|
Name |
Accession |
Description |
Interval |
E-value |
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
7-508 |
0e+00 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 761.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 7 PARLQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLGI 86
Cdd:COG3845 3 PPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 87 GMVFQHFSLFETLSVAQNIALAMGAAAGT---PKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRL 163
Cdd:COG3845 83 GMVHQHFMLVPNLTVAENIVLGLEPTKGGrldRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 164 LILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAECSDLELARLMVGDAE 243
Cdd:COG3845 163 LILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMVGREV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 244 GLTAHYDKVSGSEAFLRVDKLSWHNPDPfGCSLKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGEQTlphAQATTLRFQ 323
Cdd:COG3845 243 LLRVEKAPAEPGEVVLEVENLSVRDDRG-VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRP---PASGSIRLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 324 DTPVGDLRPDARRKHGLAFVPAERLGHGAVPELSLADNALLTAF-QQGLVSHGLIQRGKVRALADEIIRRFAVKTTDAQA 402
Cdd:COG3845 319 GEDITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGRYrRPPFSRGGFLDRKAIRAFAEELIEEFDVRTPGPDT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 403 AARSLSGGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSGG 482
Cdd:COG3845 399 PARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEG 478
|
490 500
....*....|....*....|....*.
gi 488618663 483 QLSDLIPTEQTSTVQIGGWMAGQFDH 508
Cdd:COG3845 479 RIVGEVPAAEATREEIGLLMAGVKEE 504
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-498 |
9.28e-176 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 504.17 E-value: 9.28e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 7 PARLQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLGI 86
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 87 GMVFQHFSLFETLSVAQNIALA-MGAAAGT--PKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRL 163
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFLGrEPRRGGLidWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 164 LILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAECSDLELARLMVGDAE 243
Cdd:COG1129 162 LILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVGREL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 244 GLTAHYDKVSGSEAFLRVDKLSWHNpdpfgcSLKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtLPHAQATTLRFQ 323
Cdd:COG1129 242 EDLFPKRAAAPGEVVLEVEGLSVGG------VVRDVSFSVRAGEILGIAGLVGAGRTELARALFG---ADPADSGEIRLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 324 DTPVGDLRPDARRKHGLAFVPAERLGHGAVPELSLADNALLTAFQQgLVSHGLIQRGKVRALADEIIRRFAVKTTDAQAA 403
Cdd:COG1129 313 GKPVRIRSPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDR-LSRGGLLDRRRERALAEEYIKRLRIKTPSPEQP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 404 ARSLSGGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSGGQ 483
Cdd:COG1129 392 VGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGR 471
|
490
....*....|....*
gi 488618663 484 LSDLIPTEQTSTVQI 498
Cdd:COG1129 472 IVGELDREEATEEAI 486
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-516 |
2.55e-109 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 334.71 E-value: 2.55e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 2 SNHAIPARLQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQA 81
Cdd:PRK15439 4 SDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 82 RSLGIGMVFQHFSLFETLSVAQNIALAMGAAAGTPKQLEPRIREVsqryGMAVEPQRLVHSLSIGERQKVEIIRCLMQDI 161
Cdd:PRK15439 84 HQLGIYLVPQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAAL----GCQLDLDSSAGSLEVADRQIVEILRGLMRDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 162 RLLILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAECSDLELARLM--V 239
Cdd:PRK15439 160 RILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAItpA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 240 GDAEGLTA----------HYDKVSGSEAFLRVDKLSwhnpdpfGCSLKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGe 309
Cdd:PRK15439 240 AREKSLSAsqklwlelpgNRRQQAAGAPVLTVEDLT-------GEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYG- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 310 qtLPHAQATTLRFQDTPVGDLRPDARRKHGLAFVPAERLGHGAVPELSLADNAL-LTAFQQGLvshgLIQRGKVRALADE 388
Cdd:PRK15439 312 --LRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWNVCaLTHNRRGF----WIKPARENAVLER 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 389 IIRRFAVKTTDAQAAARSLSGGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIALRDAGAAILVISEDLDE 468
Cdd:PRK15439 386 YRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEE 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 488618663 469 LFQISDRLAALSGGQLSDLIPTEQTSTVQIggwMAGQFDHSHTQAHTA 516
Cdd:PRK15439 466 IEQMADRVLVMHQGEISGALTGAAINVDTI---MRLAFGEHQAQEASC 510
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
7-498 |
2.57e-104 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 321.48 E-value: 2.57e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 7 PARLQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLGI 86
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 87 GMVFQHFSLFETLSVAQNIAL-AMGAAAG--TPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRL 163
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLYLgQLPHKGGivNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 164 LILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNG-KVSGHCIPAECSDLELARLMVGDA 242
Cdd:PRK11288 162 IAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGrYVATFDDMAQVDRDQLVQAMVGRE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 243 EGLTAHYDKVSGSEAFLRVDKLSwhnpdpfGCSLK-DLSLEVRSGEIVGIAGVAGNGQDELLALLSGeQTLPHAQATTLR 321
Cdd:PRK11288 242 IGDIYGYRPRPLGEVRLRLDGLK-------GPGLRePISFSVRAGEIVGLFGLVGAGRSELMKLLYG-ATRRTAGQVYLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 322 FQDTPVGDLRpDARRkHGLAFVPAERLGHGAVPELSLADNALLTAFQQGLVSHGLIQRGKVRALADEIIRRFAVKTTDAQ 401
Cdd:PRK11288 314 GKPIDIRSPR-DAIR-AGIMLCPEDRKAEGIIPVHSVADNINISARRHHLRAGCLINNRWEAENADRFIRSLNIKTPSRE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 402 AAARSLSGGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSG 481
Cdd:PRK11288 392 QLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMRE 471
|
490
....*....|....*..
gi 488618663 482 GQLSDLIPTEQTSTVQI 498
Cdd:PRK11288 472 GRIAGELAREQATERQA 488
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
10-493 |
4.07e-100 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 310.71 E-value: 4.07e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVtQPDA---GSIIWQGQAQTMRNPAQARSLGI 86
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHGtyeGEIIFEGEELQASNIRDTERAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 87 GMVFQHFSLFETLSVAQNIALAmgaAAGTPK------QLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQD 160
Cdd:PRK13549 85 AIIHQELALVKELSVLENIFLG---NEITPGgimdydAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 161 IRLLILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAECSDLELARLMVG 240
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMMVG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 241 daEGLTAHYDKVSGS--EAFLRVDKLS-WHNPDPFGCSLKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqTLPHAQA 317
Cdd:PRK13549 242 --RELTALYPREPHTigEVILEVRNLTaWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG--AYPGRWE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 318 TTLRFQDTPVGDLRPDARRKHGLAFVPAERLGHGAVPELSLADNALLTAFQQgLVSHGLIQRGKVRALADEIIRRFAVKT 397
Cdd:PRK13549 318 GEIFIDGKPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDR-FTGGSRIDDAAELKTILESIQRLKVKT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 398 TDAQAAARSLSGGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLA 477
Cdd:PRK13549 397 ASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVL 476
|
490
....*....|....*..
gi 488618663 478 ALSGGQL-SDLIPTEQT 493
Cdd:PRK13549 477 VMHEGKLkGDLINHNLT 493
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
10-492 |
7.24e-96 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 299.61 E-value: 7.24e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLGIGMV 89
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHFSLFETLSVAQNIAL------AMGAAAGtpKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRL 163
Cdd:PRK10762 85 HQELNLIPQLTIAENIFLgrefvnRFGRIDW--KKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 164 LILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAECSDLELARLMVG-DA 242
Cdd:PRK10762 163 IIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVGrKL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 243 EGLTAHYDKVSGsEAFLRVDKLSwhnpdpfGCSLKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqTLPHAQAtTLRF 322
Cdd:PRK10762 243 EDQYPRLDKAPG-EVRLKVDNLS-------GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYG--ALPRTSG-YVTL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 323 QDTPVGDLRPDARRKHGLAFVPAERLGHGAVPELSLADNALLTAFQQGLVSHGLIQRGKVRALADEIIRRFAVKTTDAQA 402
Cdd:PRK10762 312 DGHEVVTRSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYFSRAGGSLKHADEQQAVSDFIRLFNIKTPSMEQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 403 AARSLSGGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSGG 482
Cdd:PRK10762 392 AIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEG 471
|
490
....*....|
gi 488618663 483 QLSDLIPTEQ 492
Cdd:PRK10762 472 RISGEFTREQ 481
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
10-495 |
1.18e-95 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 299.39 E-value: 1.18e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLGIGMV 89
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHFSLFETLSVAQNIALA-------MGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIR 162
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGrhltkkvCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 163 LLILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAECSDLELARLMVGDA 242
Cdd:PRK09700 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVGRE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 243 -----EGLTAHYDKVSGSEAFlRVDKLSWHNPDpfgcSLKDLSLEVRSGEIVGIAGVAGNGQDELLALL-------SGEQ 310
Cdd:PRK09700 246 lqnrfNAMKENVSNLAHETVF-EVRNVTSRDRK----KVRDISFSVCRGEILGFAGLVGSGRTELMNCLfgvdkraGGEI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 311 TLpHAQATTLRfqdTPVgdlrpDARRKhGLAFVPAERLGHGAVPELSLADN-ALLTAFQQGLV--SHGLIQRGKVRALAD 387
Cdd:PRK09700 321 RL-NGKDISPR---SPL-----DAVKK-GMAYITESRRDNGFFPNFSIAQNmAISRSLKDGGYkgAMGLFHEVDEQRTAE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 388 EIIRRFAVKTTDAQAAARSLSGGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIALRDAGAAILVISEDLD 467
Cdd:PRK09700 391 NQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELP 470
|
490 500
....*....|....*....|....*...
gi 488618663 468 ELFQISDRLAALSGGQLSDLIPTEQTST 495
Cdd:PRK09700 471 EIITVCDRIAVFCEGRLTQILTNRDDMS 498
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
12-498 |
6.80e-87 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 276.23 E-value: 6.80e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 12 LRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLGIGMVFQ 91
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 92 HFSLFETLSVAQNIALAMGAAAG---TPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDE 168
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGRYPTKGmfvDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 169 PTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKVSGhCIPAECSDLE-LARLMVGDAegLTA 247
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIA-TQPLAGLTMDkIIAMMVGRS--LTQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 248 HYDKVSGS--EAFLRVDKLSWHNpDPfgcSLKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtLPHAQATTLRFQDT 325
Cdd:PRK10982 238 RFPDKENKpgEVILEVRNLTSLR-QP---SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFG---IREKSAGTITLHGK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 326 PVGDLRPDARRKHGLAFVPAERLGHGAVPELSLADNALLTAFQQGLVSHGLIQRGKVRALADEIIRRFAVKTTDAQAAAR 405
Cdd:PRK10982 311 KINNHNANEAINHGFALVTEERRSTGIYAYLDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 406 SLSGGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSGGQLS 485
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVA 470
|
490
....*....|...
gi 488618663 486 DLIPTEQTSTVQI 498
Cdd:PRK10982 471 GIVDTKTTTQNEI 483
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
10-494 |
4.16e-85 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 271.66 E-value: 4.16e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVtQPDA---GSIIWQGQAQTMRNPAQARSLGI 86
Cdd:NF040905 2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHGsyeGEILFDGEVCRFKDIRDSEALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 87 GMVFQHFSLFETLSVAQNIALAMGAAAG-------TPKqlepRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQ 159
Cdd:NF040905 81 VIIHQELALIPYLSIAENIFLGNERAKRgvidwneTNR----RARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 160 DIRLLILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV--SGHCIPAECSDLELARL 237
Cdd:NF040905 157 DVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTieTLDCRADEVTEDRIIRG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 238 MVGdaEGLTAHYDK--VSGSEAFLRVDKLSWHNP-DPFGCSLKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeQTLPH 314
Cdd:NF040905 237 MVG--RDLEDRYPErtPKIGEVVFEVKNWTVYHPlHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFG-RSYGR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 315 AQATTLRFQDTPVgDLR--PDArRKHGLAFVPAERLGHGAVPELSLADNALLTAFqQGLVSHGLIQRGKVRALADEIIRR 392
Cdd:NF040905 314 NISGTVFKDGKEV-DVStvSDA-IDAGLAYVTEDRKGYGLNLIDDIKRNITLANL-GKVSRRGVIDENEEIKVAEEYRKK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 393 FAVKTTDAQAAARSLSGGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQI 472
Cdd:NF040905 391 MNIKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGM 470
|
490 500
....*....|....*....|..
gi 488618663 473 SDRLAALSGGQLSDLIPTEQTS 494
Cdd:NF040905 471 CDRIYVMNEGRITGELPREEAS 492
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
10-493 |
6.82e-84 |
|
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: 268.62 E-value: 6.82e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVtQPDA---GSIIWQGQAQTMRNPAQARSLGI 86
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHGtwdGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 87 GMVFQHFSLFETLSVAQNIALA---------MGAAAGTpKQLEPRIREVSQRygmAVEPQRLVHSLSIGERQKVEIIRCL 157
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGneitlpggrMAYNAMY-LRAKNLLRELQLD---ADNVTRPVGDYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 158 MQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAECSDLELARL 237
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 238 MVG-DAEGLTAHYDKVSGSEaFLRVDKLS-WHNPDPFGCSLKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqTLPHA 315
Cdd:TIGR02633 237 MVGrEITSLYPHEPHEIGDV-ILEARNLTcWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG--AYPGK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 316 QATTLRFQDTPVGDLRPDARRKHGLAFVPAERLGHGAVPELSLADNALLTAFQQgLVSHGLIQRGKVRALADEIIRRFAV 395
Cdd:TIGR02633 314 FEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKS-FCFKMRIDAAAELQIIGSAIQRLKV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 396 KTTDAQAAARSLSGGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDR 475
Cdd:TIGR02633 393 KTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDR 472
|
490
....*....|....*....
gi 488618663 476 LAALSGGQL-SDLIPTEQT 493
Cdd:TIGR02633 473 VLVIGEGKLkGDFVNHALT 491
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-223 |
3.24e-79 |
|
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: 244.65 E-value: 3.24e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLGIGMV 89
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQhfslfetlsvaqnialamgaaagtpkqleprirevsqrygmavepqrlvhsLSIGERQKVEIIRCLMQDIRLLILDEP 169
Cdd:cd03216 81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488618663 170 TSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKVSGH 223
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
256-484 |
1.01e-66 |
|
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: 213.06 E-value: 1.01e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 256 EAFLRVDKLSWHNpdpfgcSLKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtLPHAQATTLRFQDTPVGDLRPDAR 335
Cdd:cd03215 2 EPVLEVRGLSVKG------AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFG---LRPPASGEITLDGKPVTRRSPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 336 RKHGLAFVPAERLGHGAVPELSLADNALLTAFqqglvshgliqrgkvraladeiirrfavkttdaqaaarsLSGGNLQKF 415
Cdd:cd03215 73 IRAGIAYVPEDRKREGLVLDLSVAENIALSSL---------------------------------------LSGGNQQKV 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488618663 416 ILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSGGQL 484
Cdd:cd03215 114 VLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-492 |
3.18e-60 |
|
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: 206.68 E-value: 3.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGC--LANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDA---GSIIWQGQaQTMRNPAQARSL 84
Cdd:COG1123 5 LEVRDLSVRYPGGdvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGR-DLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 85 GIGMVFQHF-SLFETLSVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRL 163
Cdd:COG1123 84 RIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 164 LILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAE--CSDLELARLMVG 240
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEilAAPQALAAVPRL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 241 DAEGLTAHyDKVSGSEAFLRVDKLSWHNPDPFGCS---LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtLPHAQA 317
Cdd:COG1123 244 GAARGRAA-PAAAAAEPLLEVRNLSKRYPVRGKGGvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLG---LLRPTS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 318 TTLRFQDTPVGDLRPDARRKHGLAFvpaerlghGAV---PELSLadNALLTAFQQ---GLVSHGLIQRGKVRALADEIIR 391
Cdd:COG1123 320 GSILFDGKDLTKLSRRSLRELRRRV--------QMVfqdPYSSL--NPRMTVGDIiaePLRLHGLLSRAERRERVAELLE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 392 RFAVKTTDAQAAARSLSGGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIALRDA-GAAILVISEDLDELF 470
Cdd:COG1123 390 RVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVR 469
|
490 500
....*....|....*....|..
gi 488618663 471 QISDRLAALSGGQLSDLIPTEQ 492
Cdd:COG1123 470 YIADRVAVMYDGRIVEDGPTEE 491
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
10-228 |
4.95e-59 |
|
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: 194.96 E-value: 4.95e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLGIGMV 89
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHFSLFETLSVAQNIALAMGAAAGTP----------KQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQ 159
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSGlllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488618663 160 DIRLLILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAE 228
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
10-220 |
1.68e-57 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 191.05 E-value: 1.68e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTmRNPAQARSLgIGMV 89
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA-RDPAEVRRR-IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHFSLFETLSVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEP 169
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488618663 170 TSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
10-220 |
1.32e-53 |
|
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: 181.39 E-value: 1.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLGIGMV 89
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIART 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHFSLFETLSVAQNIALAMGAAAGTP---------------KQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEII 154
Cdd:COG0411 85 FQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreeREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488618663 155 RCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:COG0411 165 RALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
10-220 |
1.54e-50 |
|
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: 170.66 E-value: 1.54e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQaQTMRNPAQARSLgIGMV 89
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGK-DIKKEPEEVKRR-IGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHFSLFETLSVAQNIalamgaaagtpkqleprirevsqrygmavepqrlvhSLSIGERQKVEIIRCLMQDIRLLILDEP 169
Cdd:cd03230 79 PEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488618663 170 TSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
10-220 |
1.15e-47 |
|
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: 165.42 E-value: 1.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTmRNPAQARSLgIGMV 89
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR-KEPREARRQ-IGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHFSLFETLSVAQNIALAmGAAAGTP-KQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDE 168
Cdd:COG4555 80 PDERGLYDRLTVRENIRYF-AELYGLFdEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488618663 169 PTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:COG4555 159 PTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
10-220 |
6.10e-46 |
|
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: 159.61 E-value: 6.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRnPAQARslGIGMV 89
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV-PPERR--NIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHFSLFETLSVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEP 169
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488618663 170 TSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:cd03259 158 LSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
10-220 |
1.53e-44 |
|
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: 156.37 E-value: 1.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRY----PGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAqTMRNPAQARSlG 85
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFD-VVKEPAEARR-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 86 IGMVFQHFSLFETLSVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLI 165
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488618663 166 LDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
11-219 |
1.72e-43 |
|
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: 153.01 E-value: 1.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 11 QLRHITKRYPGCLAN--DAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQaRSLGIGM 88
Cdd:cd03225 1 ELKNLSFSYPDGARPalDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE-LRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 89 VFQHFSL-FETLSVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILD 167
Cdd:cd03225 80 VFQNPDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488618663 168 EPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGK 219
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
12-220 |
1.96e-43 |
|
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: 153.89 E-value: 1.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 12 LRHITKRYPG----CLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSL--G 85
Cdd:cd03258 4 LKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKArrR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 86 IGMVFQHFSLFETLSVAQNIALAMgAAAGTPK-QLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLL 164
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFENVALPL-EIAGVPKaEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488618663 165 ILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:cd03258 163 LCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
10-220 |
2.33e-43 |
|
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: 153.36 E-value: 2.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLGIGMV 89
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHFSLFETLSVAQNiaLAMGAAAGTPKQLEPRIREV-------SQRYGmavepqRLVHSLSIGERQKVEIIRCLMQDIR 162
Cdd:cd03224 81 PEGRRIFPELTVEEN--LLLGAYARRRAKRKARLERVyelfprlKERRK------QLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488618663 163 LLILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRV 210
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
10-220 |
7.47e-41 |
|
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: 146.48 E-value: 7.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLAN----DAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQ-AQTMRNPAQA--R 82
Cdd:cd03255 1 IELKNLSKTYGGGGEKvqalKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdISKLSEKELAafR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 83 SLGIGMVFQHFSLFETLSVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIR 162
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488618663 163 LLILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLgEVRALCHSATVLRNGKV 220
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
10-222 |
1.14e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 145.96 E-value: 1.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYP-GCLANDA---VDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQA-QTMRNPAQA--R 82
Cdd:COG1136 5 LELRNLTKSYGtGEGEVTAlrgVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDiSSLSERELArlR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 83 SLGIGMVFQHFSLFETLSVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIR 162
Cdd:COG1136 85 RRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488618663 163 LLILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLgEVRALCHSATVLRNGKVSG 222
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDP-ELAARADRVIRLRDGRIVS 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
10-219 |
2.18e-40 |
|
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: 143.87 E-value: 2.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQA-QTMRNPAQARSLGIGM 88
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDlTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 89 VFQHFSLFETLSVAQNIALAmgaaagtpkqleprirevsqrygmavepqrlvhsLSIGERQKVEIIRCLMQDIRLLILDE 168
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488618663 169 PTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGK 219
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
28-171 |
3.70e-40 |
|
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: 142.02 E-value: 3.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSlGIGMVFQHFSLFETLSVAQNIAL 107
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK-EIGYVFQDPQLFPRLTVRENLRL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488618663 108 AMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLV----HSLSIGERQKVEIIRCLMQDIRLLILDEPTS 171
Cdd:pfam00005 83 GLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
10-220 |
4.37e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 144.42 E-value: 4.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYP-GCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQA-QTMRNPAQA---RSl 84
Cdd:COG2884 2 IRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlSRLKRREIPylrRR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 85 gIGMVFQHFSLFETLSVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLL 164
Cdd:COG2884 81 -IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488618663 165 ILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
10-220 |
5.30e-40 |
|
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: 144.40 E-value: 5.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYP-GCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLgIGM 88
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 89 VFQHFS--LFETlSVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLIL 166
Cdd:COG1122 80 VFQNPDdqLFAP-TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488618663 167 DEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:COG1122 159 DEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
7-220 |
1.65e-39 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 146.78 E-value: 1.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 7 PARLQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRnPAQARslGI 86
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL-PPEKR--NV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 87 GMVFQHFSLFETLSVAQNIA--LAMgaaAGTPK-QLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRL 163
Cdd:COG3842 80 GMVFQDYALFPHLTVAENVAfgLRM---RGVPKaEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488618663 164 LILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDGRI 214
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
10-220 |
2.89e-39 |
|
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: 142.81 E-value: 2.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLGIGMV 89
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHFSLFETLSVAQNiaLAMGAAAGTPKQ-----LE------PRIREVSQRYGMavepqrlvhSLSIGERQKVEIIRCLM 158
Cdd:COG0410 84 PEGRRIFPSLTVEEN--LLLGAYARRDRAevradLErvyelfPRLKERRRQRAG---------TLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488618663 159 QDIRLLILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:COG0410 153 SRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRI 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
10-249 |
2.72e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 139.89 E-value: 2.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANdaVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQaRslGIGMV 89
Cdd:COG3840 2 LRLDDLTYRYGDFPLR--FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-R--PVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHFSLFETLSVAQNIALAMGAAAG-TPKQLEpRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDE 168
Cdd:COG3840 77 FQENNLFPHLTVAQNIGLGLRPGLKlTAEQRA-QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 169 PTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKVSghcipaecSDLELARLMVGDAEGLTA 247
Cdd:COG3840 156 PFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIA--------ADGPTAALLDGEPPPALA 227
|
..
gi 488618663 248 HY 249
Cdd:COG3840 228 AY 229
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
10-220 |
4.43e-38 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 142.59 E-value: 4.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARslGIGMV 89
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRER--RVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHFSLFETLSVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEP 169
Cdd:COG1118 81 FQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488618663 170 TSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:COG1118 161 FGALDAKVRKELRRWLRRLHDElGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
10-220 |
5.78e-38 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 138.12 E-value: 5.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARslgIGMV 89
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR---IGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHFSLFETLSVAQNIALAmGAAAGTPKQlepRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEP 169
Cdd:cd03268 78 IEAPGFYPNLTARENLRLL-ARLLGIRKK---RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488618663 170 TSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
9-228 |
8.45e-38 |
|
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: 139.41 E-value: 8.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 9 RLQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQA-QTMRNPAQARSlgIG 87
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDlASLSRRELARR--IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 88 MVFQHFSLFETLSVAQNIALA----MGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRL 163
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488618663 164 LILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAE 228
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEE 224
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-220 |
4.64e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 138.70 E-value: 4.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAqtmRNPAQARSLGI--- 86
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP---LDPEDRRRIGYlpe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 87 --GmvfqhfsLFETLSVAQNIaLAMGAAAG-TPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRL 163
Cdd:COG4152 79 erG-------LYPKMKVGEQL-VYLARLKGlSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488618663 164 LILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:COG4152 151 LILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRK 207
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-248 |
1.50e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 135.60 E-value: 1.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 1 MSNHAIparLQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQaqtmrnPAQ 80
Cdd:COG1121 1 MMMMPA---IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK------PPR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 81 ARSLGIGMVFQHFSLFET--LSVAQNIAL----AMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEII 154
Cdd:COG1121 72 RARRRIGYVPQRAEVDWDfpITVRDVVLMgrygRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 155 RCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLrNGKVSGHCIPAECSDLEL 234
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPEN 230
|
250
....*....|....
gi 488618663 235 ARLMVGDAEGLTAH 248
Cdd:COG1121 231 LSRAYGGPVALLAH 244
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
10-237 |
2.65e-36 |
|
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: 134.62 E-value: 2.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCL-ANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSL--GI 86
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 87 GMVFQHFSLFETLSVAQNIALAMGAAAGT--------PKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLM 158
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRSTwrslfglfPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 159 QDIRLLILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAECSDLELARL 237
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLDEI 240
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
11-219 |
3.07e-36 |
|
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: 131.98 E-value: 3.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 11 QLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSlGIGMVF 90
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR-RIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 91 QhfslfetlsvaqnialamgaaagtpkqleprirevsqrygmavepqrlvhsLSIGERQKVEIIRCLMQDIRLLILDEPT 170
Cdd:cd00267 80 Q---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488618663 171 SVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGK 219
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
10-220 |
8.31e-36 |
|
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: 132.60 E-value: 8.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPG----CLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAqarslg 85
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 86 IGMVFQHFSLFETLSVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLI 165
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488618663 166 LDEPTSVLTPQEAEELF-VTLRHLAAEGCSILFISHKLGEVRALCHSATVL--RNGKV 220
Cdd:cd03293 155 LDEPFSALDALTREQLQeELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRI 212
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
10-220 |
1.38e-35 |
|
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: 131.93 E-value: 1.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGeIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQaQTMRNPAQARSLgIGMV 89
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQ-DVLKQPQKLRRR-IGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHFSLFETLSVAQniALAMGAAAG--TPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILD 167
Cdd:cd03264 78 PQEFGVYPNFTVRE--FLDYIAWLKgiPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488618663 168 EPTSVLTPQEAeelfVTLRHL---AAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:cd03264 156 EPTAGLDPEER----IRFRNLlseLGEDRIVILSTHIVEDVESLCNQVAVLNKGKL 207
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-220 |
3.52e-35 |
|
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: 131.85 E-value: 3.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLAN----DAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSlG 85
Cdd:COG1124 2 LEVRNLSVSYGQGGRRvpvlKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRR-R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 86 IGMVFQHF--SLFETLSVAQNIALAMgAAAGTPKQlEPRIREVSQRYGMAVE-PQRLVHSLSIGERQKVEIIRCLMQDIR 162
Cdd:COG1124 81 VQMVFQDPyaSLHPRHTVDRILAEPL-RIHGLPDR-EERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488618663 163 LLILDEPTSVLTP--QeAE--ELFVTLRhlAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:COG1124 159 LLLLDEPTSALDVsvQ-AEilNLLKDLR--EERGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
10-231 |
4.20e-35 |
|
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: 131.31 E-value: 4.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRnPAQARslGIGMV 89
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDV-PVQER--NVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHFSLFETLSVAQNIA--LAMGAAAGTPKQLEPRIR-----EVSQRYGMAvepQRLVHSLSIGERQKVEIIRCLMQDIR 162
Cdd:cd03296 80 FQHYALFRHMTVFDNVAfgLRVKPRSERPPEAEIRAKvhellKLVQLDWLA---DRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 163 LLILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAECSD 231
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
10-203 |
4.80e-35 |
|
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: 130.34 E-value: 4.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQA--QTMRNPAQARSlGIG 87
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKltDDKKNINELRQ-KVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 88 MVFQHFSLFETLSVAQNIALAMGAAAGTPK-QLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLIL 166
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPIKVKGMSKaEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 488618663 167 DEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLG 203
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMG 196
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
11-223 |
5.20e-35 |
|
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: 130.35 E-value: 5.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 11 QLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQaqtmrnPAQARSLGIGMVF 90
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK------PLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 91 QHFSlFET---LSVAQNIALA----MGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRL 163
Cdd:cd03235 75 QRRS-IDRdfpISVRDVVLMGlyghKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 164 LILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALChSATVLRNGKVSGH 223
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYF-DRVLLLNRTVVAS 212
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
10-220 |
7.87e-35 |
|
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: 129.71 E-value: 7.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTmrnpAQARSLgIGMV 89
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNR-IGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHFSLFETLSVaQNIALAMGAAAG-TPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDE 168
Cdd:cd03269 76 PEERGLYPKMKV-IDQLVYLAQLKGlKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488618663 169 PTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
10-236 |
7.91e-35 |
|
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: 130.36 E-value: 7.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLGIGMV 89
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHFSLFETLSVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEP 169
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488618663 170 TSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAECSDLELAR 236
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
10-220 |
8.12e-35 |
|
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: 130.43 E-value: 8.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTmRNPAQARslGIGMV 89
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT-NLPPHKR--PVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHFSLFETLSVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEP 169
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488618663 170 TSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:cd03300 158 LGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
8-220 |
1.39e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 133.27 E-value: 1.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 8 ARLQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTmRNPAQARslGIG 87
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT-DLPPKDR--NIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 88 MVFQHFSLFETLSVAQNIALAMgAAAGTPKQ-LEPRIREVSQRYGMavEP--QRLVHSLSIGERQKVEIIRCLMQDIRLL 164
Cdd:COG3839 79 MVFQSYALYPHMTVYENIAFPL-KLRKVPKAeIDRRVREAAELLGL--EDllDRKPKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488618663 165 ILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:COG3839 156 LLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
10-220 |
1.51e-34 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 132.51 E-value: 1.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGC----LANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSL- 84
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 85 -GIGMVFQHFSLFETLSVAQNIALAMgAAAGTPK-QLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIR 162
Cdd:COG1135 82 rKIGMIFQHFNLLSSRTVAENVALPL-EIAGVPKaEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488618663 163 LLILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
10-220 |
5.86e-34 |
|
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: 127.37 E-value: 5.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQArslGIGMV 89
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR---DIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHFSLFETLSVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEP 169
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488618663 170 TSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
10-220 |
8.06e-34 |
|
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: 127.62 E-value: 8.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPG----CLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLG 85
Cdd:cd03257 2 LEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 86 --IGMVFQH--FSLFETLSVAQNIALAMGAAAGTPKqlEPRIREVSQRYGMAVEP-----QRLVHSLSIGERQKVEIIRC 156
Cdd:cd03257 82 keIQMVFQDpmSSLNPRMTIGEQIAEPLRIHGKLSK--KEARKEAVLLLLVGVGLpeevlNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488618663 157 LMQDIRLLILDEPTS---VLTPQEAEELfvtLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:cd03257 160 LALNPKLLIADEPTSaldVSVQAQILDL---LKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
10-220 |
2.13e-33 |
|
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: 126.08 E-value: 2.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGC--LANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSiIWQGQAQTMRNPAQARSlGIG 87
Cdd:cd03263 1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGT-AYINGYSIRTDRKAARQ-SLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 88 MVFQHFSLFETLSVAQNIALaMGAAAGTPKqlEPRIREVSQ-RYGMAVEPQ--RLVHSLSIGERQKVEIIRCLMQDIRLL 164
Cdd:cd03263 79 YCPQFDALFDELTVREHLRF-YARLKGLPK--SEIKEEVELlLRVLGLTDKanKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488618663 165 ILDEPTSVLTPQEAEELFVTLRHLaAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
10-220 |
3.42e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 125.31 E-value: 3.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLgIGMV 89
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQ-VAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHFSLFETlSVAQNIALAMGAAAGTPKqlEPRIREVSQRYGMAVEP-QRLVHSLSIGERQKVEIIRCLMQDIRLLILDE 168
Cdd:COG4619 80 PQEPALWGG-TVRDNLPFPFQLRERKFD--RERALELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488618663 169 PTSVLTP---QEAEELFVTLRhlAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:COG4619 157 PTSALDPentRRVEELLREYL--AEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-243 |
1.54e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 130.14 E-value: 1.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 7 PARLQLRHITKRypGCLANdaVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLGI 86
Cdd:COG1129 254 EVVLEVEGLSVG--GVVRD--VSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 87 GMV---FQHFSLFETLSVAQNIALAMGAAAGTPKQL-EPRIREVSQRYGMAVE-----PQRLVHSLSIGERQKVEIIRCL 157
Cdd:COG1129 330 AYVpedRKGEGLVLDLSIRENITLASLDRLSRGGLLdRRRERALAEEYIKRLRiktpsPEQPVGNLSGGNQQKVVLAKWL 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 158 MQDIRLLILDEPTS---VLTPQEAEELfvtLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAECSDLEL 234
Cdd:COG1129 410 ATDPKVLILDEPTRgidVGAKAEIYRL---IRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEATEEAI 486
|
....*....
gi 488618663 235 ARLMVGDAE 243
Cdd:COG1129 487 MAAATGGAA 495
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
10-220 |
2.44e-32 |
|
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: 123.29 E-value: 2.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYP-GCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQA----QTMRNPAQARSl 84
Cdd:cd03292 1 IEFINVTKTYPnGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdlRGRAIPYLRRK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 85 gIGMVFQHFSLFETLSVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLL 164
Cdd:cd03292 80 -IGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488618663 165 ILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
10-219 |
4.68e-32 |
|
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: 120.95 E-value: 4.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLAN--DAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLgIG 87
Cdd:cd03228 1 IEFKNVSFSYPGRPKPvlKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 88 MVFQHFSLFETlSVAQNIalamgaaagtpkqleprirevsqrygmavepqrlvhsLSIGERQKVEIIRCLMQDIRLLILD 167
Cdd:cd03228 80 YVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488618663 168 EPTSVLTPQEAEELFVTLRHLaAEGCSILFISHKLGEVRaLCHSATVLRNGK 219
Cdd:cd03228 122 EATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
8-200 |
5.13e-32 |
|
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: 121.82 E-value: 5.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 8 ARLQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLGIg 87
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 88 mVFQHFSLFETLSVAQNIALAmgAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILD 167
Cdd:COG4133 80 -LGHADGLKPELTVRENLRFW--AALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190
....*....|....*....|....*....|...
gi 488618663 168 EPTSVLTPQEAEELFVTLRHLAAEGCSILFISH 200
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-220 |
1.57e-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: 128.80 E-value: 1.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 6 IPARLQLRHITKRYPGCLAN--DAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARS 83
Cdd:COG2274 470 LKGDIELENVSFRYPGDSPPvlDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 84 LgIGMVFQHFSLFETlSVAQNIALAMGAAAgtpkqlEPRIREVSQRYGMAVEPQRLVH-----------SLSIGERQKVE 152
Cdd:COG2274 550 Q-IGVVLQDVFLFSG-TIRENITLGDPDAT------DEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLA 621
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488618663 153 IIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAeGCSILFISHKLgEVRALCHSATVLRNGKV 220
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRL-STIRLADRIIVLDKGRI 687
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
29-221 |
2.22e-31 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 120.35 E-value: 2.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 29 DLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARslgIGMVFQHFSLFETLSVAQNIALA 108
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRP---VSMLFQENNLFAHLTVRQNIGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 109 MGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHL 188
Cdd:TIGR01277 95 LHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQL 174
|
170 180 190
....*....|....*....|....*....|....
gi 488618663 189 AAE-GCSILFISHKLGEVRALCHSATVLRNGKVS 221
Cdd:TIGR01277 175 CSErQRTLLMVTHHLSDARAIASQIAVVSQGKIK 208
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-220 |
2.47e-31 |
|
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: 120.48 E-value: 2.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIqPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSI-----IWQGQAQTMRNPAQARslGIGMVFQHFSLFETLSVA 102
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtVLFDSRKKINLPPQQR--KIGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 103 QNIALamGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEELF 182
Cdd:cd03297 94 ENLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 488618663 183 VTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:cd03297 172 PELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
11-220 |
2.85e-31 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 123.76 E-value: 2.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 11 QLRHITKRYPGC----LANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSL-- 84
Cdd:PRK11153 3 ELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 85 GIGMVFQHFSLFETLSVAQNIALAMgAAAGTPK-QLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRL 163
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNVALPL-ELAGTPKaEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488618663 164 LILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
11-220 |
4.78e-31 |
|
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: 118.31 E-value: 4.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 11 QLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQA-QTMRNPAQARSLGIgmv 89
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDlASLSPKELARKIAY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 fqhfslfetlsVAQNIALAmgaaagtpkqleprirevsqryGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEP 169
Cdd:cd03214 78 -----------VPQALELL----------------------GLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488618663 170 TSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
28-220 |
1.13e-30 |
|
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: 119.36 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQArslGIGMVFQHFSLFETLSVAQNIAL 107
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR---DISYVPQNYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 108 AMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRH 187
Cdd:cd03299 95 GLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKK 174
|
170 180 190
....*....|....*....|....*....|....
gi 488618663 188 LAAE-GCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:cd03299 175 IRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
29-220 |
1.41e-30 |
|
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: 118.36 E-value: 1.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 29 DLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAqARSlgIGMVFQHFSLFETLSVAQNIALA 108
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA-DRP--VSMLFQENNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 109 MGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHL 188
Cdd:cd03298 95 LSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL 174
|
170 180 190
....*....|....*....|....*....|...
gi 488618663 189 AAE-GCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:cd03298 175 HAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
10-220 |
1.71e-30 |
|
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: 118.24 E-value: 1.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQaQTMRNPAQARSlGIGMV 89
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGH-DVVREPREVRR-RIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHFSLFETLSVAQNIALaMGAAAGTP-KQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDE 168
Cdd:cd03265 79 FQDLSVDDELTGWENLYI-HARLYGVPgAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488618663 169 PTSVLTPQEAEELFVTLRHL-AAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
10-203 |
6.74e-30 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 117.02 E-value: 6.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQ--AQTMRNPAQARSlGIG 87
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEdlTDSKKDINKLRR-KVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 88 MVFQHFSLFETLSVAQNIALAMGAAAGTPK-QLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLIL 166
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKVKKMSKaEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 488618663 167 DEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLG 203
Cdd:COG1126 161 DEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMG 197
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
10-220 |
7.84e-30 |
|
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: 116.83 E-value: 7.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLG--IG 87
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRrrMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 88 MVFQHFSLFETLSVAQNIALAMGA-AAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLIL 166
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREhTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488618663 167 DEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
10-220 |
1.03e-29 |
|
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: 116.62 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSL--GIG 87
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrrRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 88 MVFQHFSLFETLSVAQNIALAMGAAAG-TPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLIL 166
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488618663 167 DEPTSVLTP---QEAEELFVTLRHlaAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:COG1127 166 DEPTAGLDPitsAVIDELIRELRD--ELGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
8-244 |
1.19e-29 |
|
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: 119.44 E-value: 1.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 8 ARLQLRhITKRYPG-CLAndaVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSI-----IWQGQAQTMRNPAQA 81
Cdd:COG4148 1 MMLEVD-FRLRRGGfTLD---VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIrlggeVLQDSARGIFLPPHR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 82 RSlgIGMVFQHFSLFETLSVAQNIALAMGAAAGTPKQlePRIREVSQRYGMavEP--QRLVHSLSIGERQKVEIIRCLMQ 159
Cdd:COG4148 77 RR--IGYVFQEARLFPHLSVRGNLLYGRKRAPRAERR--ISFDEVVELLGI--GHllDRRPATLSGGERQRVAIGRALLS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 160 DIRLLILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAE-CSDLELARL 237
Cdd:COG4148 151 SPRLLLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEvLSRPDLLPL 230
|
....*..
gi 488618663 238 MVGDAEG 244
Cdd:COG4148 231 AGGEEAG 237
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
23-220 |
4.56e-29 |
|
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: 115.82 E-value: 4.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 23 LANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSL---GIGMVFQHFSLFETL 99
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkKISMVFQSFALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 100 SVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTP---Q 176
Cdd:cd03294 118 TVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPlirR 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488618663 177 EAEELFVTLRhlAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:cd03294 198 EMQDELLRLQ--AELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
11-220 |
4.65e-29 |
|
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: 113.89 E-value: 4.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 11 QLRHITKRYP-GCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQaqtmRNPAQARSLGIGMV 89
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK----PIKAKERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQH--FSLFETlSVAQNIALAMGAAAGTPKQleprIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILD 167
Cdd:cd03226 77 MQDvdYQLFTD-SVREELLLGLKELDAGNEQ----AETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488618663 168 EPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-220 |
4.68e-29 |
|
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: 112.91 E-value: 4.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 7 PARLQLRHITKryPGCLANdaVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLGI 86
Cdd:cd03215 2 EPVLEVRGLSV--KGAVRD--VSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 87 GMV---FQHFSLFETLSVAQNIALAmgaaagtpkqleprirevsqrygmavepqrlvHSLSIGERQKVEIIRCLMQDIRL 163
Cdd:cd03215 78 AYVpedRKREGLVLDLSVAENIALS--------------------------------SLLSGGNQQKVVLARWLARDPRV 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488618663 164 LILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
7-236 |
8.87e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 113.97 E-value: 8.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 7 PARLQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTmRNPAQARS-LG 85
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIT-HLPMHKRArLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 86 IGMVFQHFSLFETLSVAQNIALAMGAAAGTPKQLEPRIRE---------VSQRYGMavepqrlvhSLSIGERQKVEIIRC 156
Cdd:COG1137 80 IGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEElleefgithLRKSKAY---------SLSGGERRRVEIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 157 LMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV--SGHciPAECSDLEL 234
Cdd:COG1137 151 LATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVlaEGT--PEEILNNPL 228
|
..
gi 488618663 235 AR 236
Cdd:COG1137 229 VR 230
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
2-173 |
1.15e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 117.24 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 2 SNHAIPARLQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQA 81
Cdd:PRK11607 12 TRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 82 RslgIGMVFQHFSLFETLSVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDI 161
Cdd:PRK11607 92 P---INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170
....*....|..
gi 488618663 162 RLLILDEPTSVL 173
Cdd:PRK11607 169 KLLLLDEPMGAL 180
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
8-219 |
4.79e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 113.75 E-value: 4.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 8 ARLQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPaQARSLgIG 87
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR-HARQR-VG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 88 MVFQHFSLFETLSVAQNIAL---AMGAAAGTPKQLEPRIREVSQRYGMAVEPqrlVHSLSIGERQKVEIIRCLMQDIRLL 164
Cdd:PRK13537 84 VVPQFDNLDPDFTVRENLLVfgrYFGLSAAAARALVPPLLEFAKLENKADAK---VGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488618663 165 ILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGK 219
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
10-220 |
5.30e-28 |
|
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: 112.01 E-value: 5.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGC-LANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSlGIGM 88
Cdd:cd03295 1 IEFENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRR-KIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 89 VFQHFSLFETLSVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMavEP----QRLVHSLSIGERQKVEIIRCLMQDIRLL 164
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGL--DPaefaDRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488618663 165 ILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
10-220 |
1.08e-27 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 114.27 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTmRNPAQARSlgIGMV 89
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT-HVPAENRH--VNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHFSLFETLSVAQNIA--LAMgaaAGTPKQ-LEPRIRE---VSQRYGMAvepQRLVHSLSIGERQKVEIIRCLMQDIRL 163
Cdd:PRK09452 92 FQSYALFPHMTVFENVAfgLRM---QKTPAAeITPRVMEalrMVQLEEFA---QRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488618663 164 LILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:PRK09452 166 LLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
10-228 |
1.20e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 112.03 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGC--LANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLgIG 87
Cdd:PRK13635 6 IRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ-VG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 88 MVFQH-FSLFETLSVAQNIALAMgAAAGTPK-QLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLI 165
Cdd:PRK13635 85 MVFQNpDNQFVGATVQDDVAFGL-ENIGVPReEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488618663 166 LDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVrALCHSATVLRNGKVSGHCIPAE 228
Cdd:PRK13635 164 LDEATSMLDPRGRREVLETVRQLKEQkGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEE 226
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
10-228 |
1.72e-27 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 110.85 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLGIGMV 89
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHFSLF------ETLSVAQNIALAMGAAAG---TP-------KQLEpRIREVSQRYGMAVEPQRLVHSLSIGERQKVEI 153
Cdd:PRK11300 86 FQHVRLFremtviENLLVAQHQQLKTGLFSGllkTPafrraesEALD-RAATWLERVGLLEHANRQAGNLAYGQQRRLEI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488618663 154 IRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAE 228
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
9-236 |
2.75e-27 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 109.67 E-value: 2.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 9 RLQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRnPAQARS-LGIG 87
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHL-PMHERArLGIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 88 MVFQHFSLFETLSVAQNI-ALAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLIL 166
Cdd:TIGR04406 80 YLPQEASIFRKLTVEENImAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 167 DEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAECSDLELAR 236
Cdd:TIGR04406 160 DEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVR 229
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
10-220 |
2.94e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 110.21 E-value: 2.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQ-ARSLGIgm 88
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElARRRAV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 89 VFQHFSLFETLSVAQNIalAMGAAAGT--PKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQ------- 159
Cdd:COG4559 80 LPQHSSLAFPFTVEEVV--ALGRAPHGssAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepvdg 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488618663 160 DIRLLILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:COG4559 158 GPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRL 218
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
8-241 |
3.52e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 109.60 E-value: 3.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 8 ARLQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRnPAQARSL-GI 86
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL-PLHARARrGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 87 GMVFQHFSLFETLSVAQNIALAMGAAAG-TPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLI 165
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDDlSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488618663 166 LDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAEC-SDLELARLMVGD 241
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIlQDEHVKRVYLGE 237
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
29-202 |
5.80e-27 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 108.90 E-value: 5.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 29 DLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQaRSlgIGMVFQHFSLFETLSVAQNIALA 108
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR-RP--VSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 109 MGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHL 188
Cdd:PRK10771 96 LNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQV 175
|
170
....*....|....*
gi 488618663 189 AAE-GCSILFISHKL 202
Cdd:PRK10771 176 CQErQLTLLMVSHSL 190
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
7-220 |
1.12e-26 |
|
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: 108.25 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 7 PARLQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVtqpdagsiIWQGQAQTMR---------N 77
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGD--------LPPTYGNDVRlfgerrggeD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 78 PAQARSLgIGMV--FQHFSLFETLSVAQNIALAMGAAAGTPKQLEP----RIREVSQRYGMAVEPQRLVHSLSIGERQKV 151
Cdd:COG1119 73 VWELRKR-IGLVspALQLRFPRDETVLDVVLSGFFDSIGLYREPTDeqreRARELLELLGLAHLADRPFGTLSQGEQRRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 152 EIIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAEG-CSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
10-492 |
2.39e-26 |
|
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: 112.20 E-value: 2.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQ--PDAGSIIWQ------------------ 69
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 70 -----------------GQAQTMRNPAQARslgIGMVFQH-FSLFETLSVAQNIALAMGAAAGTPKQLEPRIREVSQRYG 131
Cdd:TIGR03269 81 pcpvcggtlepeevdfwNLSDKLRRRIRKR---IAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 132 MAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLA-AEGCSILFISHKLGEVRALCH 210
Cdd:TIGR03269 158 LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWPEVIEDLSD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 211 SATVLRNGKVSGHCIPAECSdlelARLMVGDAEglTAHYDKVSGSEAFLRVDKLSWHNpdpfgCSLK--------DLSLE 282
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEVV----AVFMEGVSE--VEKECEVEVGEPIIKVRNVSKRY-----ISVDrgvvkavdNVSLE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 283 VRSGEIVGIAGVAGNGQDELLALLSGeQTLPHAQATTLRFQDTPVG--DLRPD--ARRKHGLAFVPAErlgHGAVPELSL 358
Cdd:TIGR03269 307 VKEGEIFGIVGTSGAGKTTLSKIIAG-VLEPTSGEVNVRVGDEWVDmtKPGPDgrGRAKRYIGILHQE---YDLYPHRTV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 359 ADNalLTAfqqglvSHGLiqrgkvrALADEIIRRFAVKTTDA----QAAARS--------LSGGNLQKFILGREILQNPK 426
Cdd:TIGR03269 383 LDN--LTE------AIGL-------ELPDELARMKAVITLKMvgfdEEKAEEildkypdeLSEGERHRVALAQVLIKEPR 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 427 LLIAAHPTWGVD----VGAAAAIHRALIALrdaGAAILVISEDLDELFQISDRLAALSGGQLSDLIPTEQ 492
Cdd:TIGR03269 448 IVILDEPTGTMDpitkVDVTHSILKAREEM---EQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEE 514
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
10-220 |
8.61e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 106.01 E-value: 8.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQ-ARSLgiGM 88
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElARRR--AV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 89 VFQHFSLFETLSVAQNIalAMGAAAGT--PKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQ------D 160
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVV--AMGRAPHGlsRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488618663 161 IRLLILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:PRK13548 159 PRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
10-204 |
2.20e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 104.78 E-value: 2.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAqtMRNPAQARslgiGMV 89
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP--VEGPGAER----GVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHFSLFETLSVAQNIALAMgAAAGTPK-QLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDE 168
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGL-QLAGVEKmQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 488618663 169 PTSVL---TPQEAEELFVTLRHlaAEGCSILFISHKLGE 204
Cdd:PRK11248 155 PFGALdafTREQMQTLLLKLWQ--ETGKQVLLITHDIEE 191
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
28-251 |
2.30e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 104.39 E-value: 2.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMrnpaqarsLGIGMVFQHfslfeTLSVAQNI-- 105
Cdd:COG1134 45 VSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSAL--------LELGAGFHP-----ELTGRENIyl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 106 -ALAMGAAAGTPKQLEPRIREVS----------QRY--GMAVepqRLVHSLSIgerqkveiirCLMQDIrlLILDEPTSV 172
Cdd:COG1134 112 nGRLLGLSRKEIDEKFDEIVEFAelgdfidqpvKTYssGMRA---RLAFAVAT----------AVDPDI--LLVDEVLAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 173 --LTPQE-AEELFvtlRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKVsghcipaecsdlelarLMVGDAEGLTAHY 249
Cdd:COG1134 177 gdAAFQKkCLARI---RELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRL----------------VMDGDPEEVIAAY 237
|
..
gi 488618663 250 DK 251
Cdd:COG1134 238 EA 239
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
9-220 |
3.07e-25 |
|
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: 103.44 E-value: 3.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 9 RLQLRHITKRYPG--CLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSlGI 86
Cdd:cd03245 2 RIEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRR-NI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 87 GMVFQHFSLFETlSVAQNIALAMGAAAgtpkqlEPRIREVSQRYGMAVEPQRLVH-----------SLSIGERQKVEIIR 155
Cdd:cd03245 81 GYVPQDVTLFYG-TLRDNITLGAPLAD------DERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488618663 156 CLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAeGCSILFISHKLgEVRALCHSATVLRNGKV 220
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRP-SLLDLVDRIIVMDSGRI 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
7-220 |
3.43e-25 |
|
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: 109.00 E-value: 3.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 7 PARLQLRHITKRYP---GCL--------ANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVtQPDAGSIIWQGQAQTM 75
Cdd:COG4172 273 PPLLEARDLKVWFPikrGLFrrtvghvkAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 76 RNPAQARSL--GIGMVFQ--HFSLFETLSVAQNIA--LAMGAAAGTPKQLEPRIREVSQRYGMAVEP-QRLVHSLSIGER 148
Cdd:COG4172 352 LSRRALRPLrrRMQVVFQdpFGSLSPRMTVGQIIAegLRVHGPGLSAAERRARVAEALEEVGLDPAArHRYPHEFSGGQR 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488618663 149 QKVEIIRCLMQDIRLLILDEPTSVL--TPQeAE--ELfvtLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:COG4172 432 QRIAIARALILEPKLLVLDEPTSALdvSVQ-AQilDL---LRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
10-203 |
5.31e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 103.63 E-value: 5.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQaqTMRNP-AQARS--LGI 86
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGL--KVNDPkVDERLirQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 87 GMVFQHFSLFETLSVAQNIALAMGAAAGTPK-QLEPRIREVSQRYGMAvepQRLVH---SLSIGERQKVEIIRCLMQDIR 162
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFGPLRVRGASKeEAEKQARELLAKVGLA---ERAHHypsELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488618663 163 LLILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLG 203
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIG 197
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
10-220 |
8.14e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.16 E-value: 8.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYP-GCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQ-----AQTMRNPAQArs 83
Cdd:PRK13636 6 LKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysRKGLMKLRES-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 84 lgIGMVFQH--FSLFeTLSVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDI 161
Cdd:PRK13636 84 --VGMVFQDpdNQLF-SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 162 RLLILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
10-220 |
1.17e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 102.91 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSI-IWQGQAQTMRNPAQARSL---- 84
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrVGDITIDTARSLSQQKGLirql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 85 --GIGMVFQHFSLFETLSVAQNIALAMGAAAGTPK-QLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDI 161
Cdd:PRK11264 84 rqHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKeEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488618663 162 RLLILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-219 |
1.60e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 104.53 E-value: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 1 MSNHAIparlQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQtmrnPAQ 80
Cdd:PRK13536 37 MSTVAI----DLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PAR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 81 ARS--LGIGMVFQHFSLFETLSVAQNIaLAMGAAAG-TPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCL 157
Cdd:PRK13536 109 ARLarARIGVVPQFDNLDLEFTVRENL-LVFGRYFGmSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARAL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488618663 158 MQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGK 219
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-202 |
2.05e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 102.47 E-value: 2.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKR-YPGcLAN-----DAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTmRNPAQARS 83
Cdd:COG1101 2 LELKNLSKTfNPG-TVNekralDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT-KLPEYKRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 84 LGIGMVFQHFSL--FETLSVAQNIALAM------GAAAGTPKQLEPRIREVSQRYGMAVEpQRL---VHSLSIGERQKVE 152
Cdd:COG1101 80 KYIGRVFQDPMMgtAPSMTIEENLALAYrrgkrrGLRRGLTKKRRELFRELLATLGLGLE-NRLdtkVGLLSGGQRQALS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488618663 153 IIRCLMQDIRLLILDEPTSVLTPQEAEEL------FVTLRHLAAegcsiLFISHKL 202
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALDPKTAALVleltekIVEENNLTT-----LMVTHNM 209
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
8-220 |
5.91e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 100.34 E-value: 5.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 8 ARLQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLGIG 87
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 88 MVFQHFSLFETLSVAQNiaLAMGAAAGTPKQLEPRIREVSQRYGMAVE--PQRlVHSLSIGERQKVEIIRCLMQDIRLLI 165
Cdd:PRK11614 84 IVPEGRRVFSRMTVEEN--LAMGGFFAERDQFQERIKWVYELFPRLHErrIQR-AGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488618663 166 LDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-220 |
2.67e-23 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 103.32 E-value: 2.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 6 IPARLQLRHITKRYPG---CLANdaVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQAR 82
Cdd:COG1132 336 VRGEIEFENVSFSYPGdrpVLKD--ISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 83 SLgIGMVFQHFSLFETlSVAQNIAL------------AMGAAagtpkQLEPRIREVSQRYGMAVEpQRLVhSLSIGERQK 150
Cdd:COG1132 414 RQ-IGVVPQDTFLFSG-TIRENIRYgrpdatdeeveeAAKAA-----QAHEFIEALPDGYDTVVG-ERGV-NLSGGQRQR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488618663 151 VEIIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAeGCSILFISHKLGEVRA----LchsatVLRNGKV 220
Cdd:COG1132 485 IAIARALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTIRNadriL-----VLDDGRI 552
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
10-202 |
4.50e-23 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 97.96 E-value: 4.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRY-PGCLANDA---VDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQA-QTMRNPAQA--R 82
Cdd:PRK11629 6 LQCDNLCKRYqEGSVQTDVlhnVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmSKLSSAAKAelR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 83 SLGIGMVFQHFSLFETLSVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIR 162
Cdd:PRK11629 86 NQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488618663 163 LLILDEPTSVLTPQEAEELFVTLRHL-AAEGCSILFISHKL 202
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDL 206
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
7-220 |
1.08e-22 |
|
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: 101.37 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 7 PARLQLRHITKRYP-GCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLg 85
Cdd:COG4988 334 PPSIELEDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 86 IGMVFQHFSLFETlSVAQNIALAMGAAAgtpkqlEPRIREVSQRYGMAVEPQRLVH-----------SLSIGERQKVEII 154
Cdd:COG4988 413 IAWVPQNPYLFAG-TIRENLRLGRPDAS------DEELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488618663 155 RCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAeGCSILFISHKLgEVRALCHSATVLRNGKV 220
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRL-ALLAQADRILVLDDGRI 549
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
7-202 |
1.43e-22 |
|
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: 101.00 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 7 PARLQLRHITKRYPG--CLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSL 84
Cdd:COG4987 331 GPSLELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 85 gIGMVFQHFSLFETlSVAQNIALAMGAAAgtpkqlEPRIREVSQRYGM----AVEPQRLV-------HSLSIGERQKVEI 153
Cdd:COG4987 411 -IAVVPQRPHLFDT-TLRENLRLARPDAT------DEELWAALERVGLgdwlAALPDGLDtwlgeggRRLSGGERRRLAL 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488618663 154 IRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAEGcSILFISHKL 202
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR-TVLLITHRL 530
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
10-220 |
1.43e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 97.01 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDA---------GSIIwQGQAQTMRNPAQ 80
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTV-QREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 81 ARSlGIGMVFQHFSLFETLSVAQNIALamGAAAGTP----------KQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQK 150
Cdd:PRK09984 84 SRA-NTGYIFQQFNLVNRLSVLENVLI--GALGSTPfwrtcfswftREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488618663 151 VEIIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHL-AAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
26-336 |
1.68e-22 |
|
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: 100.53 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 26 DAVDLTIQPGEIHALLGENGAGKS-TLMKII----YGVTQPDaGSIIWQGQ------AQTMRnpaQARSLGIGMVFQ--- 91
Cdd:COG4172 27 KGVSFDIAAGETLALVGESGSGKSvTALSILrllpDPAAHPS-GSILFDGQdllglsERELR---RIRGNRIAMIFQepm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 92 -----HFS----LFETLSVAQNIalamgaaagTPKQLEPRIREVSQRYGMAvEPQRLV----HSLSIGERQKVEIIRCLM 158
Cdd:COG4172 103 tslnpLHTigkqIAEVLRLHRGL---------SGAAARARALELLERVGIP-DPERRLdaypHQLSGGQRQRVMIAMALA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 159 QDIRLLILDEPTSVL--TPQeAE--ELFVTLRhlAAEGCSILFISHKLGEVRALCHSATVLRNGKVSGHcipAECSDLEL 234
Cdd:COG4172 173 NEPDLLIADEPTTALdvTVQ-AQilDLLKDLQ--RELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQ---GPTAELFA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 235 A-------RLMvgDAEGLTAHYDKVSGSEAFLRVDKLSWHNPDPFG---------CSLKDLSLEVRSGEIVGIAGVAGNG 298
Cdd:COG4172 247 ApqhpytrKLL--AAEPRGDPRPVPPDAPPLLEARDLKVWFPIKRGlfrrtvghvKAVDGVSLTLRRGETLGLVGESGSG 324
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 488618663 299 QDEL-LALL-----SGEqtlphaqattLRFQDTPVGDLRPDARR 336
Cdd:COG4172 325 KSTLgLALLrlipsEGE----------IRFDGQDLDGLSRRALR 358
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
10-236 |
1.82e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 97.07 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYP-GCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPA--QARSlGI 86
Cdd:PRK13639 2 LETRDLKYSYPdGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllEVRK-TV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 87 GMVFQH--FSLFETlSVAQNIA---LAMGAAAgtpKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDI 161
Cdd:PRK13639 81 GIVFQNpdDQLFAP-TVEEDVAfgpLNLGLSK---EEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488618663 162 RLLILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAEC-SDLELAR 236
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVfSDIETIR 232
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
10-220 |
2.58e-22 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 95.33 E-value: 2.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYG-----VTQPDAGSIIWQGQA-QTMRNPAQARS 83
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDiYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 84 LGIGMVFQHFSLFEtLSVAQNIALAMGAAAGTPK-QLEPRIREVSQRYGM--AVEPQRLVHSLSIGERQKVEIIRCLMQD 160
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKeELDERVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488618663 161 IRLLILDEPTSVLTP---QEAEELFVTLRHLAAegcsILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:cd03260 160 PEVLLLDEPTSALDPistAKIEELIAELKKEYT----IVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
12-220 |
2.96e-22 |
|
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: 95.48 E-value: 2.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 12 LRHITKR-YPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSlgIGMVF 90
Cdd:cd03267 23 LKSLFKRkYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRR--IGVVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 91 -QHFSLFETLSVAQNIALAMGAAAGTPKQLEPRIREVSQrygmAVEPQRLVHS----LSIGERQKVEIIRCLMQDIRLLI 165
Cdd:cd03267 101 gQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSE----LLDLEELLDTpvrqLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488618663 166 LDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
11-220 |
5.63e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 95.44 E-value: 5.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 11 QLRHITKRYPGC--LANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSlGIGM 88
Cdd:PRK13632 9 KVENVSFSYPNSenNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK-KIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 89 VFQH-FSLFETLSVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILD 167
Cdd:PRK13632 88 IFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488618663 168 EPTSVLTPQEAEELFVTLRHLAAEGC-SILFISHKLGEVrALCHSATVLRNGKV 220
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEA-ILADKVIVFSEGKL 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
12-200 |
9.08e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.21 E-value: 9.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 12 LRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQtmrnpaqarslgIGMVFQ 91
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLR------------IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 92 HFSLFETLSVAQNIALAMGAAAGTPKQL--------------------------------EPRIREVSQRYGMAVEP-QR 138
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGDAELRALEAELeeleaklaepdedlerlaelqeefealggweaEARAEEILSGLGFPEEDlDR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 139 LVHSLSIGERQKVEIIRCLMQDIRLLILDEPT------SV--LtpqeaEElfvtlrHLAAEGCSILFISH 200
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPTnhldleSIewL-----EE------FLKNYPGTVLVVSH 207
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-220 |
1.50e-21 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 94.10 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 1 MSNHAIPArLQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMR---- 76
Cdd:COG4598 1 MTDTAPPA-LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKpdrd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 77 ------NPAQARSL--GIGMVFQHFSLFETLSVAQNIALAMGAAAGTPK-QLEPRIREVSQRYGMAVEPQRLVHSLSIGE 147
Cdd:COG4598 80 gelvpaDRRQLQRIrtRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKaEAIERAEALLAKVGLADKRDAYPAHLSGGQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488618663 148 RQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:COG4598 160 QQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRI 232
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-208 |
1.54e-21 |
|
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: 97.74 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 5 AIPARLQLRHITKRYPGC-LANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARS 83
Cdd:TIGR02857 317 APASSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 84 lGIGMVFQHFSLFETlSVAQNIALAMGAAAGTpkqlepRIREVSQRYGM----AVEPQRLV-------HSLSIGERQKVE 152
Cdd:TIGR02857 397 -QIAWVPQHPFLFAG-TIAENIRLARPDASDA------EIREALERAGLdefvAALPQGLDtpigeggAGLSGGQAQRLA 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488618663 153 IIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLaAEGCSILFISHKLGEVRAL 208
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAALA 523
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
9-228 |
3.40e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 93.11 E-value: 3.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 9 RLQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTM------------R 76
Cdd:PRK10619 5 KLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLvrdkdgqlkvadK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 77 NPAQARSLGIGMVFQHFSLFETLSVAQNIALAMGAAAGTPKQlepRIREVSQRYGMAV---EPQRL---VHsLSIGERQK 150
Cdd:PRK10619 85 NQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQ---EARERAVKYLAKVgidERAQGkypVH-LSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488618663 151 VEIIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAE 228
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQ 238
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
25-220 |
4.44e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.77 E-value: 4.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 25 NDaVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMrnpAQARSLGIGMVFQHFSLFETLSVAQN 104
Cdd:PRK10851 19 ND-ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR---LHARDRKVGFVFQHYALFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 105 IALAMGAaagTPKQLEPRIREVSQRYGMAVEPQRLVH-------SLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQE 177
Cdd:PRK10851 95 IAFGLTV---LPRRERPNAAAIKAKVTQLLEMVQLAHladrypaQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488618663 178 AEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:PRK10851 172 RKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
28-200 |
5.44e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 92.05 E-value: 5.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKII-----YGVTQpdaGSIIWQGQAQTMRNPAQ-ARsLGIGMVFQHFSLFETLSV 101
Cdd:COG0396 19 VNLTIKPGEVHAIMGPNGSGKSTLAKVLmghpkYEVTS---GSILLDGEDILELSPDErAR-AGIFLAFQYPVEIPGVSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 102 AQNIALAMGAAAGTP---KQLEPRIREVSQRYGMAVE-PQRLVH-SLSIGERQKVEIIRCLMQDIRLLILDEPTS----- 171
Cdd:COG0396 95 SNFLRTALNARRGEElsaREFLKLLKEKMKELGLDEDfLDRYVNeGFSGGEKKRNEILQMLLLEPKLAILDETDSgldid 174
|
170 180 190
....*....|....*....|....*....|...
gi 488618663 172 ----VltpqeAEelfvTLRHLAAEGCSILFISH 200
Cdd:COG0396 175 alriV-----AE----GVNKLRSPDRGILIITH 198
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
27-224 |
6.33e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 95.93 E-value: 6.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 27 AVDLTIQPGEIHALLGENGAGKST----LMKIIygvtqPDAGSIIWQGQAQTMRNPAQARSL--GIGMVFQ--HFSLFET 98
Cdd:PRK15134 304 NISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVrhRIQVVFQdpNSSLNPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 99 LSVAQNIA--LAMGAAAGTPKQLEPRIREVSQRYGMAVEP-QRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTP 175
Cdd:PRK15134 379 LNVLQIIEegLRVHQPTLSAAQREQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDK 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488618663 176 QEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKV--SGHC 224
Cdd:PRK15134 459 TVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVveQGDC 510
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
10-220 |
6.82e-21 |
|
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: 91.78 E-value: 6.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRY--PGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSlGIG 87
Cdd:cd03252 1 ITFEHVRFRYkpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRR-QVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 88 MVFQHFSLFETlSVAQNIALAMGAA-------AGTPKQLEPRIREVSQRYGMAVEPQRLvhSLSIGERQKVEIIRCLMQD 160
Cdd:cd03252 80 VVLQENVLFNR-SIRDNIALADPGMsmervieAAKLAGAHDFISELPEGYDTIVGEQGA--GLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 161 IRLLILDEPTSVLTpQEAEELFVTLRHLAAEGCSILFISHKLGEVRAlCHSATVLRNGKV 220
Cdd:cd03252 157 PRILIFDEATSALD-YESEHAIMRNMHDICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRI 214
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
8-200 |
6.98e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 96.33 E-value: 6.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 8 ARLQLRHITKRYPGCLAN----DAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNP---AQ 80
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQvevlKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdalAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 81 ARSLGIGMVFQHFSLFETLSVAQNIAL-AMGAAAGTPKQLEpRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQ 159
Cdd:PRK10535 83 LRREHFGFIFQRYHLLSHLTAAQNVEVpAVYAGLERKQRLL-RAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488618663 160 DIRLLILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISH 200
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTH 202
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
8-221 |
7.54e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 94.33 E-value: 7.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 8 ARLQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQArslGIG 87
Cdd:PRK11000 2 ASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAER---GVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 88 MVFQHFSLFETLSVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILD 167
Cdd:PRK11000 79 MVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488618663 168 EPTSVLTPQeaeeLFVTLRHLAAE-----GCSILFISHKLGEVRALCHSATVLRNGKVS 221
Cdd:PRK11000 159 EPLSNLDAA----LRVQMRIEISRlhkrlGRTMIYVTHDQVEAMTLADKIVVLDAGRVA 213
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
26-228 |
9.12e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 92.10 E-value: 9.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 26 DAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLgIGMVFQH-FSLFETLSVAQN 104
Cdd:PRK13650 24 NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHK-IGMVFQNpDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 105 IALAMGAAAGTPKQLEPRIREVSQRYGMAV----EPQRlvhsLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEE 180
Cdd:PRK13650 103 VAFGLENKGIPHEEMKERVNEALELVGMQDfkerEPAR----LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488618663 181 LFVTLRHLAAE-GCSILFISHKLGEVrALCHSATVLRNGKVSGHCIPAE 228
Cdd:PRK13650 179 LIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRE 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
10-220 |
9.44e-21 |
|
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: 89.58 E-value: 9.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPG----CLANdaVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLg 85
Cdd:cd03246 1 LEVENVSFRYPGaeppVLRN--VSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 86 IGMVFQHFSLFETlSVAQNIalamgaaagtpkqleprirevsqrygmavepqrlvhsLSIGERQKVEIIRCLMQDIRLLI 165
Cdd:cd03246 78 VGYLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488618663 166 LDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLgEVRALCHSATVLRNGKV 220
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
28-236 |
9.52e-21 |
|
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: 90.28 E-value: 9.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKII-----YGVTQpdaGSIIWQGQAQTMRNPAQARSLGIGMVFQHFSLFETLSVA 102
Cdd:cd03217 19 VNLTIKKGEVHALMGPNGSGKSTLAKTImghpkYEVTE---GEILFKGEDITDLPPEERARLGIFLAFQYPPEIPGVKNA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 103 QnialamgaaagtpkqlepRIREVSQrygmavepqrlvhSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEELF 182
Cdd:cd03217 96 D------------------FLRYVNE-------------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488618663 183 VTLRHLAAEGCSILFISHkLGEVRALCHS--ATVLRNGKVsghcipAECSDLELAR 236
Cdd:cd03217 145 EVINKLREEGKSVLIITH-YQRLLDYIKPdrVHVLYDGRI------VKSGDKELAL 193
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
10-222 |
1.08e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 90.70 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCL-ANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSL--GI 86
Cdd:PRK10908 2 IRFEHVSKAYLGGRqALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLrrQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 87 GMVFQHFSLFETLSVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLIL 166
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488618663 167 DEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKVSG 222
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHG 217
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
10-203 |
1.16e-20 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 90.49 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRY-PGCLANDA---VDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQA-QTMRNPAQA--R 82
Cdd:TIGR02211 2 LKCENLGKRYqEGKLDTRVlkgVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSlSKLSSNERAklR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 83 SLGIGMVFQHFSLFETLSVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAvepQRLVH---SLSIGERQKVEIIRCLMQ 159
Cdd:TIGR02211 82 NKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLE---HRINHrpsELSGGERQRVAIARALVN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488618663 160 DIRLLILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLG 203
Cdd:TIGR02211 159 QPSLVLADEPTGNLDNNNAKIIFDLMLELNRElNTSFLVVTHDLE 203
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
39-228 |
1.35e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 91.79 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 39 ALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLgIGMVFQHF--SLFETlSVAQNIALAMGAAAGTP 116
Cdd:PRK13652 34 AVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF-VGLVFQNPddQIFSP-TVEQDIAFGPINLGLDE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 117 KQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAE-GCSI 195
Cdd:PRK13652 112 ETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTV 191
|
170 180 190
....*....|....*....|....*....|...
gi 488618663 196 LFISHKLGEVRALCHSATVLRNGKVSGHCIPAE 228
Cdd:PRK13652 192 IFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEE 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
10-250 |
1.95e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 92.48 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNpAQARSlgIGMV 89
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS-IQQRD--ICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHFSLFETLSVAQNIA--LAMgaaAGTPK-QLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLIL 166
Cdd:PRK11432 84 FQSYALFPHMSLGENVGygLKM---LGVPKeERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 167 DEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAEC----SDLELARLMvGD 241
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELyrqpASRFMASFM-GD 239
|
....*....
gi 488618663 242 AEGLTAHYD 250
Cdd:PRK11432 240 ANIFPATLS 248
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-200 |
2.25e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.98 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPG-CLANDaVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWqgqAQTMRnpaqarslgIGM 88
Cdd:COG0488 316 LELEGLSKSYGDkTLLDD-LSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL---GETVK---------IGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 89 VFQHFSLF-ETLSVAQNIalamgaAAGTPKQLEPRIREVSQRYG----MAvepQRLVHSLSIGERQKVEIIRCLMQDIRL 163
Cdd:COG0488 383 FDQHQEELdPDKTVLDEL------RDGAPGGTEQEVRGYLGRFLfsgdDA---FKPVGVLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488618663 164 LILDEPTSVLTPQ--EA-EELfvtlrhLAA-EGCsILFISH 200
Cdd:COG0488 454 LLLDEPTNHLDIEtlEAlEEA------LDDfPGT-VLLVSH 487
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
276-483 |
2.81e-20 |
|
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: 89.42 E-value: 2.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtLPHAQATTLRFQDTPVGDLRPDARRKHGLAFVPAERlghGAVPE 355
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMG---LLPPRSGSIRFDGRDITGLPPHERARAGIGYVPEGR---RIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 356 LSLADNALLTAFQQGlvshgliqRGKVRALADEIIRRFAVKTTDAQAAARSLSGGNLQKFILGREILQNPKLLIAAHPTW 435
Cdd:cd03224 90 LTVEENLLLGAYARR--------RAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488618663 436 GVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSGGQ 483
Cdd:cd03224 162 GLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-220 |
3.66e-20 |
|
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: 89.13 E-value: 3.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 2 SNHAIPARLQLRHITKRYPGC---LANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMrnp 78
Cdd:cd03220 12 TYKGGSSSLKKLGILGRKGEVgefWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 79 aqarsLGIGMVFQhfslfETLSVAQNIALaMGAAAG-TPKQLEPRIREVSQ-------------RY--GMAVepqRLVHS 142
Cdd:cd03220 89 -----LGLGGGFN-----PELTGRENIYL-NGRLLGlSRKEIDEKIDEIIEfselgdfidlpvkTYssGMKA---RLAFA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488618663 143 LSIgerqkveiirclMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:cd03220 155 IAT------------ALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
9-220 |
3.76e-20 |
|
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: 88.38 E-value: 3.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 9 RLQLRHITKRYPGCLANDaVDLTIQPGEIHALLGENGAGKSTLMKII--YGVTQPDAGSIIWQGQAQTMRNPAQArslgI 86
Cdd:cd03213 10 TVTVKSSPSKSGKQLLKN-VSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRSFRKI----I 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 87 GMVFQHFSLFETLSVAQNIalaMGAAagtpkqlepRIRevsqrygmavepqrlvhSLSIGERQKVEIIRCLMQDIRLLIL 166
Cdd:cd03213 85 GYVPQDDILHPTLTVRETL---MFAA---------KLR-----------------GLSGGERKRVSIALELVSNPSLLFL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488618663 167 DEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKL-GEVRALCHSATVLRNGKV 220
Cdd:cd03213 136 DEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
26-466 |
5.01e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 93.23 E-value: 5.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 26 DAVDLTIQPGEIHALLGENGAGKS-TLMKIIYGVTQPDA----GSIIWQGQA------QTMRnpaQARSLGIGMVFQ--- 91
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVvypsGDIRFHGESllhaseQTLR---GVRGNKIAMIFQepm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 92 ---------HFSLFETLSVAQnialAMGAAAGtpkqlEPRIREVSQRYGMAVEPQRLV---HSLSIGERQKVEIIRCLMQ 159
Cdd:PRK15134 103 vslnplhtlEKQLYEVLSLHR----GMRREAA-----RGEILNCLDRVGIRQAAKRLTdypHQLSGGERQRVMIAMALLT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 160 DIRLLILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKVSGHcipAECSDLELA--- 235
Cdd:PRK15134 174 RPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQ---NRAATLFSApth 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 236 ----RLMVGDAEGLTAHYDkvSGSEAFLRVDKLSWHNPDPFGC---------SLKDLSLEVRSGEIVGIAGVAGNGQDEL 302
Cdd:PRK15134 251 pytqKLLNSEPSGDPVPLP--EPASPLLDVEQLQVAFPIRKGIlkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 303 -LALLSgeqtLPHAQATTLrFQDTPVGDLRPDA----RRKHGLAFVPaerlghgavPELSLadNALLTAFQqgLVSHGL- 376
Cdd:PRK15134 329 gLALLR----LINSQGEIW-FDGQPLHNLNRRQllpvRHRIQVVFQD---------PNSSL--NPRLNVLQ--IIEEGLr 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 377 IQRGKVRALADE--IIRRFAVKTTDAQAAAR---SLSGGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIA 451
Cdd:PRK15134 391 VHQPTLSAAQREqqVIAVMEEVGLDPETRHRypaEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKS 470
|
490
....*....|....*.
gi 488618663 452 LR-DAGAAILVISEDL 466
Cdd:PRK15134 471 LQqKHQLAYLFISHDL 486
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
10-220 |
5.27e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 89.75 E-value: 5.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYP--GCLAN-------DAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQ 80
Cdd:PRK10419 4 LNVSGLSHHYAhgGLSGKhqhqtvlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 81 ARSL--GIGMVFQhfslfETLSvAQNIALAMGAAAGTP---------KQLEPRIREVSQRYGMAVE-PQRLVHSLSIGER 148
Cdd:PRK10419 84 RKAFrrDIQMVFQ-----DSIS-AVNPRKTVREIIREPlrhllsldkAERLARASEMLRAVDLDDSvLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488618663 149 QKVEIIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
10-220 |
1.09e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 88.83 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRN-----PAQARSL 84
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDlyalsEAERRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 85 G---IGMVFQHFS--LFETLSVAQNIA---LAMGAaagtpkQLEPRIREVSQRYGMAVE--PQR---LVHSLSIGERQKV 151
Cdd:PRK11701 87 LrteWGFVHQHPRdgLRMQVSAGGNIGerlMAVGA------RHYGDIRATAGDWLERVEidAARiddLPTTFSGGMQQRL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 152 EIIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
2.35e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 87.88 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 1 MSNHAIparlQLRHITKRYPG--CLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNP 78
Cdd:PRK13648 3 DKNSII----VFKNVSFQYQSdaSFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 79 AQARSlGIGMVFQH-FSLFETLSVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCL 157
Cdd:PRK13648 79 EKLRK-HIGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488618663 158 MQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHsATVLRNGKVSGHCIPAE 228
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAMEADH-VIVMNKGTVYKEGTPTE 228
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
276-484 |
2.36e-19 |
|
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: 87.11 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGEQTlphAQATTLRFQDTPVGDLRPDARRKHGLA--F-VPAErlghga 352
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLR---PTSGSVLFDGEDITGLPPHEIARLGIGrtFqIPRL------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 353 VPELSLADNALLTAFQQGLVSHGLIQRGK----VRALADEIIRRFAVkTTDAQAAARSLSGGNLQKFILGREILQNPKLL 428
Cdd:cd03219 87 FPELTVLENVMVAAQARTGSGLLLARARReereARERAEELLERVGL-ADLADRPAGELSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488618663 429 IAAHPTWGVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSGGQL 484
Cdd:cd03219 166 LLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
10-220 |
2.53e-19 |
|
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: 86.90 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRY-PGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGqaQTMRNPAQArSL--GI 86
Cdd:cd03253 1 IEFENVTFAYdPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDG--QDIREVTLD-SLrrAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 87 GMVFQHFSLFETlSVAQNIALA--------MGAAAGTpKQLEPRIREVSQRYGMAVEPQRLvhSLSIGERQKVEIIRCLM 158
Cdd:cd03253 78 GVVPQDTVLFND-TIGYNIRYGrpdatdeeVIEAAKA-AQIHDKIMRFPDGYDTIVGERGL--KLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488618663 159 QDIRLLILDEPTSVLTPQEAEELFVTLRHLAAeGCSILFISHKLGEVrALCHSATVLRNGKV 220
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTI-VNADKIIVLKDGRI 213
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
10-220 |
2.59e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 86.99 E-value: 2.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQA---QTMRNPAQARSL-- 84
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfSKTPSDKAIRELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 85 GIGMVFQHFSLFETLSVAQNIALAMGAAAGTPK-QLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRL 163
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKdQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488618663 164 LILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
17-209 |
3.95e-19 |
|
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: 86.33 E-value: 3.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 17 KRYPGClanDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQtMRNPAQA--------RSLGIGM 88
Cdd:COG4778 22 KRLPVL---DGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGG-WVDLAQAspreilalRRRTIGY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 89 VFQHFSLF---ETLSVAQNIALAMGAAAGTPKQlepRIREVSQRYGMavePQRLVHS----LSIGERQKVEIIRCLMQDI 161
Cdd:COG4778 98 VSQFLRVIprvSALDVVAEPLLERGVDREEARA---RARELLARLNL---PERLWDLppatFSGGEQQRVNIARGFIADP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488618663 162 RLLILDEPTSVLTPQEAE---ELfvtLRHLAAEGCSILFISHKLGEVRALC 209
Cdd:COG4778 172 PLLLLDEPTASLDAANRAvvvEL---IEEAKARGTAIIGIFHDEEVREAVA 219
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-220 |
4.89e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 87.10 E-value: 4.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 3 NHAIparlQLRHITKRYP-GCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQA 81
Cdd:PRK13647 2 DNII----EVEDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 82 RSLgIGMVFQH-----FSLFETLSVA---QNIALamgaaagTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEI 153
Cdd:PRK13647 78 RSK-VGLVFQDpddqvFSSTVWDDVAfgpVNMGL-------DKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488618663 154 IRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-220 |
5.24e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 87.84 E-value: 5.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 26 DAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSI------IWQGQAQTMRNpaqarslgIGMVF-QHFSLFET 98
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVrvlgyvPFKRRKEFARR--------IGVVFgQRSQLWWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 99 LSVAQNIALaMGAAAGTPK-QLEPRIREVSQRygMAVEP--QRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPT---SV 172
Cdd:COG4586 111 LPAIDSFRL-LKAIYRIPDaEYKKRLDELVEL--LDLGEllDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTiglDV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488618663 173 LTpQEAEELFvtLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:COG4586 188 VS-KEAIREF--LKEYNRErGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
8-202 |
6.52e-19 |
|
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: 89.73 E-value: 6.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 8 ARLQLRHITKRYPG-CLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLgI 86
Cdd:TIGR02868 333 PTLELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR-V 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 87 GMVFQHFSLFETlSVAQNIALAMGAAAgtpkqlEPRIREVSQRYGMAVEPQRLVH-----------SLSIGERQKVEIIR 155
Cdd:TIGR02868 412 SVCAQDAHLFDT-TVRENLRLARPDAT------DEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488618663 156 CLMQDIRLLILDEPTSVLTPQEAEELFVTLRHlAAEGCSILFISHKL 202
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
10-173 |
7.58e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 84.84 E-value: 7.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDA---GSIIWQGQAQTMRnPAQARslGI 86
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRRLTAL-PAEQR--RI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 87 GMVFQHFSLFETLSVAQNIALAMgAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLIL 166
Cdd:COG4136 79 GILFQDDLLFPHLSVGENLAFAL-PPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLL 157
|
....*..
gi 488618663 167 DEPTSVL 173
Cdd:COG4136 158 DEPFSKL 164
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
26-254 |
8.57e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.84 E-value: 8.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 26 DAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQ-ARSLGigMVFQHFSLFETLSVAQN 104
Cdd:PRK11231 19 NDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlARRLA--LLPQHHLTPEGITVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 105 IALA-------MGAAAGTPKQLEPRIREVSQRYGMAvepQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQE 177
Cdd:PRK11231 97 VAYGrspwlslWGRLSAEDNARVNQAMEQTRINHLA---DRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINH 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488618663 178 AEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAECSDLELARLMVG-DAEgltAHYDKVSG 254
Cdd:PRK11231 174 QVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDvEAE---IHPEPVSG 248
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
10-220 |
2.34e-18 |
|
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: 82.75 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPG--CLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQG-QAQTMRNpaqARSLGI 86
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvPVSDLEK---ALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 87 GMVFQHFSLFETlSVAQNIalamgaaaGTPkqleprirevsqrygmavepqrlvhsLSIGERQKVEIIRCLMQDIRLLIL 166
Cdd:cd03247 78 SVLNQRPYLFDT-TLRNNL--------GRR--------------------------FSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488618663 167 DEPTSVLTPQEAEELFVTLRHlAAEGCSILFISHKLGEVRALcHSATVLRNGKV 220
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIFE-VLKDKTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
27-220 |
5.38e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 85.31 E-value: 5.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 27 AVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQ-----AQTMRNPAQARslGIGMVFQHFSLFETLSV 101
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaEKGICLPPEKR--RIGYVFQDARLFPHYKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 102 AQNiaLAMGAAAGTPKQLEpRIREVsqrygMAVEP--QRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAE 179
Cdd:PRK11144 94 RGN--LRYGMAKSMVAQFD-KIVAL-----LGIEPllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488618663 180 ELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:PRK11144 166 ELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
24-215 |
1.09e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 84.19 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 24 ANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPD----AGSIIWQGQAQTMRNPAQARSL---GIGMVFQH--FS 94
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPRERRKIigrEIAMIFQEpsSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 95 LFETLSVAQNIALAMGAAAGT------PKQLEPRIREVSQRYG-------MAVEPqrlvHSLSIGERQKVEIIRCLMQDI 161
Cdd:COG4170 102 LDPSAKIGDQLIEAIPSWTFKgkwwqrFKWRKKRAIELLHRVGikdhkdiMNSYP----HELTEGECQKVMIAMAIANQP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488618663 162 RLLILDEPTSVLTPQEAEELFvtlRHLAA----EGCSILFISHKLGEVRALCHSATVL 215
Cdd:COG4170 178 RLLIADEPTNAMESTTQAQIF---RLLARlnqlQGTSILLISHDLESISQWADTITVL 232
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
26-228 |
1.45e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.51 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 26 DAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNpAQARSLGIGMVFQHFSLFETLSVAQNI 105
Cdd:PRK09536 20 DGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALS-ARAASRRVASVPQDTSLSFEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 106 ALA----MGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEEL 181
Cdd:PRK09536 99 EMGrtphRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488618663 182 FVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAE 228
Cdd:PRK09536 179 LELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPAD 225
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
28-246 |
1.63e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 82.75 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQA-QTMRNPAQARSLGIGMVFQ--HFSLFETlSVAQN 104
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPlDYSKRGLLALRQQVATVFQdpEQQIFYT-DIDSD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 105 IALAMgAAAGTPKQleprirEVSQRYGMA---VEPQRLVHS----LSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQE 177
Cdd:PRK13638 99 IAFSL-RNLGVPEA------EITRRVDEAltlVDAQHFRHQpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488618663 178 AEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAECsdleLARLMVGDAEGLT 246
Cdd:PRK13638 172 RTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV----FACTEAMEQAGLT 236
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
10-220 |
1.76e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 83.48 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYP---GCL-------ANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPA 79
Cdd:PRK11308 6 LQAIDLKKHYPvkrGLFkperlvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 80 QARSL--GIGMVFQ--HFSLFETLSVAQNIA--LAMGAAAGTPKQLEpRIREVSQRYGMAVE-PQRLVHSLSIGERQKVE 152
Cdd:PRK11308 86 AQKLLrqKIQIVFQnpYGSLNPRKKVGQILEepLLINTSLSAAERRE-KALAMMAKVGLRPEhYDRYPHMFSGGQRQRIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488618663 153 IIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:PRK11308 165 IARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRC 233
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
10-220 |
2.21e-17 |
|
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: 81.51 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLAN--DAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLgIG 87
Cdd:cd03251 1 VEFKNVTFRYPGDGPPvlRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ-IG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 88 MVFQHFSLFETlSVAQNIALamGAAAGTPKQLEPR---------IREVSQRYGMAVEpQRLVhSLSIGERQKVEIIRCLM 158
Cdd:cd03251 80 LVSQDVFLFND-TVAENIAY--GRPGATREEVEEAaraanahefIMELPEGYDTVIG-ERGV-KLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488618663 159 QDIRLLILDEPTSVLTpQEAEELF-VTLRHLaAEGCSILFISHKLGEVRAlCHSATVLRNGKV 220
Cdd:cd03251 155 KDPPILILDEATSALD-TESERLVqAALERL-MKNRTTFVIAHRLSTIEN-ADRIVVLEDGKI 214
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
10-205 |
2.44e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 80.91 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSlGIGMV 89
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQ-QVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHFSLFETlSVAQNIALAMGAAAGTPKqlEPRIREVSQRYGMAVEP-QRLVHSLSIGERQKVEIIRCLMQDIRLLILDE 168
Cdd:PRK10247 87 AQTPTLFGD-TVYDNLIFPWQIRNQQPD--PAIFLDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 488618663 169 PTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEV 205
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREqNIAVLWVTHDKDEI 201
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
27-220 |
2.85e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 80.98 E-value: 2.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 27 AVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNP---AQARSLGIGMVFQHFSLFETLSVAQ 103
Cdd:PRK10584 28 GVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearAKLRAKHVGFVFQSFMLIPTLNALE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 104 NIALAMGAAAGTPKQLEPRIREVSQRYGMAvepQRLVH---SLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEE 180
Cdd:PRK10584 108 NVELPALLRGESSRQSRNGAKALLEQLGLG---KRLDHlpaQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488618663 181 LFVTLRHLAAE-GCSILFISHKLgEVRALCHSATVLRNGKV 220
Cdd:PRK10584 185 IADLLFSLNREhGTTLILVTHDL-QLAARCDRRLRLVNGQL 224
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
26-220 |
2.95e-17 |
|
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: 80.73 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 26 DAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLgIGMVFQHFSLFETlSVAQNI 105
Cdd:cd03254 20 KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM-IGVVLQDTFLFSG-TIMENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 106 ALamgaaaGTPKQLEPRIREVSQRYGMAVEPQRLV-----------HSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLT 174
Cdd:cd03254 98 RL------GRPNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488618663 175 P------QEA-EELFvtlrhlaaEGCSILFISHKLGEVRalchSAT---VLRNGKV 220
Cdd:cd03254 172 TetekliQEAlEKLM--------KGRTSIIIAHRLSTIK----NADkilVLDDGKI 215
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
24-228 |
3.34e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.02 E-value: 3.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 24 ANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNpAQARSL--GIGMVFQH--FSLFETl 99
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKK-VKLSDIrkKVGLVFQYpeYQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 100 SVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVEP--QRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQE 177
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDykDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488618663 178 AEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAE 228
Cdd:PRK13637 180 RDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
10-258 |
4.28e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.57 E-value: 4.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYP-GCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLGIGM 88
Cdd:PRK13644 2 IRLENVSYSYPdGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 89 VFQH-FSLFETLSVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILD 167
Cdd:PRK13644 82 VFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 168 EPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRAlCHSATVLRNGKVSGHCIPAEC-SDLELARL------MVG 240
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVlSDVSLQTLgltppsLIE 240
|
250 260
....*....|....*....|...
gi 488618663 241 DAEGLTAH-----YDKVSGSEAF 258
Cdd:PRK13644 241 LAENLKMHgvvipWENTSSPSSF 263
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
259-484 |
1.67e-16 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 78.70 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 259 LRVDKLSWHNPDPFGCS--LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtLPHAQATTLRFQDTPVGDLRPDARR 336
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILG---LLKPTSGSIIFDGKDLLKLSRRLRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 337 KHG--LAFVPAErlghgavPELSLadNALLTAFQQ---GLVSHGliqRGKVRALADEIIRRFAVKTTDAQAAARS----L 407
Cdd:cd03257 79 IRRkeIQMVFQD-------PMSSL--NPRMTIGEQiaePLRIHG---KLSKKEARKEAVLLLLVGVGLPEEVLNRypheL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488618663 408 SGGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIALRDA-GAAILVISEDLDELFQISDRLAALSGGQL 484
Cdd:cd03257 147 SGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-465 |
1.73e-16 |
|
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: 82.29 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 11 QLRHITKRYPG---CLANdaVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPdagsiiWQGQAQTMRNpaqarsLGIG 87
Cdd:TIGR03719 6 TMNRVSKVVPPkkeILKD--ISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKD------FNGEARPQPG------IKVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 88 MVFQHFSLFETLSVAQNIALAMGAAagtpKQLEPRIREVSQRYG---------------------------------MAV 134
Cdd:TIGR03719 72 YLPQEPQLDPTKTVRENVEEGVAEI----KDALDRFNEISAKYAepdadfdklaaeqaelqeiidaadawdldsqleIAM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 135 EPQRL------VHSLSIGERQKVEIIRCLMQDIRLLILDEPTSvltpqeaeelfvtlrHLAAEgcSILFISHKL----GE 204
Cdd:TIGR03719 148 DALRCppwdadVTKLSGGERRRVALCRLLLSKPDMLLLDEPTN---------------HLDAE--SVAWLERHLqeypGT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 205 VRALCHSATVLRNgkVS--------GHCIPAE---CSDLE--LARL-MVGDAEG-------------------------- 244
Cdd:TIGR03719 211 VVAVTHDRYFLDN--VAgwileldrGRGIPWEgnySSWLEqkQKRLeQEEKEESarqktlkrelewvrqspkgrqakska 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 245 -LTAhYDKVSGSEAFLRVDKLSWHNPDP----------------FGCSL--KDLSLEVRSGEIVGIAGVAGNGQDELLAL 305
Cdd:TIGR03719 289 rLAR-YEELLSQEFQKRNETAEIYIPPGprlgdkvieaenltkaFGDKLliDDLSFKLPPGGIVGVIGPNGAGKSTLFRM 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 306 LSGEQTlphAQATTLRFQDTPVgdlrpdarrkhgLAFVPAERLGhgavpelsLADNAllTAFQQglVSHGL--IQRGKVR 383
Cdd:TIGR03719 368 ITGQEQ---PDSGTIEIGETVK------------LAYVDQSRDA--------LDPNK--TVWEE--ISGGLdiIKLGKRE 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 384 ALADEIIRRFAVKTTDAQAAARSLSGGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIALrdAGAAIlVIS 463
Cdd:TIGR03719 421 IPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAV-VIS 497
|
..
gi 488618663 464 ED 465
Cdd:TIGR03719 498 HD 499
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-228 |
1.93e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 79.46 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 1 MSNHAIparlQLRHITKRYPGC--LANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGS---IIWQGQAQTM 75
Cdd:PRK13640 1 MKDNIV----EFKHVSFTYPDSkkPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 76 RNPAQARSlGIGMVFQH-FSLFETLSVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMA----VEPQrlvhSLSIGERQK 150
Cdd:PRK13640 77 KTVWDIRE-KVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLdyidSEPA----NLSGGQKQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488618663 151 VEIIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVrALCHSATVLRNGKVSGHCIPAE 228
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVE 229
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-171 |
2.15e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 82.48 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 5 AIPARlqlrHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAgsiiwqGQAQTMRNPAQARSL 84
Cdd:NF033858 266 AIEAR----GLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASE------GEAWLFGQPVDAGDI 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 85 G----IGMVFQHFSLFETLSVAQNIAL-----AMGAAagtpkQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQK----V 151
Cdd:NF033858 336 AtrrrVGYMSQAFSLYGELTVRQNLELharlfHLPAA-----EIAARVAEMLERFDLADVADALPDSLPLGIRQRlslaV 410
|
170 180
....*....|....*....|
gi 488618663 152 EIIrclmQDIRLLILDEPTS 171
Cdd:NF033858 411 AVI----HKPELLILDEPTS 426
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
256-492 |
2.18e-16 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 81.87 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 256 EAFLRVDKLSWHNPDPFGCSLKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGEQTLPHAQATTLRFQDTPVGDLRPDAR 335
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 336 RKHgLAFVPAErlghgavPELSLadNALLTAFQqglVSHGLIQRGKVRALADEIIRRFAVKTTDAQAAARS---LSGGNL 412
Cdd:COG1123 82 GRR-IGMVFQD-------PMTQL--NPVTVGDQ---IAEALENLGLSRAEARARVLELLEAVGLERRLDRYphqLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 413 QKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIAL-RDAGAAILVISEDLDELFQISDRLAALSGGQLSDLIPTE 491
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
.
gi 488618663 492 Q 492
Cdd:COG1123 229 E 229
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
276-482 |
2.42e-16 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 77.96 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGEqtLPHAQATtLRFQDTPVGDLRpdarrkhglafvpaERLGHgaVPE 355
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGL--LKPTSGS-IRVFGKPLEKER--------------KRIGY--VPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 356 LSLAD-NALLTAFQ---QGLVSH-GLIQR--GKVRALADEIIRRfaVKTTD-AQAAARSLSGGNLQKFILGREILQNPKL 427
Cdd:cd03235 76 RRSIDrDFPISVRDvvlMGLYGHkGLFRRlsKADKAKVDEALER--VGLSElADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488618663 428 LIAAHPTWGVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSGG 482
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
276-484 |
3.04e-16 |
|
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: 76.28 E-value: 3.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtLPHAQATTLRFQDTPVGDLRPDARRKhgLAFVPaerlghgavPE 355
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILG---LLKPDSGEIKVLGKDIKKEPEEVKRR--IGYLP---------EE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 356 LSLADNalLTAFqqglvshgliqrgkvraladEIIRrfavkttdaqaaarsLSGGNLQKFILGREILQNPKLLIAAHPTW 435
Cdd:cd03230 82 PSLYEN--LTVR--------------------ENLK---------------LSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488618663 436 GVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSGGQL 484
Cdd:cd03230 125 GLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
276-504 |
3.43e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.22 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGEQTlphAQATTLRFQDTPVGDLRPDARRKHGLAFVPAER-LghgaVP 354
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQ---PDSGEILLDGEPVRFRSPRDAQAAGIAIIHQELnL----VP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 355 ELSLADNALLTafqQGLVSHGLIQRGKVRALADEIIRRFAVKTtDAQAAARSLSGGNlQKFI-LGREILQNPKLLIAAHP 433
Cdd:COG1129 93 NLSVAENIFLG---REPRRGGLIDWRAMRRRARELLARLGLDI-DPDTPVGDLSVAQ-QQLVeIARALSRDARVLILDEP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488618663 434 TWGVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSGGQLSDLIPTEQTSTVQIGGWMAG 504
Cdd:COG1129 168 TASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVG 238
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
28-201 |
3.57e-16 |
|
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: 77.70 E-value: 3.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDA---GSIIWQGQAqtmRNPAQARSLgIGMVFQHFSLFETLSVAQN 104
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQP---RKPDQFQKC-VAYVRQDDILLPGLTVRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 105 IALAmgAAAGTPKQLEPRIRE------VSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEA 178
Cdd:cd03234 102 LTYT--AILRLPRKSSDAIRKkrvedvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTA 179
|
170 180
....*....|....*....|...
gi 488618663 179 EELFVTLRHLAAEGCSILFISHK 201
Cdd:cd03234 180 LNLVSTLSQLARRNRIVILTIHQ 202
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
28-220 |
3.76e-16 |
|
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: 77.51 E-value: 3.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLgIGMVFQHFSLFETlSVAQNIAL 107
Cdd:cd03248 33 VSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK-VSLVGQEPVLFAR-SLQDNIAY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 108 AMGAAAgtpkqlEPRIREVSQRYG-------MAVEPQRLV----HSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTpQ 176
Cdd:cd03248 111 GLQSCS------FECVKEAAQKAHahsfiseLASGYDTEVgekgSQLSGGQKQRVAIARALIRNPQVLILDEATSALD-A 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488618663 177 EAEELFVTLRHLAAEGCSILFISHKLGEV-RAlcHSATVLRNGKV 220
Cdd:cd03248 184 ESEQQVQQALYDWPERRTVLVIAHRLSTVeRA--DQILVLDGGRI 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
276-484 |
4.59e-16 |
|
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: 77.14 E-value: 4.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtLPHAQATTLRFQDTPVGDLRPDA----RRKHgLAFVPAErlgHG 351
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGG---LDRPTSGEVRVDGTDISKLSEKElaafRRRH-IGFVFQS---FN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 352 AVPELSLADNALLTAFQQGlvshglIQRGKVRALADEIIRRfaVKTTDAQAA-ARSLSGGNLQKFILGREILQNPKLLIA 430
Cdd:cd03255 93 LLPDLTALENVELPLLLAG------VPKKERRERAEELLER--VGLGDRLNHyPSELSGGQQQRVAIARALANDPKIILA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488618663 431 AHPTWGVDVGAAAAIHRALIAL-RDAGAAILVISEDlDELFQISDRLAALSGGQL 484
Cdd:cd03255 165 DEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-248 |
6.32e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.91 E-value: 6.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 3 NHAIPARLQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQA-QTMRNPAQA 81
Cdd:PRK10575 5 TNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPlESWSSKAFA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 82 RSlgIGMVFQHFSLFETLSVAQNIAL-------AMGAAAGTPKQlepRIREVSQRYGMAVEPQRLVHSLSIGERQKVEII 154
Cdd:PRK10575 85 RK--VAYLPQQLPAAEGMTVRELVAIgrypwhgALGRFGAADRE---KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 155 RCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAECSDLE 233
Cdd:PRK10575 160 MLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
250
....*....|....*
gi 488618663 234 LARLMVGDAEGLTAH 248
Cdd:PRK10575 240 TLEQIYGIPMGILPH 254
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
276-484 |
6.91e-16 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 77.16 E-value: 6.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtLPHAQATTLRFQDTPVGDLRPDA----RRKHGLAFvpaerlGHG 351
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVG---LLRPDSGEVLIDGEDISGLSEAElyrlRRRMGMLF------QSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 352 AV-PELSLADNallTAFqqGLVSHGLIQRGKVRALADEIIRRFAVKTtDAQAAARSLSGGnLQKFI-LGREILQNPKLLI 429
Cdd:cd03261 87 ALfDSLTVFEN---VAF--PLREHTRLSEEEIREIVLEKLEAVGLRG-AEDLYPAELSGG-MKKRVaLARALALDPELLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488618663 430 AAHPTWGVDVGAAAAIHRALIALRDA-GAAILVISEDLDELFQISDRLAALSGGQL 484
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
10-218 |
8.98e-16 |
|
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: 80.83 E-value: 8.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGClANDAVD---LTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAqTMRNPAQARSlGI 86
Cdd:TIGR01257 1938 LRLNELTKVYSGT-SSPAVDrlcVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKS-ILTNISDVHQ-NM 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 87 GMVFQHFSLFETLSVAQNIALaMGAAAGTPKQLEPRIREVS-QRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLI 165
Cdd:TIGR01257 2015 GYCPQFDAIDDLLTGREHLYL-YARLRGVPAEEIEKVANWSiQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488618663 166 LDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNG 218
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
7-173 |
1.02e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 78.73 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 7 PARLQLRHITKRYPG-CLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQaRslG 85
Cdd:PRK11650 1 MAGLKLQAVRKSYDGkTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-R--D 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 86 IGMVFQHFSLFETLSVAQNIALAMgAAAGTPK-QLEPRIREVSQRygMAVEP--QRLVHSLSIGERQKVEIIRCLMQDIR 162
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYGL-KIRGMPKaEIEERVAEAARI--LELEPllDRKPRELSGGQRQRVAMGRAIVREPA 154
|
170
....*....|.
gi 488618663 163 LLILDEPTSVL 173
Cdd:PRK11650 155 VFLFDEPLSNL 165
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
28-207 |
2.41e-15 |
|
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: 74.84 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLgigMVFQHFSLFET-LSVAQNia 106
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGL---LYLGHAPGIKTtLSVLEN-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 107 LAMGAAAGTPKQLEPRIREVsqryGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLR 186
Cdd:cd03231 94 LRFWHADHSDEQVEEALARV----GLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMA 169
|
170 180
....*....|....*....|..
gi 488618663 187 -HLAAEGCSILFISHKLGEVRA 207
Cdd:cd03231 170 gHCARGGMVVLTTHQDLGLSEA 191
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
24-206 |
2.46e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 77.05 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 24 ANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSL--GIGMVFQH--FSLFETL 99
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsDIQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 100 SVAQNIA--LAMGAAAGTPKQLEPRIREVSQRYGMAvePQ---RLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLT 174
Cdd:PRK15079 116 TIGEIIAepLRTYHPKLSRQEVKDRVKAMMLKVGLL--PNlinRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190
....*....|....*....|....*....|...
gi 488618663 175 PQEAEELFVTLRHLAAE-GCSILFISHKLGEVR 206
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVK 226
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
30-228 |
2.91e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 77.77 E-value: 2.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 30 LTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSL---GIGMVFQHFSLFETLSVAQNIA 106
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkKIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 107 LAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTP---QEAEELFV 183
Cdd:PRK10070 129 FGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPlirTEMQDELV 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488618663 184 TLRhlAAEGCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAE 228
Cdd:PRK10070 209 KLQ--AKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDE 251
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
12-220 |
3.75e-15 |
|
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: 74.88 E-value: 3.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 12 LRHITKRYP---GCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLgIGM 88
Cdd:cd03249 3 FKNVSFRYPsrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQ-IGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 89 VFQHFSLFETlSVAQNIALamGAAAGTPKQLEPRIR-----------------EVSQRYGMavepqrlvhsLSIGERQKV 151
Cdd:cd03249 82 VSQEPVLFDG-TIAENIRY--GKPDATDEEVEEAAKkanihdfimslpdgydtLVGERGSQ----------LSGGQKQRI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488618663 152 EIIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLrHLAAEGCSILFISHKLGEVRAlCHSATVLRNGKV 220
Cdd:cd03249 149 AIARALLRNPKILLLDEATSALDAESEKLVQEAL-DRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQV 215
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
23-205 |
5.21e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.51 E-value: 5.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 23 LANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQG-QAQTMRNPAQARSLGiGMVFQH--FSLFETL 99
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGlDTSDEENLWDIRNKA-GMVFQNpdNQIVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 100 sVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAE 179
Cdd:PRK13633 103 -VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRR 181
|
170 180
....*....|....*....|....*..
gi 488618663 180 ELFVTLRHLAAE-GCSILFISHKLGEV 205
Cdd:PRK13633 182 EVVNTIKELNKKyGITIILITHYMEEA 208
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
275-484 |
7.55e-15 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 73.60 E-value: 7.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 275 SLKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGEQTlphAQATTLRFQDTPVGDLR----PDARRKHGLAFVPAERLgh 350
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEEL---PTSGTIRVNGQDVSDLRgraiPYLRRKIGVVFQDFRLL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 351 gavPELSLADNALLtAFQQGLVSHGLIQRgKVRALADEIIRRFAVKTTDAQaaarsLSGGNLQKFILGREILQNPKLLIA 430
Cdd:cd03292 91 ---PDRNVYENVAF-ALEVTGVPPREIRK-RVPAALELVGLSHKHRALPAE-----LSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488618663 431 AHPTWGVDVGAAAAIHRALIALRDAGAAILVISEDlDELFQ-ISDRLAALSGGQL 484
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHA-KELVDtTRHRVIALERGKL 214
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-220 |
8.80e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 74.33 E-value: 8.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 3 NHAIParLQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIwQGQAQTmrnpAQAR 82
Cdd:PRK11247 8 NQGTP--LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-AGTAPL----AEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 83 SlGIGMVFQHFSLFETLSVAQNIALamgaaaGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIR 162
Cdd:PRK11247 81 E-DTRLMFQDARLLPWKKVIDNVGL------GLKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488618663 163 LLILDEP---TSVLTPQEAEELFVTL--RHlaaeGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:PRK11247 154 LLLLDEPlgaLDALTRIEMQDLIESLwqQH----GFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
28-207 |
8.84e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.99 E-value: 8.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQaqtmrnpaqarsLGIGMVFQHFSLFETLSVAqnIAL 107
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK------------LRIGYVPQKLYLDTTLPLT--VNR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 108 AMGAAAGTPKQ-LEPRIREVSQRYGMAVEPQRlvhsLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLR 186
Cdd:PRK09544 89 FLRLRPGTKKEdILPALKRVQAGHLIDAPMQK----LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLID 164
|
170 180
....*....|....*....|..
gi 488618663 187 HLAAE-GCSILFISHKLGEVRA 207
Cdd:PRK09544 165 QLRRElDCAVLMVSHDLHLVMA 186
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
28-200 |
1.01e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 73.91 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKII-----YGVTQpdaGSIIWQGQAQTMRNPAQARSLGIGMVFQHFSLFETLSVA 102
Cdd:CHL00131 26 LNLSINKGEIHAIMGPNGSGKSTLSKVIaghpaYKILE---GDILFKGESILDLEPEERAHLGIFLAFQYPIEIPGVSNA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 103 QNIALAMGA---AAGTPKqLEP-----RIREVSQRYGMavEPQRLVHSL----SIGERQKVEIIRCLMQDIRLLILDEPT 170
Cdd:CHL00131 103 DFLRLAYNSkrkFQGLPE-LDPlefleIINEKLKLVGM--DPSFLSRNVnegfSGGEKKRNEILQMALLDSELAILDETD 179
|
170 180 190
....*....|....*....|....*....|
gi 488618663 171 SVLTPQEAEELFVTLRHLAAEGCSILFISH 200
Cdd:CHL00131 180 SGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
27-207 |
1.16e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 72.78 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 27 AVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLG-IGmvfqHFS-LFETLSVAQN 104
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILyLG----HLPgLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 105 iaLAMGAAAGTPKQLEprIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQeAEELFVT 184
Cdd:TIGR01189 94 --LHFWAAIHGGAQRT--IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA-GVALLAG 168
|
170 180
....*....|....*....|....*
gi 488618663 185 L--RHLAAEGCSILFISHKLGEVRA 207
Cdd:TIGR01189 169 LlrAHLARGGIVLLTTHQDLGLVEA 193
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
30-220 |
1.49e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 76.30 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 30 LTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSlGIGMVFQHFSLFETlSVAQNIA--- 106
Cdd:TIGR00958 502 FTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHR-QVALVGQEPVLFSG-SVRENIAygl 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 107 ----LAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRlvHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQeAEELF 182
Cdd:TIGR00958 580 tdtpDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKG--SQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE-CEQLL 656
|
170 180 190
....*....|....*....|....*....|....*...
gi 488618663 183 VTLRHLAaeGCSILFISHKLGEVRAlCHSATVLRNGKV 220
Cdd:TIGR00958 657 QESRSRA--SRTVLLIAHRLSTVER-ADQILVLKKGSV 691
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
24-228 |
1.53e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 74.05 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 24 ANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIiwQGQAQTMRNPAQARSL-----GIGMVFQ--HFSLF 96
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTV--TVDDITITHKTKDKYIrpvrkRIGMVFQfpESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 97 ETlSVAQNIALAmgaaagtPKQLEPRIREVSQR-YGMAVEP--QRLVHSLSI-----GERQKVEIIRCLMQDIRLLILDE 168
Cdd:PRK13646 100 ED-TVEREIIFG-------PKNFKMNLDEVKNYaHRLLMDLgfSRDVMSQSPfqmsgGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488618663 169 PTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAE 228
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQTDeNKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKE 232
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
28-204 |
2.66e-14 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 74.37 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSL---GIGMVFQHFSLFETLSVAQN 104
Cdd:COG4175 46 ASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKELRELrrkKMSMVFQHFALLPHRTVLEN 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 105 IA--LAMgaaAGTPK-QLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTP------ 175
Cdd:COG4175 126 VAfgLEI---QGVPKaERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirrem 202
|
170 180 190
....*....|....*....|....*....|
gi 488618663 176 QeaEELfvtLRhLAAE-GCSILFISHKLGE 204
Cdd:COG4175 203 Q--DEL---LE-LQAKlKKTIVFITHDLDE 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-220 |
3.11e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 72.64 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 26 DAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQ--PDA---GSIIWQGQAQTMRNPAQARSLgIGMVFQHFSLFETLS 100
Cdd:PRK14247 20 DGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKMDVIELRRR-VQMVFQIPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 101 VAQNIALA--MGAAAGTPKQLEPRIREVSQRYGMAVEPQ-RL---VHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLT 174
Cdd:PRK14247 99 IFENVALGlkLNRLVKSKKELQERVRWALEKAQLWDEVKdRLdapAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488618663 175 PQEA---EELFVTLRhlaaEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:PRK14247 179 PENTakiESLFLELK----KDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
27-220 |
3.60e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 72.18 E-value: 3.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 27 AVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTqPDAGSIIWQGQA-QTMRNPAQARSLgiGMVFQHFSLFETLSVAQNI 105
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPlSDWSAAELARHR--AYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 106 ALAMgAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQ-------DIRLLILDEPTSVL--TPQ 176
Cdd:COG4138 91 ALHQ-PAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLdvAQQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488618663 177 EAeeLFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:COG4138 170 AA--LDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
28-489 |
3.93e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.89 E-value: 3.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKS----TLMKIIygvtqPDAGSIIWQGQAQTMRNPAQARSLG--------------IGMV 89
Cdd:PRK10261 35 LSFSLQRGETLAIVGESGSGKSvtalALMRLL-----EQAGGLVQCDKMLLRRRSRQVIELSeqsaaqmrhvrgadMAMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQH--FSLFETLSVAQNIALAMGAAAGTPKqlEPRIREVSQRYGMAVEPQ------RLVHSLSIGERQKVEIIRCLMQDI 161
Cdd:PRK10261 110 FQEpmTSLNPVFTVGEQIAESIRLHQGASR--EEAMVEAKRMLDQVRIPEaqtilsRYPHQLSGGMRQRVMIAMALSCRP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 162 RLLILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEV-------------------------RALCHS---- 211
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVaeiadrvlvmyqgeavetgsveqifHAPQHPytra 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 212 --ATVLRNGKVSGHCIPAEcsdLELARLMVGDAEGLTAHYDKVSGSEAFLRVDKLSWHNPDPFGC---------SLKDLS 280
Cdd:PRK10261 268 llAAVPQLGAMKGLDYPRR---FPLISLEHPAKQEPPIEQDTVVDGEPILQVRNLVTRFPLRSGLlnrvtrevhAVEKVS 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 281 LEVRSGEIVGIAGVAGNGQDEL-LALLSgeqtLPHAQATTLRFQ----DT-PVGDLRPDARRKHGLAFVPAERLGhgavP 354
Cdd:PRK10261 345 FDLWPGETLSLVGESGSGKSTTgRALLR----LVESQGGEIIFNgqriDTlSPGKLQALRRDIQFIFQDPYASLD----P 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 355 ELSLADNALltafqQGLVSHGLIQRGKVRALADEIIRRFAVKTTDAQAAARSLSGGNLQKFILGREILQNPKLLIAAHPT 434
Cdd:PRK10261 417 RQTVGDSIM-----EPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAV 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 488618663 435 WGVDVGAAAAIHRALIAL-RDAGAAILVISEDLDELFQISDRLAALSGGQLSDLIP 489
Cdd:PRK10261 492 SALDVSIRGQIINLLLDLqRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGP 547
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
7-99 |
4.39e-14 |
|
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: 74.83 E-value: 4.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 7 PARLQLRHITKRYPGCLANDA-----VDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQA 81
Cdd:COG4615 325 FQTLELRGVTYRYPGEDGDEGftlgpIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAY 404
|
90
....*....|....*...
gi 488618663 82 RSLgIGMVFQHFSLFETL 99
Cdd:COG4615 405 RQL-FSAVFSDFHLFDRL 421
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
31-220 |
4.69e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.89 E-value: 4.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 31 TIQPGEIHALLGENGAGKSTLMKIIYGVTqPDAGSIIWQGQA-QTMRNPAQARSLGIgMVFQHFSLFeTLSVAQNIALAM 109
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPlEAWSAAELARHRAY-LSQQQTPPF-AMPVFQYLTLHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 110 GAAAgTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQ-------DIRLLILDEPTSVLTPQEAEELF 182
Cdd:PRK03695 95 PDKT-RTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQQAALD 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 488618663 183 VTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:PRK03695 174 RLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
10-200 |
5.91e-14 |
|
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: 69.01 E-value: 5.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPG-CLANDaVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWqgqaqtmrnpaqarslGIGM 88
Cdd:cd03221 1 IELENLSKTYGGkLLLKD-ISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW----------------GSTV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 89 VFQHFslfetlsvaqnialamgaaagtpkqleprirevsqrygmavePQrlvhsLSIGERQKVEIIRCLMQDIRLLILDE 168
Cdd:cd03221 64 KIGYF------------------------------------------EQ-----LSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190
....*....|....*....|....*....|..
gi 488618663 169 PTSVLTPQEAEELFVTLRHLaaEGCsILFISH 200
Cdd:cd03221 97 PTNHLDLESIEALEEALKEY--PGT-VILVSH 125
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
24-220 |
6.07e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 72.43 E-value: 6.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 24 ANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQ---------------------TMRNPAQAR 82
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEknkkktkekekvleklviqktRFKKIKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 83 SL--GIGMVFQ--HFSLFETlSVAQNI---ALAMGAaagTPKQLEPRIREVSQRYGMAVE-PQRLVHSLSIGERQKVEII 154
Cdd:PRK13651 102 EIrrRVGVVFQfaEYQLFEQ-TIEKDIifgPVSMGV---SKEEAKKRAAKYIELVGLDESyLQRSPFELSGGQKRRVALA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488618663 155 RCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:PRK13651 178 GILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
276-483 |
8.33e-14 |
|
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: 70.39 E-value: 8.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeQTLPhaQATTLRFQDTPVgdlrpDARRKHGLAFVPAERlghGAVPE 355
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILG-IILP--DSGEVLFDGKPL-----DIAARNRIGYLPEER---GLYPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 356 LSLADNALLTAFQQGLvshgliQRGKVRALADEIIRRFAVkTTDAQAAARSLSGGNLQKFILGREILQNPKLLIAAHPTW 435
Cdd:cd03269 85 MKVIDQLVYLAQLKGL------KKEEARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488618663 436 GVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSGGQ 483
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
9-220 |
1.63e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 73.07 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 9 RLQLRHITKRYPGCL-ANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSlGIG 87
Cdd:PRK13657 334 AVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRR-NIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 88 MVFQHFSLFETlSVAQNIALA--------MGAAAGTPKQLEpRIREVSQRYG-MAVEPQRlvhSLSIGERQKVEIIRCLM 158
Cdd:PRK13657 413 VVFQDAGLFNR-SIEDNIRVGrpdatdeeMRAAAERAQAHD-FIERKPDGYDtVVGERGR---QLSGGERQRLAIARALL 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488618663 159 QDIRLLILDEPTSVL---TPQEAEELFVTLRHlaaeGCSILFISHKLGEVRalchSAT---VLRNGKV 220
Cdd:PRK13657 488 KDPPILILDEATSALdveTEAKVKAALDELMK----GRTTFIIAHRLSTVR----NADrilVFDNGRV 547
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
28-220 |
2.08e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 70.54 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTmrnpAQARSLGI-------GMVFQ--HFSLFET 98
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLIT----STSKNKDIkqirkkvGLVFQfpESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 99 lSVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVEP-QRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQE 177
Cdd:PRK13649 102 -TVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488618663 178 AEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:PRK13649 181 RKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-220 |
2.47e-13 |
|
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: 73.12 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 24 ANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLgiGMVFQHFSLFETLSVAQ 103
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSL--GMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 104 NIALAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEELFV 183
Cdd:TIGR01257 1023 HILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
|
170 180 190
....*....|....*....|....*....|....*..
gi 488618663 184 TLRHLAAeGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:TIGR01257 1103 LLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
9-200 |
2.72e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 72.31 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 9 RLQLRHITKRYP-GCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLgIG 87
Cdd:PRK10522 322 TLELRNVTFAYQdNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL-FS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 88 MVFQHFSLFETLsvaqniaLAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVH-SLSIGERQKVEIIRCLMQDIRLLIL 166
Cdd:PRK10522 401 AVFTDFHLFDQL-------LGPEGKPANPALVEKWLERLKMAHKLELEDGRISNlKLSKGQKKRLALLLALAEERDILLL 473
|
170 180 190
....*....|....*....|....*....|....*
gi 488618663 167 DEPTSVLTPQEAEELF-VTLRHLAAEGCSILFISH 200
Cdd:PRK10522 474 DEWAADQDPHFRREFYqVLLPLLQEMGKTIFAISH 508
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
276-484 |
2.74e-13 |
|
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: 68.93 E-value: 2.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeQTLPHAQATTLRFQDTpvgdLRPDARRKHGLAFVPAERlghGAVPE 355
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAG-LLEPDAGFATVDGFDV----VKEPAEARRRLGFVSDST---GLYDR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 356 LSLADNALLTAfqqGLvsHGLiQRGKVRALADEIIRRFAVKTTdAQAAARSLSGGNLQKFILGREILQNPKLLIAAHPTW 435
Cdd:cd03266 93 LTARENLEYFA---GL--YGL-KGDELTARLEELADRLGMEEL-LDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488618663 436 GVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSGGQL 484
Cdd:cd03266 166 GLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
26-208 |
3.10e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 72.29 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 26 DAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMR---NPAQAR--------SLGIGMVFQHFS 94
Cdd:PRK11147 20 DNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARlqqDPPRNVegtvydfvAEGIEEQAEYLK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 95 LFETLS--VAQNIALAMGAAAGTPK---------QLEPRIREVSQRYGMavEPQRLVHSLSIGERQKVEIIRCLMQDIRL 163
Cdd:PRK11147 100 RYHDIShlVETDPSEKNLNELAKLQeqldhhnlwQLENRINEVLAQLGL--DPDAALSSLSGGWLRKAALGRALVSNPDV 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488618663 164 LILDEPTSVLTPQEAE--ELFVtlrhLAAEGcSILFISHKLGEVRAL 208
Cdd:PRK11147 178 LLLDEPTNHLDIETIEwlEGFL----KTFQG-SIIFISHDRSFIRNM 219
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
28-192 |
4.25e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 68.36 E-value: 4.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPA-QARSLGigmvfqHFS-LFETLSVAQNI 105
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeACHYLG------HRNaMKPALTVAENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 106 ALamgaAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPqEAEELFVTL 185
Cdd:PRK13539 95 EF----WAAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA-AAVALFAEL 169
|
....*....
gi 488618663 186 --RHLAAEG 192
Cdd:PRK13539 170 irAHLAQGG 178
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
276-483 |
4.37e-13 |
|
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: 66.88 E-value: 4.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGEQTLPHAqatTLRFQDTPVGDLRPDARRKHgLAFVPaerlghgavpe 355
Cdd:cd00267 15 LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSG---EILIDGKDIAKLPLEELRRR-IGYVP----------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 356 lsladnalltafqqglvshgliqrgkvraladeiirrfavkttdaqaaarSLSGGNLQKFILGREILQNPKLLIAAHPTW 435
Cdd:cd00267 80 --------------------------------------------------QLSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488618663 436 GVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSGGQ 483
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
26-228 |
4.66e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 69.35 E-value: 4.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 26 DAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSlGIGMVFQH-FSLFETLSVAQN 104
Cdd:PRK13642 24 NGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRR-KIGMVFQNpDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 105 IALAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEELFVT 184
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488618663 185 LRHLAAE-GCSILFISHKLGEVrALCHSATVLRNGKVSGHCIPAE 228
Cdd:PRK13642 183 IHEIKEKyQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSE 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
28-228 |
5.34e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 69.38 E-value: 5.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGS------IIWQGQAQTMRNPAQARslgIGMVFQ--HFSLFETl 99
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKvtvgdiVVSSTSKQKEIKPVRKK---VGVVFQfpESQLFEE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 100 SVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVEP-QRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEA 178
Cdd:PRK13643 101 TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488618663 179 EELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAE 228
Cdd:PRK13643 181 IEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSD 230
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1-220 |
5.39e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 70.15 E-value: 5.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 1 MSNHAIPArLQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAG--KSTLMKIIYGvtqPDAGSIIWQGQAQTMRNP 78
Cdd:NF000106 6 ISNGARNA-VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCANRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 79 AQARSLGIGMVFQHfSLFETLSVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLM 158
Cdd:NF000106 82 ALRRTIG*HRPVR*-GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488618663 159 QDIRLLILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:NF000106 161 GRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRV 222
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
28-228 |
5.58e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 69.28 E-value: 5.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSI-IWQGQAQTMRNPAQARSL--GIGMVFQ---HfSLFETlSV 101
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtIGERVITAGKKNKKLKPLrkKVGIVFQfpeH-QLFEE-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 102 AQNIALAMGAAAGTPKQLEPRIREVSQRYGMavEPQRLVHS---LSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQ-- 176
Cdd:PRK13634 104 EKDICFGPMNFGVSEEDAKQKAREMIELVGL--PEELLARSpfeLSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKgr 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488618663 177 -EAEELFVTLRHlaAEGCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAE 228
Cdd:PRK13634 182 kEMMEMFYKLHK--EKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPRE 232
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
259-483 |
6.79e-13 |
|
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: 66.83 E-value: 6.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 259 LRVDKLSWHNPDPFgcSLKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGEQTLPhaqATTLRFQDTPVGDLR---PDAR 335
Cdd:cd03229 1 LELKNVSKRYGQKT--VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPD---SGSILIDGEDLTDLEdelPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 336 RKHGLAFVPaerlgHGAVPELSLADNALLtafqqglvshgliqrgkvraladeiirrfavkttdaqaaarSLSGGNLQKF 415
Cdd:cd03229 76 RRIGMVFQD-----FALFPHLTVLENIAL-----------------------------------------GLSGGQQQRV 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488618663 416 ILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIALRD-AGAAILVISEDLDELFQISDRLAALSGGQ 483
Cdd:cd03229 110 ALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAqLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
276-492 |
8.40e-13 |
|
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: 68.68 E-value: 8.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtLPHAQATTLRFQDTPVGDLRPDARR--KHGLAFVPAERLGhgav 353
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLG---LEKPAQGTVSFRGQDLYQLDRKQRRafRRDVQLVFQDSPS---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 354 pelslADNALLTAFQ---QGLVSHGLIQRGKVRALADEIIRRFAVKTTDAQAAARSLSGGNLQKFILGREILQNPKLLIA 430
Cdd:TIGR02769 100 -----AVNPRMTVRQiigEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488618663 431 AHPTWGVDVGAAAAIHRALIALRDA-GAAILVISEDLDELFQISDRLAALSGGQLSDLIPTEQ 492
Cdd:TIGR02769 175 DEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQ 237
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
276-499 |
8.41e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.00 E-value: 8.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqTLPHaQATTLRFQDTPVGDLRPDARRKHGLAFVPAERlghGAVPE 355
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVG--IVPR-DAGNIIIDDEDISLLPLHARARRGIGYLPQEA---SIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 356 LSLADNaLLTAFQqglVSHGLIQRGKvRALADEIIRRFAVKTTdAQAAARSLSGGNLQKFILGREILQNPKLLIAAHPTW 435
Cdd:PRK10895 93 LSVYDN-LMAVLQ---IRDDLSAEQR-EDRANELMEEFHIEHL-RDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 436 GVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSGGQL------SDLIPTEQTSTVQIG 499
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLiahgtpTEILQDEHVKRVYLG 236
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
276-492 |
1.11e-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: 67.59 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSG-EQTLPHAQAT-TLRFQDTPVGDLRPDA---RRKHGLAFvpaerlGH 350
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlNDLIPGAPDEgEVLLDGKDIYDLDVDVlelRRRVGMVF------QK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 351 GAVPELSLADNALLtafqqGLVSHGLIQRGKVRALADEIIRRFAVKT-TDAQAAARSLSGGNLQKFILGREILQNPKLLI 429
Cdd:cd03260 90 PNPFPGSIYDNVAY-----GLRLHGIKLKEELDERVEEALRKAALWDeVKDRLHALGLSGGQQQRLCLARALANEPEVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488618663 430 AAHPTWGVDVGAAAAIHRALIALRDAgAAILVISEDLDELFQISDRLAALSGGQLSDLIPTEQ 492
Cdd:cd03260 165 LDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQ 226
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
26-196 |
1.44e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 66.75 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 26 DAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSL-------GIGMVfqhFSLFET 98
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLlylghqpGIKTE---LTALEN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 99 LSVAQNIALAMGAAAgtpkqleprIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEA 178
Cdd:PRK13538 95 LRFYQRLHGPGDDEA---------LWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGV 165
|
170
....*....|....*....
gi 488618663 179 EELFVTL-RHLAAEGCSIL 196
Cdd:PRK13538 166 ARLEALLaQHAEQGGMVIL 184
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-240 |
1.52e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 67.70 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 7 PARLQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSiIWQGQAQTMRNPAQARSLGI 86
Cdd:PRK10253 5 VARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGH-VWLDGEHIQHYASKEVARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 87 GMVFQHFSLFETLSVAQniALAMGAAAGTP------KQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQD 160
Cdd:PRK10253 84 GLLAQNATTPGDITVQE--LVARGRYPHQPlftrwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 161 IRLLILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVralCHSAT---VLRNGKVSGHCIPAECSDLELAR 236
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQA---CRYAShliALREGKIVAQGAPKEIVTAELIE 238
|
....
gi 488618663 237 LMVG 240
Cdd:PRK10253 239 RIYG 242
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-200 |
1.58e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 70.08 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 17 KRYPGCLANDAVDLTI--------QPGEIHALLGENGAGKSTLMKIIYGVTQPD---AGSIIWQGQ---AQTMRnpaqAR 82
Cdd:TIGR00955 25 SRLRGCFCRERPRKHLlknvsgvaKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMpidAKEMR----AI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 83 SlgiGMVFQHFSLFETLSVAQNIA----LAMGAAAGTPKQLEpRIREVSQRYGMA------VEPQRLVHSLSIGERQKVE 152
Cdd:TIGR00955 101 S---AYVQQDDLFIPTLTVREHLMfqahLRMPRRVTKKEKRE-RVDEVLQALGLRkcantrIGVPGRVKGLSGGERKRLA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488618663 153 IIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISH 200
Cdd:TIGR00955 177 FASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
278-483 |
1.80e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 68.29 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 278 DLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtLPHAQATTLRFQDTPVGDLRPDARRKHGLafVPA-ERLGhgavPEL 356
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLG---LTHPDAGSISLCGEPVPSRARHARQRVGV--VPQfDNLD----PDF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 357 SLADNALLTAFQQGLVSHgliqrgKVRALADEIIRrFAVKTTDAQAAARSLSGGNLQKFILGREILQNPKLLIAAHPTWG 436
Cdd:PRK13537 96 TVRENLLVFGRYFGLSAA------AARALVPPLLE-FAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488618663 437 VDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSGGQ 483
Cdd:PRK13537 169 LDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
24-219 |
2.37e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 67.91 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 24 ANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDagsiiWQGQAQTMR---------NPAQARSL---GIGMVFQ 91
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDN-----WRVTADRMRfddidllrlSPRERRKLvghNVSMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 92 HFSlfETLSVAQNIA--LAMGAAAGTPK-----QLEPRIR---EVSQRYGMAvEPQRLVHS----LSIGERQKVEIIRCL 157
Cdd:PRK15093 97 EPQ--SCLDPSERVGrqLMQNIPGWTYKgrwwqRFGWRKRraiELLHRVGIK-DHKDAMRSfpyeLTEGECQKVMIAIAL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488618663 158 MQDIRLLILDEPTSVLTPQEAEELFVTLRHL-AAEGCSILFISHKLGEVRALCHSATVLRNGK 219
Cdd:PRK15093 174 ANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
28-202 |
2.55e-12 |
|
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: 69.08 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAqtMRNPAQArSL--GIGMVFQHFSLFETlSVAQNI 105
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQD--IRDVTQA-SLraAIGIVPQDTVLFND-TIAYNI 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 106 ALA-MGA------AAGTPKQLEPRIREVSQRYGMAVEPQRLvhSLSIGERQKVEIIRCLMQDIRLLILDEPTSVL---TP 175
Cdd:COG5265 453 AYGrPDAseeeveAAARAAQIHDFIESLPDGYDTRVGERGL--KLSGGEKQRVAIARTLLKNPPILIFDEATSALdsrTE 530
|
170 180
....*....|....*....|....*..
gi 488618663 176 QEAEElfvTLRhLAAEGCSILFISHKL 202
Cdd:COG5265 531 RAIQA---ALR-EVARGRTTLVIAHRL 553
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
276-434 |
2.87e-12 |
|
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: 64.59 E-value: 2.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtLPHAQATTLRFQDTPVGDLRPDARRKHgLAFVPAErlgHGAVPE 355
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAG---LLSPTEGTILLDGQDLTDDERKSLRKE-IGYVFQD---PQLFPR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 356 LSLADNALLTAFQQGLvshgliQRGKVRALADEIIRRFAVKTTDAQAA---ARSLSGGNLQKFILGREILQNPKLLIAAH 432
Cdd:pfam00005 74 LTVRENLRLGLLLKGL------SKREKDARAEEALEKLGLGDLADRPVgerPGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
..
gi 488618663 433 PT 434
Cdd:pfam00005 148 PT 149
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
30-220 |
2.96e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.22 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 30 LTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQtmrNPAQARSLgIGMVFQHFSLFETLSVAQNIALAM 109
Cdd:PRK15056 28 FTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT---RQALQKNL-VAYVPQSEEVDWSFPVLVEDVVMM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 110 G--AAAGTPKQLEPRIREVSQ----RYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEELFV 183
Cdd:PRK15056 104 GryGHMGWLRRAKKRDRQIVTaalaRVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIIS 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 488618663 184 TLRHLAAEGCSILFISHKLGEVRALChSATVLRNGKV 220
Cdd:PRK15056 184 LLRELRDEGKTMLVSTHNLGSVTEFC-DYTVMVKGTV 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
276-481 |
3.91e-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: 65.57 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtLPHAQATTLRFQDTPVGDLRPDarrkhgLAFVPAErlgHGAVPE 355
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAG---LERPTSGEVLVDGEPVTGPGPD------RGYVFQQ---DALLPW 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 356 LSLADNALLtafqqGLVSHGlIQRGKVRALADEIIRRFAVKTTdAQAAARSLSGGNLQKFILGREILQNPKLLIAAHPTW 435
Cdd:cd03293 88 LTVLDNVAL-----GLELQG-VPKAEARERAEELLELVGLSGF-ENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488618663 436 GVDVGAAAAIHRALIAL-RDAGAAILVISEDLDELFQISDRLAALSG 481
Cdd:cd03293 161 ALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
10-202 |
4.12e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 68.31 E-value: 4.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPG--CLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSlGIG 87
Cdd:PRK11160 339 LTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQ-AIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 88 MVFQHFSLFETlSVAQNIALAmgaaagTPKQLEPRIREVSQRYGMavepQRLVHS--------------LSIGERQKVEI 153
Cdd:PRK11160 418 VVSQRVHLFSA-TLRDNLLLA------APNASDEALIEVLQQVGL----EKLLEDdkglnawlgeggrqLSGGEQRRLGI 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488618663 154 IRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAeGCSILFISHKL 202
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHRL 534
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
24-234 |
4.13e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 66.96 E-value: 4.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 24 ANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQA--QTMRNPAQARSL--GIGMVFQ--HFSLFE 97
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAipANLKKIKEVKRLrkEIGLVFQfpEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 98 TlSVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAVE-PQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQ 176
Cdd:PRK13645 106 E-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488618663 177 eAEELFVTL--RHLAAEGCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAEC-SDLEL 234
Cdd:PRK13645 185 -GEEDFINLfeRLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIfSNQEL 244
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
10-187 |
4.14e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 66.34 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKII--YGVTQPD---AGSIIWQGQaqTMRNP----AQ 80
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGH--NIYSPrtdtVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 81 ARSlGIGMVFQHFSLFeTLSVAQNIALAMGAAAGTPKQLEPRIREVSQRyGMAV--EPQRLVH----SLSIGERQKVEII 154
Cdd:PRK14239 84 LRK-EIGMVFQQPNPF-PMSIYENVVYGLRLKGIKDKQVLDEAVEKSLK-GASIwdEVKDRLHdsalGLSGGQQQRVCIA 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 488618663 155 RCLMQDIRLLILDEPTSVLTPQEA---EELFVTLRH 187
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAgkiEETLLGLKD 196
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
10-220 |
4.64e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.34 E-value: 4.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYP---GCL--------ANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNP 78
Cdd:PRK10261 314 LQVRNLVTRFPlrsGLLnrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSP 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 79 AQARSL--GIGMVFQ--HFSLFETLSVAQNI-------ALAMGAAAgtpkqlEPRIREVSQRYGMAVE-PQRLVHSLSIG 146
Cdd:PRK10261 394 GKLQALrrDIQFIFQdpYASLDPRQTVGDSImeplrvhGLLPGKAA------AARVAWLLERVGLLPEhAWRYPHEFSGG 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488618663 147 ERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:PRK10261 468 QRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
15-200 |
4.87e-12 |
|
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: 68.27 E-value: 4.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 15 ITKRYPGclandaVDLTIQPGEIH-----ALLGENGAGKSTLMKIIYGVTQPDAGSIIWQgqaqtmrnpaqarsLGIGMV 89
Cdd:COG1245 347 LTKSYGG------FSLEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEVDED--------------LKISYK 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHFSLFETLSVAQNIALAMGAAAGTPKQLEprirEVSQRygMAVEP--QRLVHSLSIGERQKVEIIRCLMQDIRLLILD 167
Cdd:COG1245 407 PQYISPDYDGTVEEFLRSANTDDFGSSYYKT----EIIKP--LGLEKllDKNVKDLSGGELQRVAIAACLSRDADLYLLD 480
|
170 180 190
....*....|....*....|....*....|....*..
gi 488618663 168 EPTSVLtpqEAEE-LFVT--LRHLAAE-GCSILFISH 200
Cdd:COG1245 481 EPSAHL---DVEQrLAVAkaIRRFAENrGKTAMVVDH 514
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
11-228 |
5.20e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 65.87 E-value: 5.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 11 QLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQA-QTMRNPAQARSLGIgmV 89
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDvATTPSRELAKRLAI--L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQ--HFSLfeTLSVAQNIALamGA---AAGTPKQLEPRIREVSQRYgMAVEP--QRLVHSLSIGERQKVEIIRCLMQDIR 162
Cdd:COG4604 81 RQenHINS--RLTVRELVAF--GRfpySKGRLTAEDREIIDEAIAY-LDLEDlaDRYLDELSGGQRQRAFIAMVLAQDTD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488618663 163 LLILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGevRALCHSATV--LRNGKVSGHCIPAE 228
Cdd:COG4604 156 YVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDIN--FASCYADHIvaMKDGRVVAQGTPEE 222
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-173 |
6.35e-12 |
|
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: 65.51 E-value: 6.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 31 TIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQG-------QAQTMRNPAQARSL--GIGMVFQHFSLFETlSV 101
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdtvsykpQYIKADYEGTVRDLlsSITKDFYTHPYFKT-EI 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488618663 102 AQnialamgaaagtPKQLEPRIrevsqrygmavepQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVL 173
Cdd:cd03237 100 AK------------PLQIEQIL-------------DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
275-484 |
7.04e-12 |
|
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: 65.08 E-value: 7.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 275 SLKDLSLEVRSGEIVGIAGVAGNGQDELLALLsgeqtlphaqaTTLrfqdtpvgdLRPDARRKH--GLAFV--PAE-RLG 349
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKML-----------TTL---------LKPTSGRATvaGHDVVrePREvRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 350 HGAVPELSLADNALlTAFQQgLVSHGLIQ---RGKVRALADEIIRRFAVkTTDAQAAARSLSGGNLQKFILGREILQNPK 426
Cdd:cd03265 75 IGIVFQDLSVDDEL-TGWEN-LYIHARLYgvpGAERRERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488618663 427 LLIAAHPTWGVDVGAAAAIHRALIAL-RDAGAAILVISEDLDELFQISDRLAALSGGQL 484
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
26-249 |
9.21e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 65.62 E-value: 9.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 26 DAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQ---AQTMRNPAQARSLGIGMVFQhFS---LFETl 99
Cdd:PRK13641 24 DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitPETGNKNLKKLRKKVSLVFQ-FPeaqLFEN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 100 SVAQNIALAMGAAAGTPKQLEPRIREVSQRYGMAvePQRLVHS---LSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQ 176
Cdd:PRK13641 102 TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLS--EDLISKSpfeLSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488618663 177 EAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAEcsdlelarlMVGDAEGLTAHY 249
Cdd:PRK13641 180 GRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKE---------IFSDKEWLKKHY 243
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-220 |
9.55e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 65.45 E-value: 9.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKI------IYGVTQPDAGSIIWQGQAQTMRNPAQARSlGIGMVFQHFSLFETLSV 101
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVlnrlieIYDSKIKVDGKVLYFGKDIFQIDAIKLRK-EVGMVFQQPNPFPHLSI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 102 AQNIALAMGAAAGTPKQLEPRIREVSQR-YGMAVEPQRLVHS----LSIGERQKVEIIRCLMQDIRLLILDEPTS---VL 173
Cdd:PRK14246 108 YDNIAYPLKSHGIKEKREIKKIVEECLRkVGLWKEVYDRLNSpasqLSGGQQQRLTIARALALKPKVLLMDEPTSmidIV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488618663 174 TPQEAEELFVTLRHLAAegcsILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:PRK14246 188 NSQAIEKLITELKNEIA----IVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
10-200 |
1.40e-11 |
|
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: 66.88 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWqgqAQTMRnpaqarslgIGMV 89
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI---GETVK---------LAYV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQ-HFSLFETLSVAQNIalamgaaAGTPKQLEPRIREVSQR-YG-----MAVEPQRLVHSLSIGERQKVEIIRCLMQDIR 162
Cdd:TIGR03719 391 DQsRDALDPNKTVWEEI-------SGGLDIIKLGKREIPSRaYVgrfnfKGSDQQKKVGQLSGGERNRVHLAKTLKSGGN 463
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488618663 163 LLILDEPTSVLtpqEAEelfvTLRHL--AAE---GCSILfISH 200
Cdd:TIGR03719 464 VLLLDEPTNDL---DVE----TLRALeeALLnfaGCAVV-ISH 498
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
276-484 |
2.21e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 64.30 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGEQTLPHAQ----ATTLRF-QDTpvgdLRPDA---RRKHGLAFVPAEr 347
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKikvdGKVLYFgKDI----FQIDAiklRKEVGMVFQQPN- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 348 lghgAVPELSLADNalltaFQQGLVSHGLIQRGKVRALADEIIRRFAV--KTTDA-QAAARSLSGGNLQKFILGREILQN 424
Cdd:PRK14246 101 ----PFPHLSIYDN-----IAYPLKSHGIKEKREIKKIVEECLRKVGLwkEVYDRlNSPASQLSGGQQQRLTIARALALK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 425 PKLLIAAHPTWGVDVGAAAAIHRALIALRDAgAAILVISEDLDELFQISDRLAALSGGQL 484
Cdd:PRK14246 172 PKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
32-219 |
2.48e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.06 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 32 IQPGEIHALLGENGAGKSTLMKIIYGVTQPD--AGSIIWQGqaqtmRNPAQARSLGIGMVFQHFSLFETLSVAQNiaLAM 109
Cdd:PLN03211 91 ASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANN-----RKPTKQILKRTGFVTQDDILYPHLTVRET--LVF 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 110 GAAAGTPKQLEPRIR-----EVSQRYGMA-----VEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAE 179
Cdd:PLN03211 164 CSLLRLPKSLTKQEKilvaeSVISELGLTkcentIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAY 243
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488618663 180 ELFVTLRHLAAEGCSILFISHK-LGEVRALCHSATVLRNGK 219
Cdd:PLN03211 244 RLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
26-228 |
3.13e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 64.49 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 26 DAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSI----IWQGQ------------AQTMRNPAQARSLgIGMV 89
Cdd:PRK13631 43 NNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDkknnhelitnpySKKIKNFKELRRR-VSMV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQ--HFSLFETlSVAQNIALAmGAAAGTPKQlepRIREVSQRY--GMAVEPQRLVHS---LSIGERQKVEIIRCLMQDIR 162
Cdd:PRK13631 122 FQfpEYQLFKD-TIEKDIMFG-PVALGVKKS---EAKKLAKFYlnKMGLDDSYLERSpfgLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488618663 163 LLILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAE 228
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYE 262
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
259-483 |
3.49e-11 |
|
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: 63.36 E-value: 3.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 259 LRVDKLSWHNPDPFGcSLKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtLPHAQATTLRFQDTPVGDLRP----DA 334
Cdd:cd03256 1 IEVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNG---LVEPTSGSVLIDGTDINKLKGkalrQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 335 RRKHGLAFvpaerLGHGAVPELSLADNALLTAFQQ--------GLVSHGLIQRGKvRALADEIIRRFAVKTTDAqaaars 406
Cdd:cd03256 77 RRQIGMIF-----QQFNLIERLSVLENVLSGRLGRrstwrslfGLFPKEEKQRAL-AALERVGLLDKAYQRADQ------ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488618663 407 LSGGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIAL-RDAGAAILVISEDLDELFQISDRLAALSGGQ 483
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
28-220 |
3.74e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 65.30 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMrnpaqarSLGIGMVFQhfslfetLSVAQNI-- 105
Cdd:PRK13545 43 ISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALI-------AISSGLNGQ-------LTGIENIel 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 106 -ALAMGAAAGTPKQLEPRIREVSQRYGMAVEPqrlVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEELFVT 184
Cdd:PRK13545 109 kGLMMGLTKEKIKEIIPEIIEFADIGKFIYQP---VKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDK 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 488618663 185 LRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:PRK13545 186 MNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
9-202 |
4.33e-11 |
|
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: 62.51 E-value: 4.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 9 RLQLRHITKRYP--GCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLgI 86
Cdd:cd03244 2 DIEFKNVSLRYRpnLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR-I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 87 GMVFQHFSLFETlSVAQNI-------------ALAM----GAAAGTPKQLEPRIREVSQrygmavepqrlvhSLSIGERQ 149
Cdd:cd03244 81 SIIPQDPVLFSG-TIRSNLdpfgeysdeelwqALERvglkEFVESLPGGLDTVVEEGGE-------------NLSVGQRQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488618663 150 KVEIIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHlAAEGCSILFISHKL 202
Cdd:cd03244 147 LLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRL 198
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
24-220 |
5.43e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 63.30 E-value: 5.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 24 ANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMrnpaqarSLGIGMVFQhfslfetLSVAQ 103
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVI-------AISAGLSGQ-------LTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 104 NI---ALAMGAAAGTPKQLEPRIREVSQRYGMAVEPqrlVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEE 180
Cdd:PRK13546 105 NIefkMLCMGFKRKEIKAMTPKIIEFSELGEFIYQP---VKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488618663 181 LFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:PRK13546 182 CLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
15-200 |
8.25e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.44 E-value: 8.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 15 ITKRYPGclandaVDLTIQPGEIHA-----LLGENGAGKSTLMKIIYGVTQPDAGSIIWqgqaqtmrnpaqarSLGIGMV 89
Cdd:PRK13409 346 LTKKLGD------FSLEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKPDEGEVDP--------------ELKISYK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHFSLFETLSVAQNIALAMGAAAGTPKQLeprirEVSQRygMAVEP--QRLVHSLSIGERQKVEIIRCLMQDIRLLILD 167
Cdd:PRK13409 406 PQYIKPDYDGTVEDLLRSITDDLGSSYYKS-----EIIKP--LQLERllDKNVKDLSGGELQRVAIAACLSRDADLYLLD 478
|
170 180 190
....*....|....*....|....*....|....*..
gi 488618663 168 EPTSVLtpqEAEE-LFVT--LRHLAAE-GCSILFISH 200
Cdd:PRK13409 479 EPSAHL---DVEQrLAVAkaIRRIAEErEATALVVDH 512
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
11-170 |
1.01e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 64.38 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 11 QLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTqpdagsIIWQGQAQT----MRNPAQARSL-- 84
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGAR------KIQQGRVEVlggdMADARHRRAVcp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 85 -------GIGMvfqhfSLFETLSVAQNIAL-----AMGAAagtpkQLEPRIREVSQRYGMAVEPQRLVHSLSIGERQKVE 152
Cdd:NF033858 77 riaympqGLGK-----NLYPTLSVFENLDFfgrlfGQDAA-----ERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLG 146
|
170
....*....|....*...
gi 488618663 153 IIRCLMQDIRLLILDEPT 170
Cdd:NF033858 147 LCCALIHDPDLLILDEPT 164
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
10-173 |
1.75e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 63.50 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPG--CLANDAVDLTIQPGEIHALLGENGAGKSTLMKII---YGVTQpdaGSIIWQG---QAQTMRNPAQA 81
Cdd:PRK11176 342 IEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLtrfYDIDE---GEILLDGhdlRDYTLASLRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 82 rslgIGMVFQHFSLFETlSVAQNIALA---------------MGAAAGTPKQLEPRIREVSQRYGMavepqrlvhSLSIG 146
Cdd:PRK11176 419 ----VALVSQNVHLFND-TIANNIAYArteqysreqieeaarMAYAMDFINKMDNGLDTVIGENGV---------LLSGG 484
|
170 180
....*....|....*....|....*..
gi 488618663 147 ERQKVEIIRCLMQDIRLLILDEPTSVL 173
Cdd:PRK11176 485 QRQRIAIARALLRDSPILILDEATSAL 511
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
10-200 |
2.29e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.99 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQtmrnpaqarslgIGMV 89
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENAN------------IGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQ-HFSLFET-LSVAQNIALAMgaaagTPKQLEPRIREVSQRygM---AVEPQRLVHSLSIGERQKVEIIRCLMQDIRLL 164
Cdd:PRK15064 388 AQdHAYDFENdLTLFDWMSQWR-----QEGDDEQAVRGTLGR--LlfsQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVL 460
|
170 180 190
....*....|....*....|....*....|....*.
gi 488618663 165 ILDEPTSVLTPQEAEELFVTLRHLaaEGcSILFISH 200
Cdd:PRK15064 461 VMDEPTNHMDMESIESLNMALEKY--EG-TLIFVSH 493
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
10-220 |
2.49e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 61.34 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITK--RYPGCL-------ANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQ 80
Cdd:PRK15112 5 LEVRNLSKtfRYRTGWfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 81 aRSLGIGMVFQHFSlfETLSVAQNIALAMGA-----AAGTPKQLEPRIREVSQRYGMAVEPQRLV-HSLSIGERQKVEII 154
Cdd:PRK15112 85 -RSQRIRMIFQDPS--TSLNPRQRISQILDFplrlnTDLEPEQREKQIIETLRQVGLLPDHASYYpHMLAPGQKQRLGLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488618663 155 RCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHL-AAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:PRK15112 162 RALILRPKVIIADEALASLDMSMRSQLINLMLELqEKQGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
274-484 |
2.66e-10 |
|
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: 60.63 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 274 CSLKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtLPHAQATTLRFQDTPVGDLRPDARRKHGLAFVPAErlgHGAV 353
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVG---LVKPDSGKILLDGQDITKLPMHKRARLGIGYLPQE---ASIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 354 PELSLADNALLTAFQQGLVSHGLIQRgkvralADEIIRRFAVKTTdAQAAARSLSGGNLQKFILGREILQNPKLLIAAHP 433
Cdd:cd03218 88 RKLTVEENILAVLEIRGLSKKEREEK------LEELLEEFHITHL-RKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488618663 434 TWGVDVGAAAAIhRALIA-LRDAGAAILVISEDLDELFQISDRLAALSGGQL 484
Cdd:cd03218 161 FAGVDPIAVQDI-QKIIKiLKDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-202 |
3.11e-10 |
|
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: 62.49 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 31 TIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIiwqgqaqtmrnpaqARSLGIGMVFQHFS---LFE--------TL 99
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY--------------DEEPSWDEVLKRFRgteLQDyfkklangEI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 100 SVA---QNIALAMGAAAGTPKQLEPRI------REVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPT 170
Cdd:COG1245 161 KVAhkpQYVDLIPKVFKGTVRELLEKVdergklDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190
....*....|....*....|....*....|..
gi 488618663 171 SVLTPQEAEELFVTLRHLAAEGCSILFISHKL 202
Cdd:COG1245 241 SYLDIYQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
28-220 |
4.72e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 62.17 E-value: 4.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKIIYGVTqPDAGSIIWQGQAQTMRNPAQARSLgIGMVFQHFSLFETlSVAQNIAL 107
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKH-LSWVGQNPQLPHG-TLRDNVLL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 108 AMGAAAgtpkqlEPRIREVSQRYGMA--VE--PQRLVH-------SLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQ 176
Cdd:PRK11174 446 GNPDAS------DEQLQQALENAWVSefLPllPQGLDTpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488618663 177 EAEELFVTLRHlAAEGCSILFISHKLGEVRAlCHSATVLRNGKV 220
Cdd:PRK11174 520 SEQLVMQALNA-ASRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQI 561
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
278-477 |
5.51e-10 |
|
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: 60.84 E-value: 5.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 278 DLSLEVRSGEIVGIAG-------VAGngqdelLALLsgeQTLPHAQATT--LRFQDTPVGDLRPDARRK---HGLAFVPA 345
Cdd:COG0444 23 GVSFDVRRGETLGLVGesgsgksTLA------RAIL---GLLPPPGITSgeILFDGEDLLKLSEKELRKirgREIQMIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 346 ErlghgavPELSLadNALLTAFQQ---GLVSHGLIQRGKVRALADEIIRRfaVKTTDAQAAARS----LSGGNLQKFILG 418
Cdd:COG0444 94 D-------PMTSL--NPVMTVGDQiaePLRIHGGLSKAEARERAIELLER--VGLPDPERRLDRypheLSGGMRQRVMIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 419 REILQNPKLLIAAHPTWGVDVGAAAAIHRALIALRDA-GAAILVISEDLDELFQISDRLA 477
Cdd:COG0444 163 RALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVA 222
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-200 |
7.82e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.82 E-value: 7.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 1 MSNHAIPARLQLRHITKRypgclandaVDLTIQPGEIHALLGENGAGKSTLMKIIYG--VTQPDAGSI-IWQGQaqtmrn 77
Cdd:COG2401 31 LEAFGVELRVVERYVLRD---------LNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVdVPDNQ------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 78 paqarslgigmVFQHFSLFETLSVAQNIALAMG--AAAGtpkqleprirevsqrYGMAVEPQRLVHSLSIGERQKVEIIR 155
Cdd:COG2401 96 -----------FGREASLIDAIGRKGDFKDAVEllNAVG---------------LSDAVLWLRRFKELSTGQKFRFRLAL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488618663 156 CLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISH 200
Cdd:COG2401 150 LLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRaGITLVVATH 195
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
26-244 |
8.55e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.78 E-value: 8.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 26 DAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQaqtmRNPAQARSL------GIGMVFQHFSLFETL 99
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGE----NIPAMSRSRlytvrkRMSMLFQSGALFTDM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 100 SVAQNIALAMGAAAGTPkqlEPRIREVS----QRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEP---TSV 172
Cdd:PRK11831 100 NVFDNVAYPLREHTQLP---APLLHSTVmmklEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPfvgQDP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488618663 173 LTPQEAEELFVTLRHlaAEGCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAEC---SDLELARLMVGDAEG 244
Cdd:PRK11831 177 ITMGVLVKLISELNS--ALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALqanPDPRVRQFLDGIADG 249
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
276-486 |
1.02e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 58.67 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtLPHAQATTLRFQDTPVGDLRPDAR---RKHGLAFVPAerlGHGA 352
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGG---LDTPTSGDVIFNGQPMSKLSSAAKaelRNQKLGFIYQ---FHHL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 353 VPELSLADNalltafqqglVSHGLIQRGKVRALADEIIRR-FAVKTTDAQAAARS--LSGGNLQKFILGREILQNPKLLI 429
Cdd:PRK11629 99 LPDFTALEN----------VAMPLLIGKKKPAEINSRALEmLAAVGLEHRANHRPseLSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488618663 430 AAHPTWGVDVGAAAAIHRALIAL-RDAGAAILVISEDLdelfQISDRLA---ALSGGQLSD 486
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDL----QLAKRMSrqlEMRDGRLTA 225
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
28-237 |
1.39e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.13 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLGIGMVFQH---FSLFETLSVAQN 104
Cdd:PRK10982 267 VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFALVTEErrsTGIYAYLDIGFN 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 105 IALAMGAAAGTPKQL--EPRIREVSQRY--GMAVEP---QRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQE 177
Cdd:PRK10982 347 SLISNIRNYKNKVGLldNSRMKSDTQWVidSMRVKTpghRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGA 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 178 AEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAECSDLELARL 237
Cdd:PRK10982 427 KFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQNEILRL 486
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
259-484 |
1.45e-09 |
|
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: 57.23 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 259 LRVDKLSWHNPDPFGCSLKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtLPHAQATTLRFQDTPVGDLRPDARRKH 338
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILG---LLRPTSGRVRLDGADISQWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 339 glafvpaerlgHGAVPElslaDNALLTAfqqglvshgliqrgkvrALADEIirrfavkttdaqaaarsLSGGNLQKFILG 418
Cdd:cd03246 78 -----------VGYLPQ----DDELFSG-----------------SIAENI-----------------LSGGQRQRLGLA 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488618663 419 REILQNPKLLIAAHPTWGVDVGAAAAIHRALIALRDAGAAILVISEDLdELFQISDRLAALSGGQL 484
Cdd:cd03246 109 RALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
276-484 |
2.57e-09 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 57.51 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGEQTLPHAQATtlrFQDTPVGDLRPDARRKhgLAFVPAerlghgavpe 355
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAY---INGYSIRTDRKAARQS--LGYCPQ---------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 356 lslaDNALLTAF--QQGLVSHGLIQ---RGKVRALADEIIRRF---AVKTTdaqaAARSLSGGNLQKFILGREILQNPKL 427
Cdd:cd03263 83 ----FDALFDELtvREHLRFYARLKglpKSEIKEEVELLLRVLgltDKANK----RARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488618663 428 LIAAHPTWGVDVGAAAAIHRALIALRdAGAAILVISEDLDELFQISDRLAALSGGQL 484
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
11-170 |
2.98e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.36 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 11 QLRHITKRYPG---CLANdaVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPdagsiiWQGQAQTMRNpaqarsLGIG 87
Cdd:PRK11819 8 TMNRVSKVVPPkkqILKD--ISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKE------FEGEARPAPG------IKVG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 88 MVFQHFSLFETLSVAQNIALAMGAAagtpKQLEPRIREVSQRYG---------------------------------MAV 134
Cdd:PRK11819 74 YLPQEPQLDPEKTVRENVEEGVAEV----KAALDRFNEIYAAYAepdadfdalaaeqgelqeiidaadawdldsqleIAM 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488618663 135 EPQRL------VHSLSIGERQKVEIIRCLMQDIRLLILDEPT 170
Cdd:PRK11819 150 DALRCppwdakVTKLSGGERRRVALCRLLLEKPDMLLLDEPT 191
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
275-484 |
3.20e-09 |
|
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: 57.35 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 275 SLKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGEQTlPHAQATTLRFQDtpVGDLRPDarrKHGLAFVPAerlGHGAVP 354
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIK-PDSGKILLNGKD--ITNLPPE---KRDISYVPQ---NYALFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 355 ELSLADNalltafqqglVSHGLIQRGKVRALADEIIRRFAVKTTDAQAAAR---SLSGGNLQKFILGREILQNPKLLIAA 431
Cdd:cd03299 85 HMTVYKN----------IAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRkpeTLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488618663 432 HPTWGVDVgaaaAIHRALIAL-----RDAGAAILVISEDLDELFQISDRLAALSGGQL 484
Cdd:cd03299 155 EPFSALDV----RTKEKLREElkkirKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
259-484 |
3.56e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 57.69 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 259 LRVDKLSWHNPD--PfgcSLKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGEQTlPHAQATTLRFQDTpvGDLR--PDA 334
Cdd:PRK13644 2 IRLENVSYSYPDgtP---ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLR-PQKGKVLVSGIDT--GDFSklQGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 335 RRKHGLAFVPAERLGHGAVPELSLA---DNALLTAFQqglvshglIQRGKVRALADEIIRRFAVKTtdaqaaARSLSGGN 411
Cdd:PRK13644 76 RKLVGIVFQNPETQFVGRTVEEDLAfgpENLCLPPIE--------IRKRVDRALAEIGLEKYRHRS------PKTLSGGQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488618663 412 LQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIALRDAGAAILVISEDLDELfQISDRLAALSGGQL 484
Cdd:PRK13644 142 GQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKI 213
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
7-220 |
4.07e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 57.40 E-value: 4.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 7 PARLQLRHITKRYPGCLANDaVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPD----AGSIIWQGQAQTmrnPAQAR 82
Cdd:PRK10418 2 PQQIELRNIALQAAQPLVHG-VSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVA---PCALR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 83 SLGIGMVFQH-FSLFETLSVAQNIALAMGAAAGTPKQlEPRIREVSQRYGMAvEPQRLVHS----LSIGERQKVEIIRCL 157
Cdd:PRK10418 78 GRKIATIMQNpRSAFNPLHTMHTHARETCLALGKPAD-DATLTAALEAVGLE-NAARVLKLypfeMSGGMLQRMMIALAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488618663 158 MQDIRLLILDEPTSVLTP-QEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:PRK10418 156 LCEAPFIIADEPTTDLDVvAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-200 |
4.12e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 57.16 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQ--PDA---------GSIIWQGQAqtmrNPAQARSlGIGMVFQHFSLF 96
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEArvegevrlfGRNIYSPDV----DPIEVRR-EVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 97 ETLSVAQNIALA--MGAAAGTPKQLEPRIREVSQRYGMAVEPQ-RL---VHSLSIGERQKVEIIRCLMQDIRLLILDEPT 170
Cdd:PRK14267 98 PHLTIYDNVAIGvkLNGLVKSKKELDERVEWALKKAALWDEVKdRLndyPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190
....*....|....*....|....*....|...
gi 488618663 171 SVLTP---QEAEELFVTLRhlaaEGCSILFISH 200
Cdd:PRK14267 178 ANIDPvgtAKIEELLFELK----KEYTIVLVTH 206
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
32-196 |
4.86e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 56.10 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 32 IQPGEIHALLGENGAGKSTLM------KIIYGVTqpdaGSIIWQGQAqtmRNPAQARSlgIGMVFQHFSLFETLSVaqni 105
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLdvlagrKTAGVIT----GEILINGRP---LDKNFQRS--TGYVEQQDVHSPNLTV---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 106 alamgaaagtpkqlepriREvsqrygmAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEELFVTL 185
Cdd:cd03232 97 ------------------RE-------ALRFSALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFL 151
|
170
....*....|.
gi 488618663 186 RHLAAEGCSIL 196
Cdd:cd03232 152 KKLADSGQAIL 162
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
28-186 |
5.03e-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: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKIIYGV--TQPDA---GSIIWQGQ---AQTMrNPAQARSLgIGMVFQHFSLFeTL 99
Cdd:COG1117 30 INLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGArveGEILLDGEdiyDPDV-DVVELRRR-VGMVFQKPNPF-PK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 100 SVAQNIALAmgaaagtpkqlePRIREVSQRYGMA--VEP---------------QRLVHSLSIGERQKVEIIRCLMQDIR 162
Cdd:COG1117 107 SIYDNVAYG------------LRLHGIKSKSELDeiVEEslrkaalwdevkdrlKKSALGLSGGQQQRLCIARALAVEPE 174
|
170 180
....*....|....*....|....*..
gi 488618663 163 LLILDEPTSVLTPQEA---EELFVTLR 186
Cdd:COG1117 175 VLLMDEPTSALDPISTakiEELILELK 201
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
243-484 |
6.35e-09 |
|
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: 56.57 E-value: 6.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 243 EGLTAHYDKVSGSEAFLRVDKLSWHNPDPFGCSLKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtLPHAQATTLRf 322
Cdd:cd03267 4 SNLSKSYRVYSKEPGLIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSG---LLQPTSGEVR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 323 qdtpVGDLRPDARRK---HGLAFVPAERlgHGAVPELSLADNALLTAFQQGLVSHGLIQRgkVRALADEI-IRRFaVKTt 398
Cdd:cd03267 80 ----VAGLVPWKRRKkflRRIGVVFGQK--TQLWWDLPVIDSFYLLAAIYDLPPARFKKR--LDELSELLdLEEL-LDT- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 399 daqaAARSLSGGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIAL-RDAGAAILVISEDLDELFQISDRLA 477
Cdd:cd03267 150 ----PVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVL 225
|
....*..
gi 488618663 478 ALSGGQL 484
Cdd:cd03267 226 VIDKGRL 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
276-484 |
6.61e-09 |
|
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: 55.13 E-value: 6.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGEQtlpHAQATTLRFQDTPVGDLRPDArrkhglafvpAERLGHGAVPE 355
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLY---KPDSGEILVDGKEVSFASPRD----------ARRAGIAMVYQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 356 LSLADnalltafQQGLvshgliqrgkvraladEIIRrfavkttdaqAAARslsggnlqkfilgreilqNPKLLIAAHPTW 435
Cdd:cd03216 83 LSVGE-------RQMV----------------EIAR----------ALAR------------------NARLLILDEPTA 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488618663 436 GVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSGGQL 484
Cdd:cd03216 112 ALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
259-484 |
6.90e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.05 E-value: 6.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 259 LRVDKLSW-HNPD-PFGC-SLKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtLPHAQATTLRFQDTPV------GD 329
Cdd:PRK13643 2 IKFEKVNYtYQPNsPFASrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNG---LLQPTEGKVTVGDIVVsstskqKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 330 LRPdARRKHGLAFvpaerlghgAVPELSLADNALLTAFQQGLVSHGlIQRGKVRALADEIIRRFAVKTTDAQAAARSLSG 409
Cdd:PRK13643 79 IKP-VRKKVGVVF---------QFPESQLFEETVLKDVAFGPQNFG-IPKEKAEKIAAEKLEMVGLADEFWEKSPFELSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488618663 410 GNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSGGQL 484
Cdd:PRK13643 148 GQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
35-201 |
8.01e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 55.73 E-value: 8.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 35 GEIHaLLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLgiGMVFQHFSLFETLSVAQNIALAMGAAAG 114
Cdd:PRK13540 28 GLLH-LKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQL--CFVGHRSGINPYLTLRENCLYDIHFSPG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 115 TPKqleprIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAEGCS 194
Cdd:PRK13540 105 AVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGA 179
|
....*..
gi 488618663 195 ILFISHK 201
Cdd:PRK13540 180 VLLTSHQ 186
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
276-484 |
8.51e-09 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 56.13 E-value: 8.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGEQTLPHAQATTLRFQDTPvgdLRPDARRKHgLAFVPA-ERLghgaVP 354
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQP---RKPDQFQKC-VAYVRQdDIL----LP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 355 ELSLADNALLTAfqqgLVSHGLIQRGKVRALADEIIRRFAVKTTD-AQAAARSLSGGNLQKFILGREILQNPKLLIAAHP 433
Cdd:cd03234 95 GLTVRETLTYTA----ILRLPRKSSDAIRKKRVEDVLLRDLALTRiGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488618663 434 TWGVDVGAAAAIHRAL--IALRDAGaAILVISEDLDELFQISDRLAALSGGQL 484
Cdd:cd03234 171 TSGLDSFTALNLVSTLsqLARRNRI-VILTIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
275-500 |
9.76e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.04 E-value: 9.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 275 SLKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGEqtlPHAQATTLRFQDTPVGDLRPDARRKHGLAFVPAerlGHGAVP 354
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGD---PRATSGRIVFDGKDITDWQTAKIMREAVAIVPE---GRRVFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 355 ELSLADNALLTAFqqgLVSHGLIQRgKVRALADEIIRRFAVKTTDAQaaarSLSGGNLQKFILGREILQNPKLLIAAHPT 434
Cdd:PRK11614 94 RMTVEENLAMGGF---FAERDQFQE-RIKWVYELFPRLHERRIQRAG----TMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488618663 435 WGVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSGGQL------SDLIPTEQTSTVQIGG 500
Cdd:PRK11614 166 LGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVvledtgDALLANEAVRSAYLGG 237
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
26-228 |
1.00e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 56.37 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 26 DAVDLTIQPGEIHALLGENGAGKSTLMKIIYG-VTQPDA-------GSIIWQGQAQTMRNPAQARSLGIGMVFQHFSLFe 97
Cdd:PRK13547 18 RDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAF- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 98 TLSVAQNIALAMGAAAGTPKQLEPRIREVS----QRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQ---------DIRLL 164
Cdd:PRK13547 97 AFSAREIVLLGRYPHARRAGALTHRDGEIAwqalALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPPRYL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488618663 165 ILDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAE 228
Cdd:PRK13547 177 LLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPAD 241
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
278-482 |
1.26e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 56.76 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 278 DLSLEVRSGEIVGIAGVAGNGQDELLALLSGeQTLPHAQATTLRfqDTPVgdlrPDARRkhglafvpAERLGHGAVPELS 357
Cdd:PRK13536 59 GLSFTVASGECFGLLGPNGAGKSTIARMILG-MTSPDAGKITVL--GVPV----PARAR--------LARARIGVVPQFD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 358 LADNALltAFQQGLVSHGLIQRGKVRALADEI--IRRFAVKTTDAQAAARSLSGGNLQKFILGREILQNPKLLIAAHPTW 435
Cdd:PRK13536 124 NLDLEF--TVRENLLVFGRYFGMSTREIEAVIpsLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488618663 436 GVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSGG 482
Cdd:PRK13536 202 GLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
29-200 |
1.77e-08 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 53.70 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 29 DLTIQPGEIHALLGENGAGKSTLMKIIYGvtqpdagsiIWQGQAQTMRNPAQARSLgigMVFQHfSLFETLSVAQNIALA 108
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAG---------LWPWGSGRIGMPEGEDLL---FLPQR-PYLPLGTLREQLIYP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 109 MGAAagtpkqleprirevsqrygmavepqrlvhsLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEELfvtLRHL 188
Cdd:cd03223 88 WDDV------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRL---YQLL 134
|
170
....*....|..
gi 488618663 189 AAEGCSILFISH 200
Cdd:cd03223 135 KELGITVISVGH 146
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
14-200 |
2.10e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 14 HITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIwqgqaqtmrnpaqarsLG----IGMV 89
Cdd:PRK11819 329 NLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK----------------IGetvkLAYV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHF-------SLFETLSVAQNIaLAMGAaagtpkqlepriREVSQR-YGMA-----VEPQRLVHSLSIGERQKVEIIRC 156
Cdd:PRK11819 393 DQSRdaldpnkTVWEEISGGLDI-IKVGN------------REIPSRaYVGRfnfkgGDQQKKVGVLSGGERNRLHLAKT 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488618663 157 LMQDIRLLILDEPTSvltpqeaeELFV-TLRHL--AAE---GCSILfISH 200
Cdd:PRK11819 460 LKQGGNVLLLDEPTN--------DLDVeTLRALeeALLefpGCAVV-ISH 500
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
276-484 |
2.31e-08 |
|
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: 56.77 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtLPHAQATTLRFQDTPVGDLRPDARRKHgLAFVPAE-RLGHGavp 354
Cdd:COG2274 491 LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG---LYEPTSGRILIDGIDLRQIDPASLRRQ-IGVVLQDvFLFSG--- 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 355 elSLADNalltafqqglvshglIQRGKVRALADEIIRrfAVKttDAQAAA-----------------RSLSGGNLQKFIL 417
Cdd:COG2274 564 --TIREN---------------ITLGDPDATDEEIIE--AAR--LAGLHDfiealpmgydtvvgeggSNLSGGQRQRLAI 622
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488618663 418 GREILQNPKLLIAAHPTWGVDVGAAAAIHRALIALRdAGAAILVISEDLdELFQISDRLAALSGGQL 484
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRL-STIRLADRIIVLDKGRI 687
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
253-483 |
2.32e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 55.89 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 253 SGSEAFLRVDKL--SWHNPDPFGCSLKDLSLEVRSGEIVGIAGVAGNGQDE-------LLA---LLSGEQT--------L 312
Cdd:PRK09473 7 QQADALLDVKDLrvTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQtafalmgLLAangRIGGSATfngreilnL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 313 PHAQATTLR-------FQDtPVGDLRPDARRKHGLAFVpaerlghgavpelsladnalltafqqgLVSH-GLiqrGKVRA 384
Cdd:PRK09473 87 PEKELNKLRaeqismiFQD-PMTSLNPYMRVGEQLMEV---------------------------LMLHkGM---SKAEA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 385 LADEIIRRFAVKTTDAQAAAR----SLSGGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIAL-RDAGAAI 459
Cdd:PRK09473 136 FEESVRMLDAVKMPEARKRMKmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAI 215
|
250 260
....*....|....*....|....
gi 488618663 460 LVISEDLDELFQISDRLAALSGGQ 483
Cdd:PRK09473 216 IMITHDLGVVAGICDKVLVMYAGR 239
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
7-200 |
2.45e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 56.35 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 7 PARLQLRHITKRYP-GCLANDAVDLTIQPGEihALL--GENGAGKSTLMKIIygvtqpdAGsiIWQGQAQTMRNPAQARS 83
Cdd:COG4178 360 DGALALEDLTLRTPdGRPLLEDLSLSLKPGE--RLLitGPSGSGKSTLLRAI-------AG--LWPYGSGRIARPAGARV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 84 L--------GIGmvfqhfSLFEtlsvaqniALAMGAAAGTPKqlEPRIREVSQRYGMAV------EPQRLVHSLSIGERQ 149
Cdd:COG4178 429 LflpqrpylPLG------TLRE--------ALLYPATAEAFS--DAELREALEAVGLGHlaerldEEADWDQVLSLGEQQ 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488618663 150 KVEIIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHlAAEGCSILFISH 200
Cdd:COG4178 493 RLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
28-202 |
2.55e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 56.26 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKII---YGVTQpdaGSIIWQGQAQTMRNPAQARSLgIGMVFQHFSLFETlSVAQN 104
Cdd:PRK10789 334 VNFTLKPGQMLGICGPTGSGKSTLLSLIqrhFDVSE---GDIRFHDIPLTKLQLDSWRSR-LAVVSQTPFLFSD-TVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 105 IALamGAAAGTPKQLEPRIR-----------------EVSQRYGMavepqrlvhsLSIGERQKVEIIRCLMQDIRLLILD 167
Cdd:PRK10789 409 IAL--GRPDATQQEIEHVARlasvhddilrlpqgydtEVGERGVM----------LSGGQKQRISIARALLLNAEILILD 476
|
170 180 190
....*....|....*....|....*....|....*
gi 488618663 168 EPTSVLTPQEAEELFVTLRHLaAEGCSILFISHKL 202
Cdd:PRK10789 477 DALSAVDGRTEHQILHNLRQW-GEGRTVIISAHRL 510
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
275-495 |
2.94e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 54.89 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 275 SLKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGEQTLPHAQATTLRfqdTPVGDlrpdARRKHGLAFVPAERLGHGAVP 354
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILG---QPTRQ----ALQKNLVAYVPQSEEVDWSFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 355 ELsLADNALLtafqqGLVSH-GLIQRGKV--RALADEIIRRFAVKTTDAQAAARsLSGGNLQKFILGREILQNPKLLIAA 431
Cdd:PRK15056 95 VL-VEDVVMM-----GRYGHmGWLRRAKKrdRQIVTAALARVDMVEFRHRQIGE-LSGGQKKRVFLARAIAQQGQVILLD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488618663 432 HPTWGVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSGGQLSDLiPTEQTST 495
Cdd:PRK15056 168 EPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG-PTETTFT 230
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
279-492 |
3.21e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 55.19 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 279 LSLEVRSGEIVGIAGVAGNGQDELLALLSG-EQTLPHAQATTLRFQDTPVGDLRPDARRK---HGLAFV---------PA 345
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGvTKDNWRVTADRMRFDDIDLLRLSPRERRKlvgHNVSMIfqepqscldPS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 346 ERLGHgavpelsladnALLTAFQQGLVSHGLIQR---GKVRALadEIIRRFAVKttDAQAAARS----LSGGNLQKFILG 418
Cdd:PRK15093 106 ERVGR-----------QLMQNIPGWTYKGRWWQRfgwRKRRAI--ELLHRVGIK--DHKDAMRSfpyeLTEGECQKVMIA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488618663 419 REILQNPKLLIAAHPTWGVDVGAAAAIHRALIAL-RDAGAAILVISEDLDELFQISDRLAALSGGQLSDLIPTEQ 492
Cdd:PRK15093 171 IALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKE 245
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
276-513 |
3.65e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 55.89 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSgeqTLPHAQATTLRFQDTPVGDLRPDA----RRKH-GLAFVPAERLGH 350
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILG---CLDKPTSGTYRVAGQDVATLDADAlaqlRREHfGFIFQRYHLLSH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 351 gavpeLSLADNALLTAFQQGLvshgliQRGKVRALADEIIRRFAV-KTTDAQAAarSLSGGNLQKFILGREILQNPKLLI 429
Cdd:PRK10535 101 -----LTAAQNVEVPAVYAGL------ERKQRLLRAQELLQRLGLeDRVEYQPS--QLSGGQQQRVSIARALMNGGQVIL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 430 AAHPTWGVDVGAAAAIHRALIALRDAGAAILVISED------LDELFQISD-RLAALSGGQLS-DLIPTEQTSTVQIGGW 501
Cdd:PRK10535 168 ADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDpqvaaqAERVIEIRDgEIVRNPPAQEKvNVAGGTEPVVNTASGW 247
|
250
....*....|..
gi 488618663 502 maGQFDHSHTQA 513
Cdd:PRK10535 248 --RQFVSGFREA 257
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
9-228 |
4.19e-08 |
|
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: 56.11 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 9 RLQLRHITKRY-PGC-LANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGqaqtmrnpaqarsLGI 86
Cdd:TIGR00957 1284 RVEFRNYCLRYrEDLdLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG-------------LNI 1350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 87 GMVFQHFSLFETLSVAQNIALAMGAAAgtpKQLEPRIREVSQRYGMAVE-----------PQRLVH-------SLSIGER 148
Cdd:TIGR00957 1351 AKIGLHDLRFKITIIPQDPVLFSGSLR---MNLDPFSQYSDEEVWWALElahlktfvsalPDKLDHecaeggeNLSVGQR 1427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 149 QKVEIIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRhLAAEGCSILFISHKLGEVRALCHsATVLRNGKVSGHCIPAE 228
Cdd:TIGR00957 1428 QLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIR-TQFEDCTVLTIAHRLNTIMDYTR-VIVLDKGEVAEFGAPSN 1505
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-228 |
4.34e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.14 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 32 IQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLgIGMVFQHFSLFETlSVAQNI-ALAMG 110
Cdd:PLN03232 1259 VSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV-LSIIPQSPVLFSG-TVRFNIdPFSEH 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 111 AAAGTPKQLE-PRIREVSQR--YGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRH 187
Cdd:PLN03232 1337 NDADLWEALErAHIKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIRE 1416
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488618663 188 lAAEGCSILFISHKLGEVRAlCHSATVLRNGKVSGHCIPAE 228
Cdd:PLN03232 1417 -EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQE 1455
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
356-492 |
4.65e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 54.33 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 356 LSLADNALltafqQGLVSHGLIQRGKVRALADEIIRRF----AVKTTDAQAAARsLSGGNLQKFILGREILQNPKLLIAA 431
Cdd:PRK14271 115 MSIMDNVL-----AGVRAHKLVPRKEFRGVAQARLTEVglwdAVKDRLSDSPFR-LSGGQQQLLCLARTLAVNPEVLLLD 188
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488618663 432 HPTWGVDVGAAAAIHRALIALRDAgAAILVISEDLDELFQISDRLAALSGGQLSDLIPTEQ 492
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQ 248
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
279-484 |
6.00e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.78 E-value: 6.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 279 LSLEVRSGEIVGIAGVAGNGQDELLALLSGeqTLPHAqaTTLRFQDTPVGDLRPD--ARRKHGLA--FVPAerlghGAVP 354
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG--LLPGS--GSIQFAGQPLEAWSAAelARHRAYLSqqQTPP-----FAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 355 -----ELSLADNALLTAfqqglvshgliqrgkVRALADEIIRRFavKTTDAqaAARS---LSGGNLQKFILGREILQ--- 423
Cdd:PRK03695 86 vfqylTLHQPDKTRTEA---------------VASALNEVAEAL--GLDDK--LGRSvnqLSGGEWQRVRLAAVVLQvwp 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488618663 424 --NP--KLLIAAHPTWGVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSGGQL 484
Cdd:PRK03695 147 diNPagQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
25-219 |
6.50e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 54.35 E-value: 6.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 25 NDaVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPD---AGSIIWQGQaQTMRNPAQA----RSLGIGMVFQH--FSL 95
Cdd:PRK09473 33 ND-LNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGR-EILNLPEKElnklRAEQISMIFQDpmTSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 96 FETLSVAQNIALAMGAAAGTPKQ--LEPRIR--------EVSQRYGMAvePqrlvHSLSIGERQKVEIIRCLMQDIRLLI 165
Cdd:PRK09473 111 NPYMRVGEQLMEVLMLHKGMSKAeaFEESVRmldavkmpEARKRMKMY--P----HEFSGGMRQRVMIAMALLCRPKLLI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488618663 166 LDEPTSVLTPQEAEELFVTLRHLAAE-GCSILFISHKLGEVRALCHSATVLRNGK 219
Cdd:PRK09473 185 ADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
28-176 |
8.36e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.93 E-value: 8.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIiwqgQAQTMRNPAQARSLGIGMVFQHFSLFETLSVAQNIAL 107
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI----QIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHF 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488618663 108 AMGAAAGTPKQLEPRIREVsqrYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQ 176
Cdd:PRK13543 106 LCGLHGRRAKQMPGSALAI---VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-220 |
1.05e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 53.56 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 14 HITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQP-----DAGSIIWQGQAQ-TMRNPAQARSLgIG 87
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfNYRDVLEFRRR-VG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 88 MVFQHFSLFeTLSVAQNIALAMGAAAGTPKQ-----LEPRIREV----SQRYGMAVEPQRLvhslSIGERQKVEIIRCLM 158
Cdd:PRK14271 105 MLFQRPNPF-PMSIMDNVLAGVRAHKLVPRKefrgvAQARLTEVglwdAVKDRLSDSPFRL----SGGQQQLLCLARTLA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488618663 159 QDIRLLILDEPTSVLTPQEAEELFVTLRHLaAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-173 |
1.15e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.43 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 31 TIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGsiiwqgqaQTMRNPAQARslgigmVFQHFS------LFETLS---- 100
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLG--------DYEEEPSWDE------VLKRFRgtelqnYFKKLYngei 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 101 -VA---QNIALAMGAAAGTPKQLEPRI------REVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPT 170
Cdd:PRK13409 161 kVVhkpQYVDLIPKVFKGKVRELLKKVdergklDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
...
gi 488618663 171 SVL 173
Cdd:PRK13409 241 SYL 243
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
276-484 |
1.33e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 53.88 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSG--EQTLPHAQATTLRFQDTPVGDLRPDARRKHGLAFvpaerLGHGAV 353
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRliEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVF-----QSFALM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 354 PELSLADNallTAFQQGLVSHGLIQRgkvRALADEIIRRFAVKTTdAQAAARSLSGGNLQKFILGREILQNPKLLIAAHP 433
Cdd:PRK10070 119 PHMTVLDN---TAFGMELAGINAEER---REKALDALRQVGLENY-AHSYPDELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488618663 434 TWGVDVGAAAAIHRALIALRDAGAAILV-ISEDLDELFQISDRLAALSGGQL 484
Cdd:PRK10070 192 FSALDPLIRTEMQDELVKLQAKHQRTIVfISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
276-495 |
1.34e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 52.61 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGEQTL-PHAQAT---TLRFQDT---PVGDLRpdaRRKHGLAFVPaerl 348
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELyPEARVSgevYLDGQDIfkmDVIELR---RRVQMVFQIP---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 349 ghGAVPELSLADNALLTAFQQGLVSHGLIQRGKVR------ALADEIIRRFavkttdaQAAARSLSGGNLQKFILGREIL 422
Cdd:PRK14247 92 --NPIPNLSIFENVALGLKLNRLVKSKKELQERVRwalekaQLWDEVKDRL-------DAPAGKLSGGQQQRLCIARALA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488618663 423 QNPKLLIAAHPTWGVDVGAAAAIHRALIALRDAgAAILVISEDLDELFQISDRLAALSGGQLSDLIPTEQTST 495
Cdd:PRK14247 163 FQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
28-92 |
1.72e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.49 E-value: 1.72e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKIIYGVT--QPDAGSIIWQGQAQTMRNPAQARSLGIGMVFQH 92
Cdd:PRK09580 20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQY 86
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
276-490 |
1.86e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 52.38 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtLPHAQATTLRFQDTPVGDLRPDA----RRKHGLAFVPAErlghG 351
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVG---LESPSQGNVSWRGEPLAKLNRAQrkafRRDIQMVFQDSI----S 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 352 AV-PELSLAdnALLTAFQQGLVShglIQRGKVRALADEIIRRFAVKTTDAQAAARSLSGGNLQKFILGREILQNPKLLIA 430
Cdd:PRK10419 101 AVnPRKTVR--EIIREPLRHLLS---LDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488618663 431 AHPTWGVDVGAAAAIHRALIALRD-AGAAILVISEDLDELFQISDRLAALSGGQLSDLIPT 490
Cdd:PRK10419 176 DEAVSNLDLVLQAGVIRLLKKLQQqFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPV 236
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
9-226 |
1.96e-07 |
|
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: 51.64 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 9 RLQLRHITKRY----PGCLANdaVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQ------AQTMRnp 78
Cdd:cd03369 6 EIEVENLSVRYapdlPPVLKN--VSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdistipLEDLR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 79 aqaRSLGIgmvfqhfslfetlsVAQNIALAMGAaagtpkqleprIREVSQRYGMAVEPQrLVHSLSI---------GERQ 149
Cdd:cd03369 82 ---SSLTI--------------IPQDPTLFSGT-----------IRSNLDPFDEYSDEE-IYGALRVsegglnlsqGQRQ 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488618663 150 KVEIIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAeGCSILFISHKLGEVrALCHSATVLRNGKVSGHCIP 226
Cdd:cd03369 133 LLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT-NSTILTIAHRLRTI-IDYDKILVMDAGEVKEYDHP 207
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-208 |
2.28e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 52.35 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 6 IPArLQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDaGSIIWQGQAQTMRNPAQARSLG 85
Cdd:PRK14258 5 IPA-IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRVEFFNQNIYERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 86 I-------GMVFQHFSLFeTLSVAQNIALAMGAAAGTPK-QLEPRIREVSQRYGMAVEPQRLVH----SLSIGERQKVEI 153
Cdd:PRK14258 83 LnrlrrqvSMVHPKPNLF-PMSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLWDEIKHKIHksalDLSGGQQQRLCI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488618663 154 IRCLMQDIRLLILDEPTSVLTP---QEAEELFVTLRhLAAEgCSILFISHKLGEVRAL 208
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPiasMKVESLIQSLR-LRSE-LTMVIVSHNLHQVSRL 217
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
276-484 |
2.76e-07 |
|
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: 51.10 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtLPHAQATTLRFQDTPVGDLRPDARrkhGLAFVpaerLGHGAV-P 354
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAG---LEEPTSGRIYIGGRDVTDLPPKDR---DIAMV----FQNYALyP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 355 ELSLADNalltafqqglVSHGLIQRGKVRALADEIIRRFAvKTTDAQA----AARSLSGGNLQKFILGREILQNPKLLIA 430
Cdd:cd03301 86 HMTVYDN----------IAFGLKLRKVPKDEIDERVREVA-ELLQIEHlldrKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488618663 431 AHPTWGVDVGAAAAIHRALIAL-RDAGAAILVISEDLDELFQISDRLAALSGGQL 484
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
276-484 |
3.13e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 51.60 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtLPHAQATTLRFQDTPVGDLRPDARrkhgLAFVPAeRLghgaVPE 355
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG---LETPSAGELLAGTAPLAEAREDTR----LMFQDA-RL----LPW 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 356 LSLADNalltafqqglVSHGLiqRGKVRALADEIIRrfAVKTTD-AQAAARSLSGGNLQKFILGREILQNPKLLIAAHPt 434
Cdd:PRK11247 96 KKVIDN----------VGLGL--KGQWRDAALQALA--AVGLADrANEWPAALSGGQKQRVALARALIHRPGLLLLDEP- 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488618663 435 wgvdVGAAAAIHR----ALIA--LRDAGAAILVISEDLDELFQISDRLAALSGGQL 484
Cdd:PRK11247 161 ----LGALDALTRiemqDLIEslWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-202 |
3.61e-07 |
|
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: 51.60 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 33 QPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSII----WQGQAQTMRnpaqarslgiGMVFQHF---SLFETLSVA--- 102
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdWDEILDEFR----------GSELQNYftkLLEGDVKVIvkp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 103 QNIALAMGAAAGTPKQLEPRIRE------VSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQ 176
Cdd:cd03236 94 QYVDLIPKAVKGKVGELLKKKDErgkldeLVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
|
170 180
....*....|....*....|....*.
gi 488618663 177 EAEELFVTLRHLAAEGCSILFISHKL 202
Cdd:cd03236 174 QRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
276-484 |
4.05e-07 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 51.08 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGEQTlphAQATTLRFQDTPVGDLrPDARRKHGLAFvpaerlGHGAV-P 354
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFET---PTSGEILLDGKDITNL-PPHKRPVNTVF------QNYALfP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 355 ELSLADNalltafqqglVSHGLIQRGKVRAladEIIRRFA-----VKTTD-AQAAARSLSGGNLQKFILGREILQNPKLL 428
Cdd:cd03300 86 HLTVFEN----------IAFGLRLKKLPKA---EIKERVAealdlVQLEGyANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488618663 429 IAAHPTWGVDVGAAAAIHRALIAL-RDAGAAILVISEDLDELFQISDRLAALSGGQL 484
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLqKELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
407-492 |
4.49e-07 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 51.83 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 407 LSGGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIAL-RDAGAAILVISEDLDELFQISDRLAALSGGQLS 485
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLESISQWADTITVLYCGQTV 238
|
....*..
gi 488618663 486 DLIPTEQ 492
Cdd:COG4170 239 ESGPTEQ 245
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
276-492 |
4.57e-07 |
|
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: 51.04 E-value: 4.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtLPHAQATTLRFQDTPVGDLRP----DARRKHGLAFvpaerLGHG 351
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING---LERPTSGSVLVDGTDLTLLSGkelrKARRRIGMIF-----QHFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 352 AVPELSLADNalltafqqglVSHGL----IQRGKVRALADEIIRrfAVKTTD-AQAAARSLSGGNLQKFILGREILQNPK 426
Cdd:cd03258 93 LLSSRTVFEN----------VALPLeiagVPKAEIEERVLELLE--LVGLEDkADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488618663 427 LLIAAHPTWGVDVGAAAAIHRALIAL-RDAGAAILVISEDLDELFQISDRLAALSGGQLSDLIPTEQ 492
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE 227
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
90-303 |
4.72e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.91 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHFSLFETLSVAQNIalamgaaagTPKqlEPRIREV----SQRYGMAVE-------PQRLVHSLSIGERQKVEIIRCLM 158
Cdd:PRK00635 424 FQQMSLQELFIFLSQL---------PSK--SLSIEEVlqglKSRLSILIDlglpyltPERALATLSGGEQERTALAKHLG 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 159 QDIR--LLILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEV-----------RALCHSATVLRNGKvsghci 225
Cdd:PRK00635 493 AELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMIsladriidigpGAGIFGGEVLFNGS------ 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 226 PAEcsdlelarlMVGDAEGLTAHY----------DKVSGSEAFLRVDKLSWHNpdpfgcsLKDLSLEVRSGEIVGIAGVA 295
Cdd:PRK00635 567 PRE---------FLAKSDSLTAKYlrqeltipipEKRTNSLGTLTLSKATKHN-------LKDLTISLPLGRLTVVTGVS 630
|
....*...
gi 488618663 296 GNGQDELL 303
Cdd:PRK00635 631 GSGKSSLI 638
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
32-202 |
4.75e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 49.88 E-value: 4.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 32 IQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWqgqaqtmrnpaqarslgigmvfqhfslfetlsvaqnialamga 111
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW------------------------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 112 aagtpkqlePRIRevsqrygMAVEPQRLvhSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAE 191
Cdd:cd03222 59 ---------DGIT-------PVYKPQYI--DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
170
....*....|..
gi 488618663 192 GC-SILFISHKL 202
Cdd:cd03222 121 GKkTALVVEHDL 132
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
255-483 |
5.05e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 51.08 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 255 SEAFLRVDKLSWHNPDPFGCSlkDLSLEVRSGEIVGIAGVAGNGQDELLALLSGEQTlPHAQATTLRFQDTPVGDL--RP 332
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCR--DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLA-PDAGEVHYRMRDGQLRDLyaLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 333 DARRKHGL----AFV---PAErlghGAVPELSLADNalltaFQQGLVSHGLIQRGKVRALADEIIRRFAVKTTDAQAAAR 405
Cdd:PRK11701 80 EAERRRLLrtewGFVhqhPRD----GLRMQVSAGGN-----IGERLMAVGARHYGDIRATAGDWLERVEIDAARIDDLPT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 406 SLSGGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAaihRALIALR----DAGAAILVISEDLDELFQISDRLAALSG 481
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQA---RLLDLLRglvrELGLAVVIVTHDLAVARLLAHRLLVMKQ 227
|
..
gi 488618663 482 GQ 483
Cdd:PRK11701 228 GR 229
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
28-202 |
5.14e-07 |
|
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: 50.41 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLGIGMV--FQHFSLFETLSVAQNI 105
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVayAAQKPWLLNATVEENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 106 ALamgaaaGTP--KQ----------LEPRIREVSqrYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVL 173
Cdd:cd03290 100 TF------GSPfnKQrykavtdacsLQPDIDLLP--FGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190
....*....|....*....|....*....|.
gi 488618663 174 TPQEAEELFVT--LRHLAAEGCSILFISHKL 202
Cdd:cd03290 172 DIHLSDHLMQEgiLKFLQDDKRTLVLVTHKL 202
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
276-484 |
5.93e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 50.98 E-value: 5.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELL----ALL---SGEQTLPHAQATTlrfqDTPVGDLRpDARRKHGLAFvpaerl 348
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMqhfnALLkpsSGTITIAGYHITP----ETGNKNLK-KLRKKVSLVF------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 349 ghgAVPELSLADNALLTAFQQGLVSHGLI-QRGKVRALadEIIRRFAVKTTDAQAAARSLSGGNLQKFILGREILQNPKL 427
Cdd:PRK13641 92 ---QFPEAQLFENTVLKDVEFGPKNFGFSeDEAKEKAL--KWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488618663 428 LIAAHPTWGVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSGGQL 484
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
257-484 |
7.90e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.90 E-value: 7.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 257 AFLRVDKLSWHNPD---PFGcSLKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGEQTLP-HAQATTLRFQDTPVGDLRP 332
Cdd:PRK11022 2 ALLNVDKLSVHFGDesaPFR-AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPgRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 333 DARRKhglaFVPAERLGHGAVPELSLadNALLT-AFQ--QGLVSHGLIQRGKVRALADEIIRRFAVKTTDAQ--AAARSL 407
Cdd:PRK11022 81 KERRN----LVGAEVAMIFQDPMTSL--NPCYTvGFQimEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRldVYPHQL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488618663 408 SGGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIAL-RDAGAAILVISEDLDELFQISDRLAALSGGQL 484
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
278-483 |
1.75e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.47 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 278 DLSLEVRSGEIVGIAGVAGNGQDelLALLSGEQTLPHAQATTlrfqdtPVGDLRpdarrKHGlafvpaERLGHGAVPEL- 356
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKS--VTALSILRLLPSPPVVY------PSGDIR-----FHG------ESLLHASEQTLr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 357 SLADNALLTAFQQGLVS----HGL---------IQRGKVRALA-DEIIR---RFAVKttdaQAAAR------SLSGGNLQ 413
Cdd:PRK15134 88 GVRGNKIAMIFQEPMVSlnplHTLekqlyevlsLHRGMRREAArGEILNcldRVGIR----QAAKRltdyphQLSGGERQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488618663 414 KFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIAL-RDAGAAILVISEDLDELFQISDRLAALSGGQ 483
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
377-507 |
2.07e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 49.73 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 377 IQRGKVRALADEIIRRFAVKTTDAQAAARsLSGGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIALRDAG 456
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAK-YSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDG 194
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 488618663 457 AAILVISEDLDELFQIS------DRLAALSGGQLSDLIPTEQTSTVQIGGWMAGQFD 507
Cdd:NF000106 195 ATVLLTTQYMEEAEQLAheltviDRGRVIADGKVDELKTKVGGRTLQIRPAHAAELD 251
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
276-482 |
2.09e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 49.31 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGEQTlphAQATTLRFQDTPVGDlrPDARRkhGLAFvpaerLGHGAVPE 355
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVP---YQHGSITLDGKPVEG--PGAER--GVVF-----QNEGLLPW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 356 LSLADNalltafqqglVSHGLIQRGKVRALADEIIRRFAVKTTDAQAAAR---SLSGGNLQKFILGREILQNPKLLIAAH 432
Cdd:PRK11248 85 RNVQDN----------VAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRyiwQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488618663 433 PTWGVDVGAAAAIHRALIAL-RDAGAAILVISEDLDELFQISDRLAALSGG 482
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
276-484 |
2.35e-06 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 49.00 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGEQTlphAQATTLRFQDTPVGDLRPDARrkhglafvpAERLghgAVpe 355
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELS---PDSGEVRLNGRPLADWSPAEL---------ARRR---AV-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 356 lsLADNALLT-AF------QQGLVSHGLIQRgKVRALADEIIRRfavktTDAQAAA----RSLSGGNLQKFILGREILQ- 423
Cdd:PRK13548 81 --LPQHSSLSfPFtveevvAMGRAPHGLSRA-EDDALVAAALAQ-----VDLAHLAgrdyPQLSGGEQQRVQLARVLAQl 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488618663 424 -----NPKLLIAAHPTWGVDVGAAAAIHRALIAL-RDAGAAILVISEDLDELFQISDRLAALSGGQL 484
Cdd:PRK13548 153 wepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
276-484 |
2.49e-06 |
|
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: 48.62 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLsgeQTLPHAQATTLRFQDTPVGDLrpDARRKHG-LAFVPAErlghgavP 354
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALL---ENFYQPQGGQVLLDGKPISQY--EHKYLHSkVSLVGQE-------P 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 355 EL---SLADNallTAFQQGLVSHGLIQRGKVRALADEIIRRFAVK-TTDAQAAARSLSGGNLQKFILGREILQNPKLLIA 430
Cdd:cd03248 98 VLfarSLQDN---IAYGLQSCSFECVKEAAQKAHAHSFISELASGyDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488618663 431 AHPTWGVDVGAAAAIHRALIALRDAgAAILVISEDLdELFQISDRLAALSGGQL 484
Cdd:cd03248 175 DEATSALDAESEQQVQQALYDWPER-RTVLVIAHRL-STVERADQILVLDGGRI 226
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
24-220 |
2.80e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 49.35 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 24 ANDAVDLTIQPGEIHALLGENGAGKS----TLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSL---GIGMVFQH---- 92
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLvgaEVAMIFQDpmts 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 93 --------FSLFETLSVAQnialamgaaAGTPKQLEPRIREVSQRYGMAVEPQRL---VHSLSIGERQKVEIIRCLMQDI 161
Cdd:PRK11022 102 lnpcytvgFQIMEAIKVHQ---------GGNKKTRRQRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACRP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488618663 162 RLLILDEPTSVL--TPQ-EAEELFVTLRHlaAEGCSILFISHKLGEVRALCHSATVLRNGKV 220
Cdd:PRK11022 173 KLLIADEPTTALdvTIQaQIIELLLELQQ--KENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
120-324 |
3.81e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 49.63 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 120 EPRIREVSQRYGMAVE-------PQRLVHSLSIGERQKveiIRcLMQDIR------LLILDEPTSVLTPQEAEELFVTLR 186
Cdd:TIGR00630 459 EEVLKEIRERLGFLIDvgldylsLSRAAGTLSGGEAQR---IR-LATQIGsgltgvLYVLDEPSIGLHQRDNRRLINTLK 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 187 HLAAEGCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAECSDLELARlmvgDAEGLTAHY-----------DKVSGS 255
Cdd:TIGR00630 535 RLRDLGNTLIVVEHDEDTIRAADYVIDIGPGAGEHGGEVVASGTPEEILA----NPDSLTGQYlsgrkkievpaERRPGN 610
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488618663 256 EAFLRVDKLSWHNpdpfgcsLKDLSLEVRSGEIVGIAGVAGNGQ-----DELLALLsgEQTLPHAQATTLRFQD 324
Cdd:TIGR00630 611 GKFLTLKGARENN-------LKNITVSIPLGLFTCITGVSGSGKstlinDTLYPAL--ANRLNGAKTVPGRYTS 675
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
275-505 |
3.86e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 49.44 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 275 SLKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqTLPHAQ-ATTLRFQDTPV--GDLRpDARRKhGLAFVPAERLghg 351
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG--VYPHGTwDGEIYWSGSPLkaSNIR-DTERA-GIVIIHQELT--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 352 AVPELSLADNALL---TAFQQGLVSHGLIQRgkvraLADEIIRRFAVKTTDAQAAARSLSGGNLQKFILGREILQNPKLL 428
Cdd:TIGR02633 89 LVPELSVAENIFLgneITLPGGRMAYNAMYL-----RAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488618663 429 IAAHPTWGVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSGGQLSDLIPTEQTSTVQIGGWMAGQ 505
Cdd:TIGR02633 164 ILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGR 240
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
276-483 |
3.97e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 49.66 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSgeqtlpHAQATTLRFQDTPVGDLRP-DARRKHGL-AFVPAERLghgAV 353
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALA------FRSPKGVKGSGSVLLNGMPiDAKEMRAIsAYVQQDDL---FI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 354 PELSlADNALLtaFQQGLVSHGLIQRGKVRALADEIIRRF----AVKT-TDAQAAARSLSGGNLQKFILGREILQNPKLL 428
Cdd:TIGR00955 112 PTLT-VREHLM--FQAHLRMPRRVTKKEKRERVDEVLQALglrkCANTrIGVPGRVKGLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488618663 429 IAAHPTWGVDVGAAAAIHRALIALRDAG-AAILVISEDLDELFQISDRLAALSGGQ 483
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAQKGkTIICTIHQPSSELFELFDKIILMAEGR 244
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
29-438 |
4.18e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 29 DLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQAQTMRNPAQARSLgIGMVFQH-----FSLFET---LS 100
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKL-VSDEWQRnntdmLSPGEDdtgRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 101 VAQNIALAMGAAAgtpkqlepRIREVSQRYGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEE 180
Cdd:PRK10938 102 TAEIIQDEVKDPA--------RCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 181 LFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLrngkvsghcipAECSDLELARLMVGDAEGLT---AHYDKVSG--- 254
Cdd:PRK10938 174 LAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVL-----------ADCTLAETGEREEILQQALVaqlAHSEQLEGvql 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 255 --SEAFLRVDKLSWHNPdPFgcSLKD-------------LSLEVRSGEIVGIAGVAGNGQDELLALLSGEQTLPHAQATT 319
Cdd:PRK10938 243 pePDEPSARHALPANEP-RI--VLNNgvvsyndrpilhnLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDLT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 320 LRFQDTPVGDLRPDARRKHGlaFVPAERlgHGAVPELSLADNALLTAFqqgLVSHGLIQR--GKVRALADEIIRRFAVKT 397
Cdd:PRK10938 320 LFGRRRGSGETIWDIKKHIG--YVSSSL--HLDYRVSTSVRNVILSGF---FDSIGIYQAvsDRQQKLAQQWLDILGIDK 392
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 488618663 398 TDAQAAARSLSGGNLQKFILGREILQNPKLLIAAHPTWGVD 438
Cdd:PRK10938 393 RTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
26-238 |
5.26e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.02 E-value: 5.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 26 DAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVT--QPDAGSIIWQGQAQTMRNPAQARSLGIGMVFQ---HFSLFETLS 100
Cdd:NF040905 277 DDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKEVDVSTVSDAIDAGLAYVTEdrkGYGLNLIDD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 101 VAQNIALA----------------MGAAAGTPKQLepRIR--EVSQRYGmavepqrlvhSLSIGERQKVEIIRCLMQDIR 162
Cdd:NF040905 357 IKRNITLAnlgkvsrrgvideneeIKVAEEYRKKM--NIKtpSVFQKVG----------NLSGGNQQKVVLSKWLFTDPD 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488618663 163 LLILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATVLRNGKVSGHCIPAECSDLELARLM 238
Cdd:NF040905 425 VLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGELPREEASQERIMRLI 500
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
259-482 |
5.70e-06 |
|
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: 49.24 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 259 LRVDKLSWHNPDPFGCSLKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGEQTLPHAQATTlrfqdtpvgdlrpdaRRKH 338
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATV---------------AGKS 2002
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 339 GLAFVPAERLGHGAVPELSLADNaLLTAFQQglvshgLIQRGKVRALADEIIRRFA---VK----TTDAQAAARSLSGGN 411
Cdd:TIGR01257 2003 ILTNISDVHQNMGYCPQFDAIDD-LLTGREH------LYLYARLRGVPAEEIEKVAnwsIQslglSLYADRLAGTYSGGN 2075
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488618663 412 LQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSGG 482
Cdd:TIGR01257 2076 KRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
401-466 |
5.92e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 47.80 E-value: 5.92e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488618663 401 QAAARSLSGGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIALR-DAGAAILVISEDL 466
Cdd:PRK09544 115 DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRrELDCAVLMVSHDL 181
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
10-173 |
7.44e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.63 E-value: 7.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 10 LQLRHITKRYPGCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIiwqgqaqtmrnpAQARSLGIGMV 89
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI------------GLAKGIKLGYF 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 90 FQHfsLFETLSVAQNIALAMGAAAgtPKQLEPRIREVSQRYGM----AVEPQRlvhSLSIGERQKVEIIRCLMQDIRLLI 165
Cdd:PRK10636 381 AQH--QLEFLRADESPLQHLARLA--PQELEQKLRDYLGGFGFqgdkVTEETR---RFSGGEKARLVLALIVWQRPNLLL 453
|
....*...
gi 488618663 166 LDEPTSVL 173
Cdd:PRK10636 454 LDEPTNHL 461
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
276-484 |
1.01e-05 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 46.93 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSgeqTLPHAQATTLRFQDTPVGDLRPDARRKHgLAFVPA---------- 345
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFA---RLLTPQSGTVFLGDKPISMLSSRQLARR-LALLPQhhltpegitv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 346 -ERLGHGAVPELSL------ADNALLTafqqglvshgliqrgkvRALADEIIRRFAVKTTDaqaaarSLSGGNLQKFILG 418
Cdd:PRK11231 94 rELVAYGRSPWLSLwgrlsaEDNARVN-----------------QAMEQTRINHLADRRLT------DLSGGQRQRAFLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488618663 419 REILQNPKLLIAAHPTWGVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSGGQL 484
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHV 216
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
28-206 |
1.07e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.49 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQgQAQTMR--NPAQARSlGIGMVFQHFSLFETlSVAQNI 105
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN-DSHNLKdiNLKWWRS-KIGVVSQDPLLFSN-SIKNNI 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 106 ALAM----------------GAAAGTPKQLEPRIR--------------------EVSQRYG-------MAVEPQRLVH- 141
Cdd:PTZ00265 481 KYSLyslkdlealsnyynedGNDSQENKNKRNSCRakcagdlndmsnttdsneliEMRKNYQtikdsevVDVSKKVLIHd 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 142 ------------------SLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAEGCSI-LFISHKL 202
Cdd:PTZ00265 561 fvsalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRItIIIAHRL 640
|
....
gi 488618663 203 GEVR 206
Cdd:PTZ00265 641 STIR 644
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
255-492 |
1.39e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 46.69 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 255 SEAFLRVDKLS-WHNPDPfgcSLKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGEQTL-PHAQAT-TLRFQDTPVGDLR 331
Cdd:PRK14239 2 TEPILQVSDLSvYYNKKK---ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnPEVTITgSIVYNGHNIYSPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 332 PDA---RRKHGLAFVPAERLghgavpELSLADNalltafqqglVSHGLIQRG-KVRALADEiirrfAVKTTDAQAA---- 403
Cdd:PRK14239 79 TDTvdlRKEIGMVFQQPNPF------PMSIYEN----------VVYGLRLKGiKDKQVLDE-----AVEKSLKGASiwde 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 404 --------ARSLSGGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIALRDAgAAILVISEDLDELFQISDR 475
Cdd:PRK14239 138 vkdrlhdsALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDR 216
|
250
....*....|....*..
gi 488618663 476 LAALSGGQLSDLIPTEQ 492
Cdd:PRK14239 217 TGFFLDGDLIEYNDTKQ 233
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
28-202 |
1.97e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 47.41 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQA------QTMRNpaqarslGIGMVFQH-----FSLF 96
Cdd:PRK10790 360 INLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPlsslshSVLRQ-------GVAMVQQDpvvlaDTFL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 97 ETLSVAQNIALAMGAAAGTPKQLEPRIREVSQryGMAVEPQRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVL--- 173
Cdd:PRK10790 433 ANVTLGRDISEEQVWQALETVQLAELARSLPD--GLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIdsg 510
|
170 180
....*....|....*....|....*....
gi 488618663 174 TPQEAEELFVTLRhlaaEGCSILFISHKL 202
Cdd:PRK10790 511 TEQAIQQALAAVR----EHTTLVVIAHRL 535
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
276-484 |
1.98e-05 |
|
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: 45.94 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeQTLPHAQATTLRFQDTPVGDLRPdARRKHGLAfvpaerLGHGAVPE 355
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQR-FYVPENGRVLVDGHDLALADPAW-LRRQVGVV------LQENVLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 356 LSLADNALLTafQQGLVSHGLIQRGKVrALADEIIRRF--AVKTTDAQAAArSLSGGNLQKFILGREILQNPKLLIAAHP 433
Cdd:cd03252 90 RSIRDNIALA--DPGMSMERVIEAAKL-AGAHDFISELpeGYDTIVGEQGA-GLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488618663 434 TWGVDVGAAAAIHRALIALRdAGAAILVISEDLDELfQISDRLAALSGGQL 484
Cdd:cd03252 166 TSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTV-KNADRIIVMEKGRI 214
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-200 |
2.09e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 4 HAIPA---RLQLRHITKRYpgclaNDAVDL-----TIQPGEIHALLGENGAGKSTLMKIIYG---------VT----QPD 62
Cdd:PRK10938 252 HALPAnepRIVLNNGVVSY-----NDRPILhnlswQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndLTlfgrRRG 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 63 AGSIIWQGQA----------QTMRNPAQARSLGIGMVFQHFSLFETLSVAQNIaLAMG--AAAGTPKQleprirevsqry 130
Cdd:PRK10938 327 SGETIWDIKKhigyvssslhLDYRVSTSVRNVILSGFFDSIGIYQAVSDRQQK-LAQQwlDILGIDKR------------ 393
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488618663 131 gMAVEPqrlVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHLAAEGCS-ILFISH 200
Cdd:PRK10938 394 -TADAP---FHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqLLFVSH 460
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
278-460 |
3.37e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 44.79 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 278 DLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtLPHAQATTLRFQDTPVGDLRPDARRKhgLAFvpaerLGH--GAVPE 355
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAG---LARPDAGEVLWQGEPIRRQRDEYHQD--LLY-----LGHqpGIKTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 356 LSLADNalLTAFQQGlvsHGLIQRGKVR-ALADEIIRRFavkttdAQAAARSLSGGNLQKFILGREILQNPKLLIAAHPT 434
Cdd:PRK13538 89 LTALEN--LRFYQRL---HGPGDDEALWeALAQVGLAGF------EDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180
....*....|....*....|....*..
gi 488618663 435 WGVDVGAAAAIHRALIA-LRDAGAAIL 460
Cdd:PRK13538 158 TAIDKQGVARLEALLAQhAEQGGMVIL 184
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
39-200 |
4.17e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 39 ALLGENGAGKSTLMKIIYGVTQPDAGSIIwqgqaqtmrnpaqaRSLGIGM-VF-QHFslFETLSVAQNIALAMgaAAGTP 116
Cdd:PLN03073 539 AMVGPNGIGKSTILKLISGELQPSSGTVF--------------RSAKVRMaVFsQHH--VDGLDLSSNPLLYM--MRCFP 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 117 KQLEPRIREVSQRYG----MAVEPqrlVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEELfvtLRHLAAEG 192
Cdd:PLN03073 601 GVPEQKLRAHLGSFGvtgnLALQP---MYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEAL---IQGLVLFQ 674
|
....*...
gi 488618663 193 CSILFISH 200
Cdd:PLN03073 675 GGVLMVSH 682
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
26-202 |
4.21e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.89 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 26 DAVDLTIQPGEIHALLGENGAGKSTLMK-IIYGVTqpdagsiiwqgqaqtMRNPAQARSLGIgmvfqhfslfetlSVAQN 104
Cdd:cd03227 12 VPNDVTFGEGSLTIITGPNGSGKSTILDaIGLALG---------------GAQSATRRRSGV-------------KAGCI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 105 IALAmgaaagtpkqleprirevsqrygmAVEPQRLVHSLSIGERQKVEII----RCLMQDIRLLILDEPTSVLTPQEAEE 180
Cdd:cd03227 64 VAAV------------------------SAELIFTRLQLSGGEKELSALAlilaLASLKPRPLYILDEIDRGLDPRDGQA 119
|
170 180
....*....|....*....|..
gi 488618663 181 LFVTLRHLAAEGCSILFISHKL 202
Cdd:cd03227 120 LAEAILEHLVKGAQVIVITHLP 141
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
275-505 |
4.38e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.88 E-value: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 275 SLKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtLPHAQATTLRFQDTPVGDLRPDARRKHGLAFVPAERlghGAVP 354
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFG---IYQKDSGSILFQGKEIDFKSSKEALENGISMVHQEL---NLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 355 ELSLADNALLTAF-QQGL-VSHGLIQRgKVRALADEI-IRrfavktTDAQAAARSLSGGNLQKFILGREILQNPKLLIAA 431
Cdd:PRK10982 87 QRSVMDNMWLGRYpTKGMfVDQDKMYR-DTKAIFDELdID------IDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488618663 432 HPTWGVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSGGQLSDLIPTEQTSTVQIGGWMAGQ 505
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGR 233
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
276-492 |
5.23e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 44.83 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLA----LLSGEQTLPHAQATTLRFQDTPVGDLRP-DARRKHGLAF-VPaerlg 349
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrLLELNEEARVEGEVRLFGRNIYSPDVDPiEVRREVGMVFqYP----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 350 hGAVPELSLADNALLTAFQQGLV-SHGLIQRG-----KVRALADEIIRRFAVKttdaqaaARSLSGGNLQKFILGREILQ 423
Cdd:PRK14267 95 -NPFPHLTIYDNVAIGVKLNGLVkSKKELDERvewalKKAALWDEVKDRLNDY-------PSNLSGGQRQRLVIARALAM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488618663 424 NPKLLIAAHPTWGVDVGAAAAIHRALIALRDAgAAILVISEDLDELFQISDRLAALSGGQLSDLIPTEQ 492
Cdd:PRK14267 167 KPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRK 234
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
28-199 |
5.44e-05 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 44.18 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDA---GSIIWQG-QAQTMRNPAQARSLgigMVFQHFSLFETLSVAQ 103
Cdd:cd03233 26 FSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGiPYKEFAEKYPGEII---YVSEEDVHFPTLTVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 104 NIALAMGAAAGtpkqleprirevsqrygmavepqRLVHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVLTPQEAEELFV 183
Cdd:cd03233 103 TLDFALRCKGN-----------------------EFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILK 159
|
170
....*....|....*.
gi 488618663 184 TLRHLAAEGCSILFIS 199
Cdd:cd03233 160 CIRTMADVLKTTTFVS 175
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
255-498 |
6.47e-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: 45.45 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 255 SEAFLRVDKLS--WHNPDPFGCSLKDLSLEVRSGEIVGIAGVAGNGQD-ELLALLsgeQTLPHAQATT---LRFQDTPVG 328
Cdd:COG4172 3 SMPLLSVEDLSvaFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL---RLLPDPAAHPsgsILFDGQDLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 329 DLRPDARRK---HGLAFVPAErlghgavPELSLadNALLTAFQQ---GLVSHGLIQRGKVRALADEIIRRfaVKTTDAQA 402
Cdd:COG4172 80 GLSERELRRirgNRIAMIFQE-------PMTSL--NPLHTIGKQiaeVLRLHRGLSGAAARARALELLER--VGIPDPER 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 403 AARS----LSGGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIAL-RDAGAAILVISEDLDELFQISDRLA 477
Cdd:COG4172 149 RLDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVA 228
|
250 260
....*....|....*....|.
gi 488618663 478 ALSGGQLsdlipTEQTSTVQI 498
Cdd:COG4172 229 VMRQGEI-----VEQGPTAEL 244
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
276-483 |
6.91e-05 |
|
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: 44.45 E-value: 6.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLsgeqtlphaqattLRFQDTPVG----------DLRPDARRKHgLAFVPA 345
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLL-------------ERFYDPTSGeilldgvdirDLNLRWLRSQ-IGLVSQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 346 ErlghgavPEL---SLADNALLTAFQQGLVShglIQRGKVRALADEIIRRFAvKTTDAQAAAR--SLSGGNLQKFILGRE 420
Cdd:cd03249 85 E-------PVLfdgTIAENIRYGKPDATDEE---VEEAAKKANIHDFIMSLP-DGYDTLVGERgsQLSGGQKQRIAIARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488618663 421 ILQNPKLLIAAHPTWGVDVGAAAAIHRALIALRdAGAAILVISEDLDELfQISDRLAALSGGQ 483
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLSTI-RNADLIAVLQNGQ 214
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
276-495 |
7.20e-05 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 45.22 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGEQTlPHAQATTLRFQDTPVGDLRPDARRkhgLAFVPAERlghgavpe 355
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLT-PTAGTVLVAGDDVEALSARAASRR---VASVPQDT-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 356 lSLA-DNALLTAFQQGLVSHglIQRGKVRALADEIIRRFAVKTTD-AQAAAR---SLSGGNLQKFILGREILQNPKLLIA 430
Cdd:PRK09536 87 -SLSfEFDVRQVVEMGRTPH--RSRFDTWTETDRAAVERAMERTGvAQFADRpvtSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488618663 431 AHPTWGVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSGGQLSDLIPTEQTST 495
Cdd:PRK09536 164 DEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLT 228
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
9-220 |
8.04e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 44.46 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 9 RLQLRHITKRYP--GCLANDAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDaGSIIWQGQA-QTMrnPAQARSLG 85
Cdd:cd03289 2 QMTVKDLTAKYTegGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSwNSV--PLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 86 IGMVFQHFSLF-----------------ETLSVAQNIALAMgAAAGTPKQLEPRIRevsqrYGMAVepqrlvhsLSIGER 148
Cdd:cd03289 79 FGVIPQKVFIFsgtfrknldpygkwsdeEIWKVAEEVGLKS-VIEQFPGQLDFVLV-----DGGCV--------LSHGHK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488618663 149 QKVEIIRCLMQDIRLLILDEPTSVLTPQEAEELFVTLRHlAAEGCSILFISHKLgEVRALCHSATVLRNGKV 220
Cdd:cd03289 145 QLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRI-EAMLECQRFLVIEENKV 214
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
286-483 |
9.01e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 45.26 E-value: 9.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 286 GEIVGIAGVAGNGQDELLALLSGEQTLPHAQATTLRFQDTPVgdlRPDARRkhgLAFVPAERLGHgavPELSLADNALLT 365
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPT---KQILKR---TGFVTQDDILY---PHLTVRETLVFC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 366 AFQQglVSHGLIQRGKVRAlADEIIRRFAV----KTTDAQAAARSLSGGNLQKFILGREILQNPKLLIAAHPTWGVDVGA 441
Cdd:PLN03211 165 SLLR--LPKSLTKQEKILV-AESVISELGLtkceNTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488618663 442 AAAIHRALIALRDAGAAILV-ISEDLDELFQISDRLAALSGGQ 483
Cdd:PLN03211 242 AYRLVLTLGSLAQKGKTIVTsMHQPSSRVYQMFDSVLVLSEGR 284
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
275-484 |
1.27e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 43.32 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 275 SLKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtLPHAQATTLRFQDTPVGDLR----PDARRKHGLAFvpaerLGH 350
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICG---IERPSAGKIWFSGHDITRLKnrevPFLRRQIGMIF-----QDH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 351 GAVPELSLADNALLTAFQQGLVSHGLiqRGKVRALADEIIRRFAVKTTDAQaaarsLSGGNLQKFILGREILQNPKLLIA 430
Cdd:PRK10908 89 HLLMDRTVYDNVAIPLIIAGASGDDI--RRRVSAALDKVGLLDKAKNFPIQ-----LSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488618663 431 AHPTWGVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSGGQL 484
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
28-219 |
2.21e-04 |
|
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: 42.46 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSIIWQGQ----AQ-------TMRNpaqarslGI--GMVFQHFS 94
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSiayvSQepwiqngTIRE-------NIlfGKPFDEER 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 95 LFETLSVAqnialamgaaagtpkQLEPRIR--------EVSQRyGMavepqrlvhSLSIGERQKVEIIRCLMQDIRLLIL 166
Cdd:cd03250 97 YEKVIKAC---------------ALEPDLEilpdgdltEIGEK-GI---------NLSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488618663 167 DEPTSVLTPQEAEELF--VTLRHLAAEGCSILfISHKLgEVRALCHSATVLRNGK 219
Cdd:cd03250 152 DDPLSAVDAHVGRHIFenCILGLLLNNKTRIL-VTHQL-QLLPHADQIVVLDNGR 204
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
27-66 |
2.46e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.17 E-value: 2.46e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 488618663 27 AVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSI 66
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNI 57
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
31-200 |
2.49e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.79 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 31 TIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSI---------------------------IWQGQAQTMRNPAQARS 83
Cdd:PRK11147 341 QVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgtklevayfdqhraeldpektvmdnLAEGKQEVMVNGRPRHV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 84 LGigmVFQHFsLFetlsvaqnialamgaaagTPKQleprirevsqrygmAVEPqrlVHSLSIGERQKVEIIRCLMQDIRL 163
Cdd:PRK11147 421 LG---YLQDF-LF------------------HPKR--------------AMTP---VKALSGGERNRLLLARLFLKPSNL 461
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488618663 164 LILDEPTSVL---TPQEAEELfvtlrhLAAEGCSILFISH 200
Cdd:PRK11147 462 LILDEPTNDLdveTLELLEEL------LDSYQGTVLLVSH 495
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
26-173 |
2.80e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.62 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 26 DAVDLTIQPGEIHALLGENGAGKSTLMKIIYGVTQPDAGSII----WQGQAQTMRNPAQARSlGIGMVFQHFSLFETLSV 101
Cdd:PRK10636 18 DNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTfpgnWQLAWVNQETPALPQP-ALEYVIDGDREYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 102 AQNIALAMG---AAAGTPKQLEP------RIREVSQRYGMAVEPQRL---VHSLSIGERQKVEIIRCLMQDIRLLILDEP 169
Cdd:PRK10636 97 QLHDANERNdghAIATIHGKLDAidawtiRSRAASLLHGLGFSNEQLerpVSDFSGGWRMRLNLAQALICRSDLLLLDEP 176
|
....
gi 488618663 170 TSVL 173
Cdd:PRK10636 177 TNHL 180
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
276-463 |
4.00e-04 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 42.84 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLsgeqtlphaqattLRFQD----------TPVGDLRPDARRKHgLAFVPA 345
Cdd:COG1132 356 LKDISLTIPPGETVALVGPSGSGKSTLVNLL-------------LRFYDptsgrilidgVDIRDLTLESLRRQ-IGVVPQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 346 ErlghgavPEL---SLADNALLTAFQqglVSHGLIQRGKVRALADEIIRRFAvKTTDAQAAAR--SLSGGNLQKFILGRE 420
Cdd:COG1132 422 D-------TFLfsgTIRENIRYGRPD---ATDEEVEEAAKAAQAHEFIEALP-DGYDTVVGERgvNLSGGQRQRIAIARA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488618663 421 ILQNPKLLIAAHPTWGVDVGAAAAIHRALIALRdAGAAILVIS 463
Cdd:COG1132 491 LLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIA 532
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
276-484 |
5.37e-04 |
|
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: 41.36 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtLPHAQATTLRFQDTPVGDLRPDA---RRKHGLAFVPAERLGHga 352
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINL---LEEPDSGTIIIDGLKLTDDKKNInelRQKVGMVFQQFNLFPH-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 353 vpelsladnalLTAFQQglVSHGLIQ-RGKVRALADEIIRRF--AVKTTD-AQAAARSLSGGNLQKFILGREILQNPKLL 428
Cdd:cd03262 91 -----------LTVLEN--ITLAPIKvKGMSKAEAEERALELleKVGLADkADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488618663 429 IAAHPTWGVDVGAAAAIHRALIALRDAGAAILVISEDLDELFQISDRLAALSGGQL 484
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
261-498 |
7.17e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 41.71 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 261 VDKLSWHNPDPFGCSLKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeQTLPHAQATTLRFQD--TPVGDLRPDARRKH 338
Cdd:PRK13640 8 FKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLING-LLLPDDNPNSKITVDgiTLTAKTVWDIREKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 339 GLAFvpaerlghgavpelSLADNALLTAFQQGLVSHGLIQRGKVRALADEIIRRFA--VKTTDAQAAARS-LSGGNLQKF 415
Cdd:PRK13640 87 GIVF--------------QNPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLadVGMLDYIDSEPAnLSGGQKQRV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 416 ILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIAL-RDAGAAILVISEDLDELFQiSDRLAALSGGQLSDlipteQTS 494
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLA-----QGS 226
|
....
gi 488618663 495 TVQI 498
Cdd:PRK13640 227 PVEI 230
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
9-56 |
8.26e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 41.52 E-value: 8.26e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 488618663 9 RLQLRHItkrypGCLANDAVDLTIQPGeIHALLGENGAGKSTLMKIIY 56
Cdd:COG3950 5 SLTIENF-----RGFEDLEIDFDNPPR-LTVLVGENGSGKTTLLEAIA 46
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
28-222 |
1.00e-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: 40.00 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTLMK----------IIYGVTQPDAGSIIWQGQAQTMRNpaqarsLGIGMvfqhfslfe 97
Cdd:cd03238 14 LDVSIPLNVLVVVTGVSGSGKSTLVNeglyasgkarLISFLPKFSRNKLIFIDQLQFLID------VGLGY--------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 98 tlsvaqniaLAMGAAAGTpkqleprirevsqrygmavepqrlvhsLSIGERQKVEIIRCLMQDIR--LLILDEPTSVLTP 175
Cdd:cd03238 79 ---------LTLGQKLST---------------------------LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQ 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488618663 176 QEAEELFVTLRHLAAEGCSILFISHklgEVRALCHSATVLRNGKVSG 222
Cdd:cd03238 123 QDINQLLEVIKGLIDLGNTVILIEH---NLDVLSSADWIIDFGPGSG 166
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
276-484 |
1.04e-03 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 40.53 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtLPHAQATTLRFQDTPVGDLRPDAR---RKHGLAFVPAERLghgA 352
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAG---LDDGSSGEVSLVGQPLHQMDEEARaklRAKHVGFVFQSFM---L 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 353 VPELSLADNALLTAFQQGLVSHGliQRGKVRALADEIIRRFAVKTTDAQaaarsLSGGNLQKFILGREILQNPKLLIAAH 432
Cdd:PRK10584 100 IPTLNALENVELPALLRGESSRQ--SRNGAKALLEQLGLGKRLDHLPAQ-----LSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488618663 433 PTWGVDVGAAAAIHRALIAL-RDAGAAILVISEDlDELFQISDRLAALSGGQL 484
Cdd:PRK10584 173 PTGNLDRQTGDKIADLLFSLnREHGTTLILVTHD-LQLAARCDRRLRLVNGQL 224
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
138-278 |
1.19e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 138 RLVHSLSIGERQKVEIIRCLMQDIR---LLILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRALCHSATV 214
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLEL 884
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488618663 215 LRNGKVSGHCIPAECSDLELARLMVGDAEGLTAHYdkvSGSEAFLRVDKLSWHNPDPFGCSLKD 278
Cdd:PRK00635 885 GPEGGNLGGYLLASCSPEELIHLHTPTAKALRPYL---SSPQELPYLPDPSPKPPVPADITIKN 945
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
276-308 |
1.28e-03 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 40.21 E-value: 1.28e-03
10 20 30
....*....|....*....|....*....|...
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSG 308
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAG 70
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
277-485 |
1.29e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 41.17 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 277 KDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtlphaqattlrFQDTPVGDLRPDARRKHGLAfvPAERlGHGAV--- 353
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAG-------------LEDITSGDLFIGEKRMNDVP--PAER-GVGMVfqs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 354 ----PELSLADNalltafqqglVSHGLIQRGKVRAladEIIRRFAVKTTDAQAAA------RSLSGGNLQKFILGREILQ 423
Cdd:PRK11000 84 yalyPHLSVAEN----------MSFGLKLAGAKKE---EINQRVNQVAEVLQLAHlldrkpKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488618663 424 NPKLLIAAHPTWGVDvgAA---------AAIHRALialrdaGAAILVISEDLDELFQISDRLAALSGGQLS 485
Cdd:PRK11000 151 EPSVFLLDEPLSNLD--AAlrvqmrieiSRLHKRL------GRTMIYVTHDQVEAMTLADKIVVLDAGRVA 213
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
403-483 |
1.60e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 40.41 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 403 AARSLSGGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIALR-DAGAAILVISEDLDELFQISDRLAALSG 481
Cdd:PRK14258 147 SALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKG 226
|
..
gi 488618663 482 GQ 483
Cdd:PRK14258 227 NE 228
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
28-207 |
1.83e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 39.93 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 28 VDLTIQPGEIHALLGENGAGKSTL-MKIIYGvtqpdagsiiwQGQAQTMRN-PAQARSLGIGMVFQHFSLFETLSVAqnI 105
Cdd:cd03270 14 VDVDIPRNKLVVITGVSGSGKSSLaFDTIYA-----------EGQRRYVESlSAYARQFLGQMDKPDVDSIEGLSPA--I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 106 ALAMGAAAGTPKQLEPRIREV-------------SQRYGMAVE-------PQRLVHSLSIGERQKVEIIRCLMQDIR--L 163
Cdd:cd03270 81 AIDQKTTSRNPRSTVGTVTEIydylrllfarvgiRERLGFLVDvglgyltLSRSAPTLSGGEAQRIRLATQIGSGLTgvL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488618663 164 LILDEPTSVLTPQEAEELFVTLRHLAAEGCSILFISHKLGEVRA 207
Cdd:cd03270 161 YVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRA 204
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
404-484 |
1.85e-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: 41.15 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 404 ARSLSGGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIALRdAGAAILVISEDLDELFQISDRLAALSGGQ 483
Cdd:TIGR01257 1059 AQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
.
gi 488618663 484 L 484
Cdd:TIGR01257 1138 L 1138
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
123-234 |
2.26e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.78 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 123 IREVSQRYGMAVEPQRlvHSLSIGERQKVEIIRCLMQDIRLLILDEPTSVL---TPQEAEELFVTLRHLAAEgcSILFIS 199
Cdd:PTZ00265 1341 IESLPNKYDTNVGPYG--KSLSGGQKQRIAIARALLREPKILLLDEATSSLdsnSEKLIEKTIVDIKDKADK--TIITIA 1416
|
90 100 110
....*....|....*....|....*....|....*
gi 488618663 200 HKLGEVRAlCHSATVLRNGKVSGHCIPAECSDLEL 234
Cdd:PTZ00265 1417 HRIASIKR-SDKIVVFNNPDRTGSFVQAHGTHEEL 1450
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
40-66 |
2.61e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.26 E-value: 2.61e-03
10 20
....*....|....*....|....*..
gi 488618663 40 LLGENGAGKSTLMKIIYGVTQPDAGSI 66
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNV 58
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
259-429 |
2.96e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 40.08 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 259 LRVDKLSWHNPDPFGCSLKDLSLEVRSGEIVGIAGVAGNGQDELLALLsgeQTLPHAQATTLRFQDTPVGDLRPDARRKH 338
Cdd:PRK10789 314 LDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLI---QRHFDVSEGDIRFHDIPLTKLQLDSWRSR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 339 gLAFVpaerlghGAVPEL---SLADNALL---TAFQQglvshgliQRGKVRALA---DEIIRRFAVKTTDAQAAARSLSG 409
Cdd:PRK10789 391 -LAVV-------SQTPFLfsdTVANNIALgrpDATQQ--------EIEHVARLAsvhDDILRLPQGYDTEVGERGVMLSG 454
|
170 180
....*....|....*....|
gi 488618663 410 GNLQKFILGREILQNPKLLI 429
Cdd:PRK10789 455 GQKQRISIARALLLNAEILI 474
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
276-484 |
3.14e-03 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 39.29 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 276 LKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGEqtlphaqattlrfqdtpvgdLRPDA---RRKHGLAFvPAErLGHGA 352
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGI--------------------LEPTSgrvEVNGRVSA-LLE-LGAGF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 353 VPELSLADNALLtafqQGLVsHGLiQRGKVRALADEIIrRFA---------VKTTDAQAAAR---SLSggnlqkfilgre 420
Cdd:COG1134 100 HPELTGRENIYL----NGRL-LGL-SRKEIDEKFDEIV-EFAelgdfidqpVKTYSSGMRARlafAVA------------ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488618663 421 ILQNPKLLIaahptwgVD----VGAAAAIHRA---LIALRDAGAAILVISEDLDELFQISDRLAALSGGQL 484
Cdd:COG1134 161 TAVDPDILL-------VDevlaVGDAAFQKKClarIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
274-483 |
3.31e-03 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 39.93 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 274 CSLKDLSLEVRSGEIVGIAGVAGNGQDELLALLSGeqtlphaqattlrFQDTPVGDLRPDARRkhgLAFVPAERLGHGAV 353
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAG-------------FETPDSGRIMLDGQD---ITHVPAENRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 354 -------PELSLADNalltafqqglVSHGLiqRGKVRAlADEIIRRFA-----VKTTD-AQAAARSLSGGNLQKFILGRE 420
Cdd:PRK09452 92 fqsyalfPHMTVFEN----------VAFGL--RMQKTP-AAEITPRVMealrmVQLEEfAQRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488618663 421 ILQNPKLLIAAHPTWGVDVGAAAAIHRALIAL-RDAGAAILVISEDLDELFQISDRLAALSGGQ 483
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
377-463 |
3.84e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.01 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 377 IQRGKVRALADEIIRRFAVK-TTDAQAAARSLSGGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIALRD- 454
Cdd:PTZ00265 1328 VKRACKFAAIDEFIESLPNKyDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDk 1407
|
....*....
gi 488618663 455 AGAAILVIS 463
Cdd:PTZ00265 1408 ADKTIITIA 1416
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
417-483 |
5.01e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 39.71 E-value: 5.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 417 LGREILQNPKLLI-AAHPTWGVDVGAAAAIHRALIALRDAGAAIL-VISEDLDELFQISDRLAALS-GGQ 483
Cdd:TIGR00956 912 IGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILcTIHQPSAILFEEFDRLLLLQkGGQ 981
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
408-475 |
5.27e-03 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 38.92 E-value: 5.27e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488618663 408 SGGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIAL-RDAGAAILVISEDLDELFQISDR 475
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDR 231
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
402-484 |
5.87e-03 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 37.99 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 402 AAARSLSGGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIALRDAGAAILV-ISEDLDELFQISDRLAAL- 479
Cdd:cd03232 104 ALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCtIHQPSASIFEKFDRLLLLk 183
|
....*
gi 488618663 480 SGGQL 484
Cdd:cd03232 184 RGGKT 188
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
264-483 |
6.76e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 39.07 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 264 LSWHNPDPFGCSLKDLSLEVRSGEIVGIAGVAGNGQD----ELLALLSGEQTLPHAQATTLRFQDTPVGDLRPDA----R 335
Cdd:PRK10261 20 IAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDKMLLRRRSRQVIELSEQSaaqmR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488618663 336 RKHG--LAFVPAErlghgavPELSLadNALLTAFQQGLVSHGLIQ-RGKVRALADEIIRRFAVKTTDAQAA----ARSLS 408
Cdd:PRK10261 100 HVRGadMAMIFQE-------PMTSL--NPVFTVGEQIAESIRLHQgASREEAMVEAKRMLDQVRIPEAQTIlsryPHQLS 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488618663 409 GGNLQKFILGREILQNPKLLIAAHPTWGVDVGAAAAIHRALIAL-RDAGAAILVISEDLDELFQISDRLAALSGGQ 483
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
|
| |
