQYLEFCGQIILLENGK 86
Cdd:PRK09452 144 QLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNE-LKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGR 222
|
....*.
gi 767990724 87 ICENGT 92
Cdd:PRK09452 223 IEQDGT 228
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
533-734 |
4.95e-11 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 63.04 E-value: 4.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcsiglEDLRSK---LSVIPQDPVL---LS 606
Cdd:cd03301 14 TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-----TDLPPKdrdIAMVFQNYALyphMT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 607 G--TIRFNLD--PFDRHT-DQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEA 681
Cdd:cd03301 89 VydNIAFGLKlrKVPKDEiDERVREVAELLQIEHLLDRKPKQL-----------SGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 682 TASID----METDTLIQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFD 734
Cdd:cd03301 158 LSNLDaklrVQMRAELKRLQQR--LGTTTIYVTHDQVEAMTmADRIAVMNDGQIQQIG 213
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
535-729 |
4.95e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.72 E-value: 4.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 535 LHGINLTIRGHEVVGIVGRTGSGKSSLgMALFRLVEPMA---GRILIDGVDICSIGLEDL-RSKLSVIPQDPVLLSG-TI 609
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTL-MKVLSGVYPHGtyeGEIIFEGEELQASNIRDTeRAGIAIIHQELALVKElSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 610 RFN------LDPFDRhTDqqiWDALER---TFLTKAiskfpkKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDE 680
Cdd:PRK13549 100 LENiflgneITPGGI-MD---YDAMYLraqKLLAQL------KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767990724 681 ATASI-DMETDTL--IQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGK 729
Cdd:PRK13549 170 PTASLtESETAVLldIIRDLKA--HGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
534-739 |
4.97e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 63.36 E-value: 4.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 534 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLED-LRSKLSVIPQDPVLLSG-TIRF 611
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAIVPEGRRVFSRmTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 612 NLDPFDRHTD-QQIWDALERTFltkaiSKFPKkLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDE-----ATASI 685
Cdd:PRK11614 100 NLAMGGFFAErDQFQERIKWVY-----ELFPR-LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEpslglAPIII 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767990724 686 DMETDTLIQrtIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVL 739
Cdd:PRK11614 174 QQIFDTIEQ--LRE--QGMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDAL 224
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
11-91 |
5.07e-11 |
|
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: 63.29 E-value: 5.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIK--KTLRGKTVVLVTHQLQYL-EFCGQIILLENGKI 87
Cdd:cd03257 146 LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDL-LKklQEELGLTLLFITHDLGVVaKIADRVAVMYAGKI 224
|
....
gi 767990724 88 CENG 91
Cdd:cd03257 225 VEEG 228
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
516-730 |
5.31e-11 |
|
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: 65.62 E-value: 5.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 516 GEIIFQDYHMKYRDNTPTVLHGIN---LTIRGHEVVGIVGRTGSGKSSLGMALFRLVE-PMAGRILIDG--VDICSIgLE 589
Cdd:TIGR02633 254 GDVILEARNLTCWDVINPHRKRVDdvsFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGkpVDIRNP-AQ 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 590 DLRSKLSVIPQD-------PVLLSGTiRFNLDPFDRHTDQ-QIWDALERTFLTKAISKFPKKLHTDVVENGGnFSVGERQ 661
Cdd:TIGR02633 333 AIRAGIAMVPEDrkrhgivPILGVGK-NITLSVLKSFCFKmRIDAAAELQIIGSAIQRLKVKTASPFLPIGR-LSGGNQQ 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767990724 662 LLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKV 730
Cdd:TIGR02633 411 KAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
533-747 |
5.63e-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: 63.51 E-value: 5.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDlrSKLSVIPQDPVL-----LSG 607
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVFQHYALfrhmtVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 608 TIRFNL-------DPFDRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDE 680
Cdd:cd03296 94 NVAFGLrvkprseRPPEAEIRAKVHELLKLVQLDWLADRYPAQL-----------SGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 681 ATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKPGSLF 747
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
11-87 |
5.68e-11 |
|
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: 61.68 E-value: 5.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEecIKKTLR--GKTVVLVTHQLQ-YLEFCGQIILLENGKI 87
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK--VIRRLRaqGVAVIFISHRLDeVFEIADRVTVLRDGRV 160
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
534-756 |
5.88e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.90 E-value: 5.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 534 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDL----RSKLSVIPQDPVLLSG-T 608
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLSHlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 609 IRFNLD-P-----FDRHTDQQIWDA-LERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEA 681
Cdd:PRK10535 103 AAQNVEvPavyagLERKQRLLRAQElLQRLGLEDRVEYQPSQL-----------SGGQQQRVSIARALMNGGQVILADEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 682 TASIDM---ETDTLIQRTIREafQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEfDRPEVLRKKPGSLFAALMATATS 756
Cdd:PRK10535 172 TGALDShsgEEVMAILHQLRD--RGHTVIIVTHDPQVAAQAERVIEIRDGEIVR-NPPAQEKVNVAGGTEPVVNTASG 246
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
533-752 |
5.90e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 63.54 E-value: 5.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDgvdicSIGLEDLRSKLSVIPQDPVLLsgtirfn 612
Cdd:PRK11247 26 TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAEAREDTRLMFQDARLL------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 613 ldPFDRHTD-----------QQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEA 681
Cdd:PRK11247 94 --PWKKVIDnvglglkgqwrDAALQALAAVGLADRANEWPAAL-----------SGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 682 TASID----METDTLIQRTIREafQGCTVLVIAHRVT-TVLNCDHILVMGNGKV-----VEFDRPevlRKKPGSLFAALM 751
Cdd:PRK11247 161 LGALDaltrIEMQDLIESLWQQ--HGFTVLLVTHDVSeAVAMADRVLLIEEGKIgldltVDLPRP---RRRGSARLAELE 235
|
.
gi 767990724 752 A 752
Cdd:PRK11247 236 A 236
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
11-98 |
6.76e-11 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 63.07 E-value: 6.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIKKT--LRGKTVVLVTHQLQYL-EFCGQIILLENGKI 87
Cdd:COG1127 142 LSGGMRKRVALARALALDPEILLYDEPTAGLDP-ITSAVIDELIRELrdELGLTSVVVTHDLDSAfAIADRVAVLADGKI 220
|
90
....*....|.
gi 767990724 88 CENGTHSELMQ 98
Cdd:COG1127 221 IAEGTPEELLA 231
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
522-745 |
7.88e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.06 E-value: 7.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 522 DYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSI-------------GL 588
Cdd:PRK10619 10 DLHKRYGEHE--VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 589 EDLRSKLSVIPQdpvllsgtiRFNLDPFDRHTDQQIWDALERTFLTKAIS-----KFPKKLHTDVVENGG---NFSVGER 660
Cdd:PRK10619 88 RLLRTRLTMVFQ---------HFNLWSHMTVLENVMEAPIQVLGLSKQEAreravKYLAKVGIDERAQGKypvHLSGGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 661 QLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLNC-DHILVMGNGKVVEFDRPEV 738
Cdd:PRK10619 159 QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQ 238
|
....*..
gi 767990724 739 LRKKPGS 745
Cdd:PRK10619 239 LFGNPQS 245
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
509-732 |
7.97e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 65.38 E-value: 7.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 509 PQGWPQHGEIIFQDYHMKYRDNTPTVlHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGL 588
Cdd:PRK10522 314 PQAFPDWQTLELRNVTFAYQDNGFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 589 EDLRSKLSVIPQDpvllsgtirFNLdpFDRHTD---QQIWDALERTFLtkAISKFPKKLHtdvVENGG----NFSVGERQ 661
Cdd:PRK10522 393 EDYRKLFSAVFTD---------FHL--FDQLLGpegKPANPALVEKWL--ERLKMAHKLE---LEDGRisnlKLSKGQKK 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767990724 662 LLCIARAVLRNSKIILIDEATAsidmETDTLIQRT--------IREafQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 732
Cdd:PRK10522 457 RLALLLALAEERDILLLDEWAA----DQDPHFRREfyqvllplLQE--MGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
531-745 |
8.02e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 63.18 E-value: 8.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 531 TPTVL-HGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEP----MAGRILIDGVdicSIGLEDLRSKL-SVIPQDPvl 604
Cdd:PRK10418 14 AAQPLvHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGK---PVAPCALRGRKiATIMQNP-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 605 lsgtiR--FN-LDPFDRH------------TDQQIWDALERTFLTKA---ISKFPKKLhtdvvenggnfSVGERQLLCIA 666
Cdd:PRK10418 89 -----RsaFNpLHTMHTHaretclalgkpaDDATLTAALEAVGLENAarvLKLYPFEM-----------SGGMLQRMMIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 667 RAVLRNSKIILIDEATASID----METDTLIQRTIREafQGCTVLVIAHRVTTVLNC-DHILVMGNGKVVEFDRPEVLRK 741
Cdd:PRK10418 153 LALLCEAPFIIADEPTTDLDvvaqARILDLLESIVQK--RALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETLFN 230
|
....
gi 767990724 742 KPGS 745
Cdd:PRK10418 231 APKH 234
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
533-755 |
8.14e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 64.36 E-value: 8.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLgmalFRLV----EPMAGRILIDGVDIC--SIGLEDLrsklSVIPQDPVL-- 604
Cdd:PRK11432 20 TVIDNLNLTIKQGTMVTLLGPSGCGKTTV----LRLVagleKPTEGQIFIDGEDVThrSIQQRDI----CMVFQSYALfp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 605 ---LSGTIRFNLDPFDRHTD---QQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILI 678
Cdd:PRK11432 92 hmsLGENVGYGLKMLGVPKEerkQRVKEALELVDLAGFEDRYVDQI-----------SGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 679 DEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLNC-DHILVMGNGKVVEFDRPEVLRKKPGSLF-AALMATA 754
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSEAFAVsDTVIVMNKGKIMQIGSPQELYRQPASRFmASFMGDA 240
|
.
gi 767990724 755 T 755
Cdd:PRK11432 241 N 241
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
530-732 |
8.60e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.12 E-value: 8.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 530 NTPTVLHGINLTIRGHEVVGIVGRTGSGKSSL-----GMALFRLVEpmaGRILIDGVDICSIGLEDlRSKLSVIP--QDP 602
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLskviaGHPAYKILE---GDILFKGESILDLEPEE-RAHLGIFLafQYP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 603 VLLSGT-----IRFNLDPFDRHTDQQIWDALErtFLTKAISKF------PKKLHTDVVEnggNFSVGERQLLCIARAVLR 671
Cdd:CHL00131 94 IEIPGVsnadfLRLAYNSKRKFQGLPELDPLE--FLEIINEKLklvgmdPSFLSRNVNE---GFSGGEKKRNEILQMALL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 672 NSKIILIDEATASIDMetDTLiqRTIREAF-----QGCTVLVIAH--RVTTVLNCDHILVMGNGKVVE 732
Cdd:CHL00131 169 DSELAILDETDSGLDI--DAL--KIIAEGInklmtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIK 232
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
521-711 |
1.15e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 62.49 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 521 QDYHMKYrdNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRL--VEP---MAGRILIDGVDICSIGLE--DLRS 593
Cdd:PRK14239 9 SDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIYSPRTDtvDLRK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 594 KLSVIPQDPVLLSGTIRFNLDPFDRHT---DQQIWD-ALERTFLTKAI-SKFPKKLHTDVVenggNFSVGERQLLCIARA 668
Cdd:PRK14239 87 EIGMVFQQPNPFPMSIYENVVYGLRLKgikDKQVLDeAVEKSLKGASIwDEVKDRLHDSAL----GLSGGQQQRVCIARV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767990724 669 VLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAH 711
Cdd:PRK14239 163 LATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR 205
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
11-91 |
1.25e-10 |
|
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: 61.74 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVD----AHVGKHIFEECIKktlRGKTVVLVTHQLQYLEFCGQ-IILLENG 85
Cdd:cd03298 129 LSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrAEMLDLVLDLHAE---TKMTVLMVTHQPEDAKRLAQrVVFLDNG 205
|
....*.
gi 767990724 86 KICENG 91
Cdd:cd03298 206 RIAAQG 211
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
534-739 |
1.47e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 63.31 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 534 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGlEDLRSKLSVIPQ-DPVLLSGTIRFN 612
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA-RLARARIGVVPQfDNLDLEFTVREN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 613 LDPFDRH---TDQQIwDALERTFLTKAisKFPKKLHTDVVENGGnfsvGERQLLCIARAVLRNSKIILIDEATASIDMET 689
Cdd:PRK13536 135 LLVFGRYfgmSTREI-EAVIPSLLEFA--RLESKADARVSDLSG----GMKRRLTLARALINDPQLLILDEPTTGLDPHA 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767990724 690 DTLIQRTIREAF-QGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVL 739
Cdd:PRK13536 208 RHLIWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHAL 259
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
533-734 |
1.53e-10 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 61.78 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLE-DLRSKLSVIpqDPVLLSGTIRf 611
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGgGFNPELTGR--ENIYLNGRLL- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 612 nldpfdRHTDQQIWDALERtflTKAISKFPKKLHTDVvengGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDT 691
Cdd:cd03220 113 ------GLSRKEIDEKIDE---IIEFSELGDFIDLPV----KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767990724 692 LIQRTIREAFQGCTVLVIA-HRVTTVLN-CDHILVMGNGKVVEFD 734
Cdd:cd03220 180 KCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
513-737 |
1.60e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.04 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 513 PQHGEIIFQ-----DYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALF-----RLVepmAGRILIDG-- 580
Cdd:NF040905 251 PKIGEVVFEvknwtVYHPLHPERK--VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgrsygRNI---SGTVFKDGke 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 581 VDICSI------GL----EDlRSKLSVIpqdpvlLSGTIRFN--LDPFDRHTDQQIWDALERtflTKAISKFPKKLHT-- 646
Cdd:NF040905 326 VDVSTVsdaidaGLayvtED-RKGYGLN------LIDDIKRNitLANLGKVSRRGVIDENEE---IKVAEEYRKKMNIkt 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 647 -DVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDM----ETDTLIQRTireAFQGCTVLVIAHRVTTVLN-CD 720
Cdd:NF040905 396 pSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVgakyEIYTIINEL---AAEGKGVIVISSELPELLGmCD 472
|
250
....*....|....*...
gi 767990724 721 HILVMGNGKVV-EFDRPE 737
Cdd:NF040905 473 RIYVMNEGRITgELPREE 490
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
529-737 |
1.68e-10 |
|
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: 64.32 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 529 DNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMA----GRILIDGVDICSIGLEDLR----SKLSVIPQ 600
Cdd:COG4172 20 GGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAahpsGSILFDGQDLLGLSERELRrirgNRIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 601 DPvLLSgtirfnLDPFdrHT--DQ------------------QIWDALERTFLTKA---ISKFPKKLhtdvvenggnfSV 657
Cdd:COG4172 100 EP-MTS------LNPL--HTigKQiaevlrlhrglsgaaaraRALELLERVGIPDPerrLDAYPHQL-----------SG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 658 GERQLLCIARAVLRNSKIILIDEATasidmeT--DTLIQRTI--------REafQGCTVLVIAHRVTTVLN-CDHILVMG 726
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPT------TalDVTVQAQIldllkdlqRE--LGMALLLITHDLGVVRRfADRVAVMR 231
|
250
....*....|....*...
gi 767990724 727 NGKVVE-------FDRPE 737
Cdd:COG4172 232 QGEIVEqgptaelFAAPQ 249
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
9-100 |
1.94e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 61.95 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 9 LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEecIKKTLR--GKTVVLVTHQlqyLEFCGQI----ILL 82
Cdd:PRK11124 140 LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVS--IIRELAetGITQVIVTHE---VEVARKTasrvVYM 214
|
90
....*....|....*...
gi 767990724 83 ENGKICENGTHSELMQKK 100
Cdd:PRK11124 215 ENGHIVEQGDASCFTQPQ 232
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
11-98 |
3.50e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 60.88 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH-------VGKHIFEEcikktlrGKTVVLVTHQLQYLEFCG-QIILL 82
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPElrhevlkVMQDLAEE-------GMTMVIVTHEIGFAEKVAsRLIFI 209
|
90
....*....|....*.
gi 767990724 83 ENGKICENGTHSELMQ 98
Cdd:PRK09493 210 DKGRIAEDGDPQVLIK 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
11-99 |
3.67e-10 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 61.51 E-value: 3.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIK-KTLRGKTVVLVTHQL-QYLEFCGQIILLENGKIC 88
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRlQAELQKTIVFITHDLdEALRLGDRIAIMKDGRLV 240
|
90
....*....|.
gi 767990724 89 ENGTHSELMQK 99
Cdd:cd03294 241 QVGTPEEILTN 251
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
520-731 |
4.16e-10 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 60.37 E-value: 4.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 520 FQDYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG-----VDICSIGL--ED-- 590
Cdd:cd03269 3 VENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiAARNRIGYlpEErg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 591 LRSKLSVIPQdpVLLSGTIRfNLDPfdRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVL 670
Cdd:cd03269 81 LYPKMKVIDQ--LVYLAQLK-GLKK--EEARRRIDEWLERLELSEYANKRVEEL-----------SKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767990724 671 RNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV 731
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEElCDRVLLLNKGRAV 207
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
518-731 |
4.24e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.44 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 518 IIFQDYHMKYRdNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcsigLEDLRSKL-S 596
Cdd:PRK15056 7 IVVNDVTVTWR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT----RQALQKNLvA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 597 VIPQD-------PVLLSGTI---RFNLDPFDR----HTDQQIWDALERTFLTKAiskfpkkLHTDVvengGNFSVGERQL 662
Cdd:PRK15056 82 YVPQSeevdwsfPVLVEDVVmmgRYGHMGWLRrakkRDRQIVTAALARVDMVEF-------RHRQI----GELSGGQKKR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767990724 663 LCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAF-QGCTVLVIAHRVTTVLN-CDHIlVMGNGKVV 731
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEfCDYT-VMVKGTVL 220
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
11-99 |
4.32e-10 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 60.81 E-value: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLR--GKTVVLVTHQLQYLEFCG-QIILLENGKI 87
Cdd:cd03299 130 LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREE-LKKIRKefGVTVLHVTHDFEEAWALAdKVAIMLNGKL 208
|
90
....*....|..
gi 767990724 88 CENGTHSELMQK 99
Cdd:cd03299 209 IQVGKPEEVFKK 220
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
11-87 |
4.32e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 60.85 E-value: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIKKTLR--GKTVVLVTHQL-QYLEFCGQIILLENGKI 87
Cdd:PRK11247 134 LSGGQKQRVALARALIHRPGLLLLDEPLGALDA-LTRIEMQDLIESLWQqhGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
11-109 |
4.52e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 63.20 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFeeCIKKTLR--GKTVVLVTHQLQYLEFCGQIILLENGKIC 88
Cdd:PRK10535 145 LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVM--AILHQLRdrGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
90 100
....*....|....*....|.
gi 767990724 89 ENGTHSELMQKKGKYAQLIQK 109
Cdd:PRK10535 223 RNPPAQEKVNVAGGTEPVVNT 243
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1-87 |
4.61e-10 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 60.00 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 1 MTEIGERG-LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEC--IKKTLRGkTVVLVTHQLQYLEF-C 76
Cdd:cd03297 121 LDHLLNRYpAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELkqIKKNLNI-PVIFVTHDLSEAEYlA 199
|
90
....*....|.
gi 767990724 77 GQIILLENGKI 87
Cdd:cd03297 200 DRIVVMEDGRL 210
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
533-743 |
5.07e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 61.27 E-value: 5.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAG-----RILIDGVDICSI-GLEDLRSKLSVIPQDPV--- 603
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNpfp 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 604 ------LLSGTIRFNLDPFD--------RHTDQQIWDALErtfltKAISKFPKKLhtdvvenggnfSVGERQLLCIARAV 669
Cdd:PRK14271 115 msimdnVLAGVRAHKLVPRKefrgvaqaRLTEVGLWDAVK-----DRLSDSPFRL-----------SGGQQQLLCLARTL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767990724 670 LRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKP 743
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSSP 253
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-108 |
6.10e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.12 E-value: 6.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVgkhifEECIKKTL------RGKTVVLVTHQLQYLEF 75
Cdd:PTZ00265 1350 TNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS-----EKLIEKTIvdikdkADKTIITIAHRIASIKR 1424
|
90 100 110
....*....|....*....|....*....|....*....
gi 767990724 76 CGQIILLEN----GKICE-NGTHSELMQ-KKGKYAQLIQ 108
Cdd:PTZ00265 1425 SDKIVVFNNpdrtGSFVQaHGTHEELLSvQDGVYKKYVK 1463
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
2-98 |
6.20e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 60.41 E-value: 6.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGL-NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvgkHIFEecIKKTLR-----GKTVVLVTHQL-QYLE 74
Cdd:PRK11231 129 NHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDIN---HQVE--LMRLMRelntqGKTVVTVLHDLnQASR 203
|
90 100
....*....|....*....|....
gi 767990724 75 FCGQIILLENGKICENGTHSELMQ 98
Cdd:PRK11231 204 YCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
538-749 |
6.21e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 61.78 E-value: 6.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 538 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIglEDLRSKLSVIPQDPVL-----LSGTIRFN 612
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPINMMFQSYALfphmtVEQNIAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 613 LDPfDRHTDQQIWDALERTFLTKAISKFPK-KLHtdvvenggNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDT 691
Cdd:PRK11607 116 LKQ-DKLPKAEIASRVNEMLGLVHMQEFAKrKPH--------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767990724 692 LIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKPGSLFAA 749
Cdd:PRK11607 187 RMQLEVVDILErvGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSA 247
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
10-95 |
6.32e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 61.36 E-value: 6.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFE--ECIKKTLrGKTVVLVTHQLQYL-EFCGQIILLENGK 86
Cdd:PRK11153 140 QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILEllKDINREL-GLTIVLITHEMDVVkRICDRVAVIDAGR 218
|
....*....
gi 767990724 87 ICENGTHSE 95
Cdd:PRK11153 219 LVEQGTVSE 227
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-92 |
7.66e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.41 E-value: 7.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 6 ERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEecikkTLR------GKTVVLVTHQLQY-LEFCGQ 78
Cdd:PRK09984 148 QRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMD-----TLRdinqndGITVVVTLHQVDYaLRYCER 222
|
90
....*....|....
gi 767990724 79 IILLENGKICENGT 92
Cdd:PRK09984 223 IVALRQGHVFYDGS 236
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
10-92 |
8.24e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 61.25 E-value: 8.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFE---EcIKKTLrGKTVVLVTHQLQYL-EFCGQIILLENG 85
Cdd:COG1135 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDllkD-INREL-GLTIVLITHEMDVVrRICDRVAVLENG 217
|
....*..
gi 767990724 86 KICENGT 92
Cdd:COG1135 218 RIVEQGP 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
517-746 |
9.10e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 60.42 E-value: 9.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 517 EIIFQDYHMKYRDNTP---TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIdGVDICSIG-----L 588
Cdd:PRK13634 2 DITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGkknkkL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 589 EDLRSKLSVIPQDP--VLLSGT----IRF---NLDPFDRHTDQQIWDALERTFLTKAI-SKFPKKLhtdvvenggnfSVG 658
Cdd:PRK13634 81 KPLRKKVGIVFQFPehQLFEETvekdICFgpmNFGVSEEDAKQKAREMIELVGLPEELlARSPFEL-----------SGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 659 ERQLLCIARAVLRNSKIILIDEATASID-------MEtdtLIQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKV 730
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDpkgrkemME---MFYKLHKE--KGLTTVLVTHSMEDAARyADQIVVMHKGTV 224
|
250
....*....|....*.
gi 767990724 731 VEFDRPEVLRKKPGSL 746
Cdd:PRK13634 225 FLQGTPREIFADPDEL 240
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
10-96 |
9.13e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.49 E-value: 9.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQY-LEFCGQIILLENGKIC 88
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNvLEWTKRTIFFKDGKII 244
|
....*....
gi 767990724 89 ENG-THSEL 96
Cdd:PRK13651 245 KDGdTYDIL 253
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
518-737 |
9.63e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 60.23 E-value: 9.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 518 IIFQDYHMKYRDNTPTVLHG---INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIC----SIGLED 590
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGldnISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 591 LRSKLSVIPQDP--VLLSGT----IRF---NLDPFDRHTDQQIWDALERTFL-TKAISKFPKKLhtdvvenggnfSVGER 660
Cdd:PRK13641 83 LRKKVSLVFQFPeaQLFENTvlkdVEFgpkNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFEL-----------SGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 661 QLLCIARAVLRNSKIILIDEATASIDMETdtliQRTIREAFQ-----GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFD 734
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEG----RKEMMQLFKdyqkaGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHA 227
|
...
gi 767990724 735 RPE 737
Cdd:PRK13641 228 SPK 230
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
532-737 |
1.38e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.08 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 532 PTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--VDICSIGL----------EDlRSKLSVIP 599
Cdd:PRK11288 266 PGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDairagimlcpED-RKAEGIIP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 600 ----QDPVLLSGtiRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKlHTDVvengGNFSVGERQLLCIARAVLRNSKI 675
Cdd:PRK11288 345 vhsvADNINISA--RRHHLRAGCLINNRWEAENADRFIRSLNIKTPSR-EQLI----MNLSGGNQQKAILGRWLSEDMKV 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767990724 676 ILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVV-EFDRPE 737
Cdd:PRK11288 418 ILLDEPTRGIDVGAKHEIYNVIYElAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIAgELAREQ 482
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
535-731 |
1.39e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 58.73 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 535 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLED---LRSKLSVIPQD---------- 601
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDhhllmdrtvy 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 602 -----PVLLSGTirfNLDPFDRHTDQqiwdALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKII 676
Cdd:PRK10908 98 dnvaiPLIIAGA---SGDDIRRRVSA----ALDKVGLLDKAKNFPIQL-----------SGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767990724 677 LIDEATASIDMETDTLIQRTIREAFQ-GCTVLVIAHRVTTVLNCDH-ILVMGNGKVV 731
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLISRRSYrMLTLSDGHLH 216
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
518-739 |
1.41e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 60.20 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 518 IIFQDYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGlEDLRSKLSV 597
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-RHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 598 IPQ----DPVLlsgTIRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVvengGNFSVGERQLLCIARAVLRNS 673
Cdd:PRK13537 85 VPQfdnlDPDF---TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKV----GELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 674 KIILIDEATASIDMETDTLIQRTIREAF-QGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVL 739
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHAL 225
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
10-97 |
1.58e-09 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 60.50 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVgKHifeECIK--KTLRGKT---VVLVTHQLQ-YLEFCGQIILLE 83
Cdd:COG4148 133 TLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR-KA---EILPylERLRDELdipILYVSHSLDeVARLADHVVLLE 208
|
90
....*....|....
gi 767990724 84 NGKICENGTHSELM 97
Cdd:COG4148 209 QGRVVASGPLAEVL 222
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
10-100 |
1.64e-09 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 59.37 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKhifEEcIKKTLR------GKTVVLVTHQLQYLEFCGQIILLE 83
Cdd:TIGR04520 136 LLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDP-KGR---KE-VLETIRklnkeeGITVISITHDMEEAVLADRVIVMN 210
|
90
....*....|....*..
gi 767990724 84 NGKICENGTHSELMQKK 100
Cdd:TIGR04520 211 KGKIVAEGTPREIFSQV 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
531-734 |
1.83e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 60.85 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 531 TPTVLHGINLTIRGHEVVGIVGRTGSGKSSlgmaLFRLV----EPMAGRILIDGvdicsigleDLRskLSVIPQDPVLLS 606
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKST----LLKILagelEPDSGEVSIPK---------GLR--IGYLPQEPPLDD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 607 G-TIRFNLdpFDRHTDqqIWDALERtfLTKAISKFPK---------KLHTDVVENGG----------------------- 653
Cdd:COG0488 75 DlTVLDTV--LDGDAE--LRALEAE--LEELEAKLAEpdedlerlaELQEEFEALGGweaearaeeilsglgfpeedldr 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 654 ---NFSVGERQLLCIARAVLRNSKIILIDEATASIDMET-----DTLIQrtireaFQGcTVLVIAH------RVttvlnC 719
Cdd:COG0488 149 pvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewleEFLKN------YPG-TVLVVSHdryfldRV-----A 216
|
250
....*....|....*
gi 767990724 720 DHILVMGNGKVVEFD 734
Cdd:COG0488 217 TRILELDRGKLTLYP 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
11-87 |
2.24e-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: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHI----FEecIKKTlRGKTVVLVTHQLQYLEFCGQIILLENGK 86
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIidllFE--LNRE-RGTTLVLVTHDPALAARCDRVLRLRAGR 223
|
.
gi 767990724 87 I 87
Cdd:COG4181 224 L 224
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-93 |
2.36e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 59.43 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKTL-RGKTVVLVTHQLQYLE-FCGQIILLENG-KI 87
Cdd:PRK13537 139 LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ-ARHLMWERLRSLLaRGKTILLTTHFMEEAErLCDRLCVIEEGrKI 217
|
....*.
gi 767990724 88 CENGTH 93
Cdd:PRK13537 218 AEGAPH 223
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
516-730 |
2.64e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.33 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 516 GEIIFQDYHMKYRDNTPT---VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRlVEPMA--GRILIDG--VDICS--- 585
Cdd:PRK13549 256 GEVILEVRNLTAWDPVNPhikRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPGRweGEIFIDGkpVKIRNpqq 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 586 -----IGL--EDlRSKLSVIPQDPVLLSGTIRfNLDPFDRHTdqQIWDALERTFLTKAISKFpkKLHTDVVENG-GNFSV 657
Cdd:PRK13549 335 aiaqgIAMvpED-RKRDGIVPVMGVGKNITLA-ALDRFTGGS--RIDDAAELKTILESIQRL--KVKTASPELAiARLSG 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767990724 658 GERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKV 730
Cdd:PRK13549 409 GNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQlVQQGVAIIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
6-71 |
2.70e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 58.64 E-value: 2.70e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767990724 6 ERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIfEECIKKTLRGKTVVLVTHQLQ 71
Cdd:PRK14243 147 QSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRI-EELMHELKEQYTIIIVTHNMQ 211
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-70 |
3.03e-09 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 57.24 E-value: 3.03e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQL 70
Cdd:NF040873 120 LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDL 179
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
11-87 |
3.49e-09 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 57.29 E-value: 3.49e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIKKTLR-GKTVVLVTHQLQYLE-FCGQIILLENGKI 87
Cdd:cd03269 129 LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VNVELLKDVIRELARaGKTVILSTHQMELVEeLCDRVLLLNKGRA 206
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
530-716 |
3.63e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 58.12 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 530 NTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVE-----PMAGRILIDGVDICS--IGLEDLRSKLSVIPQDP 602
Cdd:PRK14258 18 DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYErrVNLNRLRRQVSMVHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 603 VLLSGTI----RFNLDPFDRHTDQQIWDALERTFLTKAI-SKFPKKLHTDVVENGGnfsvGERQLLCIARAVLRNSKIIL 677
Cdd:PRK14258 98 NLFPMSVydnvAYGVKIVGWRPKLEIDDIVESALKDADLwDEIKHKIHKSALDLSG----GQQQRLCIARALAVKPKVLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767990724 678 IDEATASID----METDTLIQR-TIREAFqgcTVLVIAHRVTTV 716
Cdd:PRK14258 174 MDEPCFGLDpiasMKVESLIQSlRLRSEL---TMVIVSHNLHQV 214
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
533-732 |
3.74e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 57.19 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcsiGLEDLRSKLSVI-PQDPVLLSGTIRF 611
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEACHYLgHRNAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 612 NLDpFDRH----TDQQIWDALERTFLtKAISKFPkklhtdvvenGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDM 687
Cdd:PRK13539 93 NLE-FWAAflggEELDIAAALEAVGL-APLAHLP----------FGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767990724 688 ETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLNCdHILVMGNGKVVE 732
Cdd:PRK13539 161 AAVALFAELIRAhLAQGGIVIAATHIPLGLPGA-RELDLGPFAAED 205
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
533-711 |
3.74e-09 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 57.12 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFN 612
Cdd:cd03231 14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 613 LDPFDR-HTDQQIWDALERTFLTkAISKFPkklhtdvvenGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMET-D 690
Cdd:cd03231 94 LRFWHAdHSDEQVEEALARVGLN-GFEDRP----------VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGvA 162
|
170 180
....*....|....*....|.
gi 767990724 691 TLIQRTIREAFQGCTVLVIAH 711
Cdd:cd03231 163 RFAEAMAGHCARGGMVVLTTH 183
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
533-737 |
4.32e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 57.78 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGvDICSIgLE---DLRSKLSVIpqDPVLLSGTI 609
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-RVSAL-LElgaGFHPELTGR--ENIYLNGRL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 610 R-FNLDPFDRHTDQQIWDAlertfltkAISKFpkkLHTDVvengGNFSVGERQLLCIARAVLRNSKIILIDEATASIDme 688
Cdd:COG1134 116 LgLSRKEIDEKFDEIVEFA--------ELGDF---IDQPV----KTYSSGMRARLAFAVATAVDPDILLVDEVLAVGD-- 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767990724 689 tdtliqrtirEAFQ-------------GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPE 737
Cdd:COG1134 179 ----------AAFQkkclarirelresGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPE 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
518-742 |
5.04e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 58.25 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 518 IIFQDYHMKYRDNTP---TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG----LED 590
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 591 LRSKLSVIPQDP-----------VLLSGTIRFNLDpFDRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGE 659
Cdd:PRK13646 83 VRKRIGMVFQFPesqlfedtverEIIFGPKNFKMN-LDEVKNYAHRLLMDLGFSRDVMSQSPFQM-----------SGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 660 RQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIRE--AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRP 736
Cdd:PRK13646 151 MRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSP 230
|
....*.
gi 767990724 737 EVLRKK 742
Cdd:PRK13646 231 KELFKD 236
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
274-445 |
5.06e-09 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 58.17 E-value: 5.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 274 NKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLlpiFSEQFLVL---SLMVIAVLLIVSVLSPYILLMGAIIMVIC 350
Cdd:cd18544 78 RDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNEL---FTSGLVTLigdLLLLIGILIAMFLLNWRLALISLLVLPLL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 351 FIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAqnnYLLLFLSSTRWMALRLEIM 430
Cdd:cd18544 155 LLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQE---YRKANLKSIKLFALFRPLV 231
|
170
....*....|....*
gi 767990724 431 TNLVTLAVALFVAFG 445
Cdd:cd18544 232 ELLSSLALALVLWYG 246
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
534-732 |
5.31e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 57.33 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 534 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDG--------VDICSIGLedLRSKLSVIPQD---- 601
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktPSDKAIRE--LRRNVGMVFQQynlw 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 602 PVLlsgTIRFNL--DPF------DRHTDQQIWDALERTFLTKAISKFPkkLHtdvvenggnFSVGERQLLCIARAVLRNS 673
Cdd:PRK11124 95 PHL---TVQQNLieAPCrvlglsKDQALARAEKLLERLRLKPYADRFP--LH---------LSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767990724 674 KIILIDEATASIDMETDTLIQRTIREAFQ-GCTVLVIAHRVTTVLN-CDHILVMGNGKVVE 732
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKtASRVVYMENGHIVE 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
11-89 |
6.59e-09 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 56.98 E-value: 6.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGK---HIFEEcIKKtlRGKTVVLVTHQLQYLE-FCGQIILLENGK 86
Cdd:COG2884 138 LSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWeimELLEE-INR--RGTTVLIATHDLELVDrMPKRVLELEDGR 214
|
...
gi 767990724 87 ICE 89
Cdd:COG2884 215 LVR 217
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
11-87 |
7.19e-09 |
|
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: 56.77 E-value: 7.19e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQY-LEFCGQIILLENGKI 87
Cdd:cd03262 136 LSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFaREVADRVIFMDDGRI 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
6-71 |
8.59e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 56.97 E-value: 8.59e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767990724 6 ERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIfEECIKKtLRGK-TVVLVTHQLQ 71
Cdd:COG1117 150 KSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKI-EELILE-LKKDyTIVIVTHNMQ 214
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
546-731 |
9.65e-09 |
|
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: 56.15 E-value: 9.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 546 EVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGV---DIC-SIGLEDLRSKLSVIPQDPVLLSG-TIRFNL------- 613
Cdd:cd03297 24 EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRkKINLPPQQRKIGLVFQQYALFPHlNVRENLafglkrk 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 614 -DPFDRHTDQQIWDALErtfLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTL 692
Cdd:cd03297 104 rNREDRISVDELLDLLG---LDHLLNRYPAQL-----------SGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767990724 693 IQ---RTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVV 731
Cdd:cd03297 170 LLpelKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
537-743 |
9.86e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 56.92 E-value: 9.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 537 GINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICsiGLED----------------LRSKLSVIPQ 600
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE--GLPGhqiarmgvvrtfqhvrLFREMTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 601 DPV---------LLSGTirFNLDPFDRHTDQQIWDA---LERTFLTKAISKfpkklhtdvveNGGNFSVGERQLLCIARA 668
Cdd:PRK11300 101 LLVaqhqqlktgLFSGL--LKTPAFRRAESEALDRAatwLERVGLLEHANR-----------QAGNLAYGQQRRLEIARC 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767990724 669 VLRNSKIILIDEATASID-METDTLIQ--RTIREAFqGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKP 743
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNpKETKELDEliAELRNEH-NVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
245-445 |
1.00e-08 |
|
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: 57.43 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 245 LNALLLICVGVCSS----GIFT--------KVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLP 312
Cdd:cd18552 35 LEALLLVPLAIIGLfllrGLASylqtylmaYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 313 IFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIMVICFIyymmfkkAIGVF-KRLENYSR------SPLFSHILNSLQG 385
Cdd:cd18552 115 SALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAAL-------PIRRIgKRLRKISRrsqesmGDLTSVLQETLSG 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 386 LSSIHVYGKTEDFISQFKRLTDaqnNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFG 445
Cdd:cd18552 188 IRVVKAFGAEDYEIKRFRKANE---RLRRLSMKIARARALSSPLMELLGAIAIALVLWYG 244
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
533-729 |
1.10e-08 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 54.38 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLgmalFRLvepMAGRILIDGVDICSIGledlRSKLSVIPQdpvlLSGtirfn 612
Cdd:cd03221 14 LLLKDISLTINPGDRIGLVGRNGAGKSTL----LKL---IAGELEPDEGIVTWGS----TVKIGYFEQ----LSG----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 613 ldpfdrhtdqqiwdalertfltkaiskfpkklhtdvvenggnfsvGERQLLCIARAVLRNSKIILIDEATASIDMETDTL 692
Cdd:cd03221 74 ---------------------------------------------GEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEA 108
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767990724 693 IQRTIREaFQGcTVLVIAH------RVttvlnCDHILVMGNGK 729
Cdd:cd03221 109 LEEALKE-YPG-TVILVSHdryfldQV-----ATKIIELEDGK 144
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
653-729 |
1.21e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.09 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 653 GNFSVGERQLLCIARAVLRNSKIILIDEAT-ASIDMETDTLIqRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGK 729
Cdd:PRK10762 140 GELSIGEQQMVEIAKVLSFESKVIIMDEPTdALTDTETESLF-RVIRElKSQGRGIVYISHRLKEIFEiCDDVTVFRDGQ 218
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
11-87 |
1.44e-08 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 55.25 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFeecikKTLR-----GKTVVLVTHQLQYL--EFCGQIILLE 83
Cdd:cd03213 112 LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM-----SLLRrladtGRTIICSIHQPSSEifELFDKLLLLS 186
|
....
gi 767990724 84 NGKI 87
Cdd:cd03213 187 QGRV 190
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
526-735 |
1.51e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 55.73 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 526 KYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVE--PMAGRILIDGVDicsigledlrsklsvIPQDPV 603
Cdd:COG2401 37 ELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQ---------------FGREAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 604 LlsgtirfnLDPFDRHTDqqIWDALER----------TFLTKaiskfPKKLhtdvvenggnfSVGERQLLCIARAVLRNS 673
Cdd:COG2401 102 L--------IDAIGRKGD--FKDAVELlnavglsdavLWLRR-----FKEL-----------STGQKFRFRLALLLAERP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767990724 674 KIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHR--VTTVLNCDHILVMGNGKVVEFDR 735
Cdd:COG2401 156 KLLVIDEFCSHLDRQTAKRVARNLQKLARraGITLVVATHHydVIDDLQPDLLIFVGYGGVPEEKR 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
11-96 |
1.52e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 56.30 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH-VGKhifeecIKKTLRG-----KTVVLVTHQLQYL-EFCGQIILLE 83
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPElVGE------VLNTIRQlaqekRTMVIVTHEMSFArDVADRAIFMD 218
|
90
....*....|...
gi 767990724 84 NGKICENGTHSEL 96
Cdd:PRK11264 219 QGRIVEQGPAKAL 231
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
11-89 |
1.53e-08 |
|
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: 56.35 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTV-VLVTHQLQYLE-FCGQIILLENGKIC 88
Cdd:TIGR02769 151 LSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAyLFITHDLRLVQsFCQRVAVMDKGQIV 230
|
.
gi 767990724 89 E 89
Cdd:TIGR02769 231 E 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
533-731 |
1.75e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.53 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLgMALFRLVEPMA---GRILIDGVDICSIGLEDLRSK-LSVIPQDPVLLSG- 607
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTL-MKILSGVYPHGtwdGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPEl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 608 TIRFNLdpFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENG---GNFSVGERQLLCIARAVLRNSKIILIDEATAS 684
Cdd:TIGR02633 94 SVAENI--FLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTrpvGDYGGGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767990724 685 I-DMETDTLIQrTIREAFQ-GCTVLVIAHRVTTVLN-CDHILVMGNGKVV 731
Cdd:TIGR02633 172 LtEKETEILLD-IIRDLKAhGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
3-83 |
1.95e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.04 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 3 EIGErglnLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEecIKKTLR--GKTVVLVTHQL-QYLEFCGQI 79
Cdd:PRK15056 139 QIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIIS--LLRELRdeGKTMLVSTHNLgSVTEFCDYT 212
|
....
gi 767990724 80 ILLE 83
Cdd:PRK15056 213 VMVK 216
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
535-736 |
1.97e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 56.90 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 535 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICS---IGLEDLRSKLSVIPQDPVllsG---- 607
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpEAQKLLRQKIQIVFQNPY---Gslnp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 608 --TIRFNL-DPFDRHTD-------QQIWDALERTFL-TKAISKFPkklHTdvvenggnFSVGERQLLCIARAVLRNSKII 676
Cdd:PRK11308 108 rkKVGQILeEPLLINTSlsaaerrEKALAMMAKVGLrPEHYDRYP---HM--------FSGGQRQRIAIARALMLDPDVV 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767990724 677 LIDEATASIDMEtdtlIQRTIREAFQ------GCTVLVIAHRVTTVlncDHI----LVMGNGKVVE-------FDRP 736
Cdd:PRK11308 177 VADEPVSALDVS----VQAQVLNLMMdlqqelGLSYVFISHDLSVV---EHIadevMVMYLGRCVEkgtkeqiFNNP 246
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
535-732 |
2.05e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.61 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 535 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGV--------DICSIGLEDLRSKLSVIPQDPV--- 603
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasttAALAAGVAIIYQELHLVPEMTVaen 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 604 LLSGTI--RFNLdpFDRHTDQQiwDALERTfltkaiskfpKKLHTDVVENG--GNFSVGERQLLCIARAVLRNSKIILID 679
Cdd:PRK11288 100 LYLGQLphKGGI--VNRRLLNY--EAREQL----------EHLGVDIDPDTplKYLSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767990724 680 EATASIDM-ETDTLIqRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVE 732
Cdd:PRK11288 166 EPTSSLSArEIEQLF-RVIRElRAEGRVILYVSHRMEEIFAlCDAITVFKDGRYVA 220
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
8-144 |
2.24e-08 |
|
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: 56.02 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 8 GLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhvgkhIFEECIKKTLR----GKTVVLVTHQLQYLEFCGQIILLE 83
Cdd:cd03289 136 GCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP-----ITYQVIRKTLKqafaDCTVILSEHRIEAMLECQRFLVIE 210
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767990724 84 NGKICENGTHSELMQKKGKYAQLIqkmhkeATSDMLQ-----DTAKIAEKPKVESQALATSLEESL 144
Cdd:cd03289 211 ENKVRQYDSIQKLLNEKSHFKQAI------SPSDRLKlfprrNSSKSKRKPRPQIQALQEETEEEV 270
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
11-96 |
2.28e-08 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 55.39 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhvgkhifeECIK------KTL--RGKTVVLVTHQLQY-LEFCGQIIL 81
Cdd:COG1126 137 LSGGQQQRVAIARALAMEPKVMLFDEPTSALDP--------ELVGevldvmRDLakEGMTMVVVTHEMGFaREVADRVVF 208
|
90
....*....|....*
gi 767990724 82 LENGKICENGTHSEL 96
Cdd:COG1126 209 MDGGRIVEEGPPEEF 223
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
541-725 |
2.32e-08 |
|
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: 55.49 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 541 TIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcSIGLEDLRSKLSVIPQDpvLLSGTIRfnldpfdrht 620
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIKADYEGTVRD--LLSSITK---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 621 dqqiwDALERTFLTKAISKfPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREa 700
Cdd:cd03237 88 -----DFYTHPYFKTEIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR- 160
|
170 180
....*....|....*....|....*
gi 767990724 701 fqgctvlVIAHRVTTVLNCDHILVM 725
Cdd:cd03237 161 -------FAENNEKTAFVVEHDIIM 178
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
11-96 |
2.61e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 56.40 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKTLR-GKTVVLVTHQL-QYLEFCGQIILLENGKIC 88
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPK-GEHEMMQLILDAKAnNKTVFVITHTMeHVLEVADEVIVMDKGKIL 255
|
....*...
gi 767990724 89 ENGTHSEL 96
Cdd:PRK13631 256 KTGTPYEI 263
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
11-98 |
3.03e-08 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 55.51 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARA-------VYSDRQIYLLDDPLSAVD-AHvgKHIFEECIKK-TLRGKTVVLVTHQL----QYlefCG 77
Cdd:COG4559 134 LSGGEQQRVQLARVlaqlwepVDGGPRWLFLDEPTSALDlAH--QHAVLRLARQlARRGGGVVAVLHDLnlaaQY---AD 208
|
90 100
....*....|....*....|.
gi 767990724 78 QIILLENGKICENGTHSELMQ 98
Cdd:COG4559 209 RILLLHQGRLVAQGTPEEVLT 229
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
538-730 |
3.40e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.60 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 538 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLED-LRSKLSVIPQDP----VLLSGTIRFN 612
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDRqssgLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 613 LDPFdRHTDQQIWdaLERTFLTKAISKFPKKLH---TDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMET 689
Cdd:PRK15439 362 VCAL-THNRRGFW--IKPARENAVLERYRRALNikfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767990724 690 DTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKV 730
Cdd:PRK15439 439 RNDIYQLIRSiAAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
534-737 |
3.61e-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: 56.73 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 534 VLHGINLTIRGHEVVGIVGRTGSGKSSLgMALFRLV---EPMAGRIlIDGVDIC-SIGLEDLRSKlsVIPQDPVLLSGTI 609
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMdqyEPTSGRI-IYHVALCeKCGYVERPSK--VGEPCPVCGGTLE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 610 RFNLD------PFDRHTDQQIWDALERTF--------LTKAISKFPK-------------------KLHTDVVENGGNFS 656
Cdd:TIGR03269 91 PEEVDfwnlsdKLRRRIRKRIAIMLQRTFalygddtvLDNVLEALEEigyegkeavgravdliemvQLSHRITHIARDLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 657 VGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHrVTTVLN--CDHILVMGNGKVVE 732
Cdd:TIGR03269 171 GGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSH-WPEVIEdlSDKAIWLENGEIKE 249
|
....*
gi 767990724 733 FDRPE 737
Cdd:TIGR03269 250 EGTPD 254
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
526-747 |
3.74e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 56.25 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 526 KYRDNTpTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDlrSKLSVIPQDPVL- 604
Cdd:PRK10851 10 KSFGRT-QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 605 ----LSGTIRFNLDPFDRHT-------DQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNS 673
Cdd:PRK10851 87 rhmtVFDNIAFGLTVLPRRErpnaaaiKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767990724 674 KIILIDEATASIDMETDTLIQRTIR---EAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGSLF 747
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRqlhEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRF 232
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
533-732 |
4.17e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.79 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGlEDLRSKLS------------VIP- 599
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMD-EEARAKLRakhvgfvfqsfmLIPt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 600 -------QDPVLLSGTirfnldpFDRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRN 672
Cdd:PRK10584 103 lnalenvELPALLRGE-------SSRQSRNGAKALLEQLGLGKRLDHLPAQL-----------SGGEQQRVALARAFNGR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767990724 673 SKIILIDEATASIDMETDTLIQRTI----REafQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 732
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLfslnRE--HGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
11-96 |
4.35e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 55.08 E-value: 4.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEecIKKTLR---GKTVVLVTHQLQYLE-FCGQIILLENGK 86
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIR--LLKKLQqqfGTACLFITHDLRLVErFCQRVMVMDNGQ 229
|
90
....*....|
gi 767990724 87 ICENGTHSEL 96
Cdd:PRK10419 230 IVETQPVGDK 239
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
11-84 |
4.66e-08 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 54.02 E-value: 4.66e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH----VGKHIFEEcIKKtlRGKTVVLVTHQLQYLEFCGQIILLEN 84
Cdd:COG4136 134 LSGGQRARVALLRALLAEPRALLLDEPFSKLDAAlraqFREFVFEQ-IRQ--RGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
7-91 |
5.21e-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: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 7 RGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEecIKKTLR--GKTVVLVTHQLQYLE-FCGQIILLE 83
Cdd:cd03266 133 RVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALRE--FIRQLRalGKCILFSTHIMQEVErLCDRVVVLH 210
|
....*...
gi 767990724 84 NGKICENG 91
Cdd:cd03266 211 RGRVVYEG 218
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
535-743 |
5.30e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 54.79 E-value: 5.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 535 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMA-----GRILIDGVDICSIGLE--DLRSKLSVIPQDPVLLSG 607
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPgfrveGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 608 TIRFNL------DPFDRHTDQQIWDALERTFLTKAISKfpkKLHtdvvENGGNFSVGERQLLCIARAVLRNSKIILIDEA 681
Cdd:PRK14243 106 SIYDNIaygariNGYKGDMDELVERSLRQAALWDEVKD---KLK----QSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767990724 682 TASIDMETDTLIQRTIREAFQGCTVLVIAH------RV---TTVLNCDHILVMG-NGKVVEFDRPEVLRKKP 743
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHnmqqaaRVsdmTAFFNVELTEGGGrYGYLVEFDRTEKIFNSP 250
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
10-69 |
5.49e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 53.72 E-value: 5.49e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKTL-RGKTVVLVTHQ 69
Cdd:PRK13539 127 YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AVALFAELIRAHLaQGGIVIAATHI 186
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
11-92 |
5.92e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 54.61 E-value: 5.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICEN 90
Cdd:PRK13644 137 LSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLE 216
|
..
gi 767990724 91 GT 92
Cdd:PRK13644 217 GE 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
2-39 |
6.14e-08 |
|
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: 52.65 E-value: 6.14e-08
10 20 30
....*....|....*....|....*....|....*...
gi 767990724 2 TEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLS 39
Cdd:pfam00005 113 RPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-96 |
6.52e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 55.61 E-value: 6.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 1 MTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLR-GKTVVLVTH-QLQYLEFCG 77
Cdd:PRK11607 139 MQEFAKRKPHqLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTHdQEEAMTMAG 218
|
90
....*....|....*....
gi 767990724 78 QIILLENGKICENGTHSEL 96
Cdd:PRK11607 219 RIAIMNRGKFVQIGEPEEI 237
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
10-99 |
6.88e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 54.81 E-value: 6.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKTLRGK--TVVLVTHQLQYLEFCGQIILLENGKI 87
Cdd:PRK13640 143 NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA-GKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKL 221
|
90
....*....|..
gi 767990724 88 CENGTHSELMQK 99
Cdd:PRK13640 222 LAQGSPVEIFSK 233
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
11-71 |
6.97e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 54.32 E-value: 6.97e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLR-GKTVVLVTHQLQ 71
Cdd:PRK11248 129 LSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIE 190
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-91 |
7.48e-08 |
|
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: 53.69 E-value: 7.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvgkhiF-EECIKK----TLRGKTVVLVTHQLQYL-EFCGQIILLE 83
Cdd:cd03220 142 TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA-----FqEKCQRRlrelLKQGKTVILVSHDPSSIkRLCDRALVLE 216
|
....*...
gi 767990724 84 NGKICENG 91
Cdd:cd03220 217 KGKIRFDG 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-91 |
7.74e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.48 E-value: 7.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 12 SGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEecIKKTLRGKtvvlvtHQLQYL----------EFCGQIIL 81
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILA--LLKSLQQK------HQLAYLfishdlhvvrALCHQVIV 498
|
90
....*....|
gi 767990724 82 LENGKICENG 91
Cdd:PRK15134 499 LRQGEVVEQG 508
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
541-711 |
7.93e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 7.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 541 TIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDgvdicsigledlrSKLSVIPQ----DPvllSGTIRFNLDpf 616
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-------------LKISYKPQyikpDY---DGTVEDLLR-- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 617 drhtdqQIWDALERTFLTKAISKfPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRT 696
Cdd:PRK13409 423 ------SITDDLGSSYYKSEIIK-PLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKA 495
|
170
....*....|....*..
gi 767990724 697 IREAF--QGCTVLVIAH 711
Cdd:PRK13409 496 IRRIAeeREATALVVDH 512
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
11-106 |
8.43e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 54.64 E-value: 8.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHI---FEECIKKtlRGKTVVLVTHQL----QYLEfcgQIILLE 83
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMmemFYKLHKE--KGLTTVLVTHSMedaaRYAD---QIVVMH 220
|
90 100
....*....|....*....|...
gi 767990724 84 NGKICENGTHSELMQKKGKYAQL 106
Cdd:PRK13634 221 KGTVFLQGTPREIFADPDELEAI 243
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
11-68 |
9.79e-08 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 54.10 E-value: 9.79e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFE---ECIKKTlrGKTVVLVTH 68
Cdd:COG4525 135 LSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQElllDVWQRT--GKGVFLITH 193
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
534-711 |
9.85e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 53.67 E-value: 9.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 534 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDI---CSIGLEDLRS-KLSVIPQ--------- 600
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklSSAAKAELRNqKLGFIYQfhhllpdft 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 601 ------DPVLLSGTIRfnldpfdRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSK 674
Cdd:PRK11629 104 alenvaMPLLIGKKKP-------AEINSRALEMLAAVGLEHRANHRPSEL-----------SGGERQRVAIARALVNNPR 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 767990724 675 IILIDEATASIDMETDTLIQRTIRE--AFQGCTVLVIAH 711
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGElnRLQGTAFLVVTH 204
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
533-737 |
1.00e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.84 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVL-------- 604
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpgditvqe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 605 LSGTIRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKklhtdvvENGGNFSVGERQLLCIARAVLRNSKIILIDEATAS 684
Cdd:PRK10253 101 LVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLAD-------QSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 685 IDMETDT----LIQRTIREafQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPE 737
Cdd:PRK10253 174 LDISHQIdlleLLSELNRE--KGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPK 229
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
11-96 |
1.02e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 54.65 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDA--HVGKHIFEECIKKTLrGKTVVLVTH-QLQYLEFCGQIILLENGKI 87
Cdd:PRK11000 134 LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalRVQMRIEISRLHKRL-GRTMIYVTHdQVEAMTLADKIVVLDAGRV 212
|
....*....
gi 767990724 88 CENGTHSEL 96
Cdd:PRK11000 213 AQVGKPLEL 221
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
534-732 |
1.26e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 53.55 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 534 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDlrsklSVIPQDPVLLS-----GT 608
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQNEGLLPwrnvqDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 609 IRFNLD------PFDRHTDQQiwdALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEAT 682
Cdd:PRK11248 91 VAFGLQlagvekMQRLEIAHQ---MLKKVGLEGAEKRYIWQL-----------SGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767990724 683 ASIDMET----DTLIQRTIREafQGCTVLVIAHRVTTVLNCDHILVM---GNGKVVE 732
Cdd:PRK11248 157 GALDAFTreqmQTLLLKLWQE--TGKQVLLITHDIEEAVFMATELVLlspGPGRVVE 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-130 |
1.35e-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: 54.81 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 1 MTEIGER----GLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHI---FEECIKKtlRGKTVVLVTHQLQYL 73
Cdd:TIGR03269 155 MVQLSHRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVhnaLEEAVKA--SGISMVLTSHWPEVI 232
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 74 E-FCGQIILLENGKICENGTHSELMQkkgKYAQLIQKMHKEATSDMLQDTAKIAEKPK 130
Cdd:TIGR03269 233 EdLSDKAIWLENGEIKEEGTPDEVVA---VFMEGVSEVEKECEVEVGEPIIKVRNVSK 287
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
535-732 |
1.40e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 53.39 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 535 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILI---DGVDICSIGLED------LRSKLSVIPQDP--- 602
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSEaerrrlLRTEWGFVHQHPrdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 603 ----VLLSGTIRFNL-DPFDRH---TDQQIWDALERTFLTKA-ISKFPkklhtdvvengGNFSVGERQLLCIARAVLRNS 673
Cdd:PRK11701 102 lrmqVSAGGNIGERLmAVGARHygdIRATAGDWLERVEIDAArIDDLP-----------TTFSGGMQQRLQIARNLVTHP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767990724 674 KIILIDEATASIDMETDT----LIQRTIREafQGCTVLVIAHRVTTV-LNCDHILVMGNGKVVE 732
Cdd:PRK11701 171 RLVFMDEPTGGLDVSVQArlldLLRGLVRE--LGLAVVIVTHDLAVArLLAHRLLVMKQGRVVE 232
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
11-97 |
1.43e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 54.65 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIK-KTLRGKTVVLVTHQL-QYLEFCGQIILLENGKIC 88
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKlQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVV 244
|
....*....
gi 767990724 89 ENGTHSELM 97
Cdd:PRK10070 245 QVGTPDEIL 253
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
11-100 |
1.52e-07 |
|
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: 54.35 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHI--FEECIKKTLRgKTVVLVTHQLQYLE-FCGQIILLENGKI 87
Cdd:TIGR02142 132 LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIlpYLERLHAEFG-IPILYVSHSLQEVLrLADRVVVLEDGRV 210
|
90
....*....|...
gi 767990724 88 CENGTHSELMQKK 100
Cdd:TIGR02142 211 AAAGPIAEVWASP 223
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-234 |
1.87e-07 |
|
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: 55.02 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 6 ERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTlRGKTVVLVTHQLQYLEFCG-QIILLEN 84
Cdd:TIGR01257 1057 EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGdRIAIISQ 1135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 85 GKICENGTHSELMQ--KKGKYAQLIQKMHK-EATSDMLQDTAKIAEK---PKVESQALATSLEESLNGNAvpehqltqEE 158
Cdd:TIGR01257 1136 GRLYCSGTPLFLKNcfGTGFYLTLVRKMKNiQSQRGGCEGTCSCTSKgfsTRCPARVDEITPEQVLDGDV--------NE 1207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 159 EMEegslswRVYHHYIQAAggyMVSCIiffFVVLIVFLTIFSFwwlsywlEQGSGTNSSRESNGTMADLG----NIADNP 234
Cdd:TIGR01257 1208 LMD------LVYHHVPEAK---LVECI---GQELIFLLPNKNF-------KQRAYASLFRELEETLADLGlssfGISDTP 1268
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
547-734 |
2.08e-07 |
|
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: 54.17 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 547 VVGIVGRTGSGKSSLgmalFRLV----EPMAGRILI-DGVdicsigledlrsKLSVIPQdpvllsgtIRFNLDPfDRHTD 621
Cdd:TIGR03719 350 IVGVIGPNGAGKSTL----FRMItgqeQPDSGTIEIgETV------------KLAYVDQ--------SRDALDP-NKTVW 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 622 QQIWDALE------RTFLTKA-ISKFPKKlHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETdtliQ 694
Cdd:TIGR03719 405 EEISGGLDiiklgkREIPSRAyVGRFNFK-GSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVET----L 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767990724 695 RTIREA---FQGCTVlVIAH------RVTTvlncdHILVM-GNGKVVEFD 734
Cdd:TIGR03719 480 RALEEAllnFAGCAV-VISHdrwfldRIAT-----HILAFeGDSHVEWFE 523
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
11-128 |
2.29e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 53.09 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGK---HIFEECIKKtlRGKTVVLVTHQL-QYLEFCGQIILLENGK 86
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNKE--YKKRIIMVTHNMdQVLRIADEVIVMHEGK 228
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 767990724 87 ICENG------THSELMQK----KGKYAQLIQKMhKEATSDMLQDTAKIAEK 128
Cdd:PRK13645 229 VISIGspfeifSNQELLTKieidPPKLYQLMYKL-KNKGIDLLNKNIRTIEE 279
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
11-97 |
2.55e-07 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 52.53 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHI---FEEcIKKTLrGKTVVLVTHQLQYLE-FCGQIILLENGK 86
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIinlMLE-LQEKL-GISYIYVSQHLGIVKhISDKVLVMHQGE 227
|
90
....*....|.
gi 767990724 87 ICENGTHSELM 97
Cdd:COG4167 228 VVEYGKTAEVF 238
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
2-199 |
2.66e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 53.90 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 2 TEIGERGL--NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFC--G 77
Cdd:TIGR00955 156 TRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFElfD 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 78 QIILLENGKICENGTHSELMQKKGKYAQLIQKMHKEAtsDMLQDTAKIAEKPKVESQA-------------LATSLEESL 144
Cdd:TIGR00955 236 KIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPA--DFYVQVLAVIPGSENESREriekicdsfavsdIGRDMLVNT 313
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767990724 145 NGNAVPEHQLTQEEEMEEGSlswrvyhhyiqaagGYMVSCIIFFFVVLI-VFLTIF 199
Cdd:TIGR00955 314 NLWSGKAGGLVKDSENMEGI--------------GYNASWWTQFYALLKrSWLSVL 355
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
11-69 |
3.03e-07 |
|
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: 51.59 E-value: 3.03e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKTL-RGKTVVLVTHQ 69
Cdd:TIGR01189 128 LSAGQQRRLALARLWLSRRPLWILDEPTTALDKA-GVALLAGLLRAHLaRGGIVLLTTHQ 186
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
11-87 |
3.08e-07 |
|
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: 51.64 E-value: 3.08e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLE-FCGQIILLENGKI 87
Cdd:cd03292 137 LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDtTRHRVIALERGKL 214
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
521-741 |
3.73e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 52.50 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 521 QDYHMKYRDNTpTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQ 600
Cdd:PRK13652 7 RDLCYSYSGSK-EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 601 DP--VLLSGTIR-------FNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLR 671
Cdd:PRK13652 86 NPddQIFSPTVEqdiafgpINLGLDEETVAHRVSSALHMLGLEELRDRVPHHL-----------SGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 672 NSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVE-------FDRPEVLRK 741
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAygtveeiFLQPDLLAR 234
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
11-91 |
3.77e-07 |
|
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: 51.42 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIKKTLRGKTVVLVTHQLQYLE-FCGQIILLENGKICE 89
Cdd:cd03264 131 LSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP-EERIRFRNLLSELGEDRIVILSTHIVEDVEsLCNQVAVLNKGKLVF 209
|
..
gi 767990724 90 NG 91
Cdd:cd03264 210 EG 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
526-749 |
3.81e-07 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 53.03 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 526 KYRDNTpTVLHGINLTIRGHEVVGIVGRTGSGKSSlgmaLFRLV----EPMAGRILIDGVDICSIGLEDlRSKLSVIPQD 601
Cdd:PRK09452 22 KSFDGK-EVISNLDLTINNGEFLTLLGPSGCGKTT----VLRLIagfeTPDSGRIMLDGQDITHVPAEN-RHVNTVFQSY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 602 PVLLSGTIRFNLD--------PFDRhTDQQIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNS 673
Cdd:PRK09452 96 ALFPHMTVFENVAfglrmqktPAAE-ITPRVMEALRMVQLEEFAQRKPHQL-----------SGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 674 KIILIDEATASID--------METDTLiQRTIreafqGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRKKPG 744
Cdd:PRK09452 164 KVLLLDESLSALDyklrkqmqNELKAL-QRKL-----GITFVFVTHDQEEALTmSDRIVVMRDGRIEQDGTPREIYEEPK 237
|
....*
gi 767990724 745 SLFAA 749
Cdd:PRK09452 238 NLFVA 242
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
11-69 |
3.84e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 51.34 E-value: 3.84e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH---VGKHIFEECIKktlRGKTVVLVTHQ 69
Cdd:PRK13538 130 LSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQgvaRLEALLAQHAE---QGGMVILTTHQ 188
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
534-743 |
3.85e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 52.04 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 534 VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGvdicsigledlRSKLSVIPQ----DPVLLSGTI 609
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----------KLRIGYVPQklylDTTLPLTVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 610 RF-NLDPFDRHTDqqIWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEATASIDME 688
Cdd:PRK09544 88 RFlRLRPGTKKED--ILPALKRVQAGHLIDAPMQKL-----------SGGETQRVLLARALLNRPQLLVLDEPTQGVDVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 689 TDT----LIQRTIREAfqGCTVLVIAHRVTTVL-NCDHILVMgNGKVVEFDRPEVLRKKP 743
Cdd:PRK09544 155 GQValydLIDQLRREL--DCAVLMVSHDLHLVMaKTDEVLCL-NHHICCSGTPEVVSLHP 211
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
11-91 |
3.91e-07 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 52.92 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQY-LEFCGQIILLENGKICE 89
Cdd:PRK09536 140 LSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLaARYCDELVLLADGRVRA 219
|
..
gi 767990724 90 NG 91
Cdd:PRK09536 220 AG 221
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-99 |
4.27e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 51.77 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIKKTLRGKTVVLVTHQ-------LQYLEFCGQIILL 82
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDP-VGTAKIEELLFELKKEYTIVLVTHSpaqaarvSDYVAFLYLGKLI 227
|
90 100
....*....|....*....|
gi 767990724 83 ENG---KICENGTHsELMQK 99
Cdd:PRK14267 228 EVGptrKVFENPEH-ELTEK 246
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
538-747 |
4.92e-07 |
|
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: 53.48 E-value: 4.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 538 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIcSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFD 617
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 618 RHTDQQIWDalERTFLTKAISKfPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTI 697
Cdd:TIGR01257 1028 AQLKGRSWE--EAQLEMEAMLE-DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767990724 698 REAFQGCTVLVIAHRVTTV-LNCDHILVMGNGKVVEFDRPEVLRKKPGSLF 747
Cdd:TIGR01257 1105 LKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGTPLFLKNCFGTGF 1155
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
518-736 |
5.08e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 52.04 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 518 IIFQDYHMKYRDNTP---TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG----LED 590
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 591 LRSKLSVIPQDP--VLLSGT----IRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVvenggnfSVGERQLLC 664
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETvlkdVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFEL-------SGGQMRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767990724 665 IARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ-GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRP 736
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTP 228
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
9-99 |
5.08e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 52.04 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 9 LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD--AHVGKHIFEECIKKTlrGKTVVLVTHQLQYL-EFCGQIILLENG 85
Cdd:PRK13643 143 FELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDpkARIEMMQLFESIHQS--GQTVVLVTHLMDDVaDYADYVYLLEKG 220
|
90
....*....|....
gi 767990724 86 KICENGTHSELMQK 99
Cdd:PRK13643 221 HIISCGTPSDVFQE 234
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
538-743 |
5.52e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 52.05 E-value: 5.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 538 INLTIRGHEVVGIVGRTGSGKSSLGMALFRLVE-P---MAGRILIDGVDICSIGLEDLR----SKLSVIPQDPVLL---S 606
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGQDLQRISEKERRnlvgAEVAMIFQDPMTSlnpC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 607 GTIRFnldpfdrhtdqQIWDALE-------RTFLTKAI---------------SKFPKKLhtdvvenggnfSVGERQLLC 664
Cdd:PRK11022 106 YTVGF-----------QIMEAIKvhqggnkKTRRQRAIdllnqvgipdpasrlDVYPHQL-----------SGGMSQRVM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 665 IARAVLRNSKIILIDEATASIDMEtdtlIQRTIREAF------QGCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPE 737
Cdd:PRK11022 164 IAMAIACRPKLLIADEPTTALDVT----IQAQIIELLlelqqkENMALVLITHDLALVAEaAHKIIVMYAGQVVETGKAH 239
|
....*.
gi 767990724 738 VLRKKP 743
Cdd:PRK11022 240 DIFRAP 245
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
11-98 |
5.59e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 51.70 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARA------VYSDRQIYLLDDPLSAVD-AHvGKHIFEecIKKTL---RGKTVVLVTHQL----QYlefC 76
Cdd:PRK13548 135 LSGGEQQRVQLARVlaqlwePDGPPRWLLLDEPTSALDlAH-QHHVLR--LARQLaheRGLAVIVVLHDLnlaaRY---A 208
|
90 100
....*....|....*....|..
gi 767990724 77 GQIILLENGKICENGTHSELMQ 98
Cdd:PRK13548 209 DRIVLLHQGRLVADGTPAEVLT 230
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-96 |
5.69e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.59 E-value: 5.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIKKTLRGKTVVLVTHQLQYL-EFCGQIILLENGKICE 89
Cdd:PRK14246 154 LSGGQQQRLTIARALALKPKVLLMDEPTSMIDI-VNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVE 232
|
....*..
gi 767990724 90 NGTHSEL 96
Cdd:PRK14246 233 WGSSNEI 239
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
6-71 |
6.16e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 51.31 E-value: 6.16e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767990724 6 ERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIfEECIKKTLRGKTVVLVTHQLQ 71
Cdd:PRK14239 144 DSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKI-EETLLGLKDDYTMLLVTRSMQ 208
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-96 |
6.75e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 51.64 E-value: 6.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIfEECIKKTLRGKTVVLVTHQL-QYLEFCGQIILLENGKICE 89
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKI-EEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVE 242
|
....*..
gi 767990724 90 NGTHSEL 96
Cdd:PRK14271 243 EGPTEQL 249
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
10-98 |
7.76e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 51.33 E-value: 7.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD-AHVGKHIFEECIKKTLRGKTVVLVTHQLQY-LEFCGQIILLENGKI 87
Cdd:PRK10575 147 SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiAHQVDVLALVHRLSQERGLTVIAVLHDINMaARYCDYLVALRGGEM 226
|
90
....*....|.
gi 767990724 88 CENGTHSELMQ 98
Cdd:PRK10575 227 IAQGTPAELMR 237
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
513-726 |
7.89e-07 |
|
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: 52.44 E-value: 7.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 513 PQHGEIIFQDYHMKYrDNTPTV-------LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGvdics 585
Cdd:TIGR00954 440 PGRGIVEYQDNGIKF-ENIPLVtpngdvlIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA----- 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 586 igledlRSKLSVIPQDPVLLSGTIRfnldpfdrhtDQQIW-----DALERTFLTKAISKFPKKLH-TDVVENGGNF---- 655
Cdd:TIGR00954 514 ------KGKLFYVPQRPYMTLGTLR----------DQIIYpdsseDMKRRGLSDKDLEQILDNVQlTHILEREGGWsavq 577
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767990724 656 ------SVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAfqGCTVLVIAHRVTTVLNCDHILVMG 726
Cdd:TIGR00954 578 dwmdvlSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKSLWKYHEYLLYMD 652
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-98 |
9.40e-07 |
|
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: 50.51 E-value: 9.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 7 RGLNLSGGQKQRISLARAVYSDRQIYLLDDP---LSAVdahVGKHIFeECIKKtLR--GKTVVLVTHQLQY-LEFCGQII 80
Cdd:cd03224 129 LAGTLSGGEQQMLAIARALMSRPKLLLLDEPsegLAPK---IVEEIF-EAIRE-LRdeGVTILLVEQNARFaLEIADRAY 203
|
90
....*....|....*...
gi 767990724 81 LLENGKICENGTHSELMQ 98
Cdd:cd03224 204 VLERGRVVLEGTAAELLA 221
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-112 |
9.60e-07 |
|
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: 51.06 E-value: 9.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 4 IGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVgKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLE 83
Cdd:cd03288 150 VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT-ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLS 228
|
90 100 110
....*....|....*....|....*....|
gi 767990724 84 NGKICENGTHSELM-QKKGKYAQLIqKMHK 112
Cdd:cd03288 229 RGILVECDTPENLLaQEDGVFASLV-RTDK 257
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
12-96 |
1.12e-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: 50.06 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 12 SGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLR--GKTVVLVTHqlqYLE----FCGQIILLENG 85
Cdd:cd03265 133 SGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEY-IEKLKEefGMTILLTTH---YMEeaeqLCDRVAIIDHG 208
|
90
....*....|.
gi 767990724 86 KICENGTHSEL 96
Cdd:cd03265 209 RIIAEGTPEEL 219
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
227-447 |
1.13e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 51.02 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 227 LGNIADNPQLSFYQLVYGLNALLLICVGVCSS-------GIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNC 299
Cdd:cd18557 19 IGRLIDTIIKGGDLDVLNELALILLAIYLLQSvftfvryYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 300 FAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIMVICFIYYMMFKKAIgvfKRLENYSRSPLF--- 376
Cdd:cd18557 99 LSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYI---RKLSKEVQDALAkag 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767990724 377 SHILNSLQGLSSIHVYGKTEDFISQFKrltDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGIS 447
Cdd:cd18557 176 QVAEESLSNIRTVRSFSAEEKEIRRYS---EALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGY 243
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
246-404 |
1.13e-06 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 50.91 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 246 NALLLICVGVCSSGIF------------TKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFaGDLEQLDQLLPI 313
Cdd:cd18570 39 NLLNIISIGLILLYLFqsllsyirsyllLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 314 FSEQFLVLSLMVIAVLLIVSVLSPY----ILLMGAIIMVICFIYYMMFKKAIGvfKRLENYSRspLFSHILNSLQGLSSI 389
Cdd:cd18570 118 TTISLFLDLLMVIISGIILFFYNWKlfliTLLIIPLYILIILLFNKPFKKKNR--EVMESNAE--LNSYLIESLKGIETI 193
|
170
....*....|....*
gi 767990724 390 HVYGKTEDFISQFKR 404
Cdd:cd18570 194 KSLNAEEQFLKKIEK 208
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
11-98 |
1.21e-06 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 50.35 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIF----EECIKKTLrgkTVVLVTHQlqyLEFCGQI----ILL 82
Cdd:PRK10771 130 LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLtlvsQVCQERQL---TLLMVSHS---LEDAARIaprsLVV 203
|
90
....*....|....*.
gi 767990724 83 ENGKICENGTHSELMQ 98
Cdd:PRK10771 204 ADGRIAWDGPTDELLS 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
10-92 |
1.53e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 50.08 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvgkhiF-EECIKK----TLRGKTVVLVTHQLQYL-EFCGQIILLE 83
Cdd:COG1134 146 TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAA-----FqKKCLARirelRESGRTVIFVSHSMGAVrRLCDRAIWLE 220
|
....*....
gi 767990724 84 NGKICENGT 92
Cdd:COG1134 221 KGRLVMDGD 229
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-98 |
1.98e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 50.01 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIK--KTLRGKTVVLVTHQLQYLEFCGQIILLENGKIC 88
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPDIIILDEATSMLDP-RGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEIL 219
|
90
....*....|
gi 767990724 89 ENGTHSELMQ 98
Cdd:PRK13635 220 EEGTPEEIFK 229
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-144 |
2.41e-06 |
|
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: 51.45 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 8 GLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKI 87
Cdd:TIGR01271 1351 GYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP-VTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSV 1429
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 88 CENGTHSELMQKKGKYAQLIQKMHK-EATSDMLQDTAKIAEKPKVesQALATSLEESL 144
Cdd:TIGR01271 1430 KQYDSIQKLLNETSLFKQAMSAADRlKLFPLHRRNSSKRKPQPKI--TALREEAEEEV 1485
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
11-99 |
2.49e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 50.49 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEC--IKKTLrGKTVVLVTH-QLQYLEFCGQIILLENGKI 87
Cdd:PRK11432 137 ISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIreLQQQF-NITSLYVTHdQSEAFAVSDTVIVMNKGKI 215
|
90
....*....|..
gi 767990724 88 CENGTHSELMQK 99
Cdd:PRK11432 216 MQIGSPQELYRQ 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
11-85 |
2.75e-06 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 49.00 E-value: 2.75e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIK-KTLRGKTVVLVTHQL-QYLEFCGQIILLENG 85
Cdd:TIGR01184 115 LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQiWEEHRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
539-713 |
2.76e-06 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 49.20 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 539 NLTIRGHEVVGIVGRTGSGKSSL--GMALFrlVEPMAGRILIDGVDICSIGLEdlRSKLSVIPQDPVLLSG-TIRFN--- 612
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLlnLIAGF--LTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHlTVAQNigl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 613 -LDPFDRHTDQQ---IWDALERTFLTKAISKFPKKLhtdvvenggnfSVGERQLLCIARAVLRNSKIILIDEATASID-- 686
Cdd:PRK10771 95 gLNPGLKLNAAQrekLHAIARQMGIEDLLARLPGQL-----------SGGQRQRVALARCLVREQPILLLDEPFSALDpa 163
|
170 180
....*....|....*....|....*....
gi 767990724 687 --METDTLIQRTIREafQGCTVLVIAHRV 713
Cdd:PRK10771 164 lrQEMLTLVSQVCQE--RQLTLLMVSHSL 190
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
516-732 |
3.36e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.55 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 516 GEIIFQDYHMKYRDNTPtvLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDIC-SIGLEDLRSK 594
Cdd:PRK09700 262 HETVFEVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 595 LSVIPQD-------------------PVLLSGTIRFNLDPFDRHTDQQIWDAlERTFLtkAIskfpkKLHTdVVENGGNF 655
Cdd:PRK09700 340 MAYITESrrdngffpnfsiaqnmaisRSLKDGGYKGAMGLFHEVDEQRTAEN-QRELL--AL-----KCHS-VNQNITEL 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767990724 656 SVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKVVE 732
Cdd:PRK09700 411 SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITvCDRIAVFCEGRLTQ 489
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
525-743 |
3.43e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 49.38 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 525 MKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSlgmaLFRLV----EPMAGRILIDGVDICSI---GLEDLRSKLSV 597
Cdd:PRK11831 13 VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTT----LLRLIggqiAPDHGEILFDGENIPAMsrsRLYTVRKRMSM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 598 IPQdpvllSGTIRFNLDPFdrhtDQQIWDALERTFLTKAIskfpkkLHTDV---VENGG----------NFSVGERQLLC 664
Cdd:PRK11831 89 LFQ-----SGALFTDMNVF----DNVAYPLREHTQLPAPL------LHSTVmmkLEAVGlrgaaklmpsELSGGMARRAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 665 IARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ--GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRPEVLRK 741
Cdd:PRK11831 154 LARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQALQA 233
|
..
gi 767990724 742 KP 743
Cdd:PRK11831 234 NP 235
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
11-100 |
3.53e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 49.35 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQY-LEFCGQIILLENGKICE 89
Cdd:PRK13647 139 LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLaAEWADQVIVLKEGRVLA 218
|
90
....*....|.
gi 767990724 90 NGTHSELMQKK 100
Cdd:PRK13647 219 EGDKSLLTDED 229
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
11-69 |
3.53e-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: 48.26 E-value: 3.53e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQ 69
Cdd:cd03231 126 LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQ 184
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
11-89 |
3.70e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 48.62 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLR-GKTVVLVTHQLQYLEFCGQIILLENGKICE 89
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-82 |
4.72e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 48.56 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 3 EIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKTLRGK--TVVLVTHQLQYLEFCGQI 79
Cdd:PRK10247 129 TILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDES-NKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKV 207
|
...
gi 767990724 80 ILL 82
Cdd:PRK10247 208 ITL 210
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
545-737 |
5.04e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 46.98 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 545 HEVVGIVGRTGSGKSSLGMALFRLVEPMAGRIlidgvdicsigledlrsklsvipqdpvllsgtIRFNLDPFDRHTDQQI 624
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------------IYIDGEDILEEVLDQL 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 625 WdalertfltkaiskfpkklHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIR------ 698
Cdd:smart00382 50 L-------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllll 110
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767990724 699 -EAFQGCTVLVIAHRVTTVLncDHILVMGNGKVVEFDRPE 737
Cdd:smart00382 111 lKSEKNLTVILTTNDEKDLG--PALLRRRFDRRIVLLLIL 148
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
11-100 |
7.22e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 48.67 E-value: 7.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYL-EFCGQIILLENGKICE 89
Cdd:PRK13641 146 LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIK 225
|
90
....*....|.
gi 767990724 90 NGTHSELMQKK 100
Cdd:PRK13641 226 HASPKEIFSDK 236
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
227-445 |
7.98e-06 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 48.56 E-value: 7.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 227 LGNIAD---NPQLSFYQLVYglNALLLICVGVCSsGIFT--------KVTRKASTALHNKLFNKVFRCPMSFFDTIPIGR 295
Cdd:cd18541 22 IGRAIDaltAGTLTASQLLR--YALLILLLALLI-GIFRflwrylifGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 296 LLNCFAGDLEQLDQLL-P--IFSEQFLVLSLMVIAVLLIVSV-LSPYILLMgAIIMVICFIYY--MMFKKaigvFKRL-E 368
Cdd:cd18541 99 LMARATNDLNAVRMALgPgiLYLVDALFLGVLVLVMMFTISPkLTLIALLP-LPLLALLVYRLgkKIHKR----FRKVqE 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767990724 369 NYSRspLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDaqnNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFG 445
Cdd:cd18541 174 AFSD--LSDRVQESFSGIRVIKAFVQEEAEIERFDKLNE---EYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYG 245
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
11-87 |
8.01e-06 |
|
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: 47.04 E-value: 8.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDahVG--KHIFEECIKKTLRGKTVVLVTHQLQ-YLEFCGQIILLENGKI 87
Cdd:cd03215 105 LSGGNQQKVVLARWLARDPRVLILDEPTRGVD--VGakAEIYRLIRELADAGKAVLLISSELDeLLGLCDRILVMYEGRI 182
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
11-87 |
8.57e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 48.72 E-value: 8.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHI--FEECIKKTLrgKTVVL-VTHQLQ-YLEFCGQIILLENGK 86
Cdd:PRK11144 129 LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELlpYLERLAREI--NIPILyVSHSLDeILRLADRVVVLEQGK 206
|
.
gi 767990724 87 I 87
Cdd:PRK11144 207 V 207
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
9-87 |
9.17e-06 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 49.03 E-value: 9.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 9 LNLSGGQKQRISLARAVYSDRQIYLLD------DPlsavdahVGKHIF-EECI---KKtlRGKTVVLVTHQLQYLEFCGQ 78
Cdd:COG4615 456 TDLSQGQRKRLALLVALLEDRPILVFDewaadqDP-------EFRRVFyTELLpelKA--RGKTVIAISHDDRYFDLADR 526
|
....*....
gi 767990724 79 IILLENGKI 87
Cdd:COG4615 527 VLKMDYGKL 535
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
11-106 |
1.04e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 47.85 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKK--TLRGKTVVLVTHQL----QYLEfcgQIILLEN 84
Cdd:PRK13646 146 MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ-SKRQVMRLLKSlqTDENKTIILVSHDMnevaRYAD---EVIVMKE 221
|
90 100
....*....|....*....|..
gi 767990724 85 GKICENGTHSELMQKKGKYAQL 106
Cdd:PRK13646 222 GSIVSQTSPKELFKDKKKLADW 243
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
11-86 |
1.15e-05 |
|
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: 45.90 E-value: 1.15e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKtLRGkTVVLVTHQLQYL-EFCGQIILLENGK 86
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE-SIEALEEALKE-YPG-TVILVSHDRYFLdQVATKIIELEDGK 144
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-98 |
1.43e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 48.53 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEecIKKTL---RGKTVVLVTHQLQ---YLefCGQIILLEN 84
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILD--LLRDLqreHGLAYLFISHDLAvvrAL--AHRVMVMKD 501
|
90
....*....|....
gi 767990724 85 GKICENGTHSELMQ 98
Cdd:COG4172 502 GKVVEQGPTEQVFD 515
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
9-110 |
1.51e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 47.29 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 9 LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIK--KTLRGKTVVLVTHQLQYLEFCGQIILLENGK 86
Cdd:PRK13632 141 QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPK-GKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGK 219
|
90 100
....*....|....*....|....
gi 767990724 87 ICENGTHSELMQKKgkyaQLIQKM 110
Cdd:PRK13632 220 LIAQGKPKEILNNK----EILEKA 239
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
528-737 |
1.54e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 48.50 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 528 RDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMAL-FRLVEPM--AGRILIDGVdicSIGLEDLRSKLSVIPQDPVL 604
Cdd:TIGR00955 34 ERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALaFRSPKGVkgSGSVLLNGM---PIDAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 605 L-SGTIRFNLD-----PFDRHTD-----QQIWDALERTFLTKAiskfpKKLHTDVVENGGNFSVGERQLLCIARAVLRNS 673
Cdd:TIGR00955 111 IpTLTVREHLMfqahlRMPRRVTkkekrERVDEVLQALGLRKC-----ANTRIGVPGRVKGLSGGERKRLAFASELLTDP 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767990724 674 KIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLNC--DHILVMGNGKVVEFDRPE 737
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMAYSVVQVLKGlAQKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPD 252
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
541-711 |
1.70e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 48.24 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 541 TIRGHEVVGIVGRTGSGKSSLgmalfrlVEPMAGRILIDGVDIcsigleDLRSKLSVIPQ----DpvlLSGTIRFNLDpf 616
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTF-------AKILAGVLKPDEGEV------DEDLKISYKPQyispD---YDGTVEEFLR-- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 617 drhtdQQIWDALERTFLTKAISKfPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASID----METDTL 692
Cdd:COG1245 424 -----SANTDDFGSSYYKTEIIK-PLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrLAVAKA 497
|
170
....*....|....*....
gi 767990724 693 IQRTIREafQGCTVLVIAH 711
Cdd:COG1245 498 IRRFAEN--RGKTAMVVDH 514
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
535-754 |
1.76e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.08 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 535 LHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLED-LRSKLSVIPQDP----VLLSGTI 609
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYISEDRkrdgLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 610 RFN-----LDPFDRHTDQqIWDALERTFLTKAISKFPKKlhTDVVENG-GNFSVGERQLLCIARAVLRNSKIILIDEATA 683
Cdd:PRK10762 348 KENmsltaLRYFSRAGGS-LKHADEQQAVSDFIRLFNIK--TPSMEQAiGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767990724 684 SIDM----ETDTLIQRTIREafqGCTVLVIAHRVTTVLN-CDHILVMGNGKVV-EFDRPEVLRKKpgslfaaLMATA 754
Cdd:PRK10762 425 GVDVgakkEIYQLINQFKAE---GLSIILVSSEMPEVLGmSDRILVMHEGRISgEFTREQATQEK-------LMAAA 491
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-97 |
1.80e-05 |
|
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: 47.00 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 1 MTEIGERGLN-LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKK--TLRGKTVVLVTHQLQYL-EFC 76
Cdd:COG1119 132 LAHLADRPFGtLSQGEQRRVLIARALVKDPELLILDEPTAGLDLG-ARELLLALLDKlaAEGAPTLVLVTHHVEEIpPGI 210
|
90 100
....*....|....*....|.
gi 767990724 77 GQIILLENGKICENGTHSELM 97
Cdd:COG1119 211 THVLLLKDGRVVAAGPKEEVL 231
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-70 |
1.99e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 46.95 E-value: 1.99e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767990724 3 EIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGK-TVVLVTHQL 70
Cdd:PRK14258 143 KIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNL 211
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
11-69 |
2.48e-05 |
|
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: 45.22 E-value: 2.48e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECikkTLRGKTVVLVTHQ 69
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL---KELGITVISVGHR 147
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-96 |
2.54e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 46.44 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIfEECIKKTLRGKTVVLVTH-QLQYLEFCGQIILLENGKICE 89
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKI-ESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVE 225
|
....*..
gi 767990724 90 NGTHSEL 96
Cdd:PRK14247 226 WGPTREV 232
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
277-445 |
2.84e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 46.79 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 277 FNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIMVIcfIYYMM 356
Cdd:cd18565 94 YDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPL--IIAGT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 357 FKkaigvF-KRLE-NYSR-----SPLFSHILNSLQGLSSIHVYGkTEDFisQFKRLTDAQNNYLllflsSTRWMALRLEI 429
Cdd:cd18565 172 YW-----FqRRIEpRYRAvreavGDLNARLENNLSGIAVIKAFT-AEDF--ERERVADASEEYR-----DANWRAIRLRA 238
|
170 180
....*....|....*....|..
gi 767990724 430 M----TNLVTLA--VALFVAFG 445
Cdd:cd18565 239 AffpvIRLVAGAgfVATFVVGG 260
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
11-113 |
3.08e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 46.61 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLE-FCGQIILLENGKICE 89
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIK 217
|
90 100 110
....*....|....*....|....*....|....
gi 767990724 90 NGTHSELMQKKG----------KYAQLIQKMHKE 113
Cdd:PRK13639 218 EGTPKEVFSDIEtirkanlrlpRVAHLIEILNKE 251
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
11-106 |
3.30e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 46.26 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKTLR--GKTVVLVTHQLQYLEFCGQIILLENGKIC 88
Cdd:PRK13650 141 LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPE-GRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVE 219
|
90
....*....|....*...
gi 767990724 89 ENGTHSELMQKKGKYAQL 106
Cdd:PRK13650 220 STSTPRELFSRGNDLLQL 237
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
11-99 |
3.71e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 46.76 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLR--GKTVVLVTH-QLQYLEFCGQIILLENGKI 87
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLE-IQRLHRrlKTTSLYVTHdQVEAMTLADRVVVMNGGVA 213
|
90
....*....|..
gi 767990724 88 CENGTHSELMQK 99
Cdd:PRK11650 214 EQIGTPVEVYEK 225
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
547-734 |
3.73e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 547 VVGIVGRTGSGKSSLgmalFRLV----EPMAGRILI-DGVDICSI-----GLEDLRSKLSVIP--QDPVLLSGTI----- 609
Cdd:PRK11819 352 IVGIIGPNGAGKSTL----FKMItgqeQPDSGTIKIgETVKLAYVdqsrdALDPNKTVWEEISggLDIIKVGNREipsra 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 610 ---RFNLdpfdRHTDQQiwdalertfltkaiskfpKKLhtdvvengGNFSVGERQLLCIARAVLRNSKIILIDEATASID 686
Cdd:PRK11819 428 yvgRFNF----KGGDQQ------------------KKV--------GVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 687 MET-----DTLiqrtirEAFQGCTVlVIAH------RVTTvlncdHILVM-GNGKVVEFD 734
Cdd:PRK11819 478 VETlraleEAL------LEFPGCAV-VISHdrwfldRIAT-----HILAFeGDSQVEWFE 525
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
5-124 |
3.94e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 46.65 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 5 GERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLE-FCGQIILLE 83
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEqLAHELTVID 218
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 767990724 84 NGKICENGTHSELMQKKGKYAQLIQKMHKEATSDMLQDTAK 124
Cdd:NF000106 219 RGRVIADGKVDELKTKVGGRTLQIRPAHAAELDRMVGAIAQ 259
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
10-96 |
4.02e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 45.95 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHI--FEECIKKTLrGKTVVLVTHQLQYL-EFCGQIILLENGK 86
Cdd:PRK13652 137 HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELidFLNDLPETY-GMTVIFSTHQLDLVpEMADYIYVMDKGR 215
|
90
....*....|
gi 767990724 87 ICENGTHSEL 96
Cdd:PRK13652 216 IVAYGTVEEI 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
518-736 |
4.45e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 45.89 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 518 IIFQDYHMKYRDNTP---TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIG----LED 590
Cdd:PRK13649 3 INLQNVSYTYQAGTPfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 591 LRSKLSVIPQDP--VLLSGT----IRFNLDPFDRHTDQQIWDALERTFLTkAISK--FPKklhtdvveNGGNFSVGERQL 662
Cdd:PRK13649 83 IRKKVGLVFQFPesQLFEETvlkdVAFGPQNFGVSQEEAEALAREKLALV-GISEslFEK--------NPFELSGGQMRR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767990724 663 LCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQ-GCTVLVIAHRVTTVLN-CDHILVMGNGKVVEFDRP 736
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKP 229
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
247-468 |
5.27e-05 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 45.85 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 247 ALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVI 326
Cdd:cd18548 49 ALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 327 AVLLIVSVLSPYI-LLMGAIIMVICFIYYMMFKKAIGVFKRL-ENYSRsplfshiLN-----SLQGLSSIHVYGKtEDFi 399
Cdd:cd18548 129 GAIIMAFRINPKLaLILLVAIPILALVVFLIMKKAIPLFKKVqKKLDR-------LNrvvreNLTGIRVIRAFNR-EDY- 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767990724 400 sQFKRLTDAQNNYLLLFLSSTRWMALRLEIMT---NLVTLAVALFVAFGISSTPYSF-KVMA-VNIVLQLASSF 468
Cdd:cd18548 200 -EEERFDKANDDLTDTSLKAGRLMALLNPLMMlimNLAIVAILWFGGHLINAGSLQVgDLVAfINYLMQILMSL 272
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
11-95 |
5.69e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 45.81 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECikKTLRGK---TVVLVTHQLQYL-EFCGQIILLENGK 86
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKI--KELHKEynmTIILVSHSMEDVaKLADRIIVMNKGK 222
|
....*....
gi 767990724 87 ICENGTHSE 95
Cdd:PRK13637 223 CELQGTPRE 231
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
247-446 |
6.55e-05 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 45.50 E-value: 6.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 247 ALLLICVGVcSSGIFT--------KVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQF 318
Cdd:cd18542 42 ALLILGVAL-LRGVFRylqgylaeKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 319 LVLSLMVIAVLLIVSVLSPYI-LLMGAIIMVICFIYYMMFKKAIGVFKRL-ENYSRsplfshiLNS-LQ-GLSSIHV--- 391
Cdd:cd18542 121 VRAVLLFIGALIIMFSINWKLtLISLAIIPFIALFSYVFFKKVRPAFEEIrEQEGE-------LNTvLQeNLTGVRVvka 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767990724 392 YGKtEDF-ISQFkrltDAQN-NYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGI 446
Cdd:cd18542 194 FAR-EDYeIEKF----DKENeEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGG 245
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
9-95 |
6.69e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.10 E-value: 6.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 9 LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVD-------AHVGKHIFEEcikktlRGKTVVLVTHQLQYLEFCGQIIL 81
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrlnaARAIRRLSEE------GKKTALVVEHDLAVLDYLSDRIH 143
|
90
....*....|....
gi 767990724 82 LENGKICENGTHSE 95
Cdd:cd03222 144 VFEGEPGVYGIASQ 157
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
10-97 |
7.44e-05 |
|
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: 44.74 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDP---LSAVDAHVGKHIFEEcIKKtlRGKTVVLVTHQLQY-LEFCGQIILLENG 85
Cdd:cd03219 143 ELSYGQQRRLEIARALATDPKLLLLDEPaagLNPEETEELAELIRE-LRE--RGITVLLVEHDMDVvMSLADRVTVLDQG 219
|
90
....*....|..
gi 767990724 86 KICENGTHSELM 97
Cdd:cd03219 220 RVIAEGTPDEVR 231
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
11-100 |
9.24e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 45.22 E-value: 9.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIKKTLR--GKTVVLVTHQLQYLE-FCGQIILLENGKI 87
Cdd:PRK13636 142 LSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP-MGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRV 220
|
90
....*....|...
gi 767990724 88 CENGTHSELMQKK 100
Cdd:PRK13636 221 ILQGNPKEVFAEK 233
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
533-731 |
1.08e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 44.82 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALF-RLVEPMA-------GRILIDGVDICSIGLEDLRSKLSVIPQ---- 600
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQaaqp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 601 ------DPVLLSGtiRFnldPFDR------HTDQQI-WDALERTFLTKAISKfpkklhtDVVenggNFSVGERQLLCIAR 667
Cdd:PRK13547 95 afafsaREIVLLG--RY---PHARragaltHRDGEIaWQALALAGATALVGR-------DVT----TLSGGELARVQFAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767990724 668 AV---------LRNSKIILIDEATASIDME-----TDTlIQRTIREAFQGctVLVIAHRVT-TVLNCDHILVMGNGKVV 731
Cdd:PRK13547 159 VLaqlwpphdaAQPPRYLLLDEPTAALDLAhqhrlLDT-VRRLARDWNLG--VLAIVHDPNlAARHADRIAMLADGAIV 234
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
8-98 |
1.11e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 44.50 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 8 GLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhvgkhIFEECIKKTL-----RGKTVVLVTHQL-QYLEFCGQIIL 81
Cdd:PRK10895 135 GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP-----ISVIDIKRIIehlrdSGLGVLITDHNVrETLAVCERAYI 209
|
90
....*....|....*..
gi 767990724 82 LENGKICENGTHSELMQ 98
Cdd:PRK10895 210 VSQGHLIAHGTPTEILQ 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
11-99 |
1.30e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 44.69 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIKKTLR--GKTVVLVTHQLQYLEFCGQIILLENGKIC 88
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDP-SGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVV 223
|
90
....*....|.
gi 767990724 89 ENGTHSELMQK 99
Cdd:PRK13633 224 MEGTPKEIFKE 234
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
266-446 |
1.37e-04 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 44.71 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 266 RKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFagdLEQLDQLLPIFSeQFL-------VLSLMVIAVLLIVSVLSpy 338
Cdd:cd18584 66 ARVKAELRRRLLARLLALGPALLRRQSSGELATLL---TEGVDALDGYFA-RYLpqlvlaaIVPLLILVAVFPLDWVS-- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 339 illmgAIIMVICF---IYYMMFkkaIGVF------KRLENYSRspLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAq 409
Cdd:cd18584 140 -----ALILLVTApliPLFMIL---IGKAaqaasrRQWAALSR--LSGHFLDRLRGLPTLKLFGRARAQAARIARASED- 208
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767990724 410 nnylllFLSSTrwMA-LRLEIMTNLV-----TLAVALfVAFGI 446
Cdd:cd18584 209 ------YRRRT--MKvLRVAFLSSAVleffaTLSIAL-VAVYI 242
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
11-99 |
1.38e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 44.35 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYL-EFCGQIILLENGKICE 89
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVaNYADFVYVLEKGKLVL 225
|
90
....*....|
gi 767990724 90 NGTHSELMQK 99
Cdd:PRK13649 226 SGKPKDIFQD 235
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
11-85 |
1.42e-04 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 45.18 E-value: 1.42e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLRGKTVVLVTHQLQYLEFCGQIILLENG 85
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-LREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
11-75 |
1.43e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.12 E-value: 1.43e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767990724 11 LSGGQKQRISLARAV----YSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEF 75
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAEL 146
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
9-89 |
1.83e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 44.96 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 9 LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVgKHIFEECIKKTLR--GKTVVLVTHQLQYLEFCGQIILLENGK 86
Cdd:PRK10522 448 LKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF-RREFYQVLLPLLQemGKTIFAISHDDHYFIHADRLLEMRNGQ 526
|
...
gi 767990724 87 ICE 89
Cdd:PRK10522 527 LSE 529
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
7-71 |
2.04e-04 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 43.65 E-value: 2.04e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767990724 7 RGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVL-VTHQLQ 71
Cdd:PRK11629 142 RPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLvVTHDLQ 207
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
536-711 |
2.27e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 42.87 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 536 HGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGlEDLRSKLSVIPQDP---VLLSGT--IR 610
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQDLLYLGHQPgikTELTALenLR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 611 FNLDPFDRHTDQQIWDALERTFLTKaiskfpkklhtdvVEN--GGNFSVGERQLLCIARAVLRNSKIILIDEATASIDME 688
Cdd:PRK13538 97 FYQRLHGPGDDEALWEALAQVGLAG-------------FEDvpVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
170 180
....*....|....*....|....
gi 767990724 689 -TDTLIQRTIREAFQGCTVLVIAH 711
Cdd:PRK13538 164 gVARLEALLAQHAEQGGMVILTTH 187
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-111 |
2.42e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 43.44 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDahVGKHI-FEECIKKTLR--GKTVVLVTHQL-QYLEFCGQIILLENGK 86
Cdd:PRK10253 144 LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD--ISHQIdLLELLSELNRekGYTLAAVLHDLnQACRYASHLIALREGK 221
|
90 100
....*....|....*....|....*
gi 767990724 87 ICENGTHSELMQkkgkyAQLIQKMH 111
Cdd:PRK10253 222 IVAQGAPKEIVT-----AELIERIY 241
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
12-45 |
2.62e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 43.80 E-value: 2.62e-04
10 20 30
....*....|....*....|....*....|....
gi 767990724 12 SGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHV 45
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSV 189
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
521-732 |
3.00e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 43.24 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 521 QDYHMKYRDNTptVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALF--RLVEPMAGRILIDGVDICSIGLEDlRSKLSVI 598
Cdd:PRK09580 5 KDLHVSVEDKA--ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED-RAGEGIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 599 P--QDPVLLSGT-----IRFNLDPFDRHTDQQIWDALE-RTFLTKAIS--KFPKKLHTDVVENGgnFSVGERQLLCIARA 668
Cdd:PRK09580 82 MafQYPVEIPGVsnqffLQTALNAVRSYRGQEPLDRFDfQDLMEEKIAllKMPEDLLTRSVNVG--FSGGEKKRNDILQM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767990724 669 VLRNSKIILIDEATASIDMETDTLIQR---TIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVE 732
Cdd:PRK09580 160 AVLEPELCILDESDSGLDIDALKIVADgvnSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVK 226
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-96 |
3.28e-04 |
|
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: 43.50 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHI---FEEcIKKTlRGKTVVLVTHQLQYL-EFCGQIILLENGK 86
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQIlnlLKD-LQRE-LGLAILFITHDLGVVaEIADRVAVMYAGR 228
|
90
....*....|
gi 767990724 87 ICENGTHSEL 96
Cdd:COG0444 229 IVEEGPVEEL 238
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
294-470 |
3.40e-04 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 43.24 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 294 GRLLNCFAGDLEQLDQL-LPIFSEqFLVLSLMVIAVLLIVSVLSPYILLMGAIIM-----VICFIYYMMfKKAIGVFKRl 367
Cdd:cd18585 92 GDLLNRIVADIDTLDNLyLRVLSP-PVVALLVILATILFLAFFSPALALILLAGLllagvVIPLLFYRL-GKKIGQQLV- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 368 enYSRSPLFSHILNSLQGLSSIHVYGKTEdfiSQFKRLTDAQNNYL--------LLFLSSTrWMALRLEIMTNLVTLAVA 439
Cdd:cd18585 169 --QLRAELRTELVDGLQGMAELLIFGALE---RQRQQLEQLSDALIkeqrrlarLSGLSQA-LMILLSGLTVWLVLWLGA 242
|
170 180 190
....*....|....*....|....*....|....*.
gi 767990724 440 LFVAFGISSTPY----SFKVMAV-NIVLQLASSFQA 470
Cdd:cd18585 243 PLVQNGALDGALlamlVFAVLASfEAVAPLPLAFQY 278
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-101 |
3.54e-04 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 42.51 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 7 RGLN--LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEEcIKKTLR-GKTVVLVTHQLQYLEFC--GQIIL 81
Cdd:cd03217 99 RYVNegFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEV-INKLREeGKSVLIITHYQRLLDYIkpDRVHV 177
|
90 100
....*....|....*....|...
gi 767990724 82 LENGKICENGThSELMQ---KKG 101
Cdd:cd03217 178 LYDGRIVKSGD-KELALeieKKG 199
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
237-447 |
4.09e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 42.96 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 237 SFYQLVYGLNALLL--ICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAgDLEQLDQ----- 309
Cdd:cd18566 40 TLQVLVIGVVIAILleSLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERLN-SLEQIREfltgq 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 310 -LLPIFSEQFLVLSLMVIAVLLIVSVLSPyILLMGAIIMVICFIYYMMfKKAIGvfKRLENYSRSplFSHILNSLQGLSS 388
Cdd:cd18566 119 aLLALLDLPFVLIFLGLIWYLGGKLVLVP-LVLLGLFVLVAILLGPIL-RRALK--ERSRADERR--QNFLIETLTGIHT 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 389 IHVYGKTEDFISQFKRLtdaQNNYLLLFLSSTRwMALRLEIMTNLVT-LAVALFVAFGIS 447
Cdd:cd18566 193 IKAMAMEPQMLRRYERL---QANAAYAGFKVAK-INAVAQTLGQLFSqVSMVAVVAFGAL 248
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
11-131 |
4.27e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.19 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIkkTLRGK---TVVLVTHQLQYL-EFCGQIILLENGK 86
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLL--ELQQKenmALVLITHDLALVaEAAHKIIVMYAGQ 231
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 767990724 87 ICENGTHSELMQK-KGKYAQLIQKmhkeATSDMLQDTAKIAEKPKV 131
Cdd:PRK11022 232 VVETGKAHDIFRApRHPYTQALLR----ALPEFAQDKARLASLPGV 273
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
10-113 |
5.02e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.50 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSavdahVGKHIF-EECIKKTL----RGKTVVLVTHQL-QYLEFCGQIILLE 83
Cdd:PRK13546 143 KYSSGMRAKLGFSINITVNPDILVIDEALS-----VGDQTFaQKCLDKIYefkeQNKTIFFVSHNLgQVRQFCTKIAWIE 217
|
90 100 110
....*....|....*....|....*....|
gi 767990724 84 NGKICENGTHSELMQKKGKYAQLIQKMHKE 113
Cdd:PRK13546 218 GGKLKDYGELDDVLPKYEAFLNDFKKKSKA 247
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
270-445 |
5.59e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 42.65 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 270 TALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIMVI 349
Cdd:cd18561 69 QHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 350 CFIYYMMFKKAIGvfKRLENY--SRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAqnnylllFLSSTRWM---- 423
Cdd:cd18561 149 IPLSPALWDRLAK--DTGRRHwaAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAED-------LRQATMKVlavs 219
|
170 180
....*....|....*....|..
gi 767990724 424 ALRLEIMTNLVTLAVALFVAFG 445
Cdd:cd18561 220 LLSSGIMGLATALGTALALGVG 241
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
11-97 |
5.74e-04 |
|
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: 43.25 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIKKTLR--GKTVVLVTHQLQY-LEFCGQIILLENGKI 87
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDP-ITKVDVTHSILKAREemEQTFIIVSHDMDFvLDVCDRAALMRDGKI 506
|
90
....*....|
gi 767990724 88 CENGTHSELM 97
Cdd:TIGR03269 507 VKIGDPEEIV 516
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
10-75 |
6.02e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.26 E-value: 6.02e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDahvgkhIFE-----ECIKKTLRGKTVVLVTHQLQYLEF 75
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLD------IRQrlnvaRLIRELAEGKYVLVVEHDLAVLDY 276
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
656-733 |
6.16e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.02 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 656 SVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIrEAFQGcTVLVIAH-RV---TTVLNCdhILVMGNGKVV 731
Cdd:PRK11147 442 SGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELL-DSYQG-TVLLVSHdRQfvdNTVTEC--WIFEGNGKIG 517
|
..
gi 767990724 732 EF 733
Cdd:PRK11147 518 RY 519
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
11-69 |
6.46e-04 |
|
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: 43.20 E-value: 6.46e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKtlrGKTVVLVTHQ 69
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF---GITLFSVSHR 638
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
11-76 |
6.53e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 41.47 E-value: 6.53e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQ------LQYLEFC 76
Cdd:PRK13540 128 LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQdlplnkADYEEYH 199
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
10-87 |
7.09e-04 |
|
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: 41.87 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQ--LQYLEFCGQIILLENGKI 87
Cdd:cd03234 143 GISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQprSDLFRLFDRILLLSSGEI 222
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
11-99 |
7.11e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 42.05 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFeECIKKTLRGK--TVVLVTHQLQYLEFCGQIILLENGKIC 88
Cdd:PRK13648 143 LSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLL-DLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVY 221
|
90
....*....|.
gi 767990724 89 ENGTHSELMQK 99
Cdd:PRK13648 222 KEGTPTEIFDH 232
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
7-97 |
7.17e-04 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 41.89 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 7 RGLNLSGGQKQRISLARAVYSDRQIYLLDDP---LSAVdahVGKHIFeECIKKtLR--GKTVVLVTHQLQY-LEFCGQII 80
Cdd:COG0410 133 RAGTLSGGEQQMLAIGRALMSRPKLLLLDEPslgLAPL---IVEEIF-EIIRR-LNreGVTILLVEQNARFaLEIADRAY 207
|
90
....*....|....*..
gi 767990724 81 LLENGKICENGTHSELM 97
Cdd:COG0410 208 VLERGRIVLEGTAAELL 224
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
11-98 |
7.25e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 41.99 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFE--ECIKKTlRGKTVVLVTHQLQYLEFCG-QIILLENGKI 87
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDllESIVQK-RALGMLLVTHDMGVVARLAdDVAVMSHGRI 219
|
90
....*....|.
gi 767990724 88 CENGTHSELMQ 98
Cdd:PRK10418 220 VEQGDVETLFN 230
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
8-98 |
7.46e-04 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 41.76 E-value: 7.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 8 GLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEecIKKTLRGKTV-VLVT-HQL-QYLEFCGQIILLEN 84
Cdd:cd03218 131 ASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQK--IIKILKDRGIgVLITdHNVrETLSITDRAYIIYE 208
|
90
....*....|....
gi 767990724 85 GKICENGTHSELMQ 98
Cdd:cd03218 209 GKVLAEGTPEEIAA 222
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
11-100 |
7.56e-04 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 42.89 E-value: 7.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQL-QYLEFCGQIILLENGKICE 89
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELaEVLGLSDRVLVIGEGKLKG 483
|
90
....*....|.
gi 767990724 90 NGTHSELMQKK 100
Cdd:TIGR02633 484 DFVNHALTQEQ 494
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
232-446 |
8.13e-04 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 42.07 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 232 DNPQLSFYQLVYGLNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLL 311
Cdd:cd18545 35 DLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 312 -----PIFSEQFLVlsLMVIAVLLIVSV-LSpyiLLMGAIIMVICFIYYMMFKKAIGVFKRLENySRSPLFSHILNSLQG 385
Cdd:cd18545 115 sngliNLIPDLLTL--VGIVIIMFSLNVrLA---LVTLAVLPLLVLVVFLLRRRARKAWQRVRK-KISNLNAYLHESISG 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767990724 386 LSSIHVYGKTEDFISQFKRLtdaQNNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGI 446
Cdd:cd18545 189 IRVIQSFAREDENEEIFDEL---NRENRKANMRAVRLNALFWPLVELISALGTALVYWYGG 246
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
260-446 |
8.21e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 42.11 E-value: 8.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 260 IFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNcFAGDLEQLDQLLpifSEQFLVL---SLMVIAVLLIVSVLS 336
Cdd:cd18555 65 IIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLF-RANSNVYIRQIL---SNQVISLiidLLLLVIYLIYMLYYS 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 337 PYILLMGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLtdaQNNYLLLF 416
Cdd:cd18555 141 PLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENL---FKKQLKAF 217
|
170 180 190
....*....|....*....|....*....|
gi 767990724 417 LSSTRWMALRLEIMTNLVTLAVALFVAFGI 446
Cdd:cd18555 218 KKKERLSNILNSISSSIQFIAPLLILWIGA 247
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-87 |
9.28e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 42.36 E-value: 9.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDP-----LSAVDAhvgkhiFEECIKKtlRGKTVVLVTHQLQYL-EFCGQIILLE 83
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPtnhldLESIEW------LEEFLKN--YPGTVLVVSHDRYFLdRVATRILELD 223
|
....
gi 767990724 84 NGKI 87
Cdd:COG0488 224 RGKL 227
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
12-44 |
9.53e-04 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 41.27 E-value: 9.53e-04
10 20 30
....*....|....*....|....*....|...
gi 767990724 12 SGGQKQRISLARAVYSDRQIYLLDDPLSAVDAH 44
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAA 186
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
11-92 |
1.01e-03 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 41.64 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHvGKHIFEECIKKTLR--GKTVVLVTHQLQYLEFCGQIILLENGKIC 88
Cdd:PRK09544 121 LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN-GQVALYDLIDQLRRelDCAVLMVSHDLHLVMAKTDEVLCLNHHIC 199
|
....
gi 767990724 89 ENGT 92
Cdd:PRK09544 200 CSGT 203
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
6-97 |
1.06e-03 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 41.40 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 6 ERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQL-QYLEFCGQIILLEN 84
Cdd:PRK11614 133 QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnQALKLADRGYVLEN 212
|
90
....*....|...
gi 767990724 85 GKICENGTHSELM 97
Cdd:PRK11614 213 GHVVLEDTGDALL 225
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
230-353 |
1.12e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 41.76 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 230 IADNPQLSFYQLVYGLnALLLICVGVCS---SGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQ 306
Cdd:cd18572 27 VADGSREAFYRAVLLL-LLLSVLSGLFSglrGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQK 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 767990724 307 LDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIM-VICFIY 353
Cdd:cd18572 106 VSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVpVIALIT 153
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
12-121 |
1.15e-03 |
|
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: 42.69 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 12 SGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLE-FCGQIILLENGKICEN 90
Cdd:TIGR01257 2072 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEaLCTRLAIMVKGAFQCL 2151
|
90 100 110
....*....|....*....|....*....|.
gi 767990724 91 GTHSELMQKKGKYAQLIQKMhKEATSDMLQD 121
Cdd:TIGR01257 2152 GTIQHLKSKFGDGYIVTMKI-KSPKDDLLPD 2181
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-113 |
1.15e-03 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 41.53 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIKKTL-RGKTVVLVTHQLQYL-EFCGQIILLENGKIC 88
Cdd:PRK13638 137 LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP-AGRTQMIAIIRRIVaQGNHVIISSHDIDLIyEISDAVYVLRQGQIL 215
|
90 100 110
....*....|....*....|....*....|.
gi 767990724 89 ENG------THSELMQKKGKYAQLIQKMHKE 113
Cdd:PRK13638 216 THGapgevfACTEAMEQAGLTQPWLVKLHTQ 246
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
6-120 |
1.26e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.46 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 6 ERGLNLSGGQKQRISLARAVYS-DRQIYLLDDPLSAVDAHVGKHIfEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLEN 84
Cdd:PTZ00243 1441 EGGSNYSVGQRQLMCMARALLKkGSGFILMDEATANIDPALDRQI-QATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDH 1519
|
90 100 110
....*....|....*....|....*....|....*..
gi 767990724 85 GKICENGTHSEL-MQKKGKYAQLIQKMHKEATSDMLQ 120
Cdd:PTZ00243 1520 GAVAEMGSPRELvMNRQSIFHSMVEALGRSEAKRFLQ 1556
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
653-740 |
1.37e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.02 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 653 GNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIRE-AFQGCTVLVIAHRVTTVLN-CDHILVMGNGKV 730
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAElAKKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
|
90
....*....|....*.
gi 767990724 731 V------EFDRPEVLR 740
Cdd:PRK10982 470 AgivdtkTTTQNEILR 485
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
9-70 |
1.48e-03 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 41.01 E-value: 1.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767990724 9 LNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHI---FEECIKKtlrGKTVVLVTHQL 70
Cdd:PRK10908 136 IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGIlrlFEEFNRV---GVTVLMATHDI 197
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
533-735 |
1.53e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 41.79 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 533 TVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEP--MAGRILIDGVDICsiglEDLRSKLSVIPQDPVLLSG-TI 609
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGnnFTGTILANNRKPT----KQILKRTGFVTQDDILYPHlTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 610 RFNLdpfdrhtdqqIWDALERtfLTKAISKFPKKLHTDVV---------EN---GGNF----SVGERQLLCIARAVLRNS 673
Cdd:PLN03211 158 RETL----------VFCSLLR--LPKSLTKQEKILVAESViselgltkcENtiiGNSFirgiSGGERKRVSIAHEMLINP 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767990724 674 KIILIDEATASIDMETD-TLIQRTIREAFQGCTVLVIAH----RVTTVLncDHILVMGNGKVVEFDR 735
Cdd:PLN03211 226 SLLILDEPTSGLDATAAyRLVLTLGSLAQKGKTIVTSMHqpssRVYQMF--DSVLVLSEGRCLFFGK 290
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
517-576 |
1.61e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 41.23 E-value: 1.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767990724 517 EIIFQDYHMKYRDNTPT---VLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRI 576
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI 64
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
227-445 |
1.66e-03 |
|
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: 41.32 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 227 LGNIADNPQLSFYQLVYGLNALLLICV----GVCSSG---IFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNC 299
Cdd:cd18576 19 AGQLIDAALGGGDTASLNQIALLLLGLfllqAVFSFFriyLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 300 FAGDLEQLDQ----LLPIFSEQFLVLslmVIAVLLIVSVLSPYILLMGAIIMVICFIyymmfkkAIGVFKRLENYSR--- 372
Cdd:cd18576 99 LSNDVTQIQDtlttTLAEFLRQILTL---IGGVVLLFFISWKLTLLMLATVPVVVLV-------AVLFGRRIRKLSKkvq 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767990724 373 ---SPLFSHILNSLQGLSSIHVYGKtEDF-ISQFKRLTDAqnnYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFG 445
Cdd:cd18576 169 delAEANTIVEETLQGIRVVKAFTR-EDYeIERYRKALER---VVKLALKRARIRALFSSFIIFLLFGAIVAVLWYG 241
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
547-567 |
2.01e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 40.90 E-value: 2.01e-03
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-86 |
2.01e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.25 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 6 ERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQL-QYLEFCGQIILLEN 84
Cdd:PRK10982 130 AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMeEIFQLCDEITILRD 209
|
..
gi 767990724 85 GK 86
Cdd:PRK10982 210 GQ 211
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
11-42 |
2.33e-03 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 40.87 E-value: 2.33e-03
10 20 30
....*....|....*....|....*....|..
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVD 42
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
11-80 |
2.33e-03 |
|
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: 39.61 E-value: 2.33e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767990724 11 LSGGQKQRISLARAVYSD--RQIYLLDDPLSAVDaHVGKHIFEECIKKTL-RGKTVVLVTHQLQYLEFCGQII 80
Cdd:cd03238 88 LSGGELQRVKLASELFSEppGTLFILDEPSTGLH-QQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWII 159
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-87 |
2.79e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 40.45 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFE---ECIKKtlRGKTVVLVTHQLQY-LEFCGQIILLENG 85
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLElteKIVEE--NNLTTLMVTHNMEQaLDYGNRLIMMHEG 225
|
..
gi 767990724 86 KI 87
Cdd:COG1101 226 RI 227
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
6-99 |
3.04e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 6 ERGLN-LSGGQKQRISLARAVYSDRQ--IYLLDDP---LSAVDAHvgKHIfeECIKKtLR--GKTVVLVTHQLQYLEFCG 77
Cdd:PRK00635 471 ERALAtLSGGEQERTALAKHLGAELIgiTYILDEPsigLHPQDTH--KLI--NVIKK-LRdqGNTVLLVEHDEQMISLAD 545
|
90 100
....*....|....*....|....*...
gi 767990724 78 QIILLE------NGKICENGTHSELMQK 99
Cdd:PRK00635 546 RIIDIGpgagifGGEVLFNGSPREFLAK 573
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
12-87 |
3.14e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 3.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767990724 12 SGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTlrgKTVVLVTHQLQYLE-FCGQIILLENGKI 87
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP---KTFIVVSHAREFLNtVVTDILHLHGQKL 419
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
272-408 |
3.37e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 40.19 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 272 LHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIM-VIC 350
Cdd:cd18563 78 LRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVpLVV 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 351 FIYYMMFKKAIGVFKRLENySRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDA 408
Cdd:cd18563 158 WGSYFFWKKIRRLFHRQWR-RWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQE 214
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-91 |
3.59e-03 |
|
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: 39.62 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAhVGKHIFEECIKK--TLRGKTVVLVTHQLQYLE-FCGQIILLENGK 86
Cdd:cd03267 153 QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV-VAQENIRNFLKEynRERGTTVLLTSHYMKDIEaLARRVLVIDKGR 231
|
....*
gi 767990724 87 ICENG 91
Cdd:cd03267 232 LLYDG 236
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
4-80 |
3.65e-03 |
|
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: 39.91 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 4 IGERGLNLSGGQKQRISLARAVY---SDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQII 80
Cdd:cd03271 163 LGQPATTLSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWII 242
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
272-445 |
4.16e-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: 40.10 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 272 LHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIMVICF 351
Cdd:cd18554 81 IRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 352 IYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKrltDAQNNYLLLFLSSTRWMALRLEIMT 431
Cdd:cd18554 161 LAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFD---KRNGHFLTRALKHTRWNAKTFSAVN 237
|
170
....*....|....
gi 767990724 432 NLVTLAVALFVAFG 445
Cdd:cd18554 238 TITDLAPLLVIGFA 251
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-110 |
4.20e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 40.39 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEecIKKTLR--GKTVVLVTHQL-QYLEFCGQIILLENGK 86
Cdd:COG1129 140 DLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFR--IIRRLKaqGVAIIYISHRLdEVFEIADRVTVLRDGR 217
|
90 100
....*....|....*....|....
gi 767990724 87 ICENGTHSELmqkkgKYAQLIQKM 110
Cdd:COG1129 218 LVGTGPVAEL-----TEDELVRLM 236
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
11-161 |
5.04e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 39.69 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVD----AHVGKHIFEECIKKTLrgkTVVLVTHQLQYLEFCGQIILLENGK 86
Cdd:PRK13642 141 LSGGQKQRVAVAGIIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQL---TVLSITHDLDEAASSDRILVMKAGE 217
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767990724 87 ICENGTHSELMqkkgkyaqliqkmhkeATSdmlQDTAKIAEKPKVESQALAtslEESLNGNAVPEHQLTQEEEME 161
Cdd:PRK13642 218 IIKEAAPSELF----------------ATS---EDMVEIGLDVPFSSNLMK---DLRKNGFDLPEKYLSEDELVE 270
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
247-445 |
5.06e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 39.78 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 247 ALLLICVGVCSSGIFTKVTRKAST----ALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLV-- 320
Cdd:cd18546 45 YLAVVLAGWVAQRAQTRLTGRTGErllyDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVsl 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 321 LSLMVIAVLLIvsVLSPYILLMGAIIMVICFIyymmfkkAIGVFKRLEN--YSR-----SPLFSHILNSLQGLSSIHVYG 393
Cdd:cd18546 125 LTLVGIAVVLL--VLDPRLALVALAALPPLAL-------ATRWFRRRSSraYRRareriAAVNADLQETLAGIRVVQAFR 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767990724 394 KTEDFISQFKRLTDAqnnYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFG 445
Cdd:cd18546 196 RERRNAERFAELSDD---YRDARLRAQRLVAIYFPGVELLGNLATAAVLLVG 244
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
11-97 |
5.66e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 39.39 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 11 LSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFE---ECIKKtlRGKTVVLVTHQLQYLE-FCGQIILLENGK 86
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINlmlELQEK--QGISYIYVTQHLGMMKhISDQVLVMHQGE 227
|
90
....*....|.
gi 767990724 87 ICENGTHSELM 97
Cdd:PRK15112 228 VVERGSTADVL 238
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
10-80 |
8.09e-03 |
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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: 38.89 E-value: 8.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDahVGKHIFEECIKKTL--RGKTVVLVTHQLQYLEFCGQII 80
Cdd:cd03236 139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLD--IKQRLNAARLIRELaeDDNYVLVVEHDLAVLDYLSDYI 209
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| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
527-580 |
8.40e-03 |
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sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 39.06 E-value: 8.40e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 767990724 527 YRDNTPtVLHGINLTIRGHEVVGIVGRTGSGKSSlgmaLFRLV---EPM-AGRILIDG 580
Cdd:PRK11650 13 YDGKTQ-VIKGIDLDVADGEFIVLVGPSGCGKST----LLRMVaglERItSGEIWIGG 65
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| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
10-87 |
9.13e-03 |
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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: 38.48 E-value: 9.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990724 10 NLSGGQKQRISLARAVYSDRQIYLLDDP---LSAVD-AHVGKHIFEecIKKTlRGKTVVLVTHQLQYL-EFCGQIILLEN 84
Cdd:COG0411 152 NLSYGQQRRLEIARALATEPKLLLLDEPaagLNPEEtEELAELIRR--LRDE-RGITILLIEHDMDLVmGLADRIVVLDF 228
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...
gi 767990724 85 GKI 87
Cdd:COG0411 229 GRV 231
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