|
Name |
Accession |
Description |
Interval |
E-value |
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-505 |
0e+00 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 649.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 10 SDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKAREL 89
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGE-ILLDGEPVRFRSPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 90 GVQVIYQDLSLFPNLTVAENIAFElNLKGYFGWFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVAD 169
Cdd:COG1129 80 GIAIIHQELNLVPNLSVAENIFLG-REPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 170 ARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITELMTG 249
Cdd:COG1129 159 ARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 250 LDIvHERKPPNNAEDRRTVLEIKNLSRAGQYRDINLNLKRGEVlglcgllgsgRTELALSLFGITHPDSGELFIEGKPVK 329
Cdd:COG1129 239 REL-EDLFPKRAAAPGEVVLEVEGLSVGGVVRDVSFSVRAGEIlgiaglvgagRTELARALFGADPADSGEIRLDGKPVR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 330 LKNNTDAIKRGIGYVSEDRLTLGAILQQSIADNMVISILDRLkTPWHLIDEKQCQDIVQEWIADLDIKVTDPNNALSTLS 409
Cdd:COG1129 318 IRSPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDRL-SRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLS 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 410 GGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVKEI 489
Cdd:COG1129 397 GGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGEL 476
|
490
....*....|....*.
gi 491046221 490 VTDSINEQQLEEIING 505
Cdd:COG1129 477 DREEATEEAIMAAATG 492
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
10-499 |
2.13e-148 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 434.07 E-value: 2.13e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 10 SDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKAREL 89
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGE-ILIDGKPVRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 90 GVQVIYQDLSLFPNLTVAENIAfeLNLKGYFGWF-RKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVA 168
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIV--LGLEPTKGGRlDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 169 DARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITELMT 248
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 249 GLDIV-HERKPPnnAEDRRTVLEIKNLSRAGQY-----RDINLNLKRGEVlglcgllgsgrTELALSLFGITHPDSGELF 322
Cdd:COG3845 239 GREVLlRVEKAP--AEPGEVVLEVENLSVRDDRgvpalKDVSLEVRAGEIlgiagvagngqSELAEALAGLRPPASGSIR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 323 IEGKPVKLKNNTDAIKRGIGYVSEDRLTLGAILQQSIADNMVISILDRLK-TPWHLIDEKQCQDIVQEWIADLDIKVTDP 401
Cdd:COG3845 317 LDGEDITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGRYRRPPfSRGGFLDRKAIRAFAEELIEEFDVRTPGP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 402 NNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMK 481
Cdd:COG3845 397 DTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMY 476
|
490
....*....|....*...
gi 491046221 482 QGSIVKEIVTDSINEQQL 499
Cdd:COG3845 477 EGRIVGEVPAAEATREEI 494
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
10-498 |
2.89e-141 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 415.87 E-value: 2.89e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 10 SDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGS-KIEIDGKSYHRLTPDKARE 88
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEgEIIFEGEELQASNIRDTER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 89 LGVQVIYQDLSLFPNLTVAENIaFELNLKGYFGWFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVA 168
Cdd:PRK13549 82 AGIAIIHQELALVKELSVLENI-FLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 169 DARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITELMT 248
Cdd:PRK13549 161 QARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMMV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 249 GLDIVhERKPPNNAEDRRTVLEIKNLS-------RAGQYRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDS-GE 320
Cdd:PRK13549 241 GRELT-ALYPREPHTIGEVILEVRNLTawdpvnpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 321 LFIEGKPVKLKNNTDAIKRGIGYVSEDRLTLGAILQQSIADNMVISILDRLkTPWHLIDEKQCQDIVQEWIADLDIKVTD 400
Cdd:PRK13549 320 IFIDGKPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDRF-TGGSRIDDAAELKTILESIQRLKVKTAS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 401 PNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHM 480
Cdd:PRK13549 399 PELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVM 478
|
490
....*....|....*...
gi 491046221 481 KQGSIVKEIVTDSINEQQ 498
Cdd:PRK13549 479 HEGKLKGDLINHNLTQEQ 496
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
10-499 |
2.74e-135 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 400.44 E-value: 2.74e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 10 SDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKAREL 89
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGS-ILIDGQEMRFASTTAALAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 90 GVQVIYQDLSLFPNLTVAENIaFELNLKGYFGWFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVAD 169
Cdd:PRK11288 80 GVAIIYQELHLVPEMTVAENL-YLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 170 ARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPA-EGLTTRKITELMT 248
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDmAQVDRDQLVQAMV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 249 GLDI--VHERKPPNNAEDRrtvLEIKNLSRAGQYRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGK 326
Cdd:PRK11288 239 GREIgdIYGYRPRPLGEVR---LRLDGLKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 327 PVKLKNNTDAIKRGIGYVSEDRLTLGAILQQSIADNMVISIlDRLKTPW-HLIDEKQCQDIVQEWIADLDIKVTDPNNAL 405
Cdd:PRK11288 316 PIDIRSPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINISA-RRHHLRAgCLINNRWEAENADRFIRSLNIKTPSREQLI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 406 STLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSI 485
Cdd:PRK11288 395 MNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
490
....*....|....
gi 491046221 486 VKEIVTDSINEQQL 499
Cdd:PRK11288 475 AGELAREQATERQA 488
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
12-503 |
5.12e-127 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 379.90 E-value: 5.12e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 12 PLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGV 91
Cdd:PRK09700 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGT-ITINNINYNKLDHKLAAQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 92 QVIYQDLSLFPNLTVAENIAF-ELNLKGYFG-----WfrkKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRA 165
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIgRHLTKKVCGvniidW---REMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 166 LVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITE 245
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 246 LMTGLDIVHE---RKPPNNAEDRRTVLEIKNLSR--AGQYRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGE 320
Cdd:PRK09700 240 LMVGRELQNRfnaMKENVSNLAHETVFEVRNVTSrdRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 321 LFIEGKPVKLKNNTDAIKRGIGYVSEDRLTLGAILQQSIADNMVIS---ILDRLKTPWHLIDEKQCQDIVQEWIADLDIK 397
Cdd:PRK09700 320 IRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISrslKDGGYKGAMGLFHEVDEQRTAENQRELLALK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 398 VTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRI 477
Cdd:PRK09700 400 CHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRI 479
|
490 500
....*....|....*....|....*..
gi 491046221 478 LHMKQGSIVKEIV-TDSINEqqlEEII 503
Cdd:PRK09700 480 AVFCEGRLTQILTnRDDMSE---EEIM 503
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
12-495 |
1.81e-120 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 362.83 E-value: 1.81e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 12 PLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGV 91
Cdd:PRK15439 10 PLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGT-LEIGGNPCARLTPAKAHQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 92 QVIYQDLSLFPNLTVAENIAFELNlkgyfgwfrKKQLREKALE-ILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADA 170
Cdd:PRK15439 89 YLVPQEPLLFPNLSVKENILFGLP---------KRQASMQKMKqLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 171 RLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITELMT-- 248
Cdd:PRK15439 160 RILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAITpa 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 249 --GLDIVHERK----PPNNaedRRT------VLEIKNLSRAGqYRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHP 316
Cdd:PRK15439 240 arEKSLSASQKlwleLPGN---RRQqaagapVLTVEDLTGEG-FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 317 DSGELFIEGKPVKLKNNTDAIKRGIGYVSEDRLTLGAILQQSIADNmVISILDRLKTPWhlIDEKQCQDIVQEWIADLDI 396
Cdd:PRK15439 316 RGGRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWN-VCALTHNRRGFW--IKPARENAVLERYRRALNI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 397 KVTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDR 476
Cdd:PRK15439 393 KFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADR 472
|
490
....*....|....*....
gi 491046221 477 ILHMKQGSIVKEIVTDSIN 495
Cdd:PRK15439 473 VLVMHQGEISGALTGAAIN 491
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
12-499 |
1.17e-116 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 352.77 E-value: 1.17e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 12 PLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGV 91
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGS-ILYLGKEVTFNGPKSSQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 92 QVIYQDLSLFPNLTVAENIAFELNLKGYFGWFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADAR 171
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIFLGREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 172 LVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITELMTG-- 249
Cdd:PRK10762 162 VIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVGrk 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 250 LDivhERKPPNNAEDRRTVLEIKNLSRAGqYRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVK 329
Cdd:PRK10762 242 LE---DQYPRLDKAPGEVRLKVDNLSGPG-VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 330 LKNNTDAIKRGIGYVSEDRLTLGAILQQSIADNMVISILDRLKTPWHLIDEKQCQDIVQEWIADLDIKVTDPNNALSTLS 409
Cdd:PRK10762 318 TRSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYFSRAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 410 GGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVKEI 489
Cdd:PRK10762 398 GGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEF 477
|
490
....*....|
gi 491046221 490 VTDSINEQQL 499
Cdd:PRK10762 478 TREQATQEKL 487
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
16-489 |
5.47e-116 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 351.01 E-value: 5.47e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 16 LRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYApdDGS---KIEIDGKSYHRLTPDKARELGVQ 92
Cdd:NF040905 4 MRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP--HGSyegEILFDGEVCRFKDIRDSEALGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 93 VIYQDLSLFPNLTVAENIaFELNLKGYFGWFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARL 172
Cdd:NF040905 82 IIHQELALIPYLSIAENI-FLGNERAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 173 VIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWP--AEGLTTRKITELMTGL 250
Cdd:NF040905 161 LILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDcrADEVTEDRIIRGMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 251 DIVHeRKPPNNAEDRRTVLEIKNLSRAGQY-------RDINLNLKRGEVLGLCGLLGSGRTELALSLFGIT--HPDSGEL 321
Cdd:NF040905 241 DLED-RYPERTPKIGEVVFEVKNWTVYHPLhperkvvDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 322 FIEGKPVKLKNNTDAIKRGIGYVSEDRLTLGAILQQSIADNMVISILDRLkTPWHLIDEKQCQDIVQEWIADLDIKVTDP 401
Cdd:NF040905 320 FKDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLANLGKV-SRRGVIDENEEIKVAEEYRKKMNIKTPSV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 402 NNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMK 481
Cdd:NF040905 399 FQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMN 478
|
....*...
gi 491046221 482 QGSIVKEI 489
Cdd:NF040905 479 EGRITGEL 486
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-501 |
4.21e-113 |
|
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: 343.73 E-value: 4.21e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 13 LITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDgskieIDGKSYHRLTPDKAR----- 87
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGT-----WDGEIYWSGSPLKASnirdt 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 88 -ELGVQVIYQDLSLFPNLTVAENIAF--ELNLKGYFGWFRKKQLREKALeiLNELAFTIDPDT-PVQFLPIAQRQQVAIC 163
Cdd:TIGR02633 76 eRAGIVIIHQELTLVPELSVAENIFLgnEITLPGGRMAYNAMYLRAKNL--LRELQLDADNVTrPVGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 164 RALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKI 243
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 244 TELMTGLDI--VHERKPPNNAEDrrtVLEIKNLS-------RAGQYRDINLNLKRGEVLGLCGLLGSGRTELALSLFGiT 314
Cdd:TIGR02633 234 ITMMVGREItsLYPHEPHEIGDV---ILEARNLTcwdvinpHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-A 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 315 HPD--SGELFIEGKPVKLKNNTDAIKRGIGYVSEDRLTLGAILQQSIADNMVISILDRLKTPWHLIDEKQcQDIVQEWIA 392
Cdd:TIGR02633 310 YPGkfEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAE-LQIIGSAIQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 393 DLDIKVTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYY 472
Cdd:TIGR02633 389 RLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLG 468
|
490 500
....*....|....*....|....*....
gi 491046221 473 NCDRILHMKQGSIVKEIVTDSINEQQLEE 501
Cdd:TIGR02633 469 LSDRVLVIGEGKLKGDFVNHALTQEQVLA 497
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
16-503 |
1.64e-109 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 334.01 E-value: 1.64e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 16 LRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGVQVIY 95
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGS-ILFQGKEIDFKSSKEALENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 96 QDLSLFPNLTVAENIAF-ELNLKGYFgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLVI 174
Cdd:PRK10982 80 QELNLVLQRSVMDNMWLgRYPTKGMF--VDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 175 MDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITELMTGLDIVH 254
Cdd:PRK10982 158 MDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSLTQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 255 eRKPPNNAEDRRTVLEIKNLSRAGQ--YRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKN 332
Cdd:PRK10982 238 -RFPDKENKPGEVILEVRNLTSLRQpsIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 333 NTDAIKRGIGYVSEDRLTLGAILQQSIADNMVISILDRLKTPWHLIDEKQCQDIVQeWIAD-LDIKVTDPNNALSTLSGG 411
Cdd:PRK10982 317 ANEAINHGFALVTEERRSTGIYAYLDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQ-WVIDsMRVKTPGHRTQIGSLSGG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 412 NQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSiVKEIVT 491
Cdd:PRK10982 396 NQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGL-VAGIVD 474
|
490
....*....|..
gi 491046221 492 DSINEQqlEEII 503
Cdd:PRK10982 475 TKTTTQ--NEIL 484
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-232 |
1.01e-74 |
|
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: 232.70 E-value: 1.01e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGVQV 93
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGE-ILVDGKEVSFASPRDARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 94 IYQdlslfpnltvaeniafelnlkgyfgwfrkkqlrekaleilnelaftidpdtpvqfLPIAQRQQVAICRALVADARLV 173
Cdd:cd03216 80 VYQ-------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 174 IMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGT 232
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
266-485 |
3.88e-68 |
|
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: 216.53 E-value: 3.88e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 266 RTVLEIKNLSRAGQYRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTDAIKRGIGYVS 345
Cdd:cd03215 2 EPVLEVRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 346 EDRLTLGAILQQSIADNMVISILdrlktpwhlidekqcqdivqewiadldikvtdpnnalstLSGGNQQKVVLAKWILTR 425
Cdd:cd03215 82 EDRKREGLVLDLSVAENIALSSL---------------------------------------LSGGNQQKVVLARWLARD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 426 PKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSI 485
Cdd:cd03215 123 PRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-486 |
1.58e-63 |
|
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: 215.15 E-value: 1.58e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 11 DPLITLRDLSKSF--GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGvYAPDDGS---KIEIDGKSYHRLTPdK 85
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRisgEVLLDGRDLLELSE-A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 86 ARELGVQVIYQD--LSLFPnLTVAENIAFELNLKGyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAIC 163
Cdd:COG1123 80 LRGRRIGMVFQDpmTQLNP-VTVGDQIAEALENLG----LSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 164 RALVADARLVIMDEPTASLTRTEVNQLLSTVNYL-KDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRK 242
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 243 ITELMTGLDIVHERKPPNNAEDRRTVLEIKNLS-----RAGQY----RDINLNLKRGEVlglcgllgsgrteLAL----- 308
Cdd:COG1123 235 QALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSkrypvRGKGGvravDDVSLTLRRGET-------------LGLvgesg 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 309 --------SLFGITHPDSGELFIEGKPV--KLKNNTDAIKRGIGYVSED-------RLTLGAIlqqsIADNMVISildrl 371
Cdd:COG1123 302 sgkstlarLLLGLLRPTSGSILFDGKDLtkLSRRSLRELRRRVQMVFQDpysslnpRMTVGDI----IAEPLRLH----- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 372 ktpwHLIDEKQCQDIVQEWIAD--LDIKVTD--PnnalSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIY 447
Cdd:COG1123 373 ----GLLSRAERRERVAELLERvgLPPDLADryP----HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQIL 444
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 491046221 448 KLIHRLSG-VGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:COG1123 445 NLLRDLQReLGLTYLFISHDLAVVRYIADRVAVMYDGRIV 484
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
16-237 |
2.45e-61 |
|
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: 200.74 E-value: 2.45e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 16 LRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGVQVIY 95
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGS-VLFDGEDITGLPPHEIARLGIGRTF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 96 QDLSLFPNLTVAEN--IAFELNLKGYFGWFR----KKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVAD 169
Cdd:cd03219 82 QIPRLFPELTVLENvmVAAQARTGSGLLLARarreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 170 ARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIgtwpAEG 237
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVI----AEG 225
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
10-236 |
4.98e-61 |
|
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: 200.65 E-value: 4.98e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 10 SDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKAREL 89
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGR-ILFDGRDITGLPPHRIARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 90 GVQVIYQDLSLFPNLTVAENIA----------FELNLKGYFGWFRK-KQLREKALEILNELAFTIDPDTPVQFLPIAQRQ 158
Cdd:COG0411 80 GIARTFQNPRLFPELTVLENVLvaaharlgrgLLAALLRLPRARREeREARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 159 QVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEISDRITVIRDGQKI--GTwPA 235
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIaeGT-PA 238
|
.
gi 491046221 236 E 236
Cdd:COG0411 239 E 239
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
14-241 |
1.77e-58 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 193.36 E-value: 1.77e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGvqV 93
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGE-VRVLGEDVARDPAEVRRRIG--Y 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 94 IYQDLSLFPNLTVAENIAFelnLKGYFGwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLV 173
Cdd:COG1131 78 VPQEPALYPDLTVRENLRF---FARLYG-LPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 174 IMDEPTASL---TRTEVNQLLSTvnyLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTR 241
Cdd:COG1131 154 ILDEPTSGLdpeARRELWELLRE---LAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
10-236 |
3.16e-55 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 188.77 E-value: 3.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 10 SDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKaREL 89
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGR-ILLDGRDVTGLPPEK-RNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 90 GvqVIYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEILN-----ELAftidpDTPVQFLPIAQRQQVAICR 164
Cdd:COG3842 80 G--MVFQDYALFPHLTVAENVAFGLRMRG----VPKAEIRARVAELLElvgleGLA-----DRYPHQLSGGQQQRVALAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 165 ALVADARLVIMDEPTASL---TRTEVNQLLstVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDG--QKIGTwPAE 236
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALdakLREEMREEL--RRLQRELGITFIYVTHDQEEALALADRIAVMNDGriEQVGT-PEE 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-228 |
2.66e-53 |
|
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: 187.80 E-value: 2.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 3 STSKADKSDPLITLRDLSKSF-----GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKS 77
Cdd:COG1123 250 AAPAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGS-ILFDGKD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 78 YHRLTPDKARELG--VQVIYQD--LSLFPNLTVAENIAFELNLkgyFGWFRKKQLREKALEILNELAftIDPDT----PV 149
Cdd:COG1123 329 LTKLSRRSLRELRrrVQMVFQDpySSLNPRMTVGDIIAEPLRL---HGLLSRAERRERVAELLERVG--LPPDLadryPH 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 150 QFlpiaQRQQVAICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRD 226
Cdd:COG1123 404 ELsg-gQRQRVAIARALALEPKLLILDEPTSALdvsVQAQILNLLRDLQ--RELGLTYLFISHDLAVVRYIADRVAVMYD 480
|
..
gi 491046221 227 GQ 228
Cdd:COG1123 481 GR 482
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
14-228 |
7.42e-53 |
|
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: 177.71 E-value: 7.42e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKaRELGvqV 93
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGE-ILIDGRDVTGVPPER-RNIG--M 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 94 IYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLV 173
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGLKLRG----VPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 174 IMDEPTASL---TRTEVNQLLSTVnyLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03259 153 LLDEPLSALdakLREELREELKEL--QRELGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
14-228 |
1.07e-49 |
|
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: 167.96 E-value: 1.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGvqV 93
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGE-IKVLGKDIKKEPEEVKRRIG--Y 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 94 IYQDLSLFPNLTVAENIAFElnlKGyfgwfrkkqlrekaleilnelaftidpdtpvqflpiaQRQQVAICRALVADARLV 173
Cdd:cd03230 78 LPEEPSLYENLTVRENLKLS---GG-------------------------------------MKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 174 IMDEPTASL---TRTEVNQLLSTvnyLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03230 118 ILDEPTSGLdpeSRREFWELLRE---LKKEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
10-236 |
1.06e-48 |
|
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: 167.85 E-value: 1.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 10 SDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKAREL 89
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGE-ILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 90 ----GvqVIYQDLSLFPNLTVAENIAFELNlkgYFGWFRKKQLREKALEILN--ELAFTIDpdtpvqFLPiAQ-----RQ 158
Cdd:COG1127 81 rrriG--MLFQGGALFDSLTVFENVAFPLR---EHTDLSEAEIRELVLEKLElvGLPGAAD------KMP-SElsggmRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 159 QVAICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQKI--GTw 233
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLdpiTSAVIDELIRELR--DELGLTSVVVTHDLDSAFAIADRVAVLADGKIIaeGT- 225
|
...
gi 491046221 234 PAE 236
Cdd:COG1127 226 PEE 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
10-223 |
8.70e-48 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 166.03 E-value: 8.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 10 SDPLITLRDLSKSF----GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDK 85
Cdd:COG1116 4 AAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGE-VLVDGKPVTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 86 ArelgvqVIYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEILNE--LAFTID--PDTpvqfLPIAQRQQVA 161
Cdd:COG1116 83 G------VVFQEPALLPWLTVLDNVALGLELRG----VPKAERRERARELLELvgLAGFEDayPHQ----LSGGMRQRVA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 162 ICRALVADARLVIMDEPTASL---TRTEVNQLLstVNYLKDKGITVVFVSHRLEEVKEISDRITV 223
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALdalTRERLQDEL--LRLWQETGKTVLFVTHDVDEAVFLADRVVV 211
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
11-228 |
1.11e-47 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 164.45 E-value: 1.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 11 DPLITLRDLSKSFG----GHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDK- 85
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGE-VLIDGQDISSLSEREl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 86 ----ARELGvqVIYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEILNEL-------AFtidpdtPVQfLPI 154
Cdd:COG1136 81 arlrRRHIG--FVFQFFNLLPELTALENVALPLLLAG----VSRKERRERARELLERVglgdrldHR------PSQ-LSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 155 AQRQQVAICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRlEEVKEISDRITVIRDGQ 228
Cdd:COG1136 148 GQQQRVAIARALVNRPKLILADEPTGNLdskTGEEVLELLRELN--RELGTTIVMVTHD-PELAARADRVIRLRDGR 221
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
14-236 |
2.44e-46 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 164.86 E-value: 2.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPdKARelGVQV 93
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSG-EILIGGRDVTDLPP-KDR--NIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 94 IYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLREK---ALEILNelaftIDPdtpvqFL---PIA----QRQQVAIC 163
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLKLRK----VPKAEIDRRvreAAELLG-----LED-----LLdrkPKQlsggQRQRVALG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 164 RALVADARLVIMDEPTASL-------TRTEVNQLlstvnyLKDKGITVVFVSHRLEEVKEISDRITVIRDG--QKIGTwP 234
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLdaklrveMRAEIKRL------HRRLGTTTIYVTHDQVEAMTLADRIAVMNDGriQQVGT-P 218
|
..
gi 491046221 235 AE 236
Cdd:COG3839 219 EE 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
14-228 |
1.86e-45 |
|
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: 158.42 E-value: 1.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGG----HRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDK---- 85
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGE-VRVDGTDISKLSEKElaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 86 -ARELGvqVIYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICR 164
Cdd:cd03255 80 rRRHIG--FVFQSFNLLPDLTALENVELPLLLAG----VPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 165 ALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRlEEVKEISDRITVIRDGQ 228
Cdd:cd03255 154 ALANDPKIILADEPTGNLdseTGKEVMELLRELN--KEAGTTIVVVTHD-PELAEYADRIIELRDGK 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
14-240 |
2.60e-44 |
|
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: 156.12 E-value: 2.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGVQ- 92
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGE-VLIDGEDISGLSEAELYRLRRRm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 93 -VIYQDLSLFPNLTVAENIAFELNlkgYFGWFRKKQLREKALEILNELAFTIDPDT-PVQfLPIAQRQQVAICRALVADA 170
Cdd:cd03261 80 gMLFQSGALFDSLTVFENVAFPLR---EHTRLSEEEIREIVLEKLEAVGLRGAEDLyPAE-LSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 171 RLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTT 240
Cdd:cd03261 156 ELLLYDEPTAGLdpiASGVIDDLIRSLK--KELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
14-234 |
3.43e-44 |
|
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: 154.94 E-value: 3.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGG----HRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKArel 89
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGE-VLVDGEPVTGPGPDRG--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 90 gvqVIYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEILNE--LAFTIDpDTPVQfLPIAQRQQVAICRALV 167
Cdd:cd03293 77 ---YVFQQDALLPWLTVLDNVALGLELQG----VPKAEARERAEELLELvgLSGFEN-AYPHQ-LSGGMRQRVALARALA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491046221 168 ADARLVIMDEPTASL---TRTEVNQLLSTVnyLKDKGITVVFVSHRLEEVKEISDRITVI--RDGQKIGTWP 234
Cdd:cd03293 148 VDPDVLLLDEPFSALdalTREQLQEELLDI--WRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEVE 217
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-230 |
3.65e-44 |
|
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: 155.18 E-value: 3.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSF-GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARELgVQ 92
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSG-EVLVDGKDITKKNLRELRRK-VG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 93 VIYQ--DLSLFpNLTVAENIAFEL-NLKgyfgwFRKKQLREKALEILN-----ELAftidpDTPVQFLPIAQRQQVAICR 164
Cdd:COG1122 79 LVFQnpDDQLF-APTVEEDVAFGPeNLG-----LPREEIRERVEEALElvgleHLA-----DRPPHELSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 165 ALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKI 230
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIV 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
9-246 |
4.12e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 155.63 E-value: 4.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 9 KSDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRltpdKARE 88
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGT-VRLFGKPPRR----ARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 89 LGvqviY--QDLSL---FPnLTVAENIAfeLNLKGYFGWFR--KKQLREKALEILNElaftidpdtpVQFLPIA------ 155
Cdd:COG1121 77 IG----YvpQRAEVdwdFP-ITVRDVVL--MGRYGRRGLFRrpSRADREAVDEALER----------VGLEDLAdrpige 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 156 ----QRQQVAICRALVADARLVIMDEPTASL-TRTEvNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ-K 229
Cdd:COG1121 140 lsggQQQRVLLARALAQDPDLLLLDEPFAGVdAATE-EALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLvA 218
|
250
....*....|....*..
gi 491046221 230 IGTwPAEGLTTRKITEL 246
Cdd:COG1121 219 HGP-PEEVLTPENLSRA 234
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
16-228 |
5.43e-44 |
|
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: 154.16 E-value: 5.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 16 LRDLSKSFGGHR--ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARELgVQV 93
Cdd:cd03225 2 LKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSG-EVLVDGKDLTKLSLKELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 94 IYQ--DLSLFpNLTVAENIAFELNLKGYfgwfRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADAR 171
Cdd:cd03225 80 VFQnpDDQFF-GPTVEEEVAFGLENLGL----PEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 172 LVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
14-228 |
4.43e-43 |
|
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: 150.80 E-value: 4.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGK---SYHRLTPDKARELG 90
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGS-ILIDGEdltDLEDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 91 vqVIYQDLSLFPNLTVAENIAFELNlkGyfgwfrkkqlrekaleilnelaftidpdtpvqflpiAQRQQVAICRALVADA 170
Cdd:cd03229 80 --MVFQDFALFPHLTVLENIALGLS--G------------------------------------GQQQRVALARALAMDP 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 171 RLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03229 120 DVLLLDEPTSALdpiTRREVRALLKSLQ--AQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
14-236 |
5.50e-43 |
|
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: 152.39 E-value: 5.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKArelGVQV 93
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSG-EILLDGKDITNLPPHKR---PVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 94 IYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLV 173
Cdd:cd03300 77 VFQNYALFPHLTVFENIAFGLRLKK----LPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 174 IMDEPTASLTRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEISDRITVIRDG--QKIGTwPAE 236
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGkiQQIGT-PEE 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
13-228 |
3.50e-42 |
|
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: 150.04 E-value: 3.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 13 LITLRDLSKSFGGHR----ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARE 88
Cdd:cd03258 1 MIELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGS-VLVDGTDLTLLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 89 LGVQV--IYQDLSLFPNLTVAENIAFELNLKGYfgwfRKKQLREKALEILNELAFTIDPDT-PVQfLPIAQRQQVAICRA 165
Cdd:cd03258 80 ARRRIgmIFQHFNLLSSRTVFENVALPLEIAGV----PKAEIEERVLELLELVGLEDKADAyPAQ-LSGGQKQRVGIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 166 LVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03258 155 LANNPKVLLCDEATSALdpeTTQSILALLRDIN--RELGLTIVLITHEMEVVKRICDRVAVMEKGE 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
13-246 |
1.24e-41 |
|
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: 149.42 E-value: 1.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 13 LITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTP-DKARELGv 91
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGE-VLLDGRDLASLSRrELARRIA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 92 qVIYQDLSLFPNLTVAENIAfeLNLKGYFGWFRK-----KQLREKALEILN--ELAftidpDTPVQFLPIAQRQQVAICR 164
Cdd:COG1120 79 -YVPQEPPAPFGLTVRELVA--LGRYPHLGLFGRpsaedREAVEEALERTGleHLA-----DRPVDELSGGERQRVLIAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 165 ALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQKI--GTwPAEGLT 239
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLdlaHQLEVLELLRRLA--RERGRTVVMVLHDLNLAARYADRLVLLKDGRIVaqGP-PEEVLT 227
|
....*..
gi 491046221 240 TRKITEL 246
Cdd:COG1120 228 PELLEEV 234
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
13-228 |
2.02e-41 |
|
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: 148.04 E-value: 2.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 13 LITLRDLSKSF----GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARE 88
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSG-SIIFDGKDLLKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 89 LG--VQVIYQD--LSLFPNLTVAENIAfELnLKGYFGWFRKKQLREKALEILNELaftIDPDTPVQFLPIA----QRQQV 160
Cdd:cd03257 80 RRkeIQMVFQDpmSSLNPRMTIGEQIA-EP-LRIHGKLSKKEARKEAVLLLLVGV---GLPEEVLNRYPHElsggQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 161 AICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALdvsVQAQILDLLKKLQ--EELGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
14-236 |
9.20e-41 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 149.91 E-value: 9.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPdkARELGVQV 93
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSG-RIVLNGRDLFTNLP--PRERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 94 IYQDLSLFPNLTVAENIAFELNLKGYFgwfrKKQLREKALEILNElaftidpdtpVQFLPIA----------QRQQVAIC 163
Cdd:COG1118 80 VFQHYALFPHMTVAENIAFGLRVRPPS----KAEIRARVEELLEL----------VQLEGLAdrypsqlsggQRQRVALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 164 RALVADARLVIMDEPTASL---TRTEVNQLLStvNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ--KIGTwPAE 236
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALdakVRKELRRWLR--RLHDELGGTTVFVTHDQEEALELADRVVVMNQGRieQVGT-PDE 220
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
14-228 |
1.76e-40 |
|
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: 145.27 E-value: 1.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGVQV 93
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGS-IRFDGRDITGLPPHERARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 94 IYQDLSLFPNLTVAENiafeLNLKGYFGWFRK-KQLREKALE---ILNELAftidpDTPVQFLPIAQRQQVAICRALVAD 169
Cdd:cd03224 80 VPEGRRIFPELTVEEN----LLLGAYARRRAKrKARLERVYElfpRLKERR-----KQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 170 ARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
14-228 |
2.15e-39 |
|
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: 142.01 E-value: 2.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKsyhRLTPDKARELGVQV 93
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSG-RIYIGGR---DVTDLPPKDRDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 94 IYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEIlnelAFTIDPDTPVQFLPIA----QRQQVAICRALVAD 169
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAFGLKLRK----VPKDEIDERVREV----AELLQIEHLLDRKPKQlsggQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 170 ARLVIMDEPTASL-------TRTEVNQLlstvnyLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03301 149 PKVFLMDEPLSNLdaklrvqMRAELKRL------QQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
11-238 |
4.18e-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: 142.04 E-value: 4.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 11 DPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELG 90
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGS-IRFDGEDITGLPPHRIARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 91 VQVIYQDLSLFPNLTVAENiafeLNLKGYFGwfRKKQLREKALE-------ILNELAftidpDTPVQFLPIAQRQQVAIC 163
Cdd:COG0410 80 IGYVPEGRRIFPSLTVEEN----LLLGAYAR--RDRAEVRADLErvyelfpRLKERR-----RQRAGTLSGGEQQMLAIG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 164 RALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGL 238
Cdd:COG0410 149 RALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-228 |
6.28e-39 |
|
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: 141.86 E-value: 6.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 13 LITLRDLSKSFG----GHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRlTPDKARE 88
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGE-VTFDGRPVTR-RRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 89 LGVQVIYQD--LSLFPNLTVAENIAFELNLKGyfgwfrKKQLREKALEILNELAftIDPD----TPVQfLPIAQRQQVAI 162
Cdd:COG1124 79 RRVQMVFQDpyASLHPRHTVDRILAEPLRIHG------LPDREERIAELLEQVG--LPPSfldrYPHQ-LSGGQRQRVAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 163 CRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:COG1124 150 ARALILEPELLLLDEPTSALdvsVQAEILNLLKDLR--EERGLTYLFVSHDLAVVAHLCDRVAVMQNGR 216
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
14-246 |
1.18e-38 |
|
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: 141.17 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFG-GHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGVQ 92
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGS-VLIDGTDINKLKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 93 V--IYQDLSLFPNLTVAENI-----AFELNLKGYFGWFrKKQLREKALEILN-----ELAFtidpdTPVQFLPIAQRQQV 160
Cdd:cd03256 80 IgmIFQQFNLIERLSVLENVlsgrlGRRSTWRSLFGLF-PKEEKQRALAALErvgllDKAY-----QRADQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 161 AICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEG 237
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLdpaSSRQVMDLLKRIN--REEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE 231
|
....*....
gi 491046221 238 LTTRKITEL 246
Cdd:cd03256 232 LTDEVLDEI 240
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
12-214 |
1.29e-38 |
|
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: 139.92 E-value: 1.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 12 PLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGv 91
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGE-VLWNGEPIRDAREDYRRRLA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 92 qVIYQDLSLFPNLTVAENIAFELNLKGYFGwfRKKQLREkALEILN--ELAftidpDTPVQFLPIAQRQQVAICRALVAD 169
Cdd:COG4133 79 -YLGHADGLKPELTVRENLRFWAALYGLRA--DREAIDE-ALEAVGlaGLA-----DLPVRQLSAGQKRRVALARLLLSP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491046221 170 ARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEV 214
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLEL 194
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
14-228 |
1.36e-38 |
|
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: 139.97 E-value: 1.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKsyhRLTPDKA--RELGV 91
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSG-TIIIDGL---KLTDDKKniNELRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 92 QV--IYQDLSLFPNLTVAENIAFEL-NLKGyfgwFRKKQLREKALEILNE--LAFTIDpDTPVQfLPIAQRQQVAICRAL 166
Cdd:cd03262 77 KVgmVFQQFNLFPHLTVLENITLAPiKVKG----MSKAEAEERALELLEKvgLADKAD-AYPAQ-LSGGQQQRVAIARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491046221 167 VADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03262 151 AMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
11-232 |
2.66e-38 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 143.93 E-value: 2.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 11 DPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKaRElg 90
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGR-IMLDGQDITHVPAEN-RH-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 91 VQVIYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEI-----LNELAftidPDTPVQfLPIAQRQQVAICRA 165
Cdd:PRK09452 88 VNTVFQSYALFPHMTVFENVAFGLRMQK----TPAAEITPRVMEAlrmvqLEEFA----QRKPHQ-LSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 166 LVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEISDRITVIRDG--QKIGT 232
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGriEQDGT 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
14-236 |
3.75e-38 |
|
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: 139.78 E-value: 3.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKsyhRLTPDKARELGVQV 93
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGT-ILFGGE---DATDVPVQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 94 IYQDLSLFPNLTVAENIAFELNLKGYFGWFRKKQLREKALEILNELAFTIDPDT-PVQfLPIAQRQQVAICRALVADARL 172
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRyPAQ-LSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 173 VIMDEPTASLTRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEISDRITVIRDGQ--KIGTwPAE 236
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRieQVGT-PDE 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
14-228 |
5.27e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 138.65 E-value: 5.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSF-GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKA----RE 88
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSG-QVLVNGQDLSRLKRREIpylrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 89 LGvqVIYQDLSLFPNLTVAENIAFELNLKGYfgwfRKKQLREKALEILNEL-------AFtidpdtPVQfLPIAQRQQVA 161
Cdd:COG2884 81 IG--VVFQDFRLLPDRTVYENVALPLRVTGK----SRKEIRRRVREVLDLVglsdkakAL------PHE-LSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 162 ICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylkDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLdpeTSWEIMELLEEIN---RRGTTVLIATHDLELVDRMPKRVLELEDGR 214
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
14-240 |
7.33e-38 |
|
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: 138.97 E-value: 7.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHR-ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARELGVQ 92
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSG-EIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 93 VIyQDLSLFPNLTVAENIAFELNLKGYfgwfRKKQLREKALEILNELAftIDPDTPVQFLPI----AQRQQVAICRALVA 168
Cdd:cd03295 80 VI-QQIGLFPHMTVEENIALVPKLLKW----PKEKIRERADELLALVG--LDPAEFADRYPHelsgGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 169 DARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDG--QKIGTwPAEGLTT 240
Cdd:cd03295 153 DPPLLLMDEPFGALdpiTRDQLQEEFKRLQ--QELGKTIVFVTHDIDEAFRLADRIAIMKNGeiVQVGT-PDEILRS 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
29-180 |
2.61e-37 |
|
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: 134.31 E-value: 2.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARElGVQVIYQDLSLFPNLTVAE 108
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGT-ILLDGQDLTDDERKSLRK-EIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 109 NIAFELNLKGYFgwfrKKQLREKALEILNELAFTIDPDTPVQFLPIA----QRQQVAICRALVADARLVIMDEPTA 180
Cdd:pfam00005 79 NLRLGLLLKGLS----KREKDARAEEALEKLGLGDLADRPVGERPGTlsggQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
13-228 |
2.10e-36 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 134.74 E-value: 2.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 13 LITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGksyHRLTPDKA------ 86
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGT-ITVDG---EDLTDSKKdinklr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 87 RELGVqvIYQDLSLFPNLTVAENIAFEL-NLKGYfgwfRKKQLREKALEILNEL-------AFtidpdtPVQfLPIAQRQ 158
Cdd:COG1126 77 RKVGM--VFQQFNLFPHLTVLENVTLAPiKVKKM----SKAEAEERAMELLERVgladkadAY------PAQ-LSGGQQQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 159 QVAICRALVADARLVIMDEPTASL---TRTEVnqlLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:COG1126 144 RVAIARALAMEPKVMLFDEPTSALdpeLVGEV---LDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGR 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
14-240 |
2.83e-36 |
|
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: 135.46 E-value: 2.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHR------------------------ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGs 69
Cdd:cd03294 1 IKIKGLYKIFGKNPqkafkllakgkskeeilkktgqtvGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 70 KIEIDGKSYHRLTPDKAREL---GVQVIYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEILNELAFTIDPD 146
Cdd:cd03294 80 KVLIDGQDIAAMSRKELRELrrkKISMVFQSFALLPHRTVLENVAFGLEVQG----VPRAEREERAAEALELVGLEGWEH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 147 TPVQFLPIAQRQQVAICRALVADARLVIMDEPTASL---TRTEV-NQLLSTVnylKDKGITVVFVSHRLEEVKEISDRIT 222
Cdd:cd03294 156 KYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALdplIRREMqDELLRLQ---AELQKTIVFITHDLDEALRLGDRIA 232
|
250 260
....*....|....*....|
gi 491046221 223 VIRDGQ--KIGTwPAEGLTT 240
Cdd:cd03294 233 IMKDGRlvQVGT-PEEILTN 251
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
14-228 |
8.62e-36 |
|
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: 133.23 E-value: 8.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRaLRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKArelGVQV 93
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSG-KILLNGKDITNLPPEKR---DISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 94 IYQDLSLFPNLTVAENIAFELNLKGYfgwfRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLV 173
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYGLKKRKV----DKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKIL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 174 IMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03299 152 LLDEPFSALdvrTKEKLREELKKIR--KEFGVTVLHVTHDFEEAWALADKVAIMLNGK 207
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-230 |
8.77e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 134.85 E-value: 8.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGksyHRLTPDKARELGvqv 93
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGE-VLWDG---EPLDPEDRRRIG--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 94 iYqdL----SLFPNLTVAENIAFELNLKGYfgwfRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVAD 169
Cdd:COG4152 75 -Y--LpeerGLYPKMKVGEQLVYLARLKGL----SKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 170 ARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKI 230
Cdd:COG4152 148 PELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKV 208
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-223 |
9.61e-36 |
|
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: 135.18 E-value: 9.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 13 LITLRDLSKSF----GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAP---DDGSkIEIDGKSYHRLTPDK 85
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGE-ILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 86 AREL---GVQVIYQD--LSLFPNLTVAENIAFELNLkgyFGWFRKKQLREKALEILNELAFTIDPDT----PVQFLPiAQ 156
Cdd:COG0444 80 LRKIrgrEIQMIFQDpmTSLNPVMTVGDQIAEPLRI---HGGLSKAEARERAIELLERVGLPDPERRldryPHELSG-GM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 157 RQQVAICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITV 223
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALdvtIQAQILNLLKDLQ--RELGLAILFITHDLGVVAEIADRVAV 223
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
18-233 |
1.14e-35 |
|
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: 132.03 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 18 DLSKSFGGHRAlrNIDLTLNkGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDG-------KSYHrlTPDKARELG 90
Cdd:cd03297 5 DIEKRLPDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGG-TIVLNGtvlfdsrKKIN--LPPQQRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 91 VqvIYQDLSLFPNLTVAENIAFELNLKgyfgwfRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADA 170
Cdd:cd03297 79 L--VFQQYALFPHLNVRENLAFGLKRK------RNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491046221 171 RLVIMDEPTASLTRTEVNQLLSTVNYL-KDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTW 233
Cdd:cd03297 151 ELLLLDEPFSALDRALRLQLLPELKQIkKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
18-227 |
2.75e-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: 131.12 E-value: 2.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 18 DLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKsyhrltpdKARELGVQVIY-- 95
Cdd:cd03235 4 DLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSG-SIRVFGK--------PLEKERKRIGYvp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 96 QDLSL---FPnLTVAENIAFELNLK-GYFGWFRKKQlREKALEIL-----NELAftidpDTPVQFLPIAQRQQVAICRAL 166
Cdd:cd03235 75 QRRSIdrdFP-ISVRDVVLMGLYGHkGLFRRLSKAD-KAKVDEALervglSELA-----DRQIGELSGGQQQRVLLARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 167 VADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRI-----TVIRDG 227
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVlllnrTVVASG 213
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-250 |
3.57e-35 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 137.47 E-value: 3.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 6 KADKSDPLITLRDLS-KSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPD 84
Cdd:COG3845 250 PAEPGEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGS-IRLDGEDITGLSPR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 85 KARELGVQVIYQD---LSLFPNLTVAENIAFELNLKGYF---GWFRKKQLREKALEILNElaFTI---DPDTPVQFLPIA 155
Cdd:COG3845 329 ERRRLGVAYIPEDrlgRGLVPDMSVAENLILGRYRRPPFsrgGFLDRKAIRAFAEELIEE--FDVrtpGPDTPARSLSGG 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 156 QRQQVAICRALVADARLVIMDEPT-------ASLTRtevNQLLStvnyLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:COG3845 407 NQQKVILARELSRDPKLLIAAQPTrgldvgaIEFIH---QRLLE----LRDAGAAVLLISEDLDEILALSDRIAVMYEGR 479
|
250 260
....*....|....*....|..
gi 491046221 229 KIGTWPAEGLTTRKITELMTGL 250
Cdd:COG3845 480 IVGEVPAAEATREEIGLLMAGV 501
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
14-228 |
1.26e-34 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 132.89 E-value: 1.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSF----GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKAREL 89
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGS-VLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 90 --GVQVIYQDLSLFPNLTVAENIAFELNLKGYfgwfRKKQLREKALEILnEL--------AFtidpdtPVQfLPIAQRQQ 159
Cdd:COG1135 81 rrKIGMIFQHFNLLSSRTVAENVALPLEIAGV----PKAEIRKRVAELL-ELvglsdkadAY------PSQ-LSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491046221 160 VAICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALdpeTTRSILDLLKDIN--RELGLTIVLITHEMDVVRRICDRVAVLENGR 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
15-228 |
7.74e-34 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 125.05 E-value: 7.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 15 TLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARElGVQVI 94
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGE-ILIDGKDIAKLPLEELRR-RIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 95 YQdLSlfpnltvaeniafelnlKGyfgwfrkkqlrekaleilnelaftidpdtpvqflpiaQRQQVAICRALVADARLVI 174
Cdd:cd00267 79 PQ-LS-----------------GG-------------------------------------QRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491046221 175 MDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
14-230 |
1.06e-33 |
|
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: 126.63 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSyhrLTPDKARELGvqv 93
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSG-EVLFDGKP---LDIAARNRIG--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 94 iY--QDLSLFPNLTVAENIAFELNLKGYfgwfRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADAR 171
Cdd:cd03269 74 -YlpEERGLYPKMKVIDQLVYLAQLKGL----KKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 172 LVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKI 230
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
13-227 |
1.11e-33 |
|
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: 126.71 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 13 LITLRDLSKSFGGHR----ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARE 88
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAG-FATVDGFDVVKEPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 89 LGVqvIYQDLSLFPNLTVAENIafelnlkGYFGWFRKKQlREKALEILNELAFTID----PDTPVQFLPIAQRQQVAICR 164
Cdd:cd03266 80 LGF--VSDSTGLYDRLTARENL-------EYFAGLYGLK-GDELTARLEELADRLGmeelLDRRVGGFSTGMRQKVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 165 ALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDG 227
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-228 |
1.12e-33 |
|
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: 125.19 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGG--HRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELgV 91
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGE-ILIDGVDLRDLDLESLRKN-I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 92 QVIYQDLSLFpNLTVAENIafelnlkgyfgwfrkkqlrekaleilnelaftidpdtpvqfLPIAQRQQVAICRALVADAR 171
Cdd:cd03228 79 AYVPQDPFLF-SGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 172 LVIMDEPTASL-TRTEvNQLLSTVNYLKdKGITVVFVSHRLEEVKeISDRITVIRDGQ 228
Cdd:cd03228 117 ILILDEATSALdPETE-ALILEALRALA-KGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-228 |
1.80e-33 |
|
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: 134.58 E-value: 1.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHR--ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARElgv 91
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGR-ILIDGIDLRQIDPASLRR--- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 92 QVIY--QDLSLFpNLTVAENIAF---ELNLkgyfgwfrkKQLREkALEILNELAFTID-P---DTPV----QFLPIAQRQ 158
Cdd:COG2274 550 QIGVvlQDVFLF-SGTIRENITLgdpDATD---------EEIIE-AARLAGLHDFIEAlPmgyDTVVgeggSNLSGGQRQ 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 159 QVAICRALVADARLVIMDEPTASL-TRTE--VNQLLSTVnylkDKGITVVFVSHRLEEVKeISDRITVIRDGQ 228
Cdd:COG2274 619 RLAIARALLRNPRILILDEATSALdAETEaiILENLRRL----LKGRTVIIIAHRLSTIR-LADRIIVLDKGR 686
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
14-232 |
2.91e-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: 125.70 E-value: 2.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGG--HRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRlTPDKAR-ELG 90
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGT-AYINGYSIRT-DRKAARqSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 91 vqVIYQDLSLFPNLTVAENIAFELNLKGYfgwfRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADA 170
Cdd:cd03263 79 --YCPQFDALFDELTVREHLRFYARLKGL----PKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 171 RLVIMDEPTASL---TRTEVNQLLSTVNylkdKGITVVFVSHRLEEVKEISDRITVIRDGQK--IGT 232
Cdd:cd03263 153 SVLLLDEPTSGLdpaSRRAIWDLILEVR----KGRSIILTTHSMDEAEALCDRIAIMSDGKLrcIGS 215
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-228 |
3.44e-33 |
|
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: 132.57 E-value: 3.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 3 STSKADKSDPLITLRDLSKSF-GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRL 81
Cdd:COG4988 326 TAPLPAAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGS-ILINGVDLSDL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 82 TPDKARElgvQVIY--QDLSLFPnLTVAENIAF--------ELnlkgyfgwfrkkqlrEKALEILNELAFtID-----PD 146
Cdd:COG4988 405 DPASWRR---QIAWvpQNPYLFA-GTIRENLRLgrpdasdeEL---------------EAALEAAGLDEF-VAalpdgLD 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 147 TPV----QFLPIAQRQQVAICRALVADARLVIMDEPTASL-TRTEvNQLLSTVNYLKdKGITVVFVSHRLEEVKEiSDRI 221
Cdd:COG4988 465 TPLgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLdAETE-AEILQALRRLA-KGRTVILITHRLALLAQ-ADRI 541
|
....*..
gi 491046221 222 TVIRDGQ 228
Cdd:COG4988 542 LVLDDGR 548
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
11-228 |
1.35e-32 |
|
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: 122.54 E-value: 1.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 11 DPLITLRDLSksfgGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARELG 90
Cdd:cd03215 2 EPVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASG-EITLDGKPVTRRSPRDAIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 91 VQVIYQD---LSLFPNLTVAENIAFELNLKGyfGwfrkkqlrekaleilNelaftidpdtpvqflpiaqrQQ-VAICRAL 166
Cdd:cd03215 77 IAYVPEDrkrEGLVLDLSVAENIALSSLLSG--G---------------N--------------------QQkVVLARWL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 167 VADARLVIMDEPTASL---TRTEVNQLLstvNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03215 120 ARDPRVLILDEPTRGVdvgAKAEIYRLI---RELADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
14-228 |
1.50e-32 |
|
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: 124.19 E-value: 1.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARELGVQV 93
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSG-KILLDGQDITKLPMHKRARLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 94 IYQDLSLFPNLTVAENIAFELNLKGYfgwfRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLV 173
Cdd:cd03218 80 LPQEASIFRKLTVEENILAVLEIRGL----SKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 174 IMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGK 210
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
10-223 |
2.50e-32 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 126.00 E-value: 2.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 10 SDPLITLRDLSKSF----------GGH-RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSY 78
Cdd:COG4608 4 AEPLLEVRDLKKHFpvrgglfgrtVGVvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGE-ILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 79 HRLTPDKAREL--GVQVIYQD--LSLFPNLTVAENIAFELNLkgyFGWFRKKQLREKALEILNELAftIDPDT----PVQ 150
Cdd:COG4608 83 TGLSGRELRPLrrRMQMVFQDpyASLNPRMTVGDIIAEPLRI---HGLASKAERRERVAELLELVG--LRPEHadryPHE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 151 FlPIAQRQQVAICRALVADARLVIMDEPTASL---TRTEVnqllstVNYLKD----KGITVVFVSHRLEEVKEISDRITV 223
Cdd:COG4608 158 F-SGGQRQRIGIARALALNPKLIVCDEPVSALdvsIQAQV------LNLLEDlqdeLGLTYLFISHDLSVVRHISDRVAV 230
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
14-230 |
5.51e-32 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 122.81 E-value: 5.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSY---HRLTPDKAREL- 89
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQ-LNIAGHQFdfsQKPSEKAIRLLr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 90 -GVQVIYQDLSLFPNLTVAEN-IAFELNLKGyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALV 167
Cdd:COG4161 82 qKVGMVFQQYNLWPHLTVMENlIEAPCKVLG----LSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 168 ADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKI 230
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRII 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-213 |
1.69e-31 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 121.89 E-value: 1.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 12 PLITLRDLSKSFGGHR----ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKAr 87
Cdd:COG4525 2 SMLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGE-ITLDGVPVTGPGADRG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 88 elgvqVIYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALV 167
Cdd:COG4525 80 -----VVFQKDALLPWLNVLDNVAFGLRLRG----VPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491046221 168 ADARLVIMDEPTASL---TRTEVNQLLSTVnyLKDKGITVVFVSHRLEE 213
Cdd:COG4525 151 ADPRFLLMDEPFGALdalTREQMQELLLDV--WQRTGKGVFLITHSVEE 197
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
14-228 |
9.11e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 119.09 E-value: 9.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGgHRALRnIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKaRelGVQV 93
Cdd:COG3840 2 LRLDDLTYRYG-DFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGR-ILWNGQDLTALPPAE-R--PVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 94 IYQDLSLFPNLTVAENIAFEL--NLKgyfgwFRKKQlREKALEI-----LNELAftidpdtpvQFLPIA----QRQQVAI 162
Cdd:COG3840 76 LFQENNLFPHLTVAQNIGLGLrpGLK-----LTAEQ-RAQVEQAlervgLAGLL---------DRLPGQlsggQRQRVAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 163 CRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALdpaLRQEMLDLVDELC--RERGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-236 |
1.27e-30 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 122.64 E-value: 1.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 5 SKADKS-DPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTP 83
Cdd:PRK11607 10 AKTRKAlTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAG-QIMLDGVDLSHVPP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 84 DKARelgVQVIYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEILN-----ELAftidPDTPVQfLPIAQRQ 158
Cdd:PRK11607 89 YQRP---INMMFQSYALFPHMTVEQNIAFGLKQDK----LPKAEIASRVNEMLGlvhmqEFA----KRKPHQ-LSGGQRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 159 QVAICRALVADARLVIMDEPTASLTRTEVNQL-LSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ--KIGTwPA 235
Cdd:PRK11607 157 RVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKfvQIGE-PE 235
|
.
gi 491046221 236 E 236
Cdd:PRK11607 236 E 236
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
15-228 |
1.43e-30 |
|
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: 117.15 E-value: 1.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 15 TLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTP-DKARELGV-- 91
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGE-ILLDGKDLASLSPkELARKIAYvp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 92 QVIYQdlslfpnltvaeniafeLNLkgyfgwfrkKQLREKaleILNELAFtidpdtpvqflpiAQRQQVAICRALVADAR 171
Cdd:cd03214 80 QALEL-----------------LGL---------AHLADR---PFNELSG-------------GERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 172 LVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03214 118 ILLLDEPTSHLdiaHQIELLELLRRLA--RERGKTVVMVLHDLNLAARYADRVILLKDGR 175
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
11-256 |
5.67e-30 |
|
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: 117.49 E-value: 5.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 11 DPLITLRDLSKSFGGHRALRNIDLTLNKGEvHC-LAGTNGCGKSTLIKTISGVYAPDDGSKIEIDGKSYHRLTPDKARE- 88
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGE-HWaILGPNGAGKSTLLSLITGDLPPTYGNDVRLFGERRGGEDVWELRKr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 89 LGVqvIYQDLSL-FPNLTVAENIAfelnLKGYF---GWFRK--KQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAI 162
Cdd:COG1119 80 IGL--VSPALQLrFPRDETVLDVV----LSGFFdsiGLYREptDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 163 CRALVADARLVIMDEPTASLTRTEVNQLLSTVNYL-KDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWP-AEGLTT 240
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPkEEVLTS 233
|
250
....*....|....*.
gi 491046221 241 RKITELMtGLDIVHER 256
Cdd:COG1119 234 ENLSEAF-GLPVEVER 248
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
10-236 |
6.50e-30 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 117.40 E-value: 6.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 10 SDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKAREL 89
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGT-ILLRGQHIEGLPGHQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 90 GVQVIYQDLSLFPNLTVAEN--IAFELNLK-GYF-GWFRKKQLREKALEILNELAFTIDpdtPVQFLPIAQRQ------- 158
Cdd:PRK11300 81 GVVRTFQHVRLFREMTVIENllVAQHQQLKtGLFsGLLKTPAFRRAESEALDRAATWLE---RVGLLEHANRQagnlayg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 159 ---QVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEISDRITVIRDGQKI--GT 232
Cdd:PRK11300 158 qqrRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLanGT 237
|
....
gi 491046221 233 wPAE 236
Cdd:PRK11300 238 -PEE 240
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
269-502 |
1.63e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 115.93 E-value: 1.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLSRagQY------RDINLNLKRGEVlglcgllgsgrteLAL-------------SLFGITHPDSGELFIEGKPVK 329
Cdd:COG1131 1 IEVRGLTK--RYgdktalDGVSLTVEPGEI-------------FGLlgpngagktttirMLLGLLRPTSGEVRVLGEDVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 330 lkNNTDAIKRGIGYVSED-----RLTLGAILQqsiadnmvisILDRLktpwHLIDEKQCQDIVQEWIADLDIKvTDPNNA 404
Cdd:COG1131 66 --RDPAEVRRRIGYVPQEpalypDLTVRENLR----------FFARL----YGLPRKEARERIDELLELFGLT-DAADRK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 405 LSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGS 484
Cdd:COG1131 129 VGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGR 208
|
250
....*....|....*...
gi 491046221 485 IVKEIVTDSINEQQLEEI 502
Cdd:COG1131 209 IVADGTPDELKARLLEDV 226
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-228 |
2.51e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 121.43 E-value: 2.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSksF---GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELg 90
Cdd:COG1132 340 IEFENVS--FsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGR-ILIDGVDIRDLTLESLRRQ- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 91 VQVIYQDLSLFpNLTVAENIAF--------ELnlkgyfgwfrkkqlrEKALEILNELAFtID--P---DTPV----QFLP 153
Cdd:COG1132 416 IGVVPQDTFLF-SGTIRENIRYgrpdatdeEV---------------EEAAKAAQAHEF-IEalPdgyDTVVgergVNLS 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 154 IAQRQQVAICRALVADARLVIMDEPTASL-TRTE--VNQLLSTVnyLKDKgiTVVFVSHRLEEVKEiSDRITVIRDGQ 228
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALdTETEalIQEALERL--MKGR--TTIVIAHRLSTIRN-ADRILVLDDGR 551
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
10-228 |
4.11e-29 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 114.45 E-value: 4.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 10 SDPLITLRDLSKSFGGHRA----LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPD- 84
Cdd:COG4181 5 SAPIIELRGLTKTVGTGAGeltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGT-VRLAGQDLFALDEDa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 85 ----KARELGVqvIYQDLSLFPNLTVAENIAFELNLKGyfgwfrKKQLREKALEILNE--LAFTIDpDTPVQfLPIAQRQ 158
Cdd:COG4181 84 rarlRARHVGF--VFQSFQLLPTLTALENVMLPLELAG------RRDARARARALLERvgLGHRLD-HYPAQ-LSGGEQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 159 QVAICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRlEEVKEISDRITVIRDGQ 228
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLdaaTGEQIIDLLFELN--RERGTTLVLVTHD-PALAARCDRVLRLRAGR 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
14-238 |
4.63e-29 |
|
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: 114.20 E-value: 4.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVY-----APDDGsKIEIDGKS-YHRLTPDKAR 87
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEG-EVLLDGKDiYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 88 ELGVQVIYQDLSLFPnLTVAENIAFELNLKGYfgwFRKKQLREKALEILNELAFT--IDPDTPVQFLPIAQRQQVAICRA 165
Cdd:cd03260 80 RRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGI---KLKEELDERVEEALRKAALWdeVKDRLHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 166 LVADARLVIMDEPTASL---TRTEVNQLLSTvnyLKDKgITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGL 238
Cdd:cd03260 156 LANEPEVLLLDEPTSALdpiSTAKIEELIAE---LKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
14-230 |
4.66e-29 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 114.73 E-value: 4.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSY---HRLTPDKAREL- 89
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSG-TLNIAGNHFdfsKTPSDKAIRELr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 90 -GVQVIYQDLSLFPNLTVAEN-IAFELNLKGyfgwFRKKQLREKALEILNELAFTIDPDT-PVQfLPIAQRQQVAICRAL 166
Cdd:PRK11124 82 rNVGMVFQQYNLWPHLTVQQNlIEAPCRVLG----LSKDQALARAEKLLERLRLKPYADRfPLH-LSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491046221 167 VADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKI 230
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-228 |
9.69e-29 |
|
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: 119.49 E-value: 9.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 3 STSKADKSDPLITLRDLSKSFGGHR--ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHR 80
Cdd:COG4987 323 AEPAPAPGGPSLELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGS-ITLGGVDLRD 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 81 LTPDKARELgVQVIYQDLSLFpNLTVAENIAF--------ELnlkgyfgwfrkkqlrEKALEI--LNELAFTIDP--DTP 148
Cdd:COG4987 402 LDEDDLRRR-IAVVPQRPHLF-DTTLRENLRLarpdatdeEL---------------WAALERvgLGDWLAALPDglDTW 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 149 V----QFLPIAQRQQVAICRALVADARLVIMDEPTASL-TRTEvNQLLSTV-NYLKDKgiTVVFVSHRLEEVkEISDRIT 222
Cdd:COG4987 465 LgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLdAATE-QALLADLlEALAGR--TVLLITHRLAGL-ERMDRIL 540
|
....*.
gi 491046221 223 VIRDGQ 228
Cdd:COG4987 541 VLEDGR 546
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-486 |
1.50e-28 |
|
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: 118.63 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 10 SDPLITLRDLSKSFGG----HRALRNIDLTLNKGEVHCLAGTNGCGKS----TLIKTISGVYAPDDGSkIEIDGKSYHRL 81
Cdd:COG4172 3 SMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGS-ILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 82 TPDKAREL-GVQV--IYQD--LSLFPNLTVAENIAFELNL-KGyfgwFRKKQLREKALEILNELAFTiDPDTPVQFLPI- 154
Cdd:COG4172 82 SERELRRIrGNRIamIFQEpmTSLNPLHTIGKQIAEVLRLhRG----LSGAAARARALELLERVGIP-DPERRLDAYPHq 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 155 ---AQRQQVAICRALVADARLVIMDEPTASL---TRTEVNQLLSTvnyLKDK-GITVVFVSHRLEEVKEISDRITVIRDG 227
Cdd:COG4172 157 lsgGQRQRVMIAMALANEPDLLIADEPTTALdvtVQAQILDLLKD---LQRElGMALLLITHDLGVVRRFADRVAVMRQG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 228 QKIGTWPAEGLT-------TRKItelmtgLDIVHERKPPNNAEDRRTVLEIKNLS-----RAGQYR----------DINL 285
Cdd:COG4172 234 EIVEQGPTAELFaapqhpyTRKL------LAAEPRGDPRPVPPDAPPLLEARDLKvwfpiKRGLFRrtvghvkavdGVSL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 286 NLKRGEvlglcgllgsgrT-----E-------LALSLFGItHPDSGELFIEGKPVKLKNNTD--AIKRGIGYVSED---- 347
Cdd:COG4172 308 TLRRGE------------TlglvgEsgsgkstLGLALLRL-IPSEGEIRFDGQDLDGLSRRAlrPLRRRMQVVFQDpfgs 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 348 ---RLTLGAIlqqsIADNMVIsildrlktpwHLI--DEKQCQDIVQEWIAD--LDIKVTD--PNnalsTLSGGNQQKVVL 418
Cdd:COG4172 375 lspRMTVGQI----IAEGLRV----------HGPglSAAERRARVAEALEEvgLDPAARHryPH----EFSGGQRQRIAI 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 419 AKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGV-GISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:COG4172 437 ARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVV 505
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
44-232 |
2.28e-28 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 114.90 E-value: 2.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 44 LAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKArelGVQVIYQDLSLFPNLTVAENIAFELNLKGYFGWF 123
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGS-IMLDGEDVTNVPPHLR---HINMVFQSYALFPHMTVEENVAFGLKMRKVPRAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 124 RKKQLREkALEILNELAFTidPDTPVQfLPIAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDK-GI 202
Cdd:TIGR01187 77 IKPRVLE-ALRLVQLEEFA--DRKPHQ-LSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGI 152
|
170 180 190
....*....|....*....|....*....|..
gi 491046221 203 TVVFVSHRLEEVKEISDRITVIRDGQ--KIGT 232
Cdd:TIGR01187 153 TFVFVTHDQEEAMTMSDRIAIMRKGKiaQIGT 184
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
14-237 |
3.39e-28 |
|
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: 111.69 E-value: 3.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIeIDGKSYHRLTPDKARELGvqV 93
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAT-VAGHDVVREPREVRRRIG--I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 94 IYQDLSLFPNLTVAENIAFELNLKGYFGwfrkKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLV 173
Cdd:cd03265 78 VFQDLSVDDELTGWENLYIHARLYGVPG----AERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 174 IMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIgtwpAEG 237
Cdd:cd03265 154 FLDEPTIGLdpqTRAHVWEYIEKLK--EEFGMTILLTTHYMEEAEQLCDRVAIIDHGRII----AEG 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
14-227 |
5.60e-28 |
|
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: 110.96 E-value: 5.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSF-GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRL----TPDKARE 88
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGT-IRVNGQDVSDLrgraIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 89 LGVqvIYQDLSLFPNLTVAENIAFELNLKGYFGwfrkKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVA 168
Cdd:cd03292 80 IGV--VFQDFRLLPDRNVYENVAFALEVTGVPP----REIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491046221 169 DARLVIMDEPTASL---TRTEVNQLLSTVNylkDKGITVVFVSHRLEEVKEISDRITVIRDG 227
Cdd:cd03292 154 SPTILIADEPTGNLdpdTTWEIMNLLKKIN---KAGTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
14-238 |
1.28e-27 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 111.00 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGS----KIEIDGKSYHRLTPDKAREL 89
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTirvgDITIDTARSLSQQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 90 GVQV--IYQDLSLFPNLTVAENIafelnLKGYFgwFRKKQLREKAL----EILNELAFTIDPDTPVQFLPIAQRQQVAIC 163
Cdd:PRK11264 84 RQHVgfVFQNFNLFPHRTVLENI-----IEGPV--IVKGEPKEEATararELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 164 RALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGL 238
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
18-270 |
1.30e-27 |
|
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: 113.66 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 18 DLSKSFGGHrALrNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGK------SYHRLTPDKaRELGV 91
Cdd:COG4148 6 DFRLRRGGF-TL-DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGR-IRLGGEvlqdsaRGIFLPPHR-RRIGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 92 qvIYQDLSLFPNLTVAENIAFelnlkGYfgWFRKKQLRekaleilnelafTIDPDTPVQFLPIA-------------QRQ 158
Cdd:COG4148 82 --VFQEARLFPHLSVRGNLLY-----GR--KRAPRAER------------RISFDEVVELLGIGhlldrrpatlsggERQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 159 QVAICRALVADARLVIMDEPTASLTRTEVNQLLStvnYL----KDKGITVVFVSHRLEEVKEISDRITVIRDGQKIgtwp 234
Cdd:COG4148 141 RVAIGRALLSSPRLLLMDEPLAALDLARKAEILP---YLerlrDELDIPILYVSHSLDEVARLADHVVLLEQGRVV---- 213
|
250 260 270
....*....|....*....|....*....|....*.
gi 491046221 235 AEGlttrKITELMTGLDIVherkPPNNAEDRRTVLE 270
Cdd:COG4148 214 ASG----PLAEVLSRPDLL----PLAGGEEAGSVLE 241
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
13-213 |
1.41e-27 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 110.94 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 13 LITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKsyhRLTPDKArELGvq 92
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGS-ITLDGK---PVEGPGA-ERG-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 93 VIYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARL 172
Cdd:PRK11248 74 VVFQNEGLLPWRNVQDNVAFGLQLAG----VEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491046221 173 VIMDEPTASL---TRTEVNQLLSTVnyLKDKGITVVFVSHRLEE 213
Cdd:PRK11248 150 LLLDEPFGALdafTREQMQTLLLKL--WQETGKQVLLITHDIEE 191
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
15-222 |
3.04e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 108.72 E-value: 3.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 15 TLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPD---DGsKIEIDGKSYHRLtPDKARELGv 91
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSG-EVLLNGRRLTAL-PAEQRRIG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 92 qVIYQDLSLFPNLTVAENIAFELNLKgyfgwFRKKQLREKALEILNELA----FTIDPDTpvqfLPIAQRQQVAICRALV 167
Cdd:COG4136 80 -ILFQDDLLFPHLSVGENLAFALPPT-----IGRAQRRARVEQALEEAGlagfADRDPAT----LSGGQRARVALLRALL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 168 ADARLVIMDEPTASL---TRTEVNQLlsTVNYLKDKGITVVFVSHRLEEVKEISDRIT 222
Cdd:COG4136 150 AEPRALLLDEPFSKLdaaLRAQFREF--VFEQIRQRGIPALLVTHDEEDAPAAGRVLD 205
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-227 |
3.23e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 109.41 E-value: 3.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 13 LITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIeIDGKSYHRLTPDKA---REL 89
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLI-VDGLKVNDPKVDERlirQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 90 GvqVIYQDLSLFPNLTVAENIAF-ELNLKGyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVA 168
Cdd:PRK09493 80 G--MVFQQFYLFPHLTALENVMFgPLRVRG----ASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491046221 169 DARLVIMDEPTASLT---RTEVnqlLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDG 227
Cdd:PRK09493 154 KPKLMLFDEPTSALDpelRHEV---LKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKG 212
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
13-228 |
3.69e-27 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 110.10 E-value: 3.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 13 LITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDD--GSKIEIDGKSYH---RLTPD--K 85
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsaGSHIELLGRTVQregRLARDirK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 86 ARElGVQVIYQDLSLFPNLTVAENIafelnLKGYFG----------WFRKKQlREKALEILNELAFTIDPDTPVQFLPIA 155
Cdd:PRK09984 84 SRA-NTGYIFQQFNLVNRLSVLENV-----LIGALGstpfwrtcfsWFTREQ-KQRALQALTRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491046221 156 QRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYL-KDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGH 230
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
29-231 |
7.47e-27 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 108.32 E-value: 7.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKarelgvQVIYQDLSLFPNLTVAE 108
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGG-VILEGKQITEPGPDR------MVVFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 109 NIAfeLNLKGYFGWFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLVIMDEPTASL---TRT 185
Cdd:TIGR01184 74 NIA--LAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALdalTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491046221 186 EVNQLLstVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDG--QKIG 231
Cdd:TIGR01184 152 NLQEEL--MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGpaANIG 197
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
24-228 |
8.51e-27 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 113.69 E-value: 8.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 24 GGHRA-LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDkarELGVQVIY--QDLSL 100
Cdd:COG4618 342 GSKRPiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAG-SVRLDGADLSQWDRE---ELGRHIGYlpQDVEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 101 FPNlTVAENIA-FE--------------------LNL-KGYfgwfrkkqlrekaleilnelaftidpDTPV----QFLPI 154
Cdd:COG4618 418 FDG-TIAENIArFGdadpekvvaaaklagvhemiLRLpDGY--------------------------DTRIgeggARLSG 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 155 AQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHR---LEEVkeisDRITVIRDGQ 228
Cdd:COG4618 471 GQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRpslLAAV----DKLLVLRDGR 543
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
16-435 |
9.68e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 113.24 E-value: 9.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 16 LRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGksyhrltpdkarelGVQVIY 95
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGE-VSIPK--------------GLRIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 96 --QDLSLFPNLTVAENIA-------------FELNLKGYF-------------------GWfrkkQLREKALEILNELAF 141
Cdd:COG0488 66 lpQEPPLDDDLTVLDTVLdgdaelraleaelEELEAKLAEpdedlerlaelqeefealgGW----EAEARAEEILSGLGF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 142 T-IDPDTPVQFLPIAQRQQVAICRALVADARLVIMDEPTasltrtevNQL-LSTV----NYLKDKGITVVFVSH-R--LE 212
Cdd:COG0488 142 PeEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPT--------NHLdLESIewleEFLKNYPGTVLVVSHdRyfLD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 213 EVkeiSDRITVIrDGQKIGTWP-------------------AEGLTTRKITEL--------------------------M 247
Cdd:COG0488 214 RV---ATRILEL-DRGKLTLYPgnysayleqraerleqeaaAYAKQQKKIAKEeefirrfrakarkakqaqsrikalekL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 248 TGLDIVHERKPPN---NAEDR--RTVLEIKNLSRAGQ----YRDINLNLKRGEvlglcgllgsgR-----------TELA 307
Cdd:COG0488 290 EREEPPRRDKTVEirfPPPERlgKKVLELEGLSKSYGdktlLDDLSLRIDRGD-----------RigligpngagkSTLL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 308 LSLFGITHPDSGElFIEGKPVKlknntdaikrgIGYVSEDRLTLgaILQQSIADNMvisildrlktpWHLIDEKQCQDIV 387
Cdd:COG0488 359 KLLAGELEPDSGT-VKLGETVK-----------IGYFDQHQEEL--DPDKTVLDEL-----------RDGAPGGTEQEVR 413
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 491046221 388 QeWIADLDIKVTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPT 435
Cdd:COG0488 414 G-YLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPT 460
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
7-228 |
1.17e-26 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 113.24 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 7 ADKSDPLITLRDLSKSF-----------GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVyAPDDGsKIEIDG 75
Cdd:COG4172 269 PPDAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEG-EIRFDG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 76 KSYHRLTPDKAREL--GVQVIYQD--LSLFPNLTVAENIAfElNLKGYFGWFRKKQLREKALEILNELAftIDPDT---- 147
Cdd:COG4172 347 QDLDGLSRRALRPLrrRMQVVFQDpfGSLSPRMTVGQIIA-E-GLRVHGPGLSAAERRARVAEALEEVG--LDPAArhry 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 148 PVQFlPIAQRQQVAICRALVADARLVIMDEPTASLTRT---EVNQLLSTvnyLKDK-GITVVFVSHRLEEVKEISDRITV 223
Cdd:COG4172 423 PHEF-SGGQRQRIAIARALILEPKLLVLDEPTSALDVSvqaQILDLLRD---LQREhGLAYLFISHDLAVVRALAHRVMV 498
|
....*
gi 491046221 224 IRDGQ 228
Cdd:COG4172 499 MKDGK 503
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1-231 |
1.30e-26 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 108.23 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 1 MTSTSKADKSDPLiTLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGskiEIDGKSyhr 80
Cdd:PRK11247 1 MMNTARLNQGTPL-LLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG---ELLAGT--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 81 lTP-DKARElGVQVIYQDLSLFPNLTVAENIAfeLNLKGyfGWfrkkqlREKALEILNELAFTiD--PDTPVQfLPIAQR 157
Cdd:PRK11247 74 -APlAEARE-DTRLMFQDARLLPWKKVIDNVG--LGLKG--QW------RDAALQALAAVGLA-DraNEWPAA-LSGGQK 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 158 QQVAICRALVADARLVIMDEPTA---SLTRTEVNQLLstVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQkIG 231
Cdd:PRK11247 140 QRVALARALIHRPGLLLLDEPLGaldALTRIEMQDLI--ESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK-IG 213
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-230 |
1.90e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 107.86 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFG-G----HRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDK-AR 87
Cdd:COG1101 2 LELKNLSKTFNpGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSG-SILIDGKDVTKLPEYKrAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 88 ELGvQViYQDLSL--FPNLTVAENIAFELNlKG---YFGWFRKKQLREKALEILNELAFTID--PDTPVQFLPIAQRQQV 160
Cdd:COG1101 81 YIG-RV-FQDPMMgtAPSMTIEENLALAYR-RGkrrGLRRGLTKKRRELFRELLATLGLGLEnrLDTKVGLLSGGQRQAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 161 AICRALVADARLVIMDEPTASL---TRTEVNQLlsTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKI 230
Cdd:COG1101 158 SLLMATLTKPKLLLLDEHTAALdpkTAALVLEL--TEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
14-228 |
2.35e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 109.51 E-value: 2.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHR----ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKAREL 89
Cdd:PRK11153 2 IELKNISKVFPQGGrtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSG-RVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 90 GVQV--IYQDLSLFPNLTVAENIAFELNLKGYfgwfRKKQLREKALEILNELAFTIDPDT-PVQfLPIAQRQQVAICRAL 166
Cdd:PRK11153 81 RRQIgmIFQHFNLLSSRTVFDNVALPLELAGT----PKAEIKARVTELLELVGLSDKADRyPAQ-LSGGQKQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 167 VADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK11153 156 ASNPKVLLCDEATSALdpaTTRSILELLKDIN--RELGLTIVLITHEMDVVKRICDRVAVIDAGR 218
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
14-241 |
2.37e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 107.41 E-value: 2.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPdkaRELGvqv 93
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSG-TVFLGDKPISMLSS---RQLA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 94 iyQDLSLFPN-------LTVAENIAF----ELNLKGYFGWfRKKQLREKALEI--LNELAftidpDTPVQFLPIAQRQQV 160
Cdd:PRK11231 76 --RRLALLPQhhltpegITVRELVAYgrspWLSLWGRLSA-EDNARVNQAMEQtrINHLA-----DRRLTDLSGGQRQRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 161 AICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKI--GTwPAEGL 238
Cdd:PRK11231 148 FLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMaqGT-PEEVM 226
|
...
gi 491046221 239 TTR 241
Cdd:PRK11231 227 TPG 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-492 |
5.42e-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: 111.05 E-value: 5.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGV--YAPDDGSKI---------------EIDG- 75
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpSKVGe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 76 ---KSYHRLTPDKARELG------------VQVIYQ-DLSLFPNLTVAENIAFELNLKGYFGwfrkKQLREKALEILNEL 139
Cdd:TIGR03269 81 pcpVCGGTLEPEEVDFWNlsdklrrrirkrIAIMLQrTFALYGDDTVLDNVLEALEEIGYEG----KEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 140 AFTIDPDTPVQFLPIAQRQQVAICRALVADARLVIMDEPTASL---TRTEVNQLLSTVnyLKDKGITVVFVSHRLEEVKE 216
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLdpqTAKLVHNALEEA--VKASGISMVLTSHWPEVIED 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 217 ISDRITVIRDGQKIgtwpAEGLTTRKITELMTGldiVHERKPPNNAEDRRTVLEIKNLSR------AGQYR---DINLNL 287
Cdd:TIGR03269 235 LSDKAIWLENGEIK----EEGTPDEVVAVFMEG---VSEVEKECEVEVGEPIIKVRNVSKryisvdRGVVKavdNVSLEV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 288 KRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFiegkpVKLKNN-TDAIKRGIGYVSEDRLTLGAILQQ-------SI 359
Cdd:TIGR03269 308 KEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVN-----VRVGDEwVDMTKPGPDGRGRAKRYIGILHQEydlyphrTV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 360 ADNMVISI-------LDRLKTPWHL----IDEKQCQDIVQewiadldiKVTDpnnalsTLSGGNQQKVVLAKWILTRPKV 428
Cdd:TIGR03269 383 LDNLTEAIglelpdeLARMKAVITLkmvgFDEEKAEEILD--------KYPD------ELSEGERHRVALAQVLIKEPRI 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 429 LILDSPTvgvdiGAKDSIYKLihrlsGVGISILLITDEASEAYY-----------NCDRILHMKQGSIVK-----EIVTD 492
Cdd:TIGR03269 449 VILDEPT-----GTMDPITKV-----DVTHSILKAREEMEQTFIivshdmdfvldVCDRAALMRDGKIVKigdpeEIVEE 518
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
14-247 |
9.28e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 108.25 E-value: 9.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLtpdKARELGVQV 93
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSG-HIRFHGTDVSRL---HARDRKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 94 IYQDLSLFPNLTVAENIAFELNLKGyfgwfRKKQ-----LREKALEILNELAFT-IDPDTPVQfLPIAQRQQVAICRALV 167
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFGLTVLP-----RRERpnaaaIKAKVTQLLEMVQLAhLADRYPAQ-LSGGQKQRVALARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 168 ADARLVIMDEPTASL---TRTEVNQLLSTV-NYLKdkgITVVFVSHRLEEVKEISDRITVIRDG--QKIGT----W--PA 235
Cdd:PRK10851 153 VEPQILLLDEPFGALdaqVRKELRRWLRQLhEELK---FTSVFVTHDQEEAMEVADRVVVMSQGniEQAGTpdqvWrePA 229
|
250
....*....|..
gi 491046221 236 egltTRKITELM 247
Cdd:PRK10851 230 ----TRFVLEFM 237
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-230 |
4.86e-25 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 103.07 E-value: 4.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSF-GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARELgVQ 92
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKG-QILIDGIDIRDISRKSLRSM-IG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 93 VIYQDLSLFPNlTVAENIAFELNLKgyfgwfrKKQLREKALEILNELAFTI----DPDTPV----QFLPIAQRQQVAICR 164
Cdd:cd03254 81 VVLQDTFLFSG-TIMENIRLGRPNA-------TDEEVIEAAKEAGAHDFIMklpnGYDTVLgengGNLSQGERQLLAIAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 165 ALVADARLVIMDEPTASL-TRTE--VNQLLSTVNylkdKGITVVFVSHRLEEVKEiSDRITVIRDGQKI 230
Cdd:cd03254 153 AMLRDPKILILDEATSNIdTETEklIQEALEKLM----KGRTSIIIAHRLSTIKN-ADKILVLDDGKII 216
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
14-227 |
4.94e-25 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 106.27 E-value: 4.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKArelGVQV 93
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSG-DLFIGEKRMNDVPPAER---GVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 94 IYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLR---EKALEILnELAFTID--PDTpvqfLPIAQRQQVAICRALVA 168
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKLAG----AKKEEINqrvNQVAEVL-QLAHLLDrkPKA----LSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 169 DARLVIMDEPTASL-------TRTEVNQLlstvnyLKDKGITVVFVSHRLEEVKEISDRITVIRDG 227
Cdd:PRK11000 151 EPSVFLLDEPLSNLdaalrvqMRIEISRL------HKRLGRTMIYVTHDQVEAMTLADKIVVLDAG 210
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-228 |
6.81e-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: 102.28 E-value: 6.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHR--ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARElGV 91
Cdd:cd03245 3 IEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGS-VLLDGTDIRQLDPADLRR-NI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 92 QVIYQDLSLFpNLTVAENIAFelnlkgyFGWFRKKQLREKALEILNELAFT-IDP---DTPV----QFLPIAQRQQVAIC 163
Cdd:cd03245 81 GYVPQDVTLF-YGTLRDNITL-------GAPLADDERILRAAELAGVTDFVnKHPnglDLQIgergRGLSGGQRQAVALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 164 RALVADARLVIMDEPTASLTRTEVNQLLSTV-NYLKDKgiTVVFVSHRLeEVKEISDRITVIRDGQ 228
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERLrQLLGDK--TLIIITHRP-SLLDLVDRIIVMDSGR 215
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
14-228 |
7.37e-25 |
|
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: 102.19 E-value: 7.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGgHRALRnIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDkarELGVQV 93
Cdd:cd03298 1 VRLDKIRFSYG-EQPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGR-VLINGVDVTAAPPA---DRPVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 94 IYQDLSLFPNLTVAENIAFELN--LKgyfgwfRKKQLREKALEILNELAFT-IDPDTPVQfLPIAQRQQVAICRALVADA 170
Cdd:cd03298 75 LFQENNLFAHLTVEQNVGLGLSpgLK------LTAEDRQAIEVALARVGLAgLEKRLPGE-LSGGERQRVALARVLVRDK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 171 RLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03298 148 PVLLLDEPFAALdpaLRAEMLDLVLDLH--AETKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
12-241 |
9.24e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 103.08 E-value: 9.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 12 PLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKS------YHRLTPDK 85
Cdd:PRK11701 5 PLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGE-VHYRMRDgqlrdlYALSEAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 86 AR----ELGvqVIYQDL--SLFPNLTVAENIAFELNLkgyFGWFRKKQLREKALEILNELafTIDP----DTPVQFL-PI 154
Cdd:PRK11701 84 RRllrtEWG--FVHQHPrdGLRMQVSAGGNIGERLMA---VGARHYGDIRATAGDWLERV--EIDAaridDLPTTFSgGM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 155 AQRQQVAicRALVADARLVIMDEPTASLTRTEVNQLLSTVNYL-KDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTw 233
Cdd:PRK11701 157 QQRLQIA--RNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVES- 233
|
....*...
gi 491046221 234 paeGLTTR 241
Cdd:PRK11701 234 ---GLTDQ 238
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
12-240 |
9.46e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 106.08 E-value: 9.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 12 PLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTpdkARELGV 91
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGT-VLVAGDDVEALS---ARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 92 QV--IYQDLSLFPNLTVAENIafELNLKGYFGWFRK-----KQLREKALEILNELAFTidpDTPVQFLPIAQRQQVAICR 164
Cdd:PRK09536 78 RVasVPQDTSLSFEFDVRQVV--EMGRTPHRSRFDTwtetdRAAVERAMERTGVAQFA---DRPVTSLSGGERQRVLLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 165 ALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDG--QKIGTwPAEGLTT 240
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGrvRAAGP-PADVLTA 229
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
13-228 |
1.84e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 101.58 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 13 LITLRDLSKSFGgHRALRnIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSyHRLTPDKARElgVQ 92
Cdd:PRK10771 1 MLKLTDITWLYH-HLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGS-LTLNGQD-HTTTPPSRRP--VS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 93 VIYQDLSLFPNLTVAENIAFELN----LKGYfgwfRKKQLREKA-----LEILNELaftidpdtPVQfLPIAQRQQVAIC 163
Cdd:PRK10771 75 MLFQENNLFSHLTVAQNIGLGLNpglkLNAA----QREKLHAIArqmgiEDLLARL--------PGQ-LSGGQRQRVALA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 164 RALVADARLVIMDEPTASLT---RTEVNQLLSTVnyLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK10771 142 RCLVREQPILLLDEPFSALDpalRQEMLTLVSQV--CQERQLTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-228 |
3.17e-24 |
|
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: 99.21 E-value: 3.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRA--LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDkarELGV 91
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSG-RVRLDGADISQWDPN---ELGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 92 QVIY--QDLSLFPNlTVAENIafelnLKGyfgwfrkkqlrekaleilnelaftidpdtpvqflpiAQRQQVAICRALVAD 169
Cdd:cd03246 77 HVGYlpQDDELFSG-SIAENI-----LSG------------------------------------GQRQRLGLARALYGN 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 170 ARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLeEVKEISDRITVIRDGQ 228
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGR 172
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
24-228 |
4.29e-24 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 105.51 E-value: 4.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 24 GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKareLGVQVIY--QDLSLF 101
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGS-VRLDGADLKQWDRET---FGKHIGYlpQDVELF 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 102 PNlTVAENIA-FELNlkgyfgwFRKKQLREKA-LEILNEL--AFTIDPDTPV----QFLPIAQRQQVAICRALVADARLV 173
Cdd:TIGR01842 405 PG-TVAENIArFGEN-------ADPEKIIEAAkLAGVHELilRLPDGYDTVIgpggATLSGGQRQRIALARALYGDPKLV 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 174 IMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLeEVKEISDRITVIRDGQ 228
Cdd:TIGR01842 477 VLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRP-SLLGCVDKILVLQDGR 530
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
16-247 |
4.66e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 103.26 E-value: 4.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 16 LRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSyhrLTPDKARELGVQVIY 95
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEG-QIFIDGED---VTHRSIQQRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 96 QDLSLFPNLTVAENIAFELNLKGYFGWFRKKQLREkALEILNELAFTidpDTPVQFLPIAQRQQVAICRALVADARLVIM 175
Cdd:PRK11432 85 QSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKE-ALELVDLAGFE---DRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 176 DEPTASLTRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITELM 247
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFM 233
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
12-228 |
7.09e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 100.10 E-value: 7.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 12 PLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDK-AReLG 90
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSG-RIFLDGEDITHLPMHKrAR-LG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 91 VQVIYQDLSLFPNLTVAENIAFELNLKGYfgwfRKKQLREKALEILNElaFTIDP--DTPVQFLPIAQRQQVAICRALVA 168
Cdd:COG1137 80 IGYLPQEASIFRKLTVEDNILAVLELRKL----SKKEREERLEELLEE--FGITHlrKSKAYSLSGGERRRVEIARALAT 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 169 DARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:COG1137 154 NPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGK 213
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-228 |
7.87e-24 |
|
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: 100.00 E-value: 7.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHR--ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELgV 91
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGR-ILIDGHDVRDYTLASLRRQ-I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 92 QVIYQDLSLFpNLTVAENIAFelnlkGYFGWFRKKQlrEKALEILNELAFTID-P---DTPVQ----FLPIAQRQQVAIC 163
Cdd:cd03251 79 GLVSQDVFLF-NDTVAENIAY-----GRPGATREEV--EEAARAANAHEFIMElPegyDTVIGergvKLSGGQRQRIAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 164 RALVADARLVIMDEPTASL-TRTE--VNQLLStvNYLKDKgiTVVFVSHRLEEVKEiSDRITVIRDGQ 228
Cdd:cd03251 151 RALLKDPPILILDEATSALdTESErlVQAALE--RLMKNR--TTFVIAHRLSTIEN-ADRIVVLEDGK 213
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
11-211 |
7.96e-24 |
|
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: 104.75 E-value: 7.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 11 DPLITLRDLSKSF-GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKAREL 89
Cdd:TIGR02868 332 KPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGE-VTLDGVPVSSLDQDEVRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 90 gVQVIYQDLSLFpNLTVAENIAFElnlkgyfgwfRKKQLREKALEILNELAFTIDP-------DTPV----QFLPIAQRQ 158
Cdd:TIGR02868 411 -VSVCAQDAHLF-DTTVRENLRLA----------RPDATDEELWAALERVGLADWLralpdglDTVLgeggARLSGGERQ 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491046221 159 QVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYlKDKGITVVFVSHRL 211
Cdd:TIGR02868 479 RLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
12-241 |
1.01e-23 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 101.91 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 12 PLITLRDLSKSF----GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVyaPDDGSKIEID-----GKSYHRLT 82
Cdd:COG4170 2 PLLDIRNLTIEIdtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI--TKDNWHVTADrfrwnGIDLLKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 83 PDKAREL---GVQVIYQD--LSLFPNLTVAENIAFEL---NLKGYFgWFRKKQLREKALEILNELAFTIDPDT----PVQ 150
Cdd:COG4170 80 PRERRKIigrEIAMIFQEpsSCLDPSAKIGDQLIEAIpswTFKGKW-WQRFKWRKKRAIELLHRVGIKDHKDImnsyPHE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 151 fLPIAQRQQVAICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDG 227
Cdd:COG4170 159 -LTEGECQKVMIAMAIANQPRLLIADEPTNAMestTQAQIFRLLARLN--QLQGTSILLISHDLESISQWADTITVLYCG 235
|
250
....*....|....
gi 491046221 228 QKIGTWPAEGLTTR 241
Cdd:COG4170 236 QTVESGPTEQILKS 249
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
33-228 |
1.43e-23 |
|
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: 98.39 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 33 DLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPdkaRELGVQVIYQDLSLFPNLTVAENIAF 112
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGS-IKVNDQSHTGLAP---YQRPVSMLFQENNLFAHLTVRQNIGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 113 ELNLKGYFGWFRKKQLREKALE--ILNELAftidpDTPVQfLPIAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQL 190
Cdd:TIGR01277 94 GLHPGLKLNAEQQEKVVDAAQQvgIADYLD-----RLPEQ-LSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEM 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 491046221 191 LSTVNYLKD-KGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:TIGR01277 168 LALVKQLCSeRQRTLLMVTHHLSDARAIASQIAVVSQGK 206
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
14-228 |
1.78e-23 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 104.18 E-value: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGG--HRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARElGV 91
Cdd:TIGR03375 464 IEFRNVSFAYPGqeTPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGS-VLLDGVDIRQIDPADLRR-NI 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 92 QVIYQDLSLFpNLTVAENIAFELNLkgyfgwFRKKQLREkALEILNELAFT-IDP---DTPV----QFLPIAQRQQVAIC 163
Cdd:TIGR03375 542 GYVPQDPRLF-YGTLRDNIALGAPY------ADDEEILR-AAELAGVTEFVrRHPdglDMQIgergRSLSGGQRQAVALA 613
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 164 RALVADARLVIMDEPTASL-TRTEvNQLLSTVN-YLKDKgiTVVFVSHRLeEVKEISDRITVIRDGQ 228
Cdd:TIGR03375 614 RALLRDPPILLLDEPTSAMdNRSE-ERFKDRLKrWLAGK--TLVLVTHRT-SLLDLVDRIIVMDNGR 676
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
11-236 |
1.85e-23 |
|
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: 103.34 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 11 DPLITLRDLSKSF-----GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIEIDGKSYHRLTPDK 85
Cdd:TIGR03269 277 EPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 86 ARELG-----VQVIYQDLSLFPNLTVAENIAFELNLKGYFGWFRKKQL---------REKALEILNELaftidPDTpvqf 151
Cdd:TIGR03269 357 PDGRGrakryIGILHQEYDLYPHRTVLDNLTEAIGLELPDELARMKAVitlkmvgfdEEKAEEILDKY-----PDE---- 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 152 LPIAQRQQVAICRALVADARLVIMDEPTASL---TRTEVNQllSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMdpiTKVDVTH--SILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGK 505
|
....*...
gi 491046221 229 KIGTWPAE 236
Cdd:TIGR03269 506 IVKIGDPE 513
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
10-253 |
2.08e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 100.26 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 10 SDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSyhrlTPDKARE- 88
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGS-ISLCGEP----VPSRARHa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 89 -LGVQVIYQDLSLFPNLTVAENIafeLNLKGYFGwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALV 167
Cdd:PRK13537 79 rQRVGVVPQFDNLDPDFTVRENL---LVFGRYFG-LSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 168 ADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIgtwpAEGlTTRKITELM 247
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKI----AEG-APHALIESE 229
|
....*.
gi 491046221 248 TGLDIV 253
Cdd:PRK13537 230 IGCDVI 235
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
269-486 |
2.80e-23 |
|
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: 97.74 E-value: 2.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLSRA-GQY---RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVklknnTDAIKRGIGYV 344
Cdd:cd03269 1 LEVENVTKRfGRVtalDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-----DIAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 345 SEDRltlGAILQQSIADNMVisILDRLKTpwhlIDEKQCQDIVQEWIADLDIKvTDPNNALSTLSGGNQQKVVLAKWILT 424
Cdd:cd03269 76 PEER---GLYPKMKVIDQLV--YLAQLKG----LKKEEARRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491046221 425 RPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:cd03269 146 DPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
10-222 |
5.55e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 97.09 E-value: 5.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 10 SDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKAREl 89
Cdd:PRK10247 4 NSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSG-TLLFEGEDISTLKPEIYRQ- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 90 gvQVIY--QDLSLFPNlTVAENIAFELNLkgyfgwfRKKQLREKALeiLNELAFTIDPDT----PVQFLPIAQRQQVAIC 163
Cdd:PRK10247 82 --QVSYcaQTPTLFGD-TVYDNLIFPWQI-------RNQQPDPAIF--LDDLERFALPDTiltkNIAELSGGEKQRISLI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491046221 164 RALVADARLVIMDEPTASL---TRTEVNQLLStvNYLKDKGITVVFVSHRLEEVKEISDRIT 222
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALdesNKHNVNEIIH--RYVREQNIAVLWVTHDKDEINHADKVIT 209
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
10-247 |
6.46e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 98.14 E-value: 6.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 10 SDPLITLRDLSKSFGGHR--ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKAR 87
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSG-EIKIDGITISKENLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 88 ElGVQVIYQDL-SLFPNLTVAENIAFELNlkgyfgwfRKKQLREKALEILNELAFTIDP----DTPVQFLPIAQRQQVAI 162
Cdd:PRK13632 83 K-KIGIIFQNPdNQFIGATVEDDIAFGLE--------NKKVPPKKMKDIIDDLAKKVGMedylDKEPQNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 163 CRALVADARLVIMDEPTASLT---RTEVNQLLSTVNYLKDKgiTVVFVSHRLEEVKeISDRITVIRDGQ--KIGTwPAEG 237
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDpkgKREIKKIMVDLRKTRKK--TLISITHDMDEAI-LADKVIVFSEGKliAQGK-PKEI 229
|
250
....*....|
gi 491046221 238 LTTRKITELM 247
Cdd:PRK13632 230 LNNKEILEKA 239
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-228 |
8.08e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 101.71 E-value: 8.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 7 ADKSDPLITLRDLSKSF-----------GGHRALRNIDLTLNKGEVHCLAGTNGCGKST----LIKTIsgvyaPDDGSkI 71
Cdd:PRK15134 269 PEPASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGE-I 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 72 EIDGKSYHRLT-----PDKARelgVQVIYQD--LSLFPNLTVAENIAFELNLkgYFGWFRKKQLREKALEILNELAftID 144
Cdd:PRK15134 343 WFDGQPLHNLNrrqllPVRHR---IQVVFQDpnSSLNPRLNVLQIIEEGLRV--HQPTLSAAQREQQVIAVMEEVG--LD 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 145 PDT----PVQFlPIAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEISD 219
Cdd:PRK15134 416 PETrhryPAEF-SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCH 494
|
....*....
gi 491046221 220 RITVIRDGQ 228
Cdd:PRK15134 495 QVIVLRQGE 503
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
267-485 |
1.01e-22 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 97.08 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 267 TVLEIKNLSRAgqY------RDINLNLKRGEVlglcgllgsgrteLAL---------SLF----GITHPDSGELFIEGKP 327
Cdd:COG1121 5 PAIELENLTVS--YggrpvlEDVSLTIPPGEF-------------VAIvgpngagksTLLkailGLLPPTSGTVRLFGKP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 328 VKLKnntdaiKRGIGYVSedrltlgailQQSIAD-NMVISILD------RLKTPWHLIDEKQCQDIVQEWIADLDIkvTD 400
Cdd:COG1121 70 PRRA------RRRIGYVP----------QRAEVDwDFPITVRDvvlmgrYGRRGLFRRPSRADREAVDEALERVGL--ED 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 401 -PNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILH 479
Cdd:COG1121 132 lADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLL 211
|
....*.
gi 491046221 480 MKQGSI 485
Cdd:COG1121 212 LNRGLV 217
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-237 |
1.20e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 98.75 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 9 KSDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSyhrlTPDKAR- 87
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAG-KITVLGVP----VPARARl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 88 -ELGVQVIYQDLSLFPNLTVAENIafeLNLKGYFGWFRKKQlrEKALEILNELA-FTIDPDTPVQFLPIAQRQQVAICRA 165
Cdd:PRK13536 112 aRARIGVVPQFDNLDLEFTVRENL---LVFGRYFGMSTREI--EAVIPSLLEFArLESKADARVSDLSGGMKRRLTLARA 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491046221 166 LVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIgtwpAEG 237
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKI----AEG 254
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-224 |
1.27e-22 |
|
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: 100.82 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 3 STSKADKSDPLITLRDLSKSFGGHR-ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRL 81
Cdd:TIGR02857 311 KAPVTAAPASSLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGS-IAVNGVPLADA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 82 TPDKARElgvQVIY--QDLSLFPNlTVAENIAF--------ELnlkgyfgwfRKKQLREKALEILNELAFTIDpdTPV-- 149
Cdd:TIGR02857 390 DADSWRD---QIAWvpQHPFLFAG-TIAENIRLarpdasdaEI---------REALERAGLDEFVAALPQGLD--TPIge 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 150 --QFLPIAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKdKGITVVFVSHRLeEVKEISDRITVI 224
Cdd:TIGR02857 455 ggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRL-ALAALADRIVVL 529
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
13-232 |
1.51e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 97.07 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 13 LITLRDLSKSF-GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGK--SYHRLTPDKAREl 89
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSG-EVLIKGEpiKYDKKSLLEVRK- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 90 GVQVIYQ--DLSLFPNlTVAENIAF-ELNLKgyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRAL 166
Cdd:PRK13639 79 TVGIVFQnpDDQLFAP-TVEEDVAFgPLNLG-----LSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 167 VADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGT 232
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKE 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
12-228 |
2.33e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 95.65 E-value: 2.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 12 PLITLRDLSKSFGGHR----ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIeIDGKSYHRLTP-DKA 86
Cdd:PRK11629 4 ILLQCDNLCKRYQEGSvqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVI-FNGQPMSKLSSaAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 87 ----RELGVqvIYQDLSLFPNLTVAENIAFELnlkgYFGWFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAI 162
Cdd:PRK11629 83 elrnQKLGF--IYQFHHLLPDFTALENVAMPL----LIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 163 CRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISdRITVIRDGQ 228
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLdarNADSIFQLLGELN--RLQGTAFLVVTHDLQLAKRMS-RQLEMRDGR 222
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
13-249 |
2.45e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 95.73 E-value: 2.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 13 LITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVyAPDDGSKIEIDGKSYhRLTPDKAREL-GV 91
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGI-VPRDAGNIIIDDEDI-SLLPLHARARrGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 92 QVIYQDLSLFPNLTVAENIAFELNLKGYFgwfRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADAR 171
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDDL---SAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 172 LVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKI--GTwPAEGLTTRKITELMTG 249
Cdd:PRK10895 158 FILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIahGT-PTEILQDEHVKRVYLG 236
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
14-228 |
3.15e-22 |
|
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: 93.53 E-value: 3.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHR--ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLtpDKARELGV 91
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGE-ITLDGVPVSDL--EKALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 92 QVIYQDLSLFpNLTVAENIAfeLNLKGyfgwfrkkqlrekaleilnelaftidpdtpvqflpiAQRQQVAICRALVADAR 171
Cdd:cd03247 78 SVLNQRPYLF-DTTLRNNLG--RRFSG------------------------------------GERQRLALARILLQDAP 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 172 LVIMDEPTASLTRTEVNQLLSTV-NYLKDKgiTVVFVSHRLEEVKEIsDRITVIRDGQ 228
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIfEVLKDK--TLIWITHHLTGIEHM-DKILFLENGK 173
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
14-232 |
4.07e-22 |
|
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: 94.91 E-value: 4.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSF---GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELg 90
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGE-ILLDGVDIRDLNLRWLRSQ- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 91 VQVIYQDLSLFPNlTVAENIAFELNlkgyfgwFRKKQLREKALEILNELAFTID-P---DTPVQF----LPIAQRQQVAI 162
Cdd:cd03249 79 IGLVSQEPVLFDG-TIAENIRYGKP-------DATDEEVEEAAKKANIHDFIMSlPdgyDTLVGErgsqLSGGQKQRIAI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 163 CRALVADARLVIMDEPTASL-TRTE--VNQLLSTVNylkdKGITVVFVSHRLEEVKEiSDRITVIRDGQKI--GT 232
Cdd:cd03249 151 ARALLRNPKILLLDEATSALdAESEklVQEALDRAM----KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVeqGT 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
269-485 |
4.60e-22 |
|
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: 92.85 E-value: 4.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLS-RAGQY---RDINLNLKRGEVlglcgllgsgrteLAL-------------SLFGITHPDSGELFIEGKPVKlk 331
Cdd:cd03230 1 IEVRNLSkRYGKKtalDDISLTVEKGEI-------------YGLlgpngagkttlikIILGLLKPDSGEIKVLGKDIK-- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 332 NNTDAIKRGIGYVSEDrltlgailqqsiadnmvISILDRLkTPWHLIDekqcqdivqewiadldikvtdpnnalstLSGG 411
Cdd:cd03230 66 KEPEEVKRRIGYLPEE-----------------PSLYENL-TVRENLK----------------------------LSGG 99
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491046221 412 NQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSI 485
Cdd:cd03230 100 MKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-222 |
5.63e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.45 E-value: 5.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 22 SFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKieidgksyhrltpdkARELGVQVIY--QDLS 99
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV---------------RRAGGARVAYvpQRSE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 100 L---FPnLTVAEniAFELNLKGYFGWFRK-----KQLREKALEI--LNELAftidpDTPVQFLPIAQRQQVAICRALVAD 169
Cdd:NF040873 66 VpdsLP-LTVRD--LVAMGRWARRGLWRRltrddRAAVDDALERvgLADLA-----GRQLGELSGGQRQRALLAQGLAQE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491046221 170 ARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRIT 222
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVL 190
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
14-228 |
6.46e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 94.76 E-value: 6.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSF----------------------GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkI 71
Cdd:COG1134 5 IEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR-V 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 72 EIDGksyhRLTPdkarELGVQVIYQdlslfPNLTVAENIAFELNLKGyfgwFRKKQLREKALEIlneLAFT-IDP--DTP 148
Cdd:COG1134 84 EVNG----RVSA----LLELGAGFH-----PELTGRENIYLNGRLLG----LSRKEIDEKFDEI---VEFAeLGDfiDQP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 149 VQFLPIAQRQQVAICRALVADARLVIMDEPTA---------SLTRtevnqllstVNYLKDKGITVVFVSHRLEEVKEISD 219
Cdd:COG1134 144 VKTYSSGMRARLAFAVATAVDPDILLVDEVLAvgdaafqkkCLAR---------IRELRESGRTVIFVSHSMGAVRRLCD 214
|
....*....
gi 491046221 220 RITVIRDGQ 228
Cdd:COG1134 215 RAIWLEKGR 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
18-227 |
2.97e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 93.11 E-value: 2.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 18 DLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKsYHRLTPDKARELGV------ 91
Cdd:PRK10619 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGS-IVVNGQ-TINLVRDKDGQLKVadknql 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 92 -------QVIYQDLSLFPNLTVAENI-AFELNLKGyfgwFRKKQLREKALEILNELAftIDPDTPVQF---LPIAQRQQV 160
Cdd:PRK10619 88 rllrtrlTMVFQHFNLWSHMTVLENVmEAPIQVLG----LSKQEARERAVKYLAKVG--IDERAQGKYpvhLSGGQQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 161 AICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDG 227
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQG 228
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-246 |
5.35e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 92.28 E-value: 5.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIE----IDGKSYHRLTPDKAREL 89
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSgevyLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 90 gVQVIYQDLSLFPNLTVAENIAFELNLKGYFGwfRKKQLREKALEILnELAFTIDP-----DTPVQFLPIAQRQQVAICR 164
Cdd:PRK14247 84 -VQMVFQIPNPIPNLSIFENVALGLKLNRLVK--SKKELQERVRWAL-EKAQLWDEvkdrlDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 165 ALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKdKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKIT 244
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELK-KDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRH 238
|
..
gi 491046221 245 EL 246
Cdd:PRK14247 239 EL 240
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
15-228 |
6.67e-21 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 90.78 E-value: 6.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 15 TLRDLSKSFG-GHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRltpdKARELGVQV 93
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSG-SILLNGKPIKA----KERRKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 94 IYQDLS--LFPNlTVAENIAfeLNLKGYfgwfrkkqlrEKALEILNELAFTIDPDTPVQFLPIA----QRQQVAICRALV 167
Cdd:cd03226 76 VMQDVDyqLFTD-SVREELL--LGLKEL----------DAGNEQAETVLKDLDLYALKERHPLSlsggQKQRLAIAAALL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 168 ADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03226 143 SGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGA 203
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
10-230 |
7.00e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 91.76 E-value: 7.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 10 SDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTIS--GVYAPDDGSKIEIDGKSYHRLTP---- 83
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEVTITGSIVYNGHNIYSPrtdt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 84 -DKARELGvqVIYQDLSLFPnLTVAENIAFELNLKGyfgwFRKKQLREKALE-------ILNELAFTIDpDTPVQfLPIA 155
Cdd:PRK14239 82 vDLRKEIG--MVFQQPNPFP-MSIYENVVYGLRLKG----IKDKQVLDEAVEkslkgasIWDEVKDRLH-DSALG-LSGG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 156 QRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKgITVVFVSHRLEEVKEISDRITVIRDGQKI 230
Cdd:PRK14239 153 QQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
270-483 |
8.12e-21 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 90.67 E-value: 8.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 270 EIKNLS-RAGQY---RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNntdaikRGIGYVS 345
Cdd:cd03235 1 EVEDLTvSYGGHpvlEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER------KRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 346 edrltlgailQQSIAD-NMVISILD------RLKTPWHLIDEKQCQDIVQEWIADLDIkvTD-PNNALSTLSGGNQQKVV 417
Cdd:cd03235 75 ----------QRRSIDrDFPISVRDvvlmglYGHKGLFRRLSKADKAKVDEALERVGL--SElADRQIGELSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 418 LAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQG 483
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-459 |
9.10e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 95.16 E-value: 9.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 10 SDPLITLRDLSKSF--GGH--RALRNIDLTLNKGEVHCLAGTNGCGKST-------LIKTISGVYAPDDgskIEIDGKSY 78
Cdd:PRK15134 2 TQPLLAIENLSVAFrqQQTvrTVVNDVSLQIEAGETLALVGESGSGKSVtalsilrLLPSPPVVYPSGD---IRFHGESL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 79 hrLTPDKARELGVQ-----VIYQD--LSLFPNLTVAENIAFELNL-KGyfgwFRKKQLREKALEILNEL----AFTIDPD 146
Cdd:PRK15134 79 --LHASEQTLRGVRgnkiaMIFQEpmVSLNPLHTLEKQLYEVLSLhRG----MRREAARGEILNCLDRVgirqAAKRLTD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 147 TPVQfLPIAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEISDRITVIR 225
Cdd:PRK15134 153 YPHQ-LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 226 DGQKIGTWPAEGL-------TTRKItelmtgLDIVHERKPPNNAEDRRTVLEIKNLS-----RAGQYR----------DI 283
Cdd:PRK15134 232 NGRCVEQNRAATLfsapthpYTQKL------LNSEPSGDPVPLPEPASPLLDVEQLQvafpiRKGILKrtvdhnvvvkNI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 284 NLNLKRGEVLGLCGLLGSGRTELALSLFGIThPDSGELFIEGKPVKLKNNTD--AIKRGIGYVSED-------RLTlgai 354
Cdd:PRK15134 306 SFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQllPVRHRIQVVFQDpnsslnpRLN---- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 355 LQQSIADNM-----VISILDRlktpwhlidEKQCQDIVQEWIADLDIKVTDPnnalSTLSGGNQQKVVLAKWILTRPKVL 429
Cdd:PRK15134 381 VLQIIEEGLrvhqpTLSAAQR---------EQQVIAVMEEVGLDPETRHRYP----AEFSGGQRQRIAIARALILKPSLI 447
|
490 500 510
....*....|....*....|....*....|....*.
gi 491046221 430 ILDSPTVGVDIGAKDSIYKLI------HRLSGVGIS 459
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLkslqqkHQLAYLFIS 483
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
28-252 |
1.04e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 92.00 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 28 ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSyhrLTPDKARELGVQV--IYQDL-SLFPNL 104
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGT-ITVGGMV---LSEETVWDVRRQVgmVFQNPdNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 105 TVAENIAFELNLKGyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLVIMDEPTASLT- 183
Cdd:PRK13635 98 TVQDDVAFGLENIG----VPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDp 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 184 --RTEVnqlLSTVNYLKD-KGITVVFVSHRLEEVKEiSDRITVIRDGQKIgtwpAEGlTTRKITELMT-----GLDI 252
Cdd:PRK13635 174 rgRREV---LETVRQLKEqKGITVLSITHDLDEAAQ-ADRVIVMNKGEIL----EEG-TPEEIFKSGHmlqeiGLDV 241
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
26-228 |
1.30e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 91.76 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 26 HRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKA-----RELGVQVIYQDLSL 100
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGT-VTVDDITITHKTKDKYirpvrKRIGMVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 101 FPNlTVAENIA-----FELNLkgyfgwfrkKQLREKALEILNELAFTID--PDTPVQfLPIAQRQQVAICRALVADARLV 173
Cdd:PRK13646 99 FED-TVEREIIfgpknFKMNL---------DEVKNYAHRLLMDLGFSRDvmSQSPFQ-MSGGQMRKIAIVSILAMNPDII 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 174 IMDEPTASLTRTEVNQLLSTVNYLK-DKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK13646 168 VLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGS 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
11-230 |
1.45e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 91.83 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 11 DPLITLRDLSKSFG-GHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGK--SYHRLTPDKAR 87
Cdd:PRK13636 3 DYILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSG-RILFDGKpiDYSRKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 88 ElGVQVIYQ--DLSLFpNLTVAENIAF-ELNLKgyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICR 164
Cdd:PRK13636 82 E-SVGMVFQdpDNQLF-SASVYQDVSFgAVNLK-----LPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 165 ALVADARLVIMDEPTASLTRTEVNQLLS-TVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKI 230
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKlLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-228 |
2.28e-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: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 11 DPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIdGKsyhrltpdkarelG 90
Cdd:COG0488 313 KKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSG-TVKL-GE-------------T 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 91 VQVIY--QDLSLF-PNLTVAENI------AFELNLKGYFGWFRkkqlrekaleilnelaFT-IDPDTPVQFLPIAQRQQV 160
Cdd:COG0488 378 VKIGYfdQHQEELdPDKTVLDELrdgapgGTEQEVRGYLGRFL----------------FSgDDAFKPVGVLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 161 AICRALVADARLVIMDEPTASL---TRTEVNQLLStvNYlkdKGiTVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLdieTLEALEEALD--DF---PG-TVLLVSHDRYFLDRVATRILEFEDGG 506
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-228 |
2.43e-20 |
|
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: 89.98 E-value: 2.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHR-ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARElGVQ 92
Cdd:cd03253 1 IEFENVTFAYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGS-ILIDGQDIREVTLDSLRR-AIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 93 VIYQDLSLFpNLTVAENIAFElNLKGyfgwfRKKQLRE--KALEILNE-LAFTIDPDTPVQ----FLPIAQRQQVAICRA 165
Cdd:cd03253 79 VVPQDTVLF-NDTIGYNIRYG-RPDA-----TDEEVIEaaKAAQIHDKiMRFPDGYDTIVGerglKLSGGEKQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491046221 166 LVADARLVIMDEPTASL-TRTEvNQLLSTVNYLKdKGITVVFVSHRLEEVKEiSDRITVIRDGQ 228
Cdd:cd03253 152 ILKNPPILLLDEATSALdTHTE-REIQAALRDVS-KGRTTIVIAHRLSTIVN-ADKIIVLKDGR 212
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
14-230 |
3.23e-20 |
|
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: 89.70 E-value: 3.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHR---------------------ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIE 72
Cdd:cd03267 1 IEVSNLSKSYRVYSkepgligslkslfkrkyreveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGE-VR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 73 IDGKSYHRLTPDKARELGVqVIYQDLSLFPNLTVAEniAFELNLKGY-FGWFRKKQLREKALEILNELAFTidpDTPVQF 151
Cdd:cd03267 80 VAGLVPWKRRKKFLRRIGV-VFGQKTQLWWDLPVID--SFYLLAAIYdLPPARFKKRLDELSELLDLEELL---DTPVRQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 152 LPIAQRQQVAICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03267 154 LSLGQRMRAEIAAALLHEPEILFLDEPTIGLdvvAQENIRNFLKEYN--RERGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
..
gi 491046221 229 KI 230
Cdd:cd03267 232 LL 233
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
12-228 |
5.02e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 89.17 E-value: 5.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 12 PLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGV 91
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGR-IVFDGKDITDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 92 QVIYQDLSLFPNLTVAENIAFElnlkgyfGWFRKKQLREKALEILNELaftidpdTPVQFLPIAQR---------QQVAI 162
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMG-------GFFAERDQFQERIKWVYEL-------FPRLHERRIQRagtmsggeqQMLAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 163 CRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGH 214
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
27-224 |
5.05e-20 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 90.92 E-value: 5.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 27 RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKAREL--GVQVIYQD--LSLFP 102
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGE-VAWLGKDLLGMKDDEWRAVrsDIQMIFQDplASLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 103 NLTVAENIAFElnLKGYFGWFRKKQLREKALEILnelaftidpdTPVQFLP--I---------AQRQQVAICRALVADAR 171
Cdd:PRK15079 114 RMTIGEIIAEP--LRTYHPKLSRQEVKDRVKAMM----------LKVGLLPnlInryphefsgGQCQRIGIARALILEPK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 172 LVIMDEPTASLtrtEVNQLLSTVNYLKD----KGITVVFVSHRLEEVKEISDRITVI 224
Cdd:PRK15079 182 LIICDEPVSAL---DVSIQAQVVNLLQQlqreMGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
12-245 |
5.34e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 89.45 E-value: 5.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 12 PLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDK-ARELG 90
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSG-EVRLNGRPLADWSPAElARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 91 vqVIYQDLSL-FPnLTVAENIAFELnLKGYFGWFRKKQLREKALEI--LNELAftidpDTPVQFLPIAQRQQVAICRALV 167
Cdd:PRK13548 80 --VLPQHSSLsFP-FTVEEVVAMGR-APHGLSRAEDDALVAAALAQvdLAHLA-----GRDYPQLSGGEQQRVQLARVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 168 ------ADARLVIMDEPTASLTRTEVNQLLSTV-NYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKI--GTwPAEGL 238
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDLAHQHHVLRLArQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVadGT-PAEVL 229
|
....*..
gi 491046221 239 TTRKITE 245
Cdd:PRK13548 230 TPETLRR 236
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
14-236 |
6.34e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 91.06 E-value: 6.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSF-GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPdkaRELGVQ 92
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGE-IWIGGRVVNELEP---ADRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 93 VIYQDLSLFPNLTVAENIAFELNLKGyfgwFRKKQLR---EKALEILnELAftidpdtpvQFL---PIA----QRQQVAI 162
Cdd:PRK11650 80 MVFQNYALYPHMSVRENMAYGLKIRG----MPKAEIEervAEAARIL-ELE---------PLLdrkPRElsggQRQRVAM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 163 CRALVADARLVIMDEPTASL-------TRTEVNQL---LSTvnylkdkgiTVVFVSHRLEEVKEISDRITVIRDGQ--KI 230
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLdaklrvqMRLEIQRLhrrLKT---------TSLYVTHDQVEAMTLADRVVVMNGGVaeQI 216
|
....*.
gi 491046221 231 GTwPAE 236
Cdd:PRK11650 217 GT-PVE 221
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
268-486 |
1.09e-19 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 87.95 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 268 VLEIKNLS-----RAGQYR---DINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTDAIKR 339
Cdd:cd03257 1 LLEVKNLSvsfptGGGSVKaldDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 340 G--IGYVSED-------RLTLGailqQSIADNMVIsildrlktpwHLIDEKQCQDivQEWIADLDIKVTDPNNAL----S 406
Cdd:cd03257 81 RkeIQMVFQDpmsslnpRMTIG----EQIAEPLRI----------HGKLSKKEAR--KEAVLLLLVGVGLPEEVLnrypH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 407 TLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEASEAYYNCDRILHMKQGSI 485
Cdd:cd03257 145 ELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
.
gi 491046221 486 V 486
Cdd:cd03257 225 V 225
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
14-228 |
1.17e-19 |
|
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: 87.59 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSF----------------------GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKI 71
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSG-TV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 72 EIDGKSYHRLtpdkarELGVqviyqdlSLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEIL--NELAFTIdpDTPV 149
Cdd:cd03220 80 TVRGRVSSLL------GLGG-------GFNPELTGRENIYLNGRLLG----LSRKEIDEKIDEIIefSELGDFI--DLPV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 150 QFLPIAQRQQVAICRALVADARLVIMDEPTA---SLTRTEVNQLLSTvnyLKDKGITVVFVSHRLEEVKEISDRITVIRD 226
Cdd:cd03220 141 KTYSSGMKARLAFAIATALEPDILLIDEVLAvgdAAFQEKCQRRLRE---LLKQGKTVILVSHDPSSIKRLCDRALVLEK 217
|
..
gi 491046221 227 GQ 228
Cdd:cd03220 218 GK 219
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
28-228 |
1.42e-19 |
|
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: 87.93 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 28 ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGksYHRLTPDKA---RELGvqVIYQDLSLFpNL 104
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENG-RVLVDG--HDLALADPAwlrRQVG--VVLQENVLF-NR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 105 TVAENIAFE------------LNLKGYFGWFRkkQLREKALEILNELAFTidpdtpvqfLPIAQRQQVAICRALVADARL 172
Cdd:cd03252 91 SIRDNIALAdpgmsmervieaAKLAGAHDFIS--ELPEGYDTIVGEQGAG---------LSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 173 VIMDEPTASLTRTEVNQLLSTVNYLKDkGITVVFVSHRLEEVKEiSDRITVIRDGQ 228
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGR 213
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
28-232 |
1.43e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 90.86 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 28 ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKAREL---GVQVIYQDLSLFPNL 104
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRG-QVLIDGVDIAKISDAELREVrrkKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 105 TVAENIAFELNLKGyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLVIMDEPTASL-- 182
Cdd:PRK10070 122 TVLDNTAFGMELAG----INAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALdp 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491046221 183 -TRTEVNQLLSTVNYLKDKgiTVVFVSHRLEEVKEISDRITVIRDGQ--KIGT 232
Cdd:PRK10070 198 lIRTEMQDELVKLQAKHQR--TIVFISHDLDEAMRIGDRIAIMQNGEvvQVGT 248
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
12-228 |
1.43e-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: 87.49 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 12 PLITLRDLSKSF-----GGHR--ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGS--------KIEIDGK 76
Cdd:COG4778 3 TLLEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilvrhdggWVDLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 77 SYHRLTPDKARELGvqviY--QDLSLFPNLT----VAENiAFELNlkgyfgwFRKKQLREKALEILNELA-----FTIDP 145
Cdd:COG4778 83 SPREILALRRRTIG----YvsQFLRVIPRVSaldvVAEP-LLERG-------VDREEARARARELLARLNlperlWDLPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 146 DTpvqFlPIAQRQQVAICRALVADARLVIMDEPTASL---TRTEVNQLLSTvnyLKDKGITVVFVSHRLEEVKEISDRIT 222
Cdd:COG4778 151 AT---F-SGGEQQRVNIARGFIADPPLLLLDEPTASLdaaNRAVVVELIEE---AKARGTAIIGIFHDEEVREAVADRVV 223
|
....*.
gi 491046221 223 VIRDGQ 228
Cdd:COG4778 224 DVTPFS 229
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-228 |
1.58e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 92.09 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 13 LITLRDLSKSFGGH---RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPD------DGSKI-EIDGKSYHRlt 82
Cdd:TIGR00958 478 LIEFQDVSFSYPNRpdvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTggqvllDGVPLvQYDHHYLHR-- 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 83 pdkarelGVQVIYQDLSLFpNLTVAENIAFELNLKgyfgwfRKKQLREKALE------ILNelaFTIDPDTPV----QFL 152
Cdd:TIGR00958 556 -------QVALVGQEPVLF-SGSVRENIAYGLTDT------PDEEIMAAAKAanahdfIME---FPNGYDTEVgekgSQL 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 153 PIAQRQQVAICRALVADARLVIMDEPTASLTrTEVNQLLSTVNYLKDKgiTVVFVSHRLEEVkEISDRITVIRDGQ 228
Cdd:TIGR00958 619 SGGQKQRIAIARALVRKPRVLILDEATSALD-AECEQLLQESRSRASR--TVLLIAHRLSTV-ERADQILVLKKGS 690
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
12-240 |
2.60e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 87.82 E-value: 2.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 12 PLITLRDLSKSFGGH---------RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLT 82
Cdd:PRK10419 2 TLLNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQG-NVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 83 PDKAREL--GVQVIYQD-LSLF-PNLTVAENIAFEL----NLKgyfgwfrKKQLREKALEILN--ELAFTIDPDTPVQfL 152
Cdd:PRK10419 81 RAQRKAFrrDIQMVFQDsISAVnPRKTVREIIREPLrhllSLD-------KAERLARASEMLRavDLDDSVLDKRPPQ-L 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 153 PIAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEISDRITVIRDGQKIG 231
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
....*....
gi 491046221 232 TWPAEGLTT 240
Cdd:PRK10419 233 TQPVGDKLT 241
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
269-501 |
2.69e-19 |
|
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: 86.62 E-value: 2.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLS--RAGQY---RDINLNLKRGEvlglcgllgsgR-----------TELALSLFGITHPDSGELFIEGKPVKlKN 332
Cdd:COG1122 1 IELENLSfsYPGGTpalDDVSLSIEKGE-----------FvaiigpngsgkSTLLRLLNGLLKPTSGEVLVDGKDIT-KK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 333 NTDAIKRGIGYVsedrltlgaiLQQsiADNMVIS--ILD-------RLKtpwhlIDEKQCQDIVQEWIADLDI-----KV 398
Cdd:COG1122 69 NLRELRRKVGLV----------FQN--PDDQLFAptVEEdvafgpeNLG-----LPREEIRERVEEALELVGLehladRP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 399 TdpnnalSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRIL 478
Cdd:COG1122 132 P------HELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVI 205
|
250 260
....*....|....*....|....*
gi 491046221 479 HMKQGSIVKEIVTDSI--NEQQLEE 501
Cdd:COG1122 206 VLDDGRIVADGTPREVfsDYELLEE 230
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
13-231 |
3.24e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 86.47 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 13 LITLRDLSKSF-GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRL----TPDKAR 87
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAG-KIWFSGHDITRLknreVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 88 ELGvqVIYQDLSLFPNLTVAENIAFELNLKGYFGwfrkKQLREKALEILNELAFtIDP--DTPVQfLPIAQRQQVAICRA 165
Cdd:PRK10908 80 QIG--MIFQDHHLLMDRTVYDNVAIPLIIAGASG----DDIRRRVSAALDKVGL-LDKakNFPIQ-LSGGEQQRVGIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 166 LVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIG 231
Cdd:PRK10908 152 VVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHG 217
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
11-245 |
1.23e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 85.94 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 11 DPLITLRDLSKSF-GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKAREL 89
Cdd:PRK13647 2 DNIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGR-VKVMGREVNAENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 90 gVQVIYQDL--SLFPNlTVAENIAF-ELNLKgyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRAL 166
Cdd:PRK13647 81 -VGLVFQDPddQVFSS-TVWDDVAFgPVNMG-----LDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 167 VADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITE 245
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVE 232
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-228 |
1.28e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 85.83 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 13 LITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKS--YHRLTPDKARElG 90
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGA-VLWQGKPldYSKRGLLALRQ-Q 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 91 VQVIYQD--LSLFPNlTVAENIAFEL-NLkgyfGWFRKKQLR--EKALEILNELAFTidpDTPVQFLPIAQRQQVAICRA 165
Cdd:PRK13638 79 VATVFQDpeQQIFYT-DIDSDIAFSLrNL----GVPEAEITRrvDEALTLVDAQHFR---HQPIQCLSHGQKKRVAIAGA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 166 LVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQ 213
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-230 |
1.47e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 86.68 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSF---------GG------HR------ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIE 72
Cdd:COG4586 2 IEVENLSKTYrvyekepglKGalkglfRReyreveAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGE-VR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 73 IDGKSYHRLTPDKARELGVqVIYQDLSLFPNLTVAENiaFELNlkgyfgwfRK-----KQLREKALEILNELaFTIDP-- 145
Cdd:COG4586 81 VLGYVPFKRRKEFARRIGV-VFGQRSQLWWDLPAIDS--FRLL--------KAiyripDAEYKKRLDELVEL-LDLGEll 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 146 DTPVQFLPIAQRQQVAICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRIT 222
Cdd:COG4586 149 DTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLdvvSKEAIREFLKEYN--RERGTTILLTSHDMDDIEALCDRVI 226
|
....*...
gi 491046221 223 VIRDGQKI 230
Cdd:COG4586 227 VIDHGRII 234
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
281-486 |
1.89e-18 |
|
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: 83.85 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTdaikRGIGYVSEDrltLGAIL-QQSI 359
Cdd:cd03226 17 DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERR----KSIGYVMQD---VDYQLfTDSV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 360 ADNMVISILDrlktpwhlIDEKQCQdiVQEWIADLDIKVTDPNNALStLSGGNQQKVVLAKWILTRPKVLILDSPTVGVD 439
Cdd:cd03226 90 REELLLGLKE--------LDAGNEQ--AETVLKDLDLYALKERHPLS-LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491046221 440 IGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:cd03226 159 YKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
10-228 |
2.61e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 85.24 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 10 SDPLITLRDLSKSFGGHR--ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDG--SKIEIDGKSYHRLTPDK 85
Cdd:PRK13640 2 KDNIVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNpnSKITVDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 86 ARElGVQVIYQDL-SLFPNLTVAENIAFELNLKGyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICR 164
Cdd:PRK13640 82 IRE-KVGIVFQNPdNQFVGATVGDDVAFGLENRA----VPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 165 ALVADARLVIMDEPTASLTRTEVNQLLSTVNYL-KDKGITVVFVSHRLEEVkEISDRITVIRDGQ 228
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEA-NMADQVLVLDDGK 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-230 |
2.71e-18 |
|
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: 82.98 E-value: 2.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 20 SKSFGGHRA-LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISG--VYAPDDGSkIEIDGKsyhrltPDKARELGVQVIY- 95
Cdd:cd03213 15 SSPSKSGKQlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGE-VLINGR------PLDKRSFRKIIGYv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 96 -QDLSLFPNLTVAENIAFELNLKGyfgwfrkkqlrekaleilnelaftidpdtpvqfLPIAQRQQVAICRALVADARLVI 174
Cdd:cd03213 88 pQDDILHPTLTVRETLMFAAKLRG---------------------------------LSGGERKRVSIALELVSNPSLLF 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 175 MDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRL-EEVKEISDRITVIRDGQKI 230
Cdd:cd03213 135 LDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
12-240 |
3.27e-18 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 85.62 E-value: 3.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 12 PLITLRDLSKSF----GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVyaPDDGSKIEIDGKSYH-----RLT 82
Cdd:PRK15093 2 PLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV--TKDNWRVTADRMRFDdidllRLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 83 PDKAREL---GVQVIYQDlslfPN--LTVAENIAFEL--NLKG--YFG--WFRKKQLREKALEILNELAFTIDPDTPVQF 151
Cdd:PRK15093 80 PRERRKLvghNVSMIFQE----PQscLDPSERVGRQLmqNIPGwtYKGrwWQRFGWRKRRAIELLHRVGIKDHKDAMRSF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 152 ---LPIAQRQQVAICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIR 225
Cdd:PRK15093 156 pyeLTEGECQKVMIAIALANQPRLLIADEPTNAMeptTQAQIFRLLTRLN--QNNNTTILLISHDLQMLSQWADKINVLY 233
|
250
....*....|....*
gi 491046221 226 DGQKIGTWPAEGLTT 240
Cdd:PRK15093 234 CGQTVETAPSKELVT 248
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
11-228 |
3.38e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 84.46 E-value: 3.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 11 DPLITLRDLSKSF----GGHR-----ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGksyHRL 81
Cdd:PRK15112 2 ETLLEVRNLSKTFryrtGWFRrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSG-ELLIDD---HPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 82 T-PDKA-RELGVQVIYQD--LSLFPNLTVAENIAFELNLKGYFgwfrKKQLREKAL-EILNELAFTIDPDT--PVQFLPi 154
Cdd:PRK15112 78 HfGDYSyRSQRIRMIFQDpsTSLNPRQRISQILDFPLRLNTDL----EPEQREKQIiETLRQVGLLPDHASyyPHMLAP- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 155 AQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK15112 153 GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGE 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
269-488 |
4.99e-18 |
|
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: 82.80 E-value: 4.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLSRA-GQY---RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKlkNNTDAIKRGIGYV 344
Cdd:cd03265 1 IEVENLVKKyGDFeavRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV--REPREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 345 SEDrLTLGAILqqSIADNMVIsiLDRLK-TPWHLIDEKQcqDIVQEWIADLDIKvtdpNNALSTLSGGNQQKVVLAKWIL 423
Cdd:cd03265 79 FQD-LSVDDEL--TGWENLYI--HARLYgVPGAERRERI--DELLDFVGLLEAA----DRLVKTYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 424 TRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEASEAYYNCDRILHMKQGSIVKE 488
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAE 213
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-228 |
9.49e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 86.05 E-value: 9.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 4 TSKADKSDPL-ITLRDLS-KSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGvYAPDDGSkIEIDGKSYHRL 81
Cdd:PRK11174 339 EKELASNDPVtIEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGS-LKINGIELREL 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 82 TPDKARE----LGvqviyQDLSLFPNlTVAENIAF--------ELNlkgyfgwfrkkQLREKA--LEILNELAFTIDpdT 147
Cdd:PRK11174 417 DPESWRKhlswVG-----QNPQLPHG-TLRDNVLLgnpdasdeQLQ-----------QALENAwvSEFLPLLPQGLD--T 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 148 PVQ----FLPIAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKdKGITVVFVSHRLEEVKEIsDRITV 223
Cdd:PRK11174 478 PIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS-RRQTTLMVTHQLEDLAQW-DQIWV 555
|
....*
gi 491046221 224 IRDGQ 228
Cdd:PRK11174 556 MQDGQ 560
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
12-236 |
1.31e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 85.93 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 12 PLITLRDLSKSF----GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLI-------KTISGVYAPDDGSKIEIDGKSYHR 80
Cdd:PRK10535 3 ALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMnilgcldKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 81 LtpdkaRELGVQVIYQDLSLFPNLTVAENIafelNLKGYFGWFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQV 160
Cdd:PRK10535 83 L-----RREHFGFIFQRYHLLSHLTAAQNV----EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 161 AICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRlEEVKEISDRITVIRDGQKIGTWPAE 236
Cdd:PRK10535 154 SIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVRNPPAQ 228
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-228 |
1.42e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 85.46 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 2 TSTSKADKSDPLITLRDLSKSFGG--HRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYH 79
Cdd:PRK11176 330 EGKRVIERAKGDIEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGE-ILLDGHDLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 80 RLTPDKARElGVQVIYQDLSLFpNLTVAENIAFELNLKgyfgwFRKKQLrEKALEILNELAFtIDP-----DTPV----Q 150
Cdd:PRK11176 409 DYTLASLRN-QVALVSQNVHLF-NDTIANNIAYARTEQ-----YSREQI-EEAARMAYAMDF-INKmdnglDTVIgengV 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 151 FLPIAQRQQVAICRALVADARLVIMDEPTASL-TRTEvNQLLSTVNYLKdKGITVVFVSHRLEEVkEISDRITVIRDGQ 228
Cdd:PRK11176 480 LLSGGQRQRIAIARALLRDSPILILDEATSALdTESE-RAIQAALDELQ-KNRTSLVIAHRLSTI-EKADEILVVEDGE 555
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
27-273 |
1.51e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.79 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 27 RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSyhrLTPDKA------RELGVQVIYQDLSL 100
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSG-KIIIDGVD---ITDKKVklsdirKKVGLVFQYPEYQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 101 FPNlTVAENIAFELNLKGYFGWFRKKQLREkALEILNELAFTIDPDTPVQfLPIAQRQQVAICRALVADARLVIMDEPTA 180
Cdd:PRK13637 97 FEE-TIEKDIAFGPINLGLSEEEIENRVKR-AMNIVGLDYEDYKDKSPFE-LSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 181 SLTRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEISDRITVIRDGQKI--GTwPAE-----------GLTTRKITEL 246
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCElqGT-PREvfkevetlesiGLAVPQVTYL 252
|
250 260
....*....|....*....|....*..
gi 491046221 247 MTGLdivhERKPPNNAEDRRTVLEIKN 273
Cdd:PRK13637 253 VRKL----RKKGFNIPDDIFTIEEAKE 275
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
281-483 |
1.57e-17 |
|
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: 80.97 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKlKNNTDAIKRGIGYV---SEDRLtlgaiLQQ 357
Cdd:cd03225 18 DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT-KLSLKELRRKVGLVfqnPDDQF-----FGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 358 SIADNMVISiLDRLKTPWHLIDEKqcqdiVQEWIADLDIKvTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVG 437
Cdd:cd03225 92 TVEEEVAFG-LENLGLPEEEIEER-----VEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491046221 438 VDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQG 483
Cdd:cd03225 165 LDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-220 |
1.98e-17 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 82.01 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 4 TSKADKSDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKT-------ISGVYApdDGsKIEIDGK 76
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndlIPGARV--EG-EILLDGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 77 S-YHRLTPdkARELGVQV--IYQDLSLFPnLTVAENIAFELNLKGYfgwFRKKQLR---EKALEI----------LNELA 140
Cdd:COG1117 79 DiYDPDVD--VVELRRRVgmVFQKPNPFP-KSIYDNVAYGLRLHGI---KSKSELDeivEESLRKaalwdevkdrLKKSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 141 FTidpdtpvqfLPIAQRQQVAICRALVADARLVIMDEPTASL----TRTeVNQLLSTvnyLKDKgITVVFVSHRLEEVKE 216
Cdd:COG1117 153 LG---------LSGGQQQRLCIARALAVEPEVLLMDEPTSALdpisTAK-IEELILE---LKKD-YTIVIVTHNMQQAAR 218
|
....
gi 491046221 217 ISDR 220
Cdd:COG1117 219 VSDY 222
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
14-236 |
2.02e-17 |
|
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: 80.65 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGV--YAPDDGsKIEIDGKSYHRLTPDKARELGV 91
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEG-EILFKGEDITDLPPEERARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 92 QVIYQDLSLFPNLTVAENIAFeLNlKGYFGWFRKKqlrekaleilNElaftidpdtpvqflpiaqrqqvaICRALVADAR 171
Cdd:cd03217 80 FLAFQYPPEIPGVKNADFLRY-VN-EGFSGGEKKR----------NE-----------------------ILQLLLLEPD 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 172 LVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHR---LEEVKeiSDRITVIRDGQKIGTWPAE 236
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYqrlLDYIK--PDRVHVLYDGRIVKSGDKE 190
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
26-228 |
2.02e-17 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 81.36 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 26 HRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKS--------YHRLtpdkarelgVQVIYQD 97
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGG-QVLLDGKPisqyehkyLHSK---------VSLVGQE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 98 LSLFPNlTVAENIAFELNLKGyFGWFRKKQLREKALEILNELAFTIDPDTPVQ--FLPIAQRQQVAICRALVADARLVIM 175
Cdd:cd03248 97 PVLFAR-SLQDNIAYGLQSCS-FECVKEAAQKAHAHSFISELASGYDTEVGEKgsQLSGGQKQRVAIARALIRNPQVLIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 176 DEPTASL---TRTEVNQLLSTVNYLKdkgiTVVFVSHRLEEVkEISDRITVIRDGQ 228
Cdd:cd03248 175 DEATSALdaeSEQQVQQALYDWPERR----TVLVIAHRLSTV-ERADQILVLDGGR 225
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-245 |
5.10e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 80.66 E-value: 5.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIE----IDGKSYH--RLTPDKAR 87
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEgevrLFGRNIYspDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 88 ElGVQVIYQDLSLFPNLTVAENIAFELNLKGYFGwfRKKQLREKALEILNELAFTID-----PDTPVQfLPIAQRQQVAI 162
Cdd:PRK14267 85 R-EVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVK--SKKELDERVEWALKKAALWDEvkdrlNDYPSN-LSGGQRQRLVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 163 CRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKgITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPaegltTRK 242
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGP-----TRK 234
|
...
gi 491046221 243 ITE 245
Cdd:PRK14267 235 VFE 237
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
29-252 |
6.94e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 80.93 E-value: 6.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGksyHRLTPDKARELGVQV--IYQDL-SLFPNLT 105
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQ-IIIDG---DLLTEENVWDIRHKIgmVFQNPdNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 106 VAENIAFELNLKGyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLVIMDEPTASLTRT 185
Cdd:PRK13650 99 VEDDVAFGLENKG----IPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 186 EVNQLLSTVNYLKDK-GITVVFVSHRLEEVKeISDRITVIRDGQKIGTWPAEGLTTRKITELMTGLDI 252
Cdd:PRK13650 175 GRLELIKTIKGIRDDyQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFSRGNDLLQLGLDI 241
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
17-229 |
8.75e-17 |
|
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: 78.69 E-value: 8.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 17 RDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARELgVQVIYQ 96
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAG-RVLLNGGPLDFQRDSIARGL-LYLGHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 97 DlSLFPNLTVAENIAFelnlkgyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLVIMD 176
Cdd:cd03231 82 P-GIKTTLSVLENLRF----------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491046221 177 EPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEisDRITVIRDGQK 229
Cdd:cd03231 151 EPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSE--AGARELDLGFK 201
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
281-488 |
1.01e-16 |
|
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: 77.47 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVlglcgllgsgrteLAL--------S-----LFGITHPDSGELFIEGKPVKLKNNTDAIKRGIGYVSEd 347
Cdd:cd03216 17 DGVSLSVRRGEV-------------HALlgengagkStlmkiLSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMVYQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 348 rltlgailqqsiadnmvisildrlktpwhlidekqcqdivqewiadldikvtdpnnalstLSGGNQQKVVLAKWILTRPK 427
Cdd:cd03216 83 ------------------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 428 VLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVKE 488
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
12-217 |
1.07e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.76 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 12 PLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRltpDKARELGV 91
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGT-IKLDGGDIDD---PDVAEACH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 92 QVIYQDlSLFPNLTVAENIAFELNLKGyfgwfrkkQLREKALEILNelAFTIDP--DTPVQFLPIAQRQQVAICRALVAD 169
Cdd:PRK13539 77 YLGHRN-AMKPALTVAENLEFWAAFLG--------GEELDIAAALE--AVGLAPlaHLPFGYLSAGQKRRVALARLLVSN 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491046221 170 ARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHR---LEEVKEI 217
Cdd:PRK13539 146 RPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHIplgLPGAREL 196
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
27-259 |
2.02e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 79.67 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 27 RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIEID-----GKSYHRLTPDKARELGVQVIYQDLSLF 101
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipaNLKKIKEVKRLRKEIGLVFQFPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 102 PNlTVAENIAF-ELNLKGyfgwfRKKQLREKALEILNELAFTID--PDTPVQfLPIAQRQQVAICRALVADARLVIMDEP 178
Cdd:PRK13645 105 QE-TIEKDIAFgPVNLGE-----NKQEAYKKVPELLKLVQLPEDyvKRSPFE-LSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 179 TASLTRTEVNQLLSTVNYL-KDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTW-PAEGLTTRkitELMTGLDIvher 256
Cdd:PRK13645 178 TGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGsPFEIFSNQ---ELLTKIEI---- 250
|
...
gi 491046221 257 KPP 259
Cdd:PRK13645 251 DPP 253
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
266-502 |
2.13e-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: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 266 RTVLEIKNLS---RAGQY---RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPD---SGELFIEGKPVkLKNNTDA 336
Cdd:COG1123 2 TPLLEVRDLSvryPGGDVpavDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDL-LELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 337 IKRGIGYVSEDRLTlgAILQQSIADNMVISILDRLKTPwhlideKQCQDIVQEWIADLDIKvTDPNNALSTLSGGNQQKV 416
Cdd:COG1123 81 RGRRIGMVFQDPMT--QLNPVTVGDQIAEALENLGLSR------AEARARVLELLEAVGLE-RRLDRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 417 VLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSG-VGISILLITDEASEAYYNCDRILHMKQGSIVKEIVTDSI- 494
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEIl 231
|
....*....
gi 491046221 495 -NEQQLEEI 502
Cdd:COG1123 232 aAPQALAAV 240
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
269-486 |
2.15e-16 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 78.53 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLSRAG---QYRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVklkNNTDAIKRGIGYVS 345
Cdd:cd03299 1 LKVENLSKDWkefKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI---TNLPPEKRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 346 EDR-LTLGAILQQSIADNMVISILDRLKtpwhlIDEKqcqdiVQEWIADLDIK-VTDPNNAlsTLSGGNQQKVVLAKWIL 423
Cdd:cd03299 78 QNYaLFPHMTVYKNIAYGLKKRKVDKKE-----IERK-----VLEIAEMLGIDhLLNRKPE--TLSGGEQQRVAIARALV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491046221 424 TRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:cd03299 146 VNPKILLLDEPFSALDVRTKEKLREELKKIrKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLI 209
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
28-228 |
2.27e-16 |
|
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: 77.92 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 28 ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELgVQVIYQDLSLFPNlTVA 107
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGS-ILIDGVDISKIGLHDLRSR-ISIIPQDPVLFSG-TIR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 108 ENIAFelnlkgyFGWFRKKQLREkALEI--LNELAFTIDP--DTPVQ----FLPIAQRQQVAICRALVADARLVIMDEPT 179
Cdd:cd03244 96 SNLDP-------FGEYSDEELWQ-ALERvgLKEFVESLPGglDTVVEeggeNLSVGQRQLLCLARALLRKSKILVLDEAT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491046221 180 ASL---TRTEVNQLLSTvnylKDKGITVVFVSHRLEEVKEiSDRITVIRDGQ 228
Cdd:cd03244 168 ASVdpeTDALIQKTIRE----AFKDCTVLTIAHRLDTIID-SDRILVLDKGR 214
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
280-436 |
3.33e-16 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 75.76 E-value: 3.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 280 YRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVkLKNNTDAIKRGIGYVSEDrltLGAILQQSI 359
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL-TDDERKSLRKEIGYVFQD---PQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 360 ADNMVISIldRLKTPWHLIDEKQCQDIvQEWIADLDIKVTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTV 436
Cdd:pfam00005 77 RENLRLGL--LLKGLSKREKDARAEEA-LEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
29-228 |
3.55e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 77.51 E-value: 3.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVyapDDGSKIEID--GKSYHRLTPDKAREL---GVQVIYQDLSLFPN 103
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGL---DDGSSGEVSlvGQPLHQMDEEARAKLrakHVGFVFQSFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 104 LTVAENIAFELNLKGYfgwfRKKQLREKALEILNELAFTIDPD-TPVQfLPIAQRQQVAICRALVADARLVIMDEPTASL 182
Cdd:PRK10584 103 LNALENVELPALLRGE----SSRQSRNGAKALLEQLGLGKRLDhLPAQ-LSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491046221 183 TRT---EVNQLLSTVNylKDKGITVVFVSHRlEEVKEISDRITVIRDGQ 228
Cdd:PRK10584 178 DRQtgdKIADLLFSLN--REHGTTLILVTHD-LQLAARCDRRLRLVNGQ 223
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
12-249 |
3.67e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.87 E-value: 3.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 12 PLITLRDLSKsfgghRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGV 91
Cdd:PRK15439 267 PVLTVEDLTG-----EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGR-IMLNGKEINALSTAQRLARGL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 92 qvIY-----QDLSLFPNLTVAENI-AFELNLKGYfgWFRKKqlREKA-LE----ILNeLAFTiDPDTPVQFLPIAQRQQV 160
Cdd:PRK15439 341 --VYlpedrQSSGLYLDAPLAWNVcALTHNRRGF--WIKPA--RENAvLEryrrALN-IKFN-HAEQAARTLSGGNQQKV 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 161 AICRALVADARLVIMDEPTASL---TRTEVNQLLSTVnylKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEG 237
Cdd:PRK15439 413 LIAKCLEASPQLLIVDEPTRGVdvsARNDIYQLIRSI---AAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAA 489
|
250
....*....|..
gi 491046221 238 LTTRKITELMTG 249
Cdd:PRK15439 490 INVDTIMRLAFG 501
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-228 |
4.24e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 78.17 E-value: 4.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDgSKIEIDGKSYH------RLTPDKARElGVQVIYQDLSLFP 102
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYD-SKIKVDGKVLYfgkdifQIDAIKLRK-EVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 103 NLTVAENIAFELNLKGYFGWFRKKQLREKALEILNELAFTIDP-DTPVQFLPIAQRQQVAICRALVADARLVIMDEPTAS 181
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRlNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491046221 182 LTRTEVNQLLSTVNYLKDKgITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGE 229
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-246 |
4.61e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 80.73 E-value: 4.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 27 RALRN-IDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARELGVQVIYQD---LSLFP 102
Cdd:PRK11288 266 PGLREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAG-QVYLDGKPIDIRSPRDAIRAGIMLCPEDrkaEGIIP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 103 NLTVAENI---AFELNLKgyFGWF-RKKQLREKALEILNELAF-TIDPDTPVQFLPIAQRQQVAICRALVADARLVIMDE 177
Cdd:PRK11288 345 VHSVADNInisARRHHLR--AGCLiNNRWEAENADRFIRSLNIkTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 178 PTASL---TRTEVNQLLstvnY-LKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITEL 246
Cdd:PRK11288 423 PTRGIdvgAKHEIYNVI----YeLAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELAREQATERQALSL 491
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
31-249 |
5.29e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 80.36 E-value: 5.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 31 NIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIEIDGKSYHRLTPDKARELGVQVIYQDLS---LFPNLTVA 107
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWEGEIFIDGKPVKIRNPQQAIAQGIAMVPEDRKrdgIVPVMGVG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 108 ENIAFElNLKGYFGWFRKKQLREK--ALEILNELAFTidpdTPVQFLPIAQ-----RQQVAICRALVADARLVIMDEPTA 180
Cdd:PRK13549 360 KNITLA-ALDRFTGGSRIDDAAELktILESIQRLKVK----TASPELAIARlsggnQQKAVLAKCLLLNPKILILDEPTR 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491046221 181 SL---TRTEVNQLlstVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITELMTG 249
Cdd:PRK13549 435 GIdvgAKYEIYKL---INQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINHNLTQEQVMEAALR 503
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-230 |
5.98e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 80.64 E-value: 5.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 3 STSKADKSDPLITLRDLSKSF--GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHR 80
Cdd:PRK11160 328 TTSTAAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGE-ILLNGQPIAD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 81 LTPDKARElGVQVIYQDLSLFpNLTVAENIAFELNLKGyfgwfrkkqlREKALEILN--ELAFTIDPDTPV--------- 149
Cdd:PRK11160 407 YSEAALRQ-AISVVSQRVHLF-SATLRDNLLLAAPNAS----------DEALIEVLQqvGLEKLLEDDKGLnawlgeggr 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 150 QfLPIAQRQQVAICRALVADARLVIMDEPTASL---TRTEVNQLLstVNYLKDKgiTVVFVSHRLEEVKEIsDRITVIRD 226
Cdd:PRK11160 475 Q-LSGGEQRRLGIARALLHDAPLLLLDEPTEGLdaeTERQILELL--AEHAQNK--TVLMITHRLTGLEQF-DRICVMDN 548
|
....
gi 491046221 227 GQKI 230
Cdd:PRK11160 549 GQII 552
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
269-488 |
6.80e-16 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 76.70 E-value: 6.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLSrAGqY------RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTDAIKRGIG 342
Cdd:cd03224 1 LEVENLN-AG-YgksqilFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 343 YVSEDRLTLGailQQSIADN--MVISILDRLKTPWHLidekqcqdivqEWIADL-DIKVTDPNNALSTLSGGNQQKVVLA 419
Cdd:cd03224 79 YVPEGRRIFP---ELTVEENllLGAYARRRAKRKARL-----------ERVYELfPRLKERRKQLAGTLSGGEQQMLAIA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 420 KWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVKE 488
Cdd:cd03224 145 RALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLE 213
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
27-230 |
8.00e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 77.95 E-value: 8.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 27 RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKA-----RELGVQVIYQDLSLF 101
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSG-TITIAGYHITPETGNKNlkklrKKVSLVFQFPEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 102 PNlTVAENIAF-ELNlkgyFGwFRKKQLREKALEILNELAFTIDPDTPVQF-LPIAQRQQVAICRALVADARLVIMDEPT 179
Cdd:PRK13641 100 EN-TVLKDVEFgPKN----FG-FSEDEAKEKALKWLKKVGLSEDLISKSPFeLSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491046221 180 ASL---TRTEVNQLLstVNYLKdKGITVVFVSHRLEEVKEISDRITVIRDGQKI 230
Cdd:PRK13641 174 AGLdpeGRKEMMQLF--KDYQK-AGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
13-234 |
8.06e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 80.38 E-value: 8.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 13 LITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGK-SYHRLTPDKAREL-- 89
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDG-RIIYEQDlIVARLQQDPPRNVeg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 90 --------GVQVI------YQDLSLF-------PNLTVAENIAFELNLKGyfGWfrkkQLREKALEILNELAftIDPDTP 148
Cdd:PRK11147 82 tvydfvaeGIEEQaeylkrYHDISHLvetdpseKNLNELAKLQEQLDHHN--LW----QLENRINEVLAQLG--LDPDAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 149 VQFLPIAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLlstVNYLKDKGITVVFVSHRLEEVKEISDRItVIRDGQ 228
Cdd:PRK11147 154 LSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWL---EGFLKTFQGSIIFISHDRSFIRNMATRI-VDLDRG 229
|
....*.
gi 491046221 229 KIGTWP 234
Cdd:PRK11147 230 KLVSYP 235
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
13-228 |
9.48e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 77.33 E-value: 9.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 13 LITLRDLSKSF-GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKI--EIDGKSYHRLtpDKAREL 89
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsGIDTGDFSKL--QGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 90 gVQVIYQD-LSLFPNLTVAENIAF-ELNLkgyfgWFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALV 167
Cdd:PRK13644 79 -VGIVFQNpETQFVGRTVEEDLAFgPENL-----CLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 168 ADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVkEISDRITVIRDGQ 228
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGK 212
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-243 |
1.07e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 77.00 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 12 PLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDdgSKIEIDGKS-------YHRLTPD 84
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE--SEVRVEGRVeffnqniYERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 85 KARELGVQVIYQDLSLFPnLTVAENIAFELNLkgyFGWFRKKQLRE------KALEILNELAFTIDPDTpvQFLPIAQRQ 158
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKI---VGWRPKLEIDDivesalKDADLWDEIKHKIHKSA--LDLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 159 QVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKG-ITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEG 237
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLVEF 237
|
....*.
gi 491046221 238 LTTRKI 243
Cdd:PRK14258 238 GLTKKI 243
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
10-223 |
1.18e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 78.08 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 10 SDPLITLRDLSKS-------FGGHR---ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYh 79
Cdd:PRK11308 2 QQPLLQAIDLKKHypvkrglFKPERlvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGE-LYYQGQDL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 80 rLTPD----KARELGVQVIYQD--LSLFPNLTV----AENIAFELNLKgyfgwfrKKQLREKALEILNELAftIDPD--- 146
Cdd:PRK11308 80 -LKADpeaqKLLRQKIQIVFQNpyGSLNPRKKVgqilEEPLLINTSLS-------AAERREKALAMMAKVG--LRPEhyd 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 147 -TPVQFlPIAQRQQVAICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRIT 222
Cdd:PRK11308 150 rYPHMF-SGGQRQRIAIARALMLDPDVVVADEPVSALdvsVQAQVLNLMMDLQ--QELGLSYVFISHDLSVVEHIADEVM 226
|
.
gi 491046221 223 V 223
Cdd:PRK11308 227 V 227
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
14-228 |
1.48e-15 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 79.60 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSksFGGHRA----LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKAREl 89
Cdd:TIGR03796 478 VELRNIT--FGYSPLepplIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSG-EILFDGIPREEIPREVLAN- 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 90 GVQVIYQDLSLFPNlTVAENIAFelnlkgyfgWFRkkQLREKALE-------ILNE-LAFTIDPDTPV----QFLPIAQR 157
Cdd:TIGR03796 554 SVAMVDQDIFLFEG-TVRDNLTL---------WDP--TIPDADLVrackdaaIHDViTSRPGGYDAELaeggANLSGGQR 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491046221 158 QQVAICRALVADARLVIMDEPTASL-TRTEvnqlLSTVNYLKDKGITVVFVSHRLEEVKEiSDRITVIRDGQ 228
Cdd:TIGR03796 622 QRLEIARALVRNPSILILDEATSALdPETE----KIIDDNLRRRGCTCIIVAHRLSTIRD-CDEIIVLERGK 688
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
29-210 |
1.61e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 74.99 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYhrltpDKARelgvqVIYQDLSLF------- 101
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKG-EILFERQSI-----KKDL-----CTYQKQLCFvghrsgi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 102 -PNLTVAENIAFELNlkgyfgwFRKKQLREKALEILNELAFTIDpdTPVQFLPIAQRQQVAICRALVADARLVIMDEPTA 180
Cdd:PRK13540 86 nPYLTLRENCLYDIH-------FSPGAVGITELCRLFSLEHLID--YPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
|
170 180 190
....*....|....*....|....*....|
gi 491046221 181 SLTRTEVNQLLSTVNYLKDKGITVVFVSHR 210
Cdd:PRK13540 157 ALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
28-252 |
1.63e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 76.66 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 28 ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKsyhrltpDKARELGVQVIYQDLSL-FPN--- 103
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEG-KVYVDGL-------DTSDEENLWDIRNKAGMvFQNpdn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 104 ----LTVAENIAF-ELNLKgyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLVIMDEP 178
Cdd:PRK13633 97 qivaTIVEEDVAFgPENLG-----IPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 179 TASLTRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEiSDRITVIRDGQKIgtwpAEGlTTRKI---TELMT--GLDI 252
Cdd:PRK13633 172 TAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVV----MEG-TPKEIfkeVEMMKkiGLDV 245
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
9-238 |
1.68e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 76.73 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 9 KSDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGK-----SYHRLTP 83
Cdd:PRK11831 3 SVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHG-EILFDGEnipamSRSRLYT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 84 DKARelgVQVIYQDLSLFPNLTVAENIAFELNlkgyfgwfRKKQLREKALE--ILNELAfTIDPDTPVQFLP------IA 155
Cdd:PRK11831 82 VRKR---MSMLFQSGALFTDMNVFDNVAYPLR--------EHTQLPAPLLHstVMMKLE-AVGLRGAAKLMPselsggMA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 156 QRqqVAICRALVADARLVIMDEPTAS---LTRTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGT 232
Cdd:PRK11831 150 RR--AALARAIALEPDLIMFDEPFVGqdpITMGVLVKLISELN--SALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAH 225
|
....*.
gi 491046221 233 WPAEGL 238
Cdd:PRK11831 226 GSAQAL 231
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
13-230 |
1.83e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 78.85 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 13 LITLRDLSKSFGGHR-ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARElGV 91
Cdd:PRK13657 334 AVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGR-ILIDGTDIRTVTRASLRR-NI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 92 QVIYQDLSLFpNLTVAENI------AFELNLkgyfgwfRKKQLREKALEIL--NELAFtidpDTPV----QFLPIAQRQQ 159
Cdd:PRK13657 412 AVVFQDAGLF-NRSIEDNIrvgrpdATDEEM-------RAAAERAQAHDFIerKPDGY----DTVVgergRQLSGGERQR 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491046221 160 VAICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylkdKGITVVFVSHRLEEVKEiSDRITVIRDGQKI 230
Cdd:PRK13657 480 LAIARALLKDPPILILDEATSALdveTEAKVKAALDELM----KGRTTFIIAHRLSTVRN-ADRILVFDNGRVV 548
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
34-227 |
3.33e-15 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 74.89 E-value: 3.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 34 LTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSyhrlTPDKARELGVQVIYQDLSL-FPnLTVAENIaf 112
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGT-VKVAGAS----PGKGWRHIGYVPQRHEFAWdFP-ISVAHTV-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 113 eLNLK-GYFGWFRKKQLRE-----KALEI--LNELAftidpDTPVQFLPIAQRQQVAICRALVADARLVIMDEPTASLTR 184
Cdd:TIGR03771 73 -MSGRtGHIGWLRRPCVADfaavrDALRRvgLTELA-----DRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDM 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491046221 185 TEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRI-----TVIRDG 227
Cdd:TIGR03771 147 PTQELLTELFIELAGAGTAILMTTHDLAQAMATCDRVvllngRVIADG 194
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
14-228 |
4.32e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 77.84 E-value: 4.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSF-GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARElGVQ 92
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEG-EIRLDGRPLSSLSHSVLRQ-GVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 93 VIYQDL-----SLFPNLTVAENIAFELNlkgyfgWfrkkqlreKALEI--LNELAFTIdPD---TPV----QFLPIAQRQ 158
Cdd:PRK10790 419 MVQQDPvvladTFLANVTLGRDISEEQV------W--------QALETvqLAELARSL-PDglyTPLgeqgNNLSVGQKQ 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 159 QVAICRALVADARLVIMDEPTASL---TRTEVNQLLSTVNylkdKGITVVFVSHRLEEVKEiSDRITVIRDGQ 228
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANIdsgTEQAIQQALAAVR----EHTTLVVIAHRLSTIVE-ADTILVLHRGQ 551
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
13-231 |
4.70e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 75.22 E-value: 4.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 13 LITLRDLSKSFGGHR-ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSyhrLTPDKARELG- 90
Cdd:PRK13652 3 LIETRDLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSG-SVLIRGEP---ITKENIREVRk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 91 -VQVIYQ--DLSLFpNLTVAENIAF-ELNLKgyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRAL 166
Cdd:PRK13652 79 fVGLVFQnpDDQIF-SPTVEQDIAFgPINLG-----LDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 167 VADARLVIMDEPTASLTRTEVNQLLSTVNYL-KDKGITVVFVSHRLEEVKEISDRITVIRDGQKIG 231
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVA 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
12-228 |
4.83e-15 |
|
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: 78.52 E-value: 4.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 12 PLITLRDLSKSF--GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYhrltpdkarEL 89
Cdd:TIGR01257 927 PGVCVKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGT-VLVGGKDI---------ET 996
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 90 GVQVIYQDLS-------LFPNLTVAENIAFELNLKGYfGWfRKKQLREKALeiLNELAFTIDPDTPVQFLPIAQRQQVAI 162
Cdd:TIGR01257 997 NLDAVRQSLGmcpqhniLFHHLTVAEHILFYAQLKGR-SW-EEAQLEMEAM--LEDTGLHHKRNEEAQDLSGGMQRKLSV 1072
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 163 CRALVADARLVIMDEPTASL---TRTEVNQLLstvnyLKDK-GITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:TIGR01257 1073 AIAFVGDAKVVVLDEPTSGVdpySRRSIWDLL-----LKYRsGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
10-205 |
7.74e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 73.34 E-value: 7.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 10 SDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKsyHRLTPDKAREl 89
Cdd:PRK13543 8 APPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESG-QIQIDGK--TATRGDRSRF- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 90 gVQVIYQDLSLFPNLTVAENIAFELNLKGYfgwfRKKQLREKALEIlneLAFTIDPDTPVQFLPIAQRQQVAICRALVAD 169
Cdd:PRK13543 84 -MAYLGHLPGLKADLSTLENLHFLCGLHGR----RAKQMPGSALAI---VGLAGYEDTLVRQLSAGQKKRLALARLWLSP 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 491046221 170 ARLVIMDEPTASLTR---TEVNQLLSTvnYLKDKGITVV 205
Cdd:PRK13543 156 APLWLLDEPYANLDLegiTLVNRMISA--HLRGGGAALV 192
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
14-228 |
9.51e-15 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 71.33 E-value: 9.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkieidgksyhrltpdkarelgvqv 93
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 94 iyqdLSLFPNLTVaeniafelnlkGYFgwfrkKQLR--EKAleilnelaftidpdtpvqflpiaqrqQVAICRALVADAR 171
Cdd:cd03221 57 ----VTWGSTVKI-----------GYF-----EQLSggEKM--------------------------RLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 172 LVIMDEPTASLTRTEVNQLlstVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:cd03221 91 LLLLDEPTNHLDLESIEAL---EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
27-230 |
1.05e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 74.77 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 27 RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGS----KIEIDGKSYHRLTPDKARELGVQVIYQDLSLFP 102
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKvtvgDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 103 NlTVAENIAFElnlKGYFGwFRKKQLREKALEILNELAFTID--PDTPVQfLPIAQRQQVAICRALVADARLVIMDEPTA 180
Cdd:PRK13643 100 E-TVLKDVAFG---PQNFG-IPKEKAEKIAAEKLEMVGLADEfwEKSPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491046221 181 SL---TRTEVNQLLSTVNylkDKGITVVFVSHRLEEVKEISDRITVIRDGQKI 230
Cdd:PRK13643 174 GLdpkARIEMMQLFESIH---QSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
281-488 |
1.31e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 74.11 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPV--------KLKNNTdaikrGIGYVSEDRLTLG 352
Cdd:PRK13636 23 KGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrkglmKLRESV-----GMVFQDPDNQLFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 353 AILQQSIADNMVisildRLKTPWHLIDEKQCQDIVQEWIADLDIKVTdpnnalSTLSGGNQQKVVLAKWILTRPKVLILD 432
Cdd:PRK13636 98 ASVYQDVSFGAV-----NLKLPEDEVRKRVDNALKRTGIEHLKDKPT------HCLSFGQKKRVAIAGVLVMEPKVLVLD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 433 SPTVGVDIGAKDSIYKLIHRLS-GVGISILLITDEASEAYYNCDRILHMKQGSIVKE 488
Cdd:PRK13636 167 EPTAGLDPMGVSEIMKLLVEMQkELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQ 223
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
269-488 |
1.53e-14 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 72.92 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNL--SRAGQ--YRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPV-KLKNNTD-AIKRGIG 342
Cdd:cd03261 1 IELRGLtkSFGGRtvLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsGLSEAELyRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 343 YVSEDrltlGAILQQ-SIADNMVISILDRLKTPwhlidEKQCQDIVQEWIADLDIKVTD---PnnalSTLSGGNQQKVVL 418
Cdd:cd03261 81 MLFQS----GALFDSlTVFENVAFPLREHTRLS-----EEEIREIVLEKLEAVGLRGAEdlyP----AELSGGMKKRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 419 AKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGV-GISILLITDEASEAYYNCDRILHMKQGSIVKE 488
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAE 218
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
19-250 |
1.64e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 73.48 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 19 LSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRL-TPDKARELGvqVIYQD 97
Cdd:PRK10253 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGH-VWLDGEHIQHYaSKEVARRIG--LLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 98 LSLFPNLTVAENIAF-ELNLKGYFGWFRKKQlREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLVIMD 176
Cdd:PRK10253 90 ATTPGDITVQELVARgRYPHQPLFTRWRKED-EEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 177 EPTASLT---RTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITELMTGL 250
Cdd:PRK10253 169 EPTTWLDishQIDLLELLSELN--REKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGL 243
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-487 |
1.67e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 76.05 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 1 MTSTSKADKSDPLiTLRDLSKSFGGHR----ALRNIDLTLNKGEVHCLAGTNGCGKST-------LIKTISGVYAPD--- 66
Cdd:PRK10261 1 MPHSDELDARDVL-AVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVQCDkml 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 67 ----DGSKIEIDGKSYHRLTpdKARELGVQVIYQD--LSLFPNLTVAENIAFELNLKGYFGwfRKKQLREkALEILNEL- 139
Cdd:PRK10261 80 lrrrSRQVIELSEQSAAQMR--HVRGADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGAS--REEAMVE-AKRMLDQVr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 140 ---AFTIDPDTPVQfLPIAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYL-KDKGITVVFVSHRLEEVK 215
Cdd:PRK10261 155 ipeAQTILSRYPHQ-LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 216 EISDRITVIRDGQKIGTWPAEGL-------TTRKITEL------MTGLDIVH----------ERKPPNNAEDR----RTV 268
Cdd:PRK10261 234 EIADRVLVMYQGEAVETGSVEQIfhapqhpYTRALLAAvpqlgaMKGLDYPRrfplislehpAKQEPPIEQDTvvdgEPI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLS-----RAGQY----------RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNN 333
Cdd:PRK10261 314 LQVRNLVtrfplRSGLLnrvtrevhavEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 334 T--DAIKRGIGYVSED-------RLTLGailqqsiadnmvISILDRLKTpwH-LIDEKQCQDIVQEWIADLDIKvtdPNN 403
Cdd:PRK10261 394 GklQALRRDIQFIFQDpyasldpRQTVG------------DSIMEPLRV--HgLLPGKAAAARVAWLLERVGLL---PEH 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 404 ALS---TLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLS-GVGISILLITDEASEAYYNCDRILH 479
Cdd:PRK10261 457 AWRyphEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQrDFGIAYLFISHDMAVVERISHRVAV 536
|
....*...
gi 491046221 480 MKQGSIVK 487
Cdd:PRK10261 537 MYLGQIVE 544
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
408-483 |
1.80e-14 |
|
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: 70.74 E-value: 1.80e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQG 483
Cdd:cd00267 81 LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
8-227 |
2.66e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 72.86 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 8 DKSDPLITLRDLSKSFGGHRA--LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIEIDgksyHRLTPDK 85
Cdd:PRK13648 2 EDKNSIIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNN----QAITDDN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 86 AREL--GVQVIYQDL-SLFPNLTVAENIAFEL--NLKGYfgwfrkKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQV 160
Cdd:PRK13648 78 FEKLrkHIGIVFQNPdNQFVGSIVKYDVAFGLenHAVPY------DEMHRRVSEALKQVDMLERADYEPNALSGGQKQRV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 161 AICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLK-DKGITVVFVSHRLEEVKEiSDRITVIRDG 227
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKsEHNITIISITHDLSEAME-ADHVIVMNKG 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
14-230 |
3.26e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 73.20 E-value: 3.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGH-----RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGS------------------- 69
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 70 ---KIEIDGKSYHRLTPDKA--RELGVQVIYQDLSLFPNlTVAENIAFELNLKGyfgwFRKKQLREKALEILnELAftid 144
Cdd:PRK13651 83 vleKLVIQKTRFKKIKKIKEirRRVGVVFQFAEYQLFEQ-TIEKDIIFGPVSMG----VSKEEAKKRAAKYI-ELV---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 145 pDTPVQFLPIA-------QRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEI 217
Cdd:PRK13651 153 -GLDESYLQRSpfelsggQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEW 231
|
250
....*....|...
gi 491046221 218 SDRITVIRDGQKI 230
Cdd:PRK13651 232 TKRTIFFKDGKII 244
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
269-486 |
4.13e-14 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 71.88 E-value: 4.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLSRA-GQYR---DINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVklkNNTDAIKRGIGYV 344
Cdd:cd03300 1 IELENVSKFyGGFValdGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI---TNLPPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 345 SEDRltlgAILQQ-SIADNMVISiLDRLKTPWHLIDEK--QCQDIVQ-EWIADLDIkvtdpnnalSTLSGGNQQKVVLAK 420
Cdd:cd03300 78 FQNY----ALFPHlTVFENIAFG-LRLKKLPKAEIKERvaEALDLVQlEGYANRKP---------SQLSGGQQQRVAIAR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 421 WILTRPKVLILDSPTVGVDIGAKDSI---YKLIHRlsGVGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDLKLRKDMqleLKRLQK--ELGITFVFVTHDQEEALTMSDRIAVMNKGKIQ 210
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
268-486 |
4.71e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 72.83 E-value: 4.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 268 VLEIKNLSRagQY------RDINLNLKRGEVlglcgllgsgrteLAL---------SLF----GITHPDSGELFIEGKPV 328
Cdd:COG4152 1 MLELKGLTK--RFgdktavDDVSFTVPKGEI-------------FGLlgpngagktTTIriilGILAPDSGEVLWDGEPL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 329 klknnTDAIKRGIGYVSEDRltlGAILQQSIADNMVisILDRLktpwHLIDEKQCQDIVQEWIADLDIKvtD-PNNALST 407
Cdd:COG4152 66 -----DPEDRRRIGYLPEER---GLYPKMKVGEQLV--YLARL----KGLSKAEAKRRADEWLERLGLG--DrANKKVEE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLIT---DEASEAyynCDRILHMKQGS 484
Cdd:COG4152 130 LSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSShqmELVEEL---CDRIVIINKGR 206
|
..
gi 491046221 485 IV 486
Cdd:COG4152 207 KV 208
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
13-236 |
5.71e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 72.85 E-value: 5.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 13 LITLRDLSKSFGGH----RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISG-------VYApddgSKIEIDGKSYHRL 81
Cdd:PRK11022 3 LLNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGlidypgrVMA----EKLEFNGQDLQRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 82 TPDKAREL---GVQVIYQD--LSLFPNLTVAENI--AFELNLKGyfgwfRKKQLREKALEILNELAFTiDPDTPVQFLP- 153
Cdd:PRK11022 79 SEKERRNLvgaEVAMIFQDpmTSLNPCYTVGFQImeAIKVHQGG-----NKKTRRQRAIDLLNQVGIP-DPASRLDVYPh 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 154 -----IAQRqqVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEISDRITVIRDG 227
Cdd:PRK11022 153 qlsggMSQR--VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAG 230
|
....*....
gi 491046221 228 QKIGTWPAE 236
Cdd:PRK11022 231 QVVETGKAH 239
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
18-228 |
6.57e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 72.98 E-value: 6.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 18 DLSKSFGGHRAlrNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDG-----SKIEIDGKSYHRLTPDKARelgVQ 92
Cdd:PRK11144 5 NFKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGrivlnGRVLFDAEKGICLPPEKRR---IG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 93 VIYQDLSLFPNLTVAENIAFELnlkgyfgwfrKKQLREKALEILNELAftIDPdtPVQFLPIA----QRQQVAICRALVA 168
Cdd:PRK11144 80 YVFQDARLFPHYKVRGNLRYGM----------AKSMVAQFDKIVALLG--IEP--LLDRYPGSlsggEKQRVAIGRALLT 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491046221 169 DARLVIMDEPTASLTRTEVNQLLstvNYL----KDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK11144 146 APELLLMDEPLASLDLPRKRELL---PYLerlaREINIPILYVSHSLDEILRLADRVVVLEQGK 206
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-219 |
6.92e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 71.74 E-value: 6.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 4 TSKADKSDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKT-------ISGVYApdDGsKIEIDGK 76
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndlIPGFRV--EG-KVTFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 77 SYH--RLTPDKARELgVQVIYQDLSLFPNlTVAENIAFELNLKGYFG---WFRKKQLREKAL--EILNELaftidpDTPV 149
Cdd:PRK14243 78 NLYapDVDPVEVRRR-IGMVFQKPNPFPK-SIYDNIAYGARINGYKGdmdELVERSLRQAALwdEVKDKL------KQSG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 150 QFLPIAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKgITVVFVSHRLEEVKEISD 219
Cdd:PRK14243 150 LSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSD 218
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
8-236 |
7.00e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 71.60 E-value: 7.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 8 DKSDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISG--VYAPDDGsKIEIDGKSYHRLTPDK 85
Cdd:CHL00131 2 NKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEG-DILFKGESILDLEPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 86 ARELGVQVIYQDLSLFPNLTVAENIAFELNLKgyfgwfRKKQLREKA-----LEILNELAFTIDPDTpvQFLPI------ 154
Cdd:CHL00131 81 RAHLGIFLAFQYPIEIPGVSNADFLRLAYNSK------RKFQGLPELdplefLEIINEKLKLVGMDP--SFLSRnvnegf 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 155 --AQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSH--RLEEVKeISDRITVIRDGQKI 230
Cdd:CHL00131 153 sgGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHyqRLLDYI-KPDYVHVMQNGKII 231
|
....*.
gi 491046221 231 GTWPAE 236
Cdd:CHL00131 232 KTGDAE 237
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
269-483 |
8.31e-14 |
|
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: 69.52 E-value: 8.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLS-RAGQY---RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPV-KLKNNTDAIKRGIGY 343
Cdd:cd03229 1 LELKNVSkRYGQKtvlNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 344 VsedrltlgailqqsIADNMVISILDRLktpwhlidekqcqdivqewiadldikvtdpNNALSTLSGGNQQKVVLAKWIL 423
Cdd:cd03229 81 V--------------FQDFALFPHLTVL------------------------------ENIALGLSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 424 TRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEASEAYYNCDRILHMKQG 483
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
29-252 |
1.08e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 71.28 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKsyhRLTPDKAREL--GVQVIYQDL-SLFPNLT 105
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGK-VKIDGE---LLTAENVWNLrrKIGMVFQNPdNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 106 VAENIAFELNLKGYFgwfRKKQLR--EKALEILNELAF-TIDPDTpvqfLPIAQRQQVAICRALVADARLVIMDEPTASL 182
Cdd:PRK13642 99 VEDDVAFGMENQGIP---REEMIKrvDEALLAVNMLDFkTREPAR----LSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 183 TRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEiSDRITVIRDGQKIGTWPAEGLTTRKITELMTGLDI 252
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVEIGLDV 241
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
27-232 |
1.35e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 71.20 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 27 RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEI------DGKSYHRLTPDKARelgVQVIYQdlsl 100
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSG-TVTIgervitAGKKNKKLKPLRKK---VGIVFQ---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 101 FPNL-----TVAENIAF-ELNlkgyFGwFRKKQLREKALEILNELAFTIDPDTPVQF-LPIAQRQQVAICRALVADARLV 173
Cdd:PRK13634 93 FPEHqlfeeTVEKDICFgPMN----FG-VSEEDAKQKAREMIELVGLPEELLARSPFeLSGGQMRRVAIAGVLAMEPEVL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491046221 174 IMDEPTASLT---RTEVNQLLSTVNylKDKGITVVFVSHRLEEVKEISDRITVIRDGQ--KIGT 232
Cdd:PRK13634 168 VLDEPTAGLDpkgRKEMMEMFYKLH--KEKGLTTVLVTHSMEDAARYADQIVVMHKGTvfLQGT 229
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
269-486 |
1.60e-13 |
|
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: 69.84 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLS----RAGQY--RDINLNLKRGEVlglcgllgsgrteLAL---------SLF----GITHPDSGELFIEGKPVK 329
Cdd:cd03263 1 LQIRNLTktykKGTKPavDDLSLNVYKGEI-------------FGLlghngagktTTLkmltGELRPTSGTAYINGYSIR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 330 lkNNTDAIKRGIGYVSEDRltlgailqqsiadnmvisILDRLKTPW-HL--------IDEKQCQDIVQEWIADLDIkvTD 400
Cdd:cd03263 68 --TDRKAARQSLGYCPQFD------------------ALFDELTVReHLrfyarlkgLPKSEIKEEVELLLRVLGL--TD 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 401 PNNAL-STLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGvGISILLITDEASEAYYNCDRILH 479
Cdd:cd03263 126 KANKRaRTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK-GRSIILTTHSMDEAEALCDRIAI 204
|
....*..
gi 491046221 480 MKQGSIV 486
Cdd:cd03263 205 MSDGKLR 211
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
16-228 |
1.65e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 70.10 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 16 LRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISG--VYAPDDGSkIEIDGKSYHRLTPDK-AReLGVQ 92
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGS-ILLDGEDILELSPDErAR-AGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 93 VIYQDLSLFPNLTV------AENIAFELNLKGYFgwFRKKqLREKaLEILNelaftIDPDtpvqFL-------------- 152
Cdd:COG0396 81 LAFQYPVEIPGVSVsnflrtALNARRGEELSARE--FLKL-LKEK-MKELG-----LDED----FLdryvnegfsggekk 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 153 --PIAQrqqvaicrALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSH--R-LEEVKeiSDRITVIRDG 227
Cdd:COG0396 148 rnEILQ--------MLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHyqRiLDYIK--PDFVHVLVDG 217
|
.
gi 491046221 228 Q 228
Cdd:COG0396 218 R 218
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
14-228 |
1.78e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 72.70 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHR-ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARELgVQ 92
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSG-EILLDGKPVTAEQPEDYRKL-FS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 93 VIYQDLSLFPNLTVAENiaFELNLKGYFGWFRKKQLREKaLEILNELAFTIDpdtpvqfLPIAQRQQVAICRALVADARL 172
Cdd:PRK10522 401 AVFTDFHLFDQLLGPEG--KPANPALVEKWLERLKMAHK-LELEDGRISNLK-------LSKGQKKRLALLLALAEERDI 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 173 VIMDEPTASLT---RTEVNQLLstVNYLKDKGITVVFVSHRlEEVKEISDRITVIRDGQ 228
Cdd:PRK10522 471 LLLDEWAADQDphfRREFYQVL--LPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQ 526
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
12-221 |
1.81e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.14 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 12 PLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKarelgv 91
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG-VIKRNGKLRIGYVPQK------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 92 qvIYQDLSLfpNLTVAENIAFELNLKgyfgwfrkkqlREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADAR 171
Cdd:PRK09544 76 --LYLDTTL--PLTVNRFLRLRPGTK-----------KEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491046221 172 LVIMDEPTASLtrtEVN---QLLSTVNYLKDK-GITVVFVSHRLEEVKEISDRI 221
Cdd:PRK09544 141 LLVLDEPTQGV---DVNgqvALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEV 191
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
316-494 |
2.11e-13 |
|
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: 69.52 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 316 PDSGELFIEGKPVKLKNNTdaikrgigyVSEDRLTLGAILQQ------SIADNmvISILDRLktpwHLIDEKQCQDIVQE 389
Cdd:cd03260 57 PDEGEVLLDGKDIYDLDVD---------VLELRRRVGMVFQKpnpfpgSIYDN--VAYGLRL----HGIKLKEELDERVE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 390 W---IADLDIKVTDPNNALStLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVgISILLITDE 466
Cdd:cd03260 122 EalrKAALWDEVKDRLHALG-LSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHN 199
|
170 180
....*....|....*....|....*...
gi 491046221 467 ASEAYYNCDRILHMKQGSIVKEIVTDSI 494
Cdd:cd03260 200 MQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
269-485 |
2.42e-13 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 69.68 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLS-RAGQYR---DINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVklkNNTDAIKRGIGYV 344
Cdd:cd03296 3 IEVRNVSkRFGDFValdDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA---TDVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 345 SEDRltlgAILQQ-SIADNMVISILDR---LKTPWHLIDEK--QCQDIVQ-EWIADldikvTDPNNalstLSGGNQQKVV 417
Cdd:cd03296 80 FQHY----ALFRHmTVFDNVAFGLRVKprsERPPEAEIRAKvhELLKLVQlDWLAD-----RYPAQ----LSGGQRQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 418 LAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEASEAYYNCDRILHMKQGSI 485
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLhDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
281-494 |
3.48e-13 |
|
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: 69.11 E-value: 3.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTDAIKRGIGYVSED-----RLTlgail 355
Cdd:cd03218 17 NGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYLPQEasifrKLT----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 356 qqsIADNmVISILDRLKtpwhlIDEKQCQDIVQEWIADLDIKVTDPNNAlSTLSGGNQQKVVLAKWILTRPKVLILDSPT 435
Cdd:cd03218 92 ---VEEN-ILAVLEIRG-----LSKKEREEKLEELLEEFHITHLRKSKA-SSLSGGERRRVEIARALATNPKFLLLDEPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 436 VGVDIGAKDSIYKLIHRLSGVGISIlLITDE-ASEAYYNCDRILHMKQGSIVKEIVTDSI 494
Cdd:cd03218 162 AGVDPIAVQDIQKIIKILKDRGIGV-LITDHnVRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
13-228 |
5.09e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.91 E-value: 5.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 13 LITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKAREL--- 89
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGE-VLWQGEPIRRQRDEYHQDLlyl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 90 ----GVQviyqdlslfPNLTVAENIAFELNLKGYFGwfrkkqlREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRA 165
Cdd:PRK13538 80 ghqpGIK---------TELTALENLRFYQRLHGPGD-------DEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 166 LVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRleEVKEISDRITVIRDGQ 228
Cdd:PRK13538 144 WLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQ--DLPVASDKVRKLRLGQ 204
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
14-228 |
5.43e-13 |
|
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: 67.82 E-value: 5.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGH--RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARElGV 91
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEG-KIEIDGIDISTIPLEDLRS-SL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 92 QVIYQDLSLFPNlTVAENIafelnlkGYFGWFRKKQLREkALEI----LNelaftidpdtpvqfLPIAQRQQVAICRALV 167
Cdd:cd03369 85 TIIPQDPTLFSG-TIRSNL-------DPFDEYSDEEIYG-ALRVseggLN--------------LSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 168 ADARLVIMDEPTASLTrTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEIsDRITVIRDGQ 228
Cdd:cd03369 142 KRPRVLVLDEATASID-YATDALIQKTIREEFTNSTILTIAHRLRTIIDY-DKILVMDAGE 200
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
268-497 |
5.58e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.77 E-value: 5.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 268 VLEIKNLSRAGQYR----DINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTDAIKRGIGY 343
Cdd:PRK10895 3 TLTAKNLAKAYKGRrvveDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 344 VSEDrltlGAILQQ-SIADNM--VISILDRLKTpwhlideKQCQDIVQEWIADLDIKVTDpNNALSTLSGGNQQKVVLAK 420
Cdd:PRK10895 83 LPQE----ASIFRRlSVYDNLmaVLQIRDDLSA-------EQREDRANELMEEFHIEHLR-DSMGQSLSGGERRRVEIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 421 WILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVKEIVTDSI--NEQ 497
Cdd:PRK10895 151 ALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIlqDEH 229
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
28-228 |
5.73e-13 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 69.07 E-value: 5.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 28 ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKsyhrltpdkarelgVQVIYQDLSLFPNLTVA 107
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVG-KVDRNGE--------------VSVIAISAGLSGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 108 ENIAFELNLKGyfgwFRKKQLREKALEIL--NELAFTIdpDTPVQFLPIAQRQQVAICRALVADARLVIMDEPTASLTRT 185
Cdd:PRK13546 104 ENIEFKMLCMG----FKRKEIKAMTPKIIefSELGEFI--YQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491046221 186 EVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK13546 178 FAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGK 220
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-238 |
7.95e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 68.97 E-value: 7.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 2 TSTSKADKSDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIEID----GKS 77
Cdd:PRK14271 10 SGAADVDAAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDvllgGRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 78 Y--HRLTPDKARELGVqvIYQDLSLFPnLTVAENI-----AFELNLKGYFGWFRKKQLREKAL--EILNELAftidpDTP 148
Cdd:PRK14271 90 IfnYRDVLEFRRRVGM--LFQRPNPFP-MSIMDNVlagvrAHKLVPRKEFRGVAQARLTEVGLwdAVKDRLS-----DSP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 149 VQfLPIAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKgITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK14271 162 FR-LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGR 239
|
250
....*....|
gi 491046221 229 KIGTWPAEGL 238
Cdd:PRK14271 240 LVEEGPTEQL 249
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
10-250 |
9.35e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 68.28 E-value: 9.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 10 SDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTIsGVYAPDDGSKIEIDGKSyhrLTPDKAREL 89
Cdd:PRK10575 8 SDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPSEGEILLDAQP---LESWSSKAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 90 GVQVIY--QDLSLFPNLTVAENIAF-ELNLKGYFGWFRKKQlREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRAL 166
Cdd:PRK10575 84 ARKVAYlpQQLPAAEGMTVRELVAIgRYPWHGALGRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 167 VADARLVIMDEPTASLTRTEVNQLLSTVNYL-KDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITE 245
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLE 242
|
....*
gi 491046221 246 LMTGL 250
Cdd:PRK10575 243 QIYGI 247
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
26-439 |
1.03e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 70.04 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 26 HRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKiEIDGKSYHRLTPDKARELgVQVIYQD-----LSL 100
Cdd:PRK10938 16 TKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGER-QSQFSHITRLSFEQLQKL-VSDEWQRnntdmLSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 101 FPN---LTVAENIafelnlkgyfgwfrkkQLREKALEILNELA--FTIDP--DTPVQFLPIAQRQQVAICRALVADARLV 173
Cdd:PRK10938 94 GEDdtgRTTAEII----------------QDEVKDPARCEQLAqqFGITAllDRRFKYLSTGETRKTLLCQALMSEPDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 174 IMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKI------TELM 247
Cdd:PRK10938 158 ILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALvaqlahSEQL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 248 TGLDI-------VHERKPPNNAedrRTVLeiknlsRAG--QYRD------INLNLKRGEVLGLCGLLGSGRTELaLSLFG 312
Cdd:PRK10938 238 EGVQLpepdepsARHALPANEP---RIVL------NNGvvSYNDrpilhnLSWQVNPGEHWQIVGPNGAGKSTL-LSLIT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 313 ITHPD--SGELFIEGKPVKLKNNTDAIKRGIGYVSeDRLTLGAILQQSIADNMVISILDRLKTpWHLIDEKQcQDIVQEW 390
Cdd:PRK10938 308 GDHPQgySNDLTLFGRRRGSGETIWDIKKHIGYVS-SSLHLDYRVSTSVRNVILSGFFDSIGI-YQAVSDRQ-QKLAQQW 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 491046221 391 IADLDIKVTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVD 439
Cdd:PRK10938 385 LDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
270-488 |
1.24e-12 |
|
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: 66.30 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 270 EIKNLS-RAGQY---RDINLNLKRGEVlglcgllgsgrteLAL-------------SLFGITHPDSGELFIEGKPVKLKN 332
Cdd:cd03214 1 EVENLSvGYGGRtvlDDLSLSIEAGEI-------------VGIlgpngagkstllkTLAGLLKPSSGEILLDGKDLASLS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 333 NTDAIKRgIGYVSEdrltlgailqqsiadnmvisILDRLKTpWHLIDEKqcqdivqewiadldikvtdpnnaLSTLSGGN 412
Cdd:cd03214 68 PKELARK-IAYVPQ--------------------ALELLGL-AHLADRP-----------------------FNELSGGE 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 413 QQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSG-VGISILLITDEASEAYYNCDRILHMKQGSIVKE 488
Cdd:cd03214 103 RQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
268-488 |
1.36e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 68.18 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 268 VLEIKNLSRAgqYRD-------INLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTdaikrg 340
Cdd:PRK13639 1 ILETRDLKYS--YPDgtealkgINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKS------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 341 igyVSEDRLTLGAILQQSiaDNMVISIL---DRLKTPWHL-IDEKQCQDIVQEWIADLDIKVTDpNNALSTLSGGNQQKV 416
Cdd:PRK13639 73 ---LLEVRKTVGIVFQNP--DDQLFAPTveeDVAFGPLNLgLSKEEVEKRVKEALKAVGMEGFE-NKPPHHLSGGQKKRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491046221 417 VLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVKE 488
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKE 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
281-488 |
1.56e-12 |
|
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: 67.01 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGkpVKLKNNTDAIKRGIGYVSE-----DRLTLGAIL 355
Cdd:cd03266 22 DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAEARRRLGFVSDstglyDRLTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 356 QqsiadnmvisILDRLktpwHLIDEKQCQDIVQEWIADLDIKVTdPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPT 435
Cdd:cd03266 100 E----------YFAGL----YGLKGDELTARLEELADRLGMEEL-LDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491046221 436 VGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVKE 488
Cdd:cd03266 165 TGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
27-230 |
1.82e-12 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 66.91 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 27 RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVyAPDDGSK---IEIDGKSyhrLTPDKARELgVQVIYQDLSLFPN 103
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR-VEGGGTTsgqILFNGQP---RKPDQFQKC-VAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 104 LTVAENIAFELNLKGYFGwFRKKQLREK-ALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLVIMDEPTASL 182
Cdd:cd03234 96 LTVRETLTYTAILRLPRK-SSDAIRKKRvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491046221 183 TRTEVNQLLSTVNYLKDKGITVVFVSHR-LEEVKEISDRITVIRDGQKI 230
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIV 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
269-485 |
2.03e-12 |
|
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: 66.36 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLSRagQY----------RDINLNLKRGEVLGLCGLLGSGRTELaLSLF-GITHPDSGELFIEGKPV-KLKNNTDA 336
Cdd:cd03255 1 IELKNLSK--TYggggekvqalKGVSLSIEKGEFVAIVGPSGSGKSTL-LNILgGLDRPTSGEVRVDGTDIsKLSEKELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 337 IKRgigyvsedRLTLGAILQQSiadNMV--ISILDRLKTPWHL--IDEKQCQDIVQEWIADLDIKvtdpnNAL----STL 408
Cdd:cd03255 78 AFR--------RRHIGFVFQSF---NLLpdLTALENVELPLLLagVPKKERRERAEELLERVGLG-----DRLnhypSEL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 409 SGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLS-GVGISILLITDEASEAYYnCDRILHMKQGSI 485
Cdd:cd03255 142 SGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
264-486 |
2.23e-12 |
|
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: 66.93 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 264 DRRTVLEIKNL--SRAGQ--YRDINLNLKRGEVlglcgllgsgrteLAL-------------SLFGITHPDSGELFIEGK 326
Cdd:COG1127 1 MSEPMIEVRNLtkSFGDRvvLDGVSLDVPRGEI-------------LAIiggsgsgksvllkLIIGLLRPDSGEILVDGQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 327 PV-KLKNNT-DAIKRGIGYVsedrltlgaiLQQ-------SIADNMVISILDRLKtpwhlIDEKQCQDIVQEWIADLDIK 397
Cdd:COG1127 68 DItGLSEKElYELRRRIGML----------FQGgalfdslTVFENVAFPLREHTD-----LSEAEIRELVLEKLELVGLP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 398 vtdpnNAL----STLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGV-GISILLITDEASEAYY 472
Cdd:COG1127 133 -----GAAdkmpSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFA 207
|
250
....*....|....
gi 491046221 473 NCDRILHMKQGSIV 486
Cdd:COG1127 208 IADRVAVLADGKII 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
281-486 |
2.59e-12 |
|
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: 66.56 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKlknNTDAIK--RGIGYVSEDrltLGAILQQS 358
Cdd:cd03295 18 NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIR---EQDPVElrRKIGYVIQQ---IGLFPHMT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 359 IADNmvISILDRLKTpWhliDEKQCQDIVQEWIADLDIkvtDPNNAL----STLSGGNQQKVVLAKWILTRPKVLILDSP 434
Cdd:cd03295 92 VEEN--IALVPKLLK-W---PKEKIRERADELLALVGL---DPAEFAdrypHELSGGQQQRVGVARALAADPPLLLMDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491046221 435 TVGVDIGAKDSIYKLIHRL-SGVGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:cd03295 163 FGALDPITRDQLQEEFKRLqQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIV 215
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
312-487 |
2.63e-12 |
|
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: 66.16 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 312 GITHPDSGELFIEGKPV---KLKNNTDAIKRGIGYVsedrltlgaiLQQ-------SIADNMVISIldRLKTPwhlideK 381
Cdd:cd03297 45 GLEKPDGGTIVLNGTVLfdsRKKINLPPQQRKIGLV----------FQQyalfphlNVRENLAFGL--KRKRN------R 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 382 QCQDIVQEWIADLDIkvtDP--NNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSG-VGI 458
Cdd:cd03297 107 EDRISVDELLDLLGL---DHllNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKnLNI 183
|
170 180
....*....|....*....|....*....
gi 491046221 459 SILLITDEASEAYYNCDRILHMKQGSIVK 487
Cdd:cd03297 184 PVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
20-230 |
2.69e-12 |
|
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: 65.75 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 20 SKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYapddGSKIEIDGK-SYHRLTPDKARE-LGVQVIY-- 95
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRT----EGNVSVEGDiHYNGIPYKEFAEkYPGEIIYvs 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 96 QDLSLFPNLTVAENIAFELNLKGyfgwfrkkqlrekaleilNELaftidpdtpVQFLPIAQRQQVAICRALVADARLVIM 175
Cdd:cd03233 90 EEDVHFPTLTVRETLDFALRCKG------------------NEF---------VRGISGGERKRVSIAEALVSRASVLCW 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 176 DEPTASLTRTEVNQLLSTVNYLKD--KGITVVFVSHRLEEVKEISDRITVIRDGQKI 230
Cdd:cd03233 143 DNSTRGLDSSTALEILKCIRTMADvlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
28-248 |
3.11e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 67.57 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 28 ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGS----------KIEIDGKSYHRLTP-----DKARELgVQ 92
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTiqvgdiyigdKKNNHELITNPYSKkiknfKELRRR-VS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 93 VIYQ--DLSLFPNlTVAENIAF-ELNLKgyfgwFRKKQLREKALEILNELAFTID--PDTPVQfLPIAQRQQVAICRALV 167
Cdd:PRK13631 120 MVFQfpEYQLFKD-TIEKDIMFgPVALG-----VKKSEAKKLAKFYLNKMGLDDSylERSPFG-LSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 168 ADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ--KIGTwPAEGLTTRKITE 245
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKilKTGT-PYEIFTDQHIIN 271
|
...
gi 491046221 246 LMT 248
Cdd:PRK13631 272 STS 274
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
2-228 |
3.42e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.44 E-value: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 2 TSTSKADKSDPLITLRDLSKSF----GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPD---DGSKI--- 71
Cdd:PRK09473 1 TVPLAQQQADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATfng 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 72 -EIDGKSYHRLTPDKARElgVQVIYQD--LSLFPNLTVAENIAFELNL-KGYfgwfRKKQLREKALEILNELAFtidPDT 147
Cdd:PRK09473 81 rEILNLPEKELNKLRAEQ--ISMIFQDpmTSLNPYMRVGEQLMEVLMLhKGM----SKAEAFEESVRMLDAVKM---PEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 148 -------PVQFlPIAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDK-GITVVFVSHRLEEVKEISD 219
Cdd:PRK09473 152 rkrmkmyPHEF-SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICD 230
|
....*....
gi 491046221 220 RITVIRDGQ 228
Cdd:PRK09473 231 KVLVMYAGR 239
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
282-501 |
4.16e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 66.19 E-value: 4.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 282 DINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTDAIKrgigyVSEDRLTLGAILQQ---- 357
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKA-----IRELRRNVGMVFQQynlw 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 358 ---SIADNMV---ISILDrlktpwhlIDEKQCQDIVQEWIADLdiKVTDPNNALST-LSGGNQQKVVLAKWILTRPKVLI 430
Cdd:PRK11124 95 phlTVQQNLIeapCRVLG--------LSKDQALARAEKLLERL--RLKPYADRFPLhLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 431 LDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVKEIVTDSINEQQLEE 501
Cdd:PRK11124 165 FDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQPQTEA 235
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
10-236 |
4.54e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.44 E-value: 4.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 10 SDPLITLRDLSKSF-GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARE 88
Cdd:PRK15056 3 QQAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASG-KISILGQPTRQALQKNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 89 LGVQVIYQDLSlFPNLTvaENIAFeLNLKGYFGWFRK-----KQLREKALEILNELAFTidpDTPVQFLPIAQRQQVAIC 163
Cdd:PRK15056 82 YVPQSEEVDWS-FPVLV--EDVVM-MGRYGHMGWLRRakkrdRQIVTAALARVDMVEFR---HRQIGELSGGQKKRVFLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491046221 164 RALVADARLVIMDEP-TASLTRTEVnQLLSTVNYLKDKGITVVFVSHRLEEVKEISDrITVIRDGQKIGTWPAE 236
Cdd:PRK15056 155 RAIAQQGQVILLDEPfTGVDVKTEA-RIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTE 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
281-488 |
5.12e-12 |
|
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: 65.59 E-value: 5.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTdAIKRGIGYVSEDRLtlgaILQQSIA 360
Cdd:cd03252 19 DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPA-WLRRQVGVVLQENV----LFNRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 361 DNMVisiLDRLKTPWHLIDEKQCQDIVQEWIADL----DIKVTDPNnalSTLSGGNQQKVVLAKWILTRPKVLILDSPTV 436
Cdd:cd03252 94 DNIA---LADPGMSMERVIEAAKLAGAHDFISELpegyDTIVGEQG---AGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491046221 437 GVDIGAKDSIYKLIHRLSGvGISILLITDEASeAYYNCDRILHMKQGSIVKE 488
Cdd:cd03252 168 ALDYESEHAIMRNMHDICA-GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQ 217
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
27-228 |
5.51e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 66.31 E-value: 5.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 27 RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGS----KIEIDGKSYHRLTPDKARELGVQVIYQDLSLFP 102
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSvrvdDTLITSTSKNKDIKQIRKKVGLVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 103 NlTVAENIAFELNLKGYFGWFRKKQLREK-ALEILNELAFTIDPdtpvqF-LPIAQRQQVAICRALVADARLVIMDEPTA 180
Cdd:PRK13649 101 E-TVLKDVAFGPQNFGVSQEEAEALAREKlALVGISESLFEKNP-----FeLSGGQMRRVAIAGILAMEPKILVLDEPTA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491046221 181 SLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK13649 175 GLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGK 222
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
303-505 |
6.52e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 66.78 E-value: 6.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 303 RTELALSLFGITHPDSGELFIEGKPVKLKnnTDAIKRGIGYVSE-DRLTLGAILQQSIadnMVISILDRLKTpwhlideK 381
Cdd:PRK13536 80 KSTIARMILGMTSPDAGKITVLGVPVPAR--ARLARARIGVVPQfDNLDLEFTVRENL---LVFGRYFGMST-------R 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 382 QCQDIVQEWI--ADLDIKVtdpNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGIS 459
Cdd:PRK13536 148 EIEAVIPSLLefARLESKA---DARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKT 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491046221 460 ILLITDEASEAYYNCDRILHMKQG-SIVKEIVTDSINEQ---QLEEIING 505
Cdd:PRK13536 225 ILLTTHFMEEAERLCDRLCVLEAGrKIAEGRPHALIDEHigcQVIEIYGG 274
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
269-489 |
7.11e-12 |
|
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: 64.55 E-value: 7.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLSRA-GQYR---DINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKpvKLKNNTDAIKRgigyv 344
Cdd:cd03268 1 LKTNDLTKTyGKKRvldDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--SYQKNIEALRR----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 345 sedrltLGAILQ-QSIADNMV----ISILDRLktpwHLIDEKQCQDIVQEW----IADLDIKvtdpnnalsTLSGGNQQK 415
Cdd:cd03268 74 ------IGALIEaPGFYPNLTarenLRLLARL----LGIRKKRIDEVLDVVglkdSAKKKVK---------GFSLGMKQR 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 416 VVLAKWILTRPKVLILDSPTVGVD-IGAKDsIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVKEI 489
Cdd:cd03268 135 LGIALALLGNPDLLILDEPTNGLDpDGIKE-LRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
12-228 |
9.85e-12 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 67.22 E-value: 9.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 12 PLITLRDLSKSFGG---HRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSyhrltpdkare 88
Cdd:PRK13545 20 PFDKLKDLFFRSKDgeyHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKG-TVDIKGSA----------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 89 lgvQVIYQDLSLFPNLTVAENIafelNLKGYFGWFRKKQLREKALEILNELAFTIDPDTPVQFLPIAQRQQVAICRALVA 168
Cdd:PRK13545 88 ---ALIAISSGLNGQLTGIENI----ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 169 DARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK13545 161 NPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQ 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
281-486 |
1.39e-11 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 63.81 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVklkNNTDAIKRGIGYVsedrltlgaiLQQ--- 357
Cdd:cd03301 17 DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV---TDLPPKDRDIAMV----------FQNyal 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 358 ----SIADNMVISiLDRLKTPWHLIDEKqcqdiVQEWIADLDIKvTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDS 433
Cdd:cd03301 84 yphmTVYDNIAFG-LKLRKVPKDEIDER-----VREVAELLQIE-HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 434 PTVGVD----IGAKDSIYKLIHRLsgvGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:cd03301 157 PLSNLDaklrVQMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
283-486 |
1.86e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 63.74 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 283 INLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPV-KLKNN-TDAIKRGIGYVSEDRLTLgaiLQQSIA 360
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItRLKNReVPFLRRQIGMIFQDHHLL---MDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 361 DNMVISILdrlktpwhlIDEKQCQDIVQEWIADLDiKVTDPNNALS---TLSGGNQQKVVLAKWILTRPKVLILDSPTVG 437
Cdd:PRK10908 98 DNVAIPLI---------IAGASGDDIRRRVSAALD-KVGLLDKAKNfpiQLSGGEQQRVGIARAVVNKPAVLLADEPTGN 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491046221 438 VDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:PRK10908 168 LDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
14-483 |
2.52e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 66.30 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDG----KSYHRltpdkaREL 89
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGR-VEVLGgdmaDARHR------RAV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 90 GVQVIY--QDL--SLFPNLTVAENIAFELNLkgyFGwFRKKQLREKALEILNE---LAFtidPDTPVQFLPIAQRQQVAI 162
Cdd:NF033858 75 CPRIAYmpQGLgkNLYPTLSVFENLDFFGRL---FG-QDAAERRRRIDELLRAtglAPF---ADRPAGKLSGGMKQKLGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 163 CRALVADARLVIMDEPTAS---LTRtevNQLLSTVNYLKDK--GITVVFVSHRLEEVkEISDRITVIRDGQKIGTWPAEG 237
Cdd:NF033858 148 CCALIHDPDLLILDEPTTGvdpLSR---RQFWELIDRIRAErpGMSVLVATAYMEEA-ERFDWLVAMDAGRVLATGTPAE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 238 LTTRkitelmTG---LD--IVH----ERK---------PPNNAEDRRTVLEIKNLS-RAGQY---RDINLNLKRGEVlgl 295
Cdd:NF033858 224 LLAR------TGadtLEaaFIAllpeEKRrghqpvvipPRPADDDDEPAIEARGLTmRFGDFtavDHVSFRIRRGEI--- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 296 cgllgsgrtelalslFG---------------IT---HPDSGE--LFieGKPVKLKNNtdAIKRGIGYVSE--------- 346
Cdd:NF033858 295 ---------------FGflgsngcgksttmkmLTgllPASEGEawLF--GQPVDAGDI--ATRRRVGYMSQafslygelt 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 347 --DRLTLGAilqqsiadnmvisildRLktpWHLiDEKQCQDIVQEWIADLDIK-VTDpnnAL-STLSGGNQQKVVLAKWI 422
Cdd:NF033858 356 vrQNLELHA----------------RL---FHL-PAAEIAARVAEMLERFDLAdVAD---ALpDSLPLGIRQRLSLAVAV 412
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 423 LTRPKVLILDSPTVGVDIGAKDSIYKLIHRLS---GVGISIllitdeaSEAYYN----CDRILHMKQG 483
Cdd:NF033858 413 IHKPELLILDEPTSGVDPVARDMFWRLLIELSredGVTIFI-------STHFMNeaerCDRISLMHAG 473
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
273-494 |
2.54e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 63.94 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 273 NLSRAGQY----RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPV-KLKN-NTDAIKRGIGYVSE 346
Cdd:PRK10419 17 GLSGKHQHqtvlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaKLNRaQRKAFRRDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 347 D-------RLTLGAILQQSIAdnmvisildrlktpwHL--IDEKQCQDIVQEWIADLDIKVTDPNNALSTLSGGNQQKVV 417
Cdd:PRK10419 97 DsisavnpRKTVREIIREPLR---------------HLlsLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVC 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 418 LAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSG-VGISILLITDEASEAYYNCDRILHMKQGSIVKEI-VTDSI 494
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQpVGDKL 240
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
269-492 |
2.77e-11 |
|
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: 63.26 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLSRAgqYR----------DINLNLKRGEVlglcgllgsgrteLAL---------SLF----GITHPDSGELFIEG 325
Cdd:cd03293 1 LEVRNVSKT--YGggggavtaleDISLSVEEGEF-------------VALvgpsgcgksTLLriiaGLERPTSGEVLVDG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 326 KPVKlknntdAIKRGIGYVsedrltlgaiLQQ-------SIADNmvISILDRLKtpwhLIDEKQCQDIVQEWIADLDIKv 398
Cdd:cd03293 66 EPVT------GPGPDRGYV----------FQQdallpwlTVLDN--VALGLELQ----GVPKAEARERAEELLELVGLS- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 399 tDPNNAL-STLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEASEAYYNCDR 476
Cdd:cd03293 123 -GFENAYpHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADR 201
|
250
....*....|....*...
gi 491046221 477 ILHMKQ--GSIVKEIVTD 492
Cdd:cd03293 202 VVVLSArpGRIVAEVEVD 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
269-485 |
4.80e-11 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 62.16 E-value: 4.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLSRA-GQY---RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKL-KNNTDAIKRGIGY 343
Cdd:cd03262 1 IEIKNLHKSfGDFhvlKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 344 VsedrltlgaiLQQ-------SIADNMVISILDRLKtpwhlIDEKQCQDIVQEWIAdlDIKVTDPNNAL-STLSGGNQQK 415
Cdd:cd03262 81 V----------FQQfnlfphlTVLENITLAPIKVKG-----MSKAEAEERALELLE--KVGLADKADAYpAQLSGGQQQR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 416 VVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSI 485
Cdd:cd03262 144 VAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
15-228 |
5.10e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.29 E-value: 5.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 15 TLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISG-VYAPDDGSKIEIDGKsyhRLTPDKARELGVqv 93
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQGNNFTGTILANNR---KPTKQILKRTGF-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 94 IYQDLSLFPNLTVAENIAFELNLKGYFGWFRKKQLReKALEILNELAF-----TIDPDTPVQFLPIAQRQQVAICRALVA 168
Cdd:PLN03211 145 VTQDDILYPHLTVRETLVFCSLLRLPKSLTKQEKIL-VAESVISELGLtkcenTIIGNSFIRGISGGERKRVSIAHEMLI 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 169 DARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHR-LEEVKEISDRITVIRDGQ 228
Cdd:PLN03211 224 NPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
310-488 |
5.43e-11 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 62.21 E-value: 5.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 310 LFGITHPDSGELFIEGKPVKlkNNTDAIKRGIGYVSEDrltlgailqQSIADNM-VISILD---RLKTpwhlIDEKQCQD 385
Cdd:cd03264 45 LATLTPPSSGTIRIDGQDVL--KQPQKLRRRIGYLPQE---------FGVYPNFtVREFLDyiaWLKG----IPSKEVKA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 386 IVQEWIADLDikVTDPNN-ALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLsGVGISILLIT 464
Cdd:cd03264 110 RVDEVLELVN--LGDRAKkKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSEL-GEDRIVILST 186
|
170 180
....*....|....*....|....
gi 491046221 465 DEASEAYYNCDRILHMKQGSIVKE 488
Cdd:cd03264 187 HIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
263-502 |
6.13e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.85 E-value: 6.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 263 EDRRTVLEIKNLSRagQYR--------DINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNT 334
Cdd:PRK13648 2 EDKNSIIVFKNVSF--QYQsdasftlkDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 335 DaIKRGIGYV--SEDRLTLGAILQQSIA---DNmvisildrlktpwHLIDEKQCQDIVQEWIADLDIkVTDPNNALSTLS 409
Cdd:PRK13648 80 K-LRKHIGIVfqNPDNQFVGSIVKYDVAfglEN-------------HAVPYDEMHRRVSEALKQVDM-LERADYEPNALS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 410 GGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEASEAyYNCDRILHMKQGSIVKE 488
Cdd:PRK13648 145 GGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEA-MEADHVIVMNKGTVYKE 223
|
250
....*....|....*.
gi 491046221 489 IVTDSI--NEQQLEEI 502
Cdd:PRK13648 224 GTPTEIfdHAEELTRI 239
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
30-215 |
7.10e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.05 E-value: 7.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 30 RNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIEIDGKSYHRLTPDKARElGVQVIYQDLSLFPNlTVAEN 109
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKWWRS-KIGVVSQDPLLFSN-SIKNN 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 110 IAFEL-NLK---------------GYFGWFRKKQLREKALEILNELAFTIDPDTPVQF---------------------- 151
Cdd:PTZ00265 480 IKYSLySLKdlealsnyynedgndSQENKNKRNSCRAKCAGDLNDMSNTTDSNELIEMrknyqtikdsevvdvskkvlih 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 152 --------------------LPIAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLK--DKGITVVfVSH 209
Cdd:PTZ00265 560 dfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITII-IAH 638
|
....*.
gi 491046221 210 RLEEVK 215
Cdd:PTZ00265 639 RLSTIR 644
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
14-104 |
7.61e-11 |
|
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: 64.43 E-value: 7.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRN-----IDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARE 88
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGftlgpIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGE-ILLDGQPVTADNREAYRQ 406
|
90
....*....|....*.
gi 491046221 89 LgVQVIYQDLSLFPNL 104
Cdd:COG4615 407 L-FSAVFSDFHLFDRL 421
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-223 |
1.16e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.67 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 3 STSKADKSDPLITLRDLSKSFGGHRaLRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGK-SY--H 79
Cdd:PRK13409 330 PPRDESERETLVEYPDLTKKLGDFS-LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGE-VDPELKiSYkpQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 80 RLTPDkarelgvqviyqdlslfPNLTVAENIAfelNLKGYFG--WFRkkqlrekaLEILNELAftIDP--DTPVQFLPIA 155
Cdd:PRK13409 408 YIKPD-----------------YDGTVEDLLR---SITDDLGssYYK--------SEIIKPLQ--LERllDKNVKDLSGG 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491046221 156 QRQQVAICRALVADARLVIMDEPTASLtrtEVNQLLSTV----NYLKDKGITVVFVSHRLEEVKEISDRITV 223
Cdd:PRK13409 458 ELQRVAIAACLSRDADLYLLDEPSAHL---DVEQRLAVAkairRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
307-486 |
1.24e-10 |
|
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: 60.64 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 307 ALSLFGITHPDSGELFIEGKPVKLKNntdaIKRGIGYVSEDRLTLGailQQSIADNMVISIldrlktpwhlidekqcqdi 386
Cdd:cd03213 54 ALAGRRTGLGVSGEVLINGRPLDKRS----FRKIIGYVPQDDILHP---TLTVRETLMFAA------------------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 387 vqewiadldikvtdpnnALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDE 466
Cdd:cd03213 108 -----------------KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQ 170
|
170 180
....*....|....*....|.
gi 491046221 467 AS-EAYYNCDRILHMKQGSIV 486
Cdd:cd03213 171 PSsEIFELFDKLLLLSQGRVI 191
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
268-488 |
1.38e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 62.03 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 268 VLEIKNL-------SRAGQYRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTDaIKRG 340
Cdd:PRK13642 4 ILEVENLvfkyekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWN-LRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 341 IGYVSE--DRLTLGAILQQSIADNMVISILDRlktpwhlidEKQCQDIVQEWIA--DLDIKVTDPnnalSTLSGGNQQKV 416
Cdd:PRK13642 83 IGMVFQnpDNQFVGATVEDDVAFGMENQGIPR---------EEMIKRVDEALLAvnMLDFKTREP----ARLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 417 VLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSG-VGISILLITDEASEAyYNCDRILHMKQGSIVKE 488
Cdd:PRK13642 150 AVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEkYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKE 221
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
247-486 |
1.39e-10 |
|
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: 63.70 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 247 MTGLDIVHErKPPNNAEDRRTV--------LEIKNLS----RAGQY--RDINLNLKRGEVlglcgllgsgrteLALS--- 309
Cdd:COG2274 445 LERLDDILD-LPPEREEGRSKLslprlkgdIELENVSfrypGDSPPvlDNISLTIKPGER-------------VAIVgrs 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 310 ----------LFGITHPDSGELFIEGKPVKlKNNTDAIKRGIGYVSEDrltlGAILQQSIADNmvISI------LDRLkt 373
Cdd:COG2274 511 gsgkstllklLLGLYEPTSGRILIDGIDLR-QIDPASLRRQIGVVLQD----VFLFSGTIREN--ITLgdpdatDEEI-- 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 374 pWHLIDEKQCQDIVQEWIADLDIKVTDPNnalSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL 453
Cdd:COG2274 582 -IEAARLAGLHDFIEALPMGYDTVVGEGG---SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL 657
|
250 260 270
....*....|....*....|....*....|...
gi 491046221 454 SGvGISILLITDEASeAYYNCDRILHMKQGSIV 486
Cdd:COG2274 658 LK-GRTVIIIAHRLS-TIRLADRIIVLDKGRIV 688
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
312-488 |
1.63e-10 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 61.20 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 312 GITHPDSGELFIEGKPVklknnTD------AiKRGIGYVSED-----RLTlgailqqsIADNmVISILDRLKtpwhlIDE 380
Cdd:COG1137 51 GLVKPDSGRIFLDGEDI-----THlpmhkrA-RLGIGYLPQEasifrKLT--------VEDN-ILAVLELRK-----LSK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 381 KQCQDIVQEWIADLDI-KVTDpNNALStLSGGNQQKVVLAKWILTRPKVLILDSPTVGVD-IGAKDsIYKLIHRLSGVGI 458
Cdd:COG1137 111 KEREERLEELLEEFGItHLRK-SKAYS-LSGGERRRVEIARALATNPKFILLDEPFAGVDpIAVAD-IQKIIRHLKERGI 187
|
170 180 190
....*....|....*....|....*....|....*....
gi 491046221 459 SIlLITDeaseayYN-------CDR--ILHmkQGSIVKE 488
Cdd:COG1137 188 GV-LITD------HNvretlgiCDRayIIS--EGKVLAE 217
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
29-228 |
2.36e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 62.76 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPD--DGSKIEIDGksyHRLTPDKARELGVQVIYQDLsLFPNLTV 106
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkGSGSVLLNG---MPIDAKEMRAISAYVQQDDL-FIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 107 AENIAF--ELNLKGYFGwfrKKQLREKALEILNELAFTIDPDT------PVQFLPIAQRQQVAICRALVADARLVIMDEP 178
Cdd:TIGR00955 117 REHLMFqaHLRMPRRVT---KKEKRERVDEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491046221 179 TASLTRTEVNQLLSTVNYLKDKGITVVFVSHR-LEEVKEISDRITVIRDGQ 228
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGR 244
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
281-488 |
3.09e-10 |
|
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: 60.29 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTD--AIKRGIGYVSEDrltLGAILQQS 358
Cdd:cd03258 22 KDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrKARRRIGMIFQH---FNLLSSRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 359 IADNmVISILDRLKTPWHLIDEKqcqdiVQEWIADLDIkvTDPNNAL-STLSGGNQQKVVLAKWILTRPKVLILDSPTVG 437
Cdd:cd03258 99 VFEN-VALPLEIAGVPKAEIEER-----VLELLELVGL--EDKADAYpAQLSGGQKQRVGIARALANNPKVLLCDEATSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491046221 438 VDIGAKDSIYKLIHRL-SGVGISILLITDEASEAYYNCDRILHMKQGSIVKE 488
Cdd:cd03258 171 LDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEE 222
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-228 |
4.60e-10 |
|
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: 59.41 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 20 SKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGK-SYhrltpdkarelgvqviyqdL 98
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGS-VSVPGSiAY-------------------V 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 99 SLFP---NLTVAENIAF--ELNlkgyfgwfrkKQLREKALEilnelAFTIDPDtpVQFLP-----------IA----QRQ 158
Cdd:cd03250 72 SQEPwiqNGTIRENILFgkPFD----------EERYEKVIK-----ACALEPD--LEILPdgdlteigekgINlsggQKQ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 159 QVAICRALVADARLVIMDEPtasltrtevnqlLSTV-----NYLKDKGI--------TVVFVSHRLEEVKEiSDRITVIR 225
Cdd:cd03250 135 RISLARAVYSDADIYLLDDP------------LSAVdahvgRHIFENCIlglllnnkTRILVTHQLQLLPH-ADQIVVLD 201
|
...
gi 491046221 226 DGQ 228
Cdd:cd03250 202 NGR 204
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
282-488 |
4.72e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 60.49 E-value: 4.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 282 DINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTDAIKRGIGYVSE--DRLTLGAILQQSI 359
Cdd:PRK13633 28 DVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQnpDNQIVATIVEEDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 360 A---DNMVI---SILDRlktpwhlIDEkqCQDIVQEWiadlDIKVTDPNnalsTLSGGNQQKVVLAKWILTRPKVLILDS 433
Cdd:PRK13633 108 AfgpENLGIppeEIRER-------VDE--SLKKVGMY----EYRRHAPH----LLSGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 434 PTVGVDIGAKDSIYKLIHRLSGV-GISILLIT---DEASEAyyncDRILHMKQGSIVKE 488
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELNKKyGITIILIThymEEAVEA----DRIIVMDSGKVVME 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-223 |
6.58e-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: 61.34 E-value: 6.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 2 TSTSKADKSDPLITLRDLSKSFGGHRalrnidLTLNKGEVHC-----LAGTNGCGKSTLIKTISGVYAPDDGskiEIDGK 76
Cdd:COG1245 330 HAPRREKEEETLVEYPDLTKSYGGFS------LEVEGGEIREgevlgIVGPNGIGKTTFAKILAGVLKPDEG---EVDED 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 77 syhrltpdkarelgVQVIY--QDLSLFPNLTVAENIaFELNLKGYFG-WFRkkqlrekaLEILNELAftIDP--DTPVQF 151
Cdd:COG1245 401 --------------LKISYkpQYISPDYDGTVEEFL-RSANTDDFGSsYYK--------TEIIKPLG--LEKllDKNVKD 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 152 LPIAQRQQVAICRALVADARLVIMDEPTASLtrtEVNQLLSTV----NYLKDKGITVVFVSHRLEEVKEISDRITV 223
Cdd:COG1245 456 LSGGELQRVAIAACLSRDADLYLLDEPSAHL---DVEQRLAVAkairRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-210 |
7.11e-10 |
|
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: 57.93 E-value: 7.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLS-KSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYaPDDGSKIEIdgksyhrltPDKARELGV- 91
Cdd:cd03223 1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLW-PWGSGRIGM---------PEGEDLLFLp 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 92 QVIYqdlslFPNLTVAENIAFElnlkgyfgWFRKkqlrekaleilnelaftidpdtpvqfLPIAQRQQVAICRALVADAR 171
Cdd:cd03223 71 QRPY-----LPLGTLREQLIYP--------WDDV--------------------------LSGGEQQRLAFARLLLHKPK 111
|
170 180 190
....*....|....*....|....*....|....*....
gi 491046221 172 LVIMDEPTASLTRTEVNQLLSTvnyLKDKGITVVFVSHR 210
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQL---LKELGITVISVGHR 147
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
269-488 |
9.45e-10 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 58.99 E-value: 9.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLSRagQY------RDINLNLKRGEVlglcgllgsgrteLAL---------SLF----GITHPDSGELFIEGKPVK 329
Cdd:cd03219 1 LEVRGLTK--RFgglvalDDVSFSVRPGEI-------------HGLigpngagktTLFnlisGFLRPTSGSVLFDGEDIT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 330 LKNNTDAIKRGIGyvsedR---LTlgAILQQ-SIADNMVISILDRLKTPWHLI----DEKQCQDIVQEWIADLDIkvTDP 401
Cdd:cd03219 66 GLPPHEIARLGIG-----RtfqIP--RLFPElTVLENVMVAAQARTGSGLLLArarrEEREARERAEELLERVGL--ADL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 402 NNAL-STLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLItdeasE-------AYyn 473
Cdd:cd03219 137 ADRPaGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLV-----EhdmdvvmSL-- 209
|
250
....*....|....*
gi 491046221 474 CDRILHMKQGSIVKE 488
Cdd:cd03219 210 ADRVTVLDQGRVIAE 224
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
337-492 |
9.48e-10 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 58.94 E-value: 9.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 337 IKRGIGYVSEDrltlgaiLQQSI-----ADNMVIS----ILDRlktpWHLIDEKQcQDIVQEWIADLDIKvTDPNNALST 407
Cdd:COG1119 76 LRKRIGLVSPA-------LQLRFprdetVLDVVLSgffdSIGL----YREPTDEQ-RERARELLELLGLA-HLADRPFGT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVG-ISILLIT---DEASEAYyncDRILHMKQG 483
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVThhvEEIPPGI---THVLLLKDG 219
|
170
....*....|....
gi 491046221 484 SIV-----KEIVTD 492
Cdd:COG1119 220 RVVaagpkEEVLTS 233
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
282-468 |
9.89e-10 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 58.57 E-value: 9.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 282 DINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPV-KLKNN-TDAIKRGIGYVSEDRLTLgaiLQQSI 359
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsDLRGRaIPYLRRKIGVVFQDFRLL---PDRNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 360 ADNMVISILdrlktpwhlIDEKQCQDIVQEWIADLD-IKVTDPNNAL-STLSGGNQQKVVLAKWILTRPKVLILDSPTVG 437
Cdd:cd03292 96 YENVAFALE---------VTGVPPREIRKRVPAALElVGLSHKHRALpAELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180 190
....*....|....*....|....*....|.
gi 491046221 438 VDIGAKDSIYKLIHRLSGVGISILLITDEAS 468
Cdd:cd03292 167 LDPDTTWEIMNLLKKINKAGTTVVVATHAKE 197
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
29-227 |
1.10e-09 |
|
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: 58.50 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGK--SYHRLTPDKARELGVQVIYQDLSLFPNLTV 106
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEG-KVHWSNKneSEPSFEATRSRNRYSVAYAAQKPWLLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 107 AENIAFElnlkGYFGWFRKKQLREkaleilnelAFTIDPDtpVQFLPI---------------AQRQQVAICRALVADAR 171
Cdd:cd03290 96 EENITFG----SPFNKQRYKAVTD---------ACSLQPD--IDLLPFgdqteigerginlsgGQRQRICVARALYQNTN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 172 LVIMDEPTASLTRTEVNQLLST--VNYLKDKGITVVFVSHRLEEVKEiSDRITVIRDG 227
Cdd:cd03290 161 IVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
281-502 |
1.31e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 58.85 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTDAIKR-GIGYVSEDRLTLGAILQQSI 359
Cdd:PRK13632 26 KNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKiGIIFQNPDNQFIGATVEDDI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 360 AdnmvISILDRLktpwhlIDEKQCQDIVQEWIADLDIK---VTDPNNalstLSGGNQQKVVLAKWILTRPKVLILDSPTV 436
Cdd:PRK13632 106 A----FGLENKK------VPPKKMKDIIDDLAKKVGMEdylDKEPQN----LSGGQKQRVAIASVLALNPEIIIFDESTS 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491046221 437 GVDIGAKDSIYKLIHRLSGVGISILL-ITDEASEAyYNCDRILHMKQGSIV-----KEIVTdsiNEQQLEEI 502
Cdd:PRK13632 172 MLDPKGKREIKKIMVDLRKTRKKTLIsITHDMDEA-ILADKVIVFSEGKLIaqgkpKEILN---NKEILEKA 239
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
312-503 |
1.90e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.68 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 312 GITHPDSGELFIEGKPVKLKNNTDAIKRGIGYVSEDRLTLGailQQSIADNmvisILDRLktPWHLIDEKQCQDIVQEWI 391
Cdd:PRK15439 59 GIVPPDSGTLEIGGNPCARLTPAKAHQLGIYLVPQEPLLFP---NLSVKEN----ILFGL--PKRQASMQKMKQLLAALG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 392 ADLDIKVtdpnnALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAY 471
Cdd:PRK15439 130 CQLDLDS-----SAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIR 204
|
170 180 190
....*....|....*....|....*....|..
gi 491046221 472 YNCDRILHMKQGSIVKEIVTDSINEqqlEEII 503
Cdd:PRK15439 205 QLADRISVMRDGTIALSGKTADLST---DDII 233
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
25-240 |
2.18e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.30 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 25 GHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSK-------IEIDGKSYHRLTPDK-ARELGVqviyq 96
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRgarvtgdVTLNGEPLAAIDAPRlARLRAV----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 97 dlslfpnLTVAENIAF-----ELNLKGYFGWFRKK-QLREKALEILNELAFTIDPDT----PVQFLPIAQRQQVAICRAL 166
Cdd:PRK13547 88 -------LPQAAQPAFafsarEIVLLGRYPHARRAgALTHRDGEIAWQALALAGATAlvgrDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 167 ---------VADARLVIMDEPTASLTRTEVNQLLSTVNYL-KDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAE 236
Cdd:PRK13547 161 aqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
....
gi 491046221 237 GLTT 240
Cdd:PRK13547 241 DVLT 244
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
281-494 |
2.23e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 58.46 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTDAIKRGIGYVSEDRLT--LGAILQQS 358
Cdd:PRK13644 19 ENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNPETqfVGRTVEED 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 359 IA---DNMVISILDRLKtpwhLIDEKQCQDIVQEWiadldikvtdPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPT 435
Cdd:PRK13644 99 LAfgpENLCLPPIEIRK----RVDRALAEIGLEKY----------RHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 436 VGVDIGAKDSIYKLIHRLSGVGISILLITDEASEaYYNCDRILHMKQGSIVKEIVTDSI 494
Cdd:PRK13644 165 SMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENV 222
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
316-483 |
2.42e-09 |
|
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: 56.24 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 316 PDSGELFIEGKPVKlKNNTDAIKRGIGYVSEDrltlGAILQQSIADNMvisildrlktpwhlidekqcqdivqewiadld 395
Cdd:cd03228 54 PTSGEILIDGVDLR-DLDLESLRKNIAYVPQD----PFLFSGTIRENI-------------------------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 396 ikvtdpnnalstLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGvGISILLITDEASEAyYNCD 475
Cdd:cd03228 97 ------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTI-RDAD 162
|
....*...
gi 491046221 476 RILHMKQG 483
Cdd:cd03228 163 RIIVLDDG 170
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
14-228 |
2.47e-09 |
|
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: 58.33 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSF--GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDdgSKIEIDGKSYHRLTPDKARElGV 91
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE--GDIQIDGVSWNSVPLQKWRK-AF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 92 QVIYQDLSLFPNltvaeniAFELNLKGYFGWFRKKQLR---EKALEILNE-----LAFTIDPDTPVqfLPIAQRQQVAIC 163
Cdd:cd03289 80 GVIPQKVFIFSG-------TFRKNLDPYGKWSDEEIWKvaeEVGLKSVIEqfpgqLDFVLVDGGCV--LSHGHKQLMCLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 164 RALVADARLVIMDEPTASLTRTEVNQLLSTVNYlKDKGITVVFVSHRLEEVKEiSDRITVIRDGQ 228
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIEAMLE-CQRFLVIEENK 213
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-228 |
2.73e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 57.80 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 35 TLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDG-SKIEIDGKSYhrlTPdkarelgvQVIYQDLSlfpnLTVAENIAFE 113
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGdIEIELDTVSY---KP--------QYIKADYE----GTVRDLLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 114 LNLKGYFGWFRKkqlrekalEILNELAftIDP--DTPVQFLPIAQRQQVAICRALVADARLVIMDEPTASLtrtEVNQ-- 189
Cdd:cd03237 86 TKDFYTHPYFKT--------EIAKPLQ--IEQilDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL---DVEQrl 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491046221 190 LLSTV--NYLKDKGITVVFVSHRLEEVKEISDRITVIrDGQ 228
Cdd:cd03237 153 MASKVirRFAENNEKTAFVVEHDIIMIDYLADRLIVF-EGE 192
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-230 |
3.14e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.74 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGvyaPDDGSKIEIDGK-SYHRLTPDK-ARELGVQVIY--QDLSLFPNL 104
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS---NTDGFHIGVEGViTYDGITPEEiKKHYRGDVVYnaETDVHFPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 105 TVAENIAFELNLKG----YFGWFRKKQLREKALEILNELAFTIDPDTPV-----QFLPIAQRQQVAICRALVADARLVIM 175
Cdd:TIGR00956 154 TVGETLDFAARCKTpqnrPDGVSREEYAKHIADVYMATYGLSHTRNTKVgndfvRGVSGGERKRVSIAEASLGGAKIQCW 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 176 DEPTASL---TRTE-VNQLLSTVNYLKdkgiTVVFVS--HRLEEVKEISDRITVIRDGQKI 230
Cdd:TIGR00956 234 DNATRGLdsaTALEfIRALKTSANILD----TTPLVAiyQCSQDAYELFDKVIVLYEGYQI 290
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
267-453 |
3.67e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.43 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 267 TVLEIKNLSRA-GQYR---DINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELfieGKPVKLKnntdaikrgIG 342
Cdd:PRK09544 3 SLVSLENVSVSfGQRRvlsDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---KRNGKLR---------IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 343 YVSEdRLTLGAILQQSIADNM----------VISILDRLKTPwHLIDEkqcqdivqewiadldikvtdpnnALSTLSGGN 412
Cdd:PRK09544 71 YVPQ-KLYLDTTLPLTVNRFLrlrpgtkkedILPALKRVQAG-HLIDA-----------------------PMQKLSGGE 125
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491046221 413 QQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL 453
Cdd:PRK09544 126 TQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQL 166
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
11-210 |
4.05e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 59.05 E-value: 4.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 11 DPLITLRDLS-KSFGGHRALRNIDLTLNKGEvHCL-AGTNGCGKSTLIKTISG--------VYAPDDGSKIEIDGKSYhr 80
Cdd:COG4178 360 DGALALEDLTlRTPDGRPLLEDLSLSLKPGE-RLLiTGPSGSGKSTLLRAIAGlwpygsgrIARPAGARVLFLPQRPY-- 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 81 LTPDKARElgvQVIYqdlslfPNLtvAENIAFElnlkgyfgwfrkkQLREkALEILN--ELAFTIDPDTP-VQFLPIAQR 157
Cdd:COG4178 437 LPLGTLRE---ALLY------PAT--AEAFSDA-------------ELRE-ALEAVGlgHLAERLDEEADwDQVLSLGEQ 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 158 QQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTvnyLKD--KGITVVFVSHR 210
Cdd:COG4178 492 QRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL---LREelPGTTVISVGHR 543
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
283-488 |
4.58e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.81 E-value: 4.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 283 INLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTDAIKRGIGYVSEDRLTLGailQQSIADN 362
Cdd:PRK11614 24 VSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRRVFS---RMTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 363 MVISILdrlktpwhLIDEKQCQDIVqEWIADLDIKVTDPNNALS-TLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIG 441
Cdd:PRK11614 101 LAMGGF--------FAERDQFQERI-KWVYELFPRLHERRIQRAgTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPI 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491046221 442 AKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVKE 488
Cdd:PRK11614 172 IIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
269-487 |
4.75e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 58.19 E-value: 4.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLS-RAGQYR---DINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVklknnTD-AIK-RGIG 342
Cdd:PRK11432 7 VVLKNITkRFGSNTvidNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-----THrSIQqRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 343 YVSEdrlTLGAILQQSIADNmVISILDRLKTPWHLIDEKqcqdiVQEWIADLDIKVTDpNNALSTLSGGNQQKVVLAKWI 422
Cdd:PRK11432 82 MVFQ---SYALFPHMSLGEN-VGYGLKMLGVPKEERKQR-----VKEALELVDLAGFE-DRYVDQISGGQQQRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 423 LTRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEASEAYYNCDRILHMKQGSIVK 487
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELqQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQ 217
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
310-488 |
5.22e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 57.51 E-value: 5.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 310 LFGITHPDSGELFIEGKPVKlknntdaikrgiGYVSEDRLTLGAILQqsiADNM-----VISILdRLKTPWHLIDEKQCQ 384
Cdd:PRK13537 53 LLGLTHPDAGSISLCGEPVP------------SRARHARQRVGVVPQ---FDNLdpdftVRENL-LVFGRYFGLSAAAAR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 385 DIVQEWI--ADLDIKVTDPnnaLSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILL 462
Cdd:PRK13537 117 ALVPPLLefAKLENKADAK---VGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILL 193
|
170 180
....*....|....*....|....*.
gi 491046221 463 ITDEASEAYYNCDRILHMKQGSIVKE 488
Cdd:PRK13537 194 TTHFMEEAERLCDRLCVIEEGRKIAE 219
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
318-486 |
1.07e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 57.75 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 318 SGELFIEGKPVklknNTDAIKRGIGYVSEDRLTLGAIlqqSIADNMVISIldRLKTPWHLiDEKQCQDIVQEWIADL--- 394
Cdd:TIGR00955 82 SGSVLLNGMPI----DAKEMRAISAYVQQDDLFIPTL---TVREHLMFQA--HLRMPRRV-TKKEKRERVDEVLQALglr 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 395 ---DIKVTDPNNaLSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVG-ISILLITDEASEA 470
Cdd:TIGR00955 152 kcaNTRIGVPGR-VKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGkTIICTIHQPSSEL 230
|
170
....*....|....*.
gi 491046221 471 YYNCDRILHMKQGSIV 486
Cdd:TIGR00955 231 FELFDKIILMAEGRVA 246
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
281-486 |
1.13e-08 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 55.80 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGK-PVKLKNNtdaIKRGIGYVSEDRLTL-------- 351
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvPWKRRKK---FLRRIGVVFGQKTQLwwdlpvid 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 352 GAILQQSIADNMVISILDRLKtpwHLIDEKQCQDIvqewiadLDIKVtdpnnalSTLSGGNQQKVVLAKWILTRPKVLIL 431
Cdd:cd03267 115 SFYLLAAIYDLPPARFKKRLD---ELSELLDLEEL-------LDTPV-------RQLSLGQRMRAEIAAALLHEPEILFL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 432 DSPTVGVDIGAKDSIYKLIHRLSGV-GISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:cd03267 178 DEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
365-496 |
1.32e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.82 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 365 ISILDRLKTPWH---LIDEKQCQDIVQEWIADLDI--KVTDP-NNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGV 438
Cdd:PRK14246 105 LSIYDNIAYPLKshgIKEKREIKKIVEECLRKVGLwkEVYDRlNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 439 DIGAKDSIYKLIHRLSGvGISILLITDEASEAYYNCDRILHMKQGSIVK-----EIVTDSINE 496
Cdd:PRK14246 185 DIVNSQAIEKLITELKN-EIAIVIVSHNPQQVARVADYVAFLYNGELVEwgssnEIFTSPKNE 246
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
35-228 |
1.40e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 55.71 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 35 TLNKGEVHCLAGTNGCGKSTLIKTISGVYaPDDGSkIEIDGKSyhrLTPDKARELGVQVIYqdlslfpnLTVAENIAFEL 114
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGS-IQFAGQP---LEAWSAAELARHRAY--------LSQQQTPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 115 NLKGYFGWFRKKQLREKALE-ILNELA--FTIDP--DTPVQFLPIAQRQQV---AIC----RALVADARLVIMDEPTASL 182
Cdd:PRK03695 85 PVFQYLTLHQPDKTRTEAVAsALNEVAeaLGLDDklGRSVNQLSGGEWQRVrlaAVVlqvwPDINPAGQLLLLDEPMNSL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491046221 183 TRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK03695 165 DVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGK 210
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
256-487 |
1.81e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 56.38 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 256 RKPPNNAEDRRTVLEIKNLSRA--GQY--RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEG------ 325
Cdd:PRK11607 7 RPQAKTRKALTPLLEIRNLTKSfdGQHavDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvdlshv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 326 ----KPVKLKNNTDA------IKRGIGY-VSEDRLTLGailqqsiadnmviSILDRLKTPWHLIDekqcqdiVQEWIAdl 394
Cdd:PRK11607 87 ppyqRPINMMFQSYAlfphmtVEQNIAFgLKQDKLPKA-------------EIASRVNEMLGLVH-------MQEFAK-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 395 dikvTDPNNalstLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSI-YKLIHRLSGVGISILLITDEASEAYYN 473
Cdd:PRK11607 145 ----RKPHQ----LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTM 216
|
250
....*....|....
gi 491046221 474 CDRILHMKQGSIVK 487
Cdd:PRK11607 217 AGRIAIMNRGKFVQ 230
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
26-238 |
1.89e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 55.48 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 26 HRAL-RNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAP---DDGSKIEIDGKSYHrltPDKARELGVQVIYQD-LSL 100
Cdd:PRK10418 15 AQPLvHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrQTAGRVLLDGKPVA---PCALRGRKIATIMQNpRSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 101 F-PNLTVAENIAFELNLKGyfgwfrKKQLREKALEILNELAFTiDPDTPVQFLP------IAQRQQVAIcrALVADARLV 173
Cdd:PRK10418 92 FnPLHTMHTHARETCLALG------KPADDATLTAALEAVGLE-NAARVLKLYPfemsggMLQRMMIAL--ALLCEAPFI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 174 IMDEPTASL---TRTEVNQLLSTVnyLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGL 238
Cdd:PRK10418 163 IADEPTTDLdvvAQARILDLLESI--VQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
269-485 |
2.11e-08 |
|
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: 53.76 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLS-RAGQ-----YRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKlKNNTDAIKRGIG 342
Cdd:cd03246 1 LEVENVSfRYPGaeppvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIS-QWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 343 YVSEDRLTLGAilqqSIADNMvisildrlktpwhlidekqcqdivqewiadldikvtdpnnalstLSGGNQQKVVLAKWI 422
Cdd:cd03246 80 YLPQDDELFSG----SIAENI--------------------------------------------LSGGQRQRLGLARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 423 LTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEaSEAYYNCDRILHMKQGSI 485
Cdd:cd03246 112 YGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-209 |
2.32e-08 |
|
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: 56.48 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 11 DPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIdGKSyhrltpdkarelg 90
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGT-IEI-GET------------- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 91 VQVIYQDLS---LFPNLTVAENIA----------FELNLKGYFGWFR-KKQLREKaleilnelaftidpdtPVQFLPIAQ 156
Cdd:TIGR03719 385 VKLAYVDQSrdaLDPNKTVWEEISggldiiklgkREIPSRAYVGRFNfKGSDQQK----------------KVGQLSGGE 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491046221 157 RQQVAICRALVADARLVIMDEPTASLtrtEVNQLLSTVNYLKDKGITVVFVSH 209
Cdd:TIGR03719 449 RNRVHLAKTLKSGGNVLLLDEPTNDL---DVETLRALEEALLNFAGCAVVISH 498
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
264-502 |
2.35e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 55.41 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 264 DRRTVLEIKNLS----RAGQY--RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTDaI 337
Cdd:PRK13635 1 MKEEIIRVEHISfrypDAATYalKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWD-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 338 KRGIGYVSE--DRLTLGAILQQSIA----------DNMVISILDRLKtpwhlidEKQCQDIVQEwiadldikvtDPnnal 405
Cdd:PRK13635 80 RRQVGMVFQnpDNQFVGATVQDDVAfglenigvprEEMVERVDQALR-------QVGMEDFLNR----------EP---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 406 STLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSG-VGISILLIT---DEASEAyyncDRILHMK 481
Cdd:PRK13635 139 HRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEqKGITVLSIThdlDEAAQA----DRVIVMN 214
|
250 260
....*....|....*....|...
gi 491046221 482 QGSIVKEIVTDSINE--QQLEEI 502
Cdd:PRK13635 215 KGEILEEGTPEEIFKsgHMLQEI 237
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
406-485 |
2.72e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 54.68 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 406 STLSGGNQQKVVLAKWILTRPKVLILDSPtvgvdIGAKDSIYK-----LIHRL-SGVGISILLITDEASEAYYNCDRILH 479
Cdd:PRK11247 132 AALSGGQKQRVALARALIHRPGLLLLDEP-----LGALDALTRiemqdLIESLwQQHGFTVLLVTHDVSEAVAMADRVLL 206
|
....*.
gi 491046221 480 MKQGSI 485
Cdd:PRK11247 207 IEEGKI 212
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
266-485 |
2.76e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 55.02 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 266 RTVLEIKNLSRAGQYRD----INLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSgelfIEGKPVKLKNNT-DAIKRG 340
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQalhaVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDK----SAGSHIELLGRTvQREGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 341 IGYVSEDRLTLGAILQQ-------SIADNMVISILDrlKTP-------WHLIDEKQ--CQDIVQEWIADLdikvtdPNNA 404
Cdd:PRK09984 78 ARDIRKSRANTGYIFQQfnlvnrlSVLENVLIGALG--STPfwrtcfsWFTREQKQraLQALTRVGMVHF------AHQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 405 LSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGV-GISILLITDEASEAYYNCDRILHMKQG 483
Cdd:PRK09984 150 VSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQG 229
|
..
gi 491046221 484 SI 485
Cdd:PRK09984 230 HV 231
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
281-488 |
2.85e-08 |
|
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: 54.54 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKlKNNTDAIKRGIGYVSEDRLtlgaILQQSIA 360
Cdd:cd03254 20 KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIR-DISRKSLRSMIGVVLQDTF----LFSGTIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 361 DNMvisildRLKTPwhLIDEKQCQDIVQEWIADLDIK------VTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSP 434
Cdd:cd03254 95 ENI------RLGRP--NATDEEVIEAAKEAGAHDFIMklpngyDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 435 TVGVDIGA----KDSIYKLI---------HRLSGVgisillitdeaseayYNCDRILHMKQGSIVKE 488
Cdd:cd03254 167 TSNIDTETekliQEALEKLMkgrtsiiiaHRLSTI---------------KNADKILVLDDGKIIEE 218
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
310-486 |
3.13e-08 |
|
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: 54.13 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 310 LFGITHPDSGELFIEGKPVKLKNNTDaIKRGIGYVSED-RLTLGailqqSIADNMVISILdrlktpwhLIDEKQCQDIVQ 388
Cdd:cd03245 50 LAGLYKPTSGSVLLDGTDIRQLDPAD-LRRNIGYVPQDvTLFYG-----TLRDNITLGAP--------LADDERILRAAE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 389 ewIADLDIKVTDPNNALST--------LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDsiyKLIHRLSGV--GI 458
Cdd:cd03245 116 --LAGVTDFVNKHPNGLDLqigergrgLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEE---RLKERLRQLlgDK 190
|
170 180
....*....|....*....|....*...
gi 491046221 459 SILLITDEASeAYYNCDRILHMKQGSIV 486
Cdd:cd03245 191 TLIIITHRPS-LLDLVDRIIVMDSGRIV 217
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
29-227 |
3.57e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.46 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGK-SYHRLTPdkarelgvqviyqdlSLFPNlTVA 107
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEG-KIKHSGRiSFSPQTS---------------WIMPG-TIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 108 ENIAFELNlkgyFGWFRKKQLReKALEILNELAFTIDPDTPVQF-----LPIAQRQQVAICRALVADARLVIMDEPTASL 182
Cdd:TIGR01271 505 DNIIFGLS----YDEYRYTSVI-KACQLEEDIALFPEKDKTVLGeggitLSGGQRARISLARAVYKDADLYLLDSPFTHL 579
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491046221 183 TRTEVNQLLST--VNYLKDKgiTVVFVSHRLEEVKEiSDRITVIRDG 227
Cdd:TIGR01271 580 DVVTEKEIFESclCKLMSNK--TRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
308-505 |
4.05e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.41 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 308 LSLFGITHPDS-GELFIEGKPVKlKNNTDAIKRGIGYVSEdrltlgailQQSIADNMVISILDRL-KTPWH-------LI 378
Cdd:PRK10575 54 LKMLGRHQPPSeGEILLDAQPLE-SWSSKAFARKVAYLPQ---------QLPAAEGMTVRELVAIgRYPWHgalgrfgAA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 379 DEKQcqdiVQEWIADLDIKvtdP--NNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGV 456
Cdd:PRK10575 124 DREK----VEEAISLVGLK---PlaHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQE 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491046221 457 -GISILLITDEASEAYYNCDRILHMKQGSIVKEIVTDSINEQQLEEIING 505
Cdd:PRK10575 197 rGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYG 246
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
318-486 |
4.37e-08 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 53.81 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 318 SGELFIEGKPVKlknnTDAIKRGIGYVSE-DRLTLGAILQQSIAdNMVISILDRLKTpwHLIDEKQCQDIVQEWIADLDI 396
Cdd:cd03234 64 SGQILFNGQPRK----PDQFQKCVAYVRQdDILLPGLTVRETLT-YTAILRLPRKSS--DAIRKKRVEDVLLRDLALTRI 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 397 KvtdpNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGakdSIYKLIHRLS--GVGISILLITDEA--SEAYY 472
Cdd:cd03234 137 G----GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF---TALNLVSTLSqlARRNRIVILTIHQprSDLFR 209
|
170
....*....|....
gi 491046221 473 NCDRILHMKQGSIV 486
Cdd:cd03234 210 LFDRILLLSSGEIV 223
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
389-494 |
4.61e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.16 E-value: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 389 EWIADLDIKVTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEA 467
Cdd:PRK11701 133 DWLERVEIDAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDL 212
|
90 100
....*....|....*....|....*..
gi 491046221 468 SEAYYNCDRILHMKQGSIVKEIVTDSI 494
Cdd:PRK11701 213 AVARLLAHRLLVMKQGRVVESGLTDQV 239
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
269-485 |
6.62e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 54.32 E-value: 6.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLS----RAGQYRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVklkNNTDAIKRGIGYV 344
Cdd:PRK10851 3 IEIANIKksfgRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV---SRLHARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 345 SEDRltlgAILQQ-SIADNMV--ISILDRLKTP-WHLIDEKQCQ--DIVQewIADLdikvtdPNNALSTLSGGNQQKVVL 418
Cdd:PRK10851 80 FQHY----ALFRHmTVFDNIAfgLTVLPRRERPnAAAIKAKVTQllEMVQ--LAHL------ADRYPAQLSGGQKQRVAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 419 AKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEASEAYYNCDRILHMKQGSI 485
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLhEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
26-228 |
6.90e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 55.10 E-value: 6.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 26 HRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARELgVQVIYQDLSLFPNlT 105
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEG-DIRFHDIPLTKLQLDSWRSR-LAVVSQTPFLFSD-T 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 106 VAENIAFElnlkgyfgwfrKKQLREKALEILNELAFTIDP--------DTPVQ----FLPIAQRQQVAICRALVADARLV 173
Cdd:PRK10789 405 VANNIALG-----------RPDATQQEIEHVARLASVHDDilrlpqgyDTEVGergvMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 174 IMDEP-TASLTRTEvNQLLSTVNYLKdKGITVVFVSHRLEEVKEiSDRITVIRDGQ 228
Cdd:PRK10789 474 ILDDAlSAVDGRTE-HQILHNLRQWG-EGRTVIISAHRLSALTE-ASEILVMQHGH 526
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
312-488 |
7.49e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 53.65 E-value: 7.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 312 GITHPDSGELFIEGKPVKlKNNTDAIKRGIGYV--SEDRLTLGAILQQSIADNMVISILDRlKTPWHLIDEKqcqdIVQE 389
Cdd:PRK13652 52 GILKPTSGSVLIRGEPIT-KENIREVRKFVGLVfqNPDDQIFSPTVEQDIAFGPINLGLDE-ETVAHRVSSA----LHML 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 390 WIADLDIKVtdPNNalstLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLS-GVGISILLITDEAS 468
Cdd:PRK13652 126 GLEELRDRV--PHH----LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPeTYGMTVIFSTHQLD 199
|
170 180
....*....|....*....|
gi 491046221 469 EAYYNCDRILHMKQGSIVKE 488
Cdd:PRK13652 200 LVPEMADYIYVMDKGRIVAY 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
408-486 |
8.25e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 53.90 E-value: 8.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
29-243 |
9.65e-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: 54.95 E-value: 9.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKAReLGVQVIYQDLSLFPNltvae 108
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEG-EIIIDGLNIAKIGLHDLR-FKITIIPQDPVLFSG----- 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 109 niAFELNLKGyFGWFRKKQLReKALEILNELAFTIDPDTPVQF--------LPIAQRQQVAICRALVADARLVIMDEPTA 180
Cdd:TIGR00957 1375 --SLRMNLDP-FSQYSDEEVW-WALELAHLKTFVSALPDKLDHecaeggenLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 181 SLTRTEVNQLLSTVNYLKDKgITVVFVSHRLEEVKEISdRITVIRDG--QKIGTwPAEGLTTRKI 243
Cdd:TIGR00957 1451 AVDLETDNLIQSTIRTQFED-CTVLTIAHRLNTIMDYT-RVIVLDKGevAEFGA-PSNLLQQRGI 1512
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
29-234 |
1.24e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 53.32 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKsyhrltpdkarelgVQVIYQDLSLFPNlTVAE 108
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG-KIKHSGR--------------ISFSSQFSWIMPG-TIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 109 NIAFELNLKGYfgwfRKKQLReKALEILNELAFTIDPDTPVQ-----FLPIAQRQQVAICRALVADARLVIMDEPTASL- 182
Cdd:cd03291 117 NIIFGVSYDEY----RYKSVV-KACQLEEDITKFPEKDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLd 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491046221 183 TRTEVNQLLSTVNYLKDKGiTVVFVSHRLEEVKeISDRITVIRDGQKI--GTWP 234
Cdd:cd03291 192 VFTEKEIFESCVCKLMANK-TRILVTSKMEHLK-KADKILILHEGSSYfyGTFS 243
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
93-256 |
1.42e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.26 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 93 VIYQDLSLFpNLTVAENIAFelnlkGYFGWFRKKQLREKALEILNELAFTIDP--DTPV----QFLPIAQRQQVAICRAL 166
Cdd:PTZ00265 1300 IVSQEPMLF-NMSIYENIKF-----GKEDATREDVKRACKFAAIDEFIESLPNkyDTNVgpygKSLSGGQKQRIAIARAL 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 167 VADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKG-ITVVFVSHRLEEVKEiSDRITVIRDGQKIGTW-PAEGLTtrkiT 244
Cdd:PTZ00265 1374 LREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKR-SDKIVVFNNPDRTGSFvQAHGTH----E 1448
|
170
....*....|..
gi 491046221 245 ELMTGLDIVHER 256
Cdd:PTZ00265 1449 ELLSVQDGVYKK 1460
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
408-488 |
1.43e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.94 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSG-VGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQeLNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
..
gi 491046221 487 KE 488
Cdd:PRK15134 237 EQ 238
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-209 |
1.46e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.79 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 15 TLRDLSKSFGGHRA-LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVyapDDgskiEIDGKSyhRLTPdkarelGVQV 93
Cdd:TIGR03719 6 TMNRVSKVVPPKKEiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV---DK----DFNGEA--RPQP------GIKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 94 IY--QDLSLFPNLTVAENIAF-------------ELNLK-----GYFGWFRKKQ--LREK-----ALEILNELAFTID-- 144
Cdd:TIGR03719 71 GYlpQEPQLDPTKTVRENVEEgvaeikdaldrfnEISAKyaepdADFDKLAAEQaeLQEIidaadAWDLDSQLEIAMDal 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 145 ----PDTPVQFLPIAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLlstVNYLKDKGITVVFVSH 209
Cdd:TIGR03719 151 rcppWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWL---ERHLQEYPGTVVAVTH 216
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
28-246 |
1.55e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.58 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 28 ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIDGKSYHRLTPDKARELGVQVIYQD---LSLFPNL 104
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGT-ITLHGKKINNHNANEAINHGFALVTEErrsTGIYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 105 TVAEN--IAFELNLKGYFGWFRKKQLREKALEILNELAF-TIDPDTPVQFLPIAQRQQVAICRALVADARLVIMDEPTAS 181
Cdd:PRK10982 342 DIGFNslISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVkTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRG 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 182 L---TRTEVNQLLSTVNYlKDKGItvVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITEL 246
Cdd:PRK10982 422 IdvgAKFEIYQLIAELAK-KDKGI--IIISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQNEILRL 486
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
14-228 |
1.70e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.74 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKieidgksyhrltpdKARElGVQV 93
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------------KWSE-NANI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 94 IY--QDlslfpnltVAENIAFELNLKGYFGWFRKKQLREKALE-ILNELAFTIDpDT--PVQFLPIAQRQQVAICRALVA 168
Cdd:PRK15064 385 GYyaQD--------HAYDFENDLTLFDWMSQWRQEGDDEQAVRgTLGRLLFSQD-DIkkSVKVLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 169 DARLVIMDEPTASLTRTEVNQL-LSTVNYlkdKGiTVVFVSHRLEEVKEISDRITVIRDGQ 228
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMESIESLnMALEKY---EG-TLIFVSHDREFVSSLATRIIEITPDG 512
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
371-483 |
2.10e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 52.30 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 371 LKTPWHLIDEKQCQDIVQEWiadLD-IKVTD-PNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYK 448
Cdd:PRK11300 118 LKTPAFRRAESEALDRAATW---LErVGLLEhANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDE 194
|
90 100 110
....*....|....*....|....*....|....*.
gi 491046221 449 LIHRLSG-VGISILLITDEASEAYYNCDRILHMKQG 483
Cdd:PRK11300 195 LIAELRNeHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
281-483 |
2.26e-07 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 51.70 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKnntdaikrgigyvSEDRLTlgaILQQ--- 357
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEP-------------GPDRMV---VFQNysl 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 358 ----SIADNMVISIlDRLKtpwHLIDEKQCQDIVQEWIADLDIKVTdPNNALSTLSGGNQQKVVLAKWILTRPKVLILDS 433
Cdd:TIGR01184 66 lpwlTVRENIALAV-DRVL---PDLSKSERRAIVEEHIALVGLTEA-ADKRPGQLSGGMKQRVAIARALSIRPKVLLLDE 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 434 PtvgvdIGAKDSIYK--LIHRLSGV----GISILLITDEASEAYYNCDRILHMKQG 483
Cdd:TIGR01184 141 P-----FGALDALTRgnLQEELMQIweehRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
310-485 |
2.26e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.86 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 310 LFGITHPDSGELFIEGKPVKlkNNTDAIKRGIGYVSEDRLTLGAIlqqSIADNMVISILDRLKTpWhliDEKQCQdiVQE 389
Cdd:TIGR01257 976 LTGLLPPTSGTVLVGGKDIE--TNLDAVRQSLGMCPQHNILFHHL---TVAEHILFYAQLKGRS-W---EEAQLE--MEA 1044
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 390 WIADLDIKvTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGvGISILLITDEASE 469
Cdd:TIGR01257 1045 MLEDTGLH-HKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDE 1122
|
170
....*....|....*.
gi 491046221 470 AYYNCDRILHMKQGSI 485
Cdd:TIGR01257 1123 ADLLGDRIAIISQGRL 1138
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
16-209 |
2.54e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.42 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 16 LRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGS-----KIEIDGKSYHR--LTPDKare 88
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRihcgtKLEVAYFDQHRaeLDPEK--- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 89 lgvqviyqdlslfpnlTVAENIA---FELNLKGyfgwfRKKQlrekALEILNELAFTidPD---TPVQFLPIAQRQQVAI 162
Cdd:PRK11147 399 ----------------TVMDNLAegkQEVMVNG-----RPRH----VLGYLQDFLFH--PKramTPVKALSGGERNRLLL 451
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491046221 163 CRALVADARLVIMDEPTASLTrTEVNQLLSTVnyLKDKGITVVFVSH 209
Cdd:PRK11147 452 ARLFLKPSNLLILDEPTNDLD-VETLELLEEL--LDSYQGTVLLVSH 495
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
268-485 |
2.79e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 51.63 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 268 VLEIKNLS-RAGQ---YRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVklkNNTDAIKRGIgy 343
Cdd:PRK09493 1 MIEFKNVSkHFGPtqvLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV---NDPKVDERLI-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 344 vsedRLTLGAILQQ-------SIADNMVISildrlktPWHL--IDEKQCQDIVQEWIAdldiKV---TDPNNALSTLSGG 411
Cdd:PRK09493 76 ----RQEAGMVFQQfylfphlTALENVMFG-------PLRVrgASKEEAEKQARELLA----KVglaERAHHYPSELSGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491046221 412 NQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSI 485
Cdd:PRK09493 141 QQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
13-96 |
2.89e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 51.72 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 13 LITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGV--YAPDDGSkIEIDGKSYHRLTPDKARELG 90
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGT-VEFKGKDLLELSPEDRAGEG 79
|
....*.
gi 491046221 91 VQVIYQ 96
Cdd:PRK09580 80 IFMAFQ 85
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
407-484 |
3.03e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 52.89 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 407 TLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLI-HRLSgvGISILLITDEAS-EAYYncDRILHMKQGS 484
Cdd:COG4178 485 VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLrEELP--GTTVISVGHRSTlAAFH--DRVLELTGDG 560
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
385-488 |
3.16e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 52.09 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 385 DIVQEWIADLDIKVTDPNNALST----LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLS-GVGIS 459
Cdd:PRK13646 119 DEVKNYAHRLLMDLGFSRDVMSQspfqMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKT 198
|
90 100
....*....|....*....|....*....
gi 491046221 460 ILLITDEASEAYYNCDRILHMKQGSIVKE 488
Cdd:PRK13646 199 IILVSHDMNEVARYADEVIVMKEGSIVSQ 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-232 |
3.25e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.48 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 5 SKADKSDpLITLRDLSKSFGGHR--ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIeIDGKSYhrLT 82
Cdd:TIGR01257 1930 SGGNKTD-ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDAT-VAGKSI--LT 2005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 83 pdkarelGVQVIYQDLSLFPN-------LTVAENIAFELNLKGyfgwFRKKQLREKALEILNELAFTIDPDTPVQFLPIA 155
Cdd:TIGR01257 2006 -------NISDVHQNMGYCPQfdaiddlLTGREHLYLYARLRG----VPAEEIEKVANWSIQSLGLSLYADRLAGTYSGG 2074
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 156 QRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDG--QKIGT 232
Cdd:TIGR01257 2075 NKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGafQCLGT 2153
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
241-498 |
3.27e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 53.19 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 241 RKITELMtgldivhERKP--PNNAEDR----RTVLEIKNLSRAGQYR-------DINLNLKRGEVLGLCGLLGSGRTELA 307
Cdd:TIGR00958 452 EKVFEYL-------DRKPniPLTGTLAplnlEGLIEFQDVSFSYPNRpdvpvlkGLTFTLHPGEVVALVGPSGSGKSTVA 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 308 LSLFGITHPDSGELFIEGKPVKlKNNTDAIKRGIGYVSEDRLTLGAILQQSIA-------DNMVISIldrlktpwhlIDE 380
Cdd:TIGR00958 525 ALLQNLYQPTGGQVLLDGVPLV-QYDHHYLHRQVALVGQEPVLFSGSVRENIAygltdtpDEEIMAA----------AKA 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 381 KQCQDIVQEWIADLDikvTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLihrLSGVGISI 460
Cdd:TIGR00958 594 ANAHDFIMEFPNGYD---TEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES---RSRASRTV 667
|
250 260 270
....*....|....*....|....*....|....*...
gi 491046221 461 LLITDEASEAyYNCDRILHMKQGSIVKEIVTDSINEQQ 498
Cdd:TIGR00958 668 LLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
407-480 |
3.30e-07 |
|
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: 50.23 E-value: 3.30e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 407 TLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLsgvGISILLITDEAS-EAYYncDRILHM 480
Cdd:cd03223 91 VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL---GITVISVGHRPSlWKFH--DRVLDL 160
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-216 |
3.61e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.99 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSF--GGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDdgSKIEIDGKSYHRLTPDKARElGV 91
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE--GEIQIDGVSWNSVTLQTWRK-AF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 92 QVIYQDLSLFPNltvaeniAFELNLKGYFGWFRKK--------QLREKALEILNELAFTIDPDTPVqfLPIAQRQQVAIC 163
Cdd:TIGR01271 1295 GVIPQKVFIFSG-------TFRKNLDPYEQWSDEEiwkvaeevGLKSVIEQFPDKLDFVLVDGGYV--LSNGHKQLMCLA 1365
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 164 RALVADARLVIMDEPTASLTRTEVNQLLSTvnyLKD--KGITVVFVSHRLEEVKE 216
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLDPVTLQIIRKT---LKQsfSNCTVILSEHRVEALLE 1417
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
269-464 |
3.68e-07 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 50.57 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNL--SRAGQ--YRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPvkLKNNTDAIKRGIGYV 344
Cdd:cd03231 1 LEADELtcERDGRalFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGP--LDFQRDSIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 345 SEdrltlgailqqsiADNM--VISILDRLkTPWHLIDEKqcqDIVQEWIADLDIKVTDpNNALSTLSGGNQQKVVLAKWI 422
Cdd:cd03231 79 GH-------------APGIktTLSVLENL-RFWHADHSD---EQVEEALARVGLNGFE-DRPVAQLSAGQQRRVALARLL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491046221 423 LTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLIT 464
Cdd:cd03231 141 LSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTT 182
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-227 |
4.52e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 12 PLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISG----VYAPD-------DGSKIEI-DGKsyh 79
Cdd:PRK10938 259 PRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqGYSNDltlfgrrRGSGETIwDIK--- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 80 rltpdkaRELGvqviYQDLSLFPNLTVAENIafeLN--LKGYF---GWF-----RKKQLREKALEILN---ELAftidpD 146
Cdd:PRK10938 336 -------KHIG----YVSSSLHLDYRVSTSV---RNviLSGFFdsiGIYqavsdRQQKLAQQWLDILGidkRTA-----D 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 147 TPVQFLPIAQRQQVAICRALVADARLVIMDEPTASLtrTEVNQLL--STVNYLKDKGIT-VVFVSHRLEEVKE-ISDRIT 222
Cdd:PRK10938 397 APFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGL--DPLNRQLvrRFVDVLISEGETqLLFVSHHAEDAPAcITHRLE 474
|
....*
gi 491046221 223 VIRDG 227
Cdd:PRK10938 475 FVPDG 479
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
306-486 |
4.98e-07 |
|
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: 50.57 E-value: 4.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 306 LALSLFGITHPDSGELFIEGKPVKlKNNTDAIKRGIGYVSEDRLTLGAILQQSI------ADNMVISILDRLktpwhlid 379
Cdd:cd03244 46 LLLALFRLVELSSGSILIDGVDIS-KIGLHDLRSRISIIPQDPVLFSGTIRSNLdpfgeySDEELWQALERV-------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 380 ekQCQDIVQEWIADLDIKVTDPNNALSTlsgGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLI--------- 450
Cdd:cd03244 117 --GLKEFVESLPGGLDTVVEEGGENLSV---GQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIreafkdctv 191
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491046221 451 ----HRLSGvgisillITDeaseayynCDRILHMKQGSIV 486
Cdd:cd03244 192 ltiaHRLDT-------IID--------SDRILVLDKGRVV 216
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
261-485 |
5.36e-07 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 51.87 E-value: 5.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 261 NAEDRRTVLEIKNLSRAgqY------RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVklkNNT 334
Cdd:PRK09452 7 QPSSLSPLVELRGISKS--FdgkeviSNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI---THV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 335 DAIKRGIGYVsedrltlgaiLQQ-------SIADNmVISILDRLKTPWHLIDEK--------QCQDIVQEWIADLdikvt 399
Cdd:PRK09452 82 PAENRHVNTV----------FQSyalfphmTVFEN-VAFGLRMQKTPAAEITPRvmealrmvQLEEFAQRKPHQL----- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 400 dpnnalstlSGGNQQKVVLAKWILTRPKVLILDSPTVGVDigakdsiYKL-------IHRLS-GVGISILLITDEASEAY 471
Cdd:PRK09452 146 ---------SGGQQQRVAIARAVVNKPKVLLLDESLSALD-------YKLrkqmqneLKALQrKLGITFVFVTHDQEEAL 209
|
250
....*....|....
gi 491046221 472 YNCDRILHMKQGSI 485
Cdd:PRK09452 210 TMSDRIVVMRDGRI 223
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
316-480 |
5.49e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 50.48 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 316 PDSGELFIEGKPVkLKNNTDAIKRGIGYVSEDRLTLGailqQSIADNMVISILDRLKTPwhliDEKQCQDIVQEWIADLD 395
Cdd:PRK10247 59 PTSGTLLFEGEDI-STLKPEIYRQQVSYCAQTPTLFG----DTVYDNLIFPWQIRNQQP----DPAIFLDDLERFALPDT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 396 IkVTDPNNAlstLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEASEAYYnC 474
Cdd:PRK10247 130 I-LTKNIAE---LSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDEINH-A 204
|
....*.
gi 491046221 475 DRILHM 480
Cdd:PRK10247 205 DKVITL 210
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
409-483 |
6.06e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 51.26 E-value: 6.06e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491046221 409 SGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEASEAYYNCDRILHMKQG 483
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAIIMITHDLGVVAGICDKVLVMYAG 238
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-216 |
6.25e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 50.34 E-value: 6.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 16 LRDLSKSFG------GHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVyapddgskieidgksyHRLTPDKArel 89
Cdd:COG2401 27 VAIVLEAFGvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA----------------LKGTPVAG--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 90 gvQVIYQDLSLFPNLTVAENIAFELNLKgyfgwfrkkqlreKALEILNEL----AFTIdpDTPVQFLPIAQRQQVAICRA 165
Cdd:COG2401 88 --CVDVPDNQFGREASLIDAIGRKGDFK-------------DAVELLNAVglsdAVLW--LRRFKELSTGQKFRFRLALL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491046221 166 LVADARLVIMDEPTASLTRTEVNQLLSTVNYL-KDKGITVVFVSHRlEEVKE 216
Cdd:COG2401 151 LAERPKLLVIDEFCSHLDRQTAKRVARNLQKLaRRAGITLVVATHH-YDVID 201
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
375-503 |
9.33e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 50.42 E-value: 9.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 375 WHliDEKQCQDIVQEWIADLD----IKVTDPNNALStLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLI 450
Cdd:PRK14258 117 WR--PKLEIDDIVESALKDADlwdeIKHKIHKSALD-LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLI 193
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491046221 451 HRL---SGVGISILL--------ITDEASEAYYNCDRILHMKQGSIVKEIVTDSINEQQLEEII 503
Cdd:PRK14258 194 QSLrlrSELTMVIVShnlhqvsrLSDFTAFFKGNENRIGQLVEFGLTKKIFNSPHDSRTREYVL 257
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
282-486 |
1.07e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 50.50 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 282 DINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTDAIKrgigyvsEDRLTLGAILQQSIAD 361
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIK-------PVRKKVGVVFQFPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 362 NMVISIL-DRLKTPWHL-IDEKQCQDIVQEWIADLDIKVTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVD 439
Cdd:PRK13643 97 LFEETVLkDVAFGPQNFgIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491046221 440 IGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:PRK13643 177 PKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
269-502 |
1.85e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 49.16 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLSRAGQYRDINLNLKRGEVLGLCGLLGSGRTELALSLFGIThPDSGELFIEGKPVK-LKNNTDAIKRgiGYVSEd 347
Cdd:PRK03695 1 MQLNDVAVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEaWSAAELARHR--AYLSQ- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 348 rltlgailQQSIADNM-VISILDRlktpwHLIDEKQCQDI--VQEWIADLdIKVTDP-NNALSTLSGGNQQKVVLAKWIL 423
Cdd:PRK03695 77 --------QQTPPFAMpVFQYLTL-----HQPDKTRTEAVasALNEVAEA-LGLDDKlGRSVNQLSGGEWQRVRLAAVVL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 424 -----TRP--KVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVKEIVTDSI-N 495
Cdd:PRK03695 143 qvwpdINPagQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVlT 222
|
....*..
gi 491046221 496 EQQLEEI 502
Cdd:PRK03695 223 PENLAQV 229
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
312-485 |
1.99e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 49.34 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 312 GITHPDSGELFIEGKPVKLKNNTDaIKRGIGYVSE--DRLTLGAILQQSIADNmvisiLDRLKTPWHLIDEKQCQDIvqE 389
Cdd:PRK13650 55 GLLEAESGQIIIDGDLLTEENVWD-IRHKIGMVFQnpDNQFVGATVEDDVAFG-----LENKGIPHEEMKERVNEAL--E 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 390 WIADLDIKVTDPnnalSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEAS 468
Cdd:PRK13650 127 LVGMQDFKEREP----ARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIrDDYQMTVISITHDLD 202
|
170
....*....|....*..
gi 491046221 469 EAYYNcDRILHMKQGSI 485
Cdd:PRK13650 203 EVALS-DRVLVMKNGQV 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
408-488 |
2.07e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 49.01 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLS-GVGISILLITDEASEAyYNCDRILHMKQGSIV 486
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNrEHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQ 225
|
..
gi 491046221 487 KE 488
Cdd:PRK10584 226 EE 227
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
14-123 |
2.38e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.12 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 14 ITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSkIEIdGKSyhrltpdkarelgVQV 93
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGT-IKI-GET-------------VKL 389
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 491046221 94 IYQDLS---LFPNLTVAENIA----------FELNLKGYFGWF 123
Cdd:PRK11819 390 AYVDQSrdaLDPNKTVWEEISggldiikvgnREIPSRAYVGRF 432
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
267-486 |
2.97e-06 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 48.61 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 267 TVLEIKNLS-RAGQYR---DINLNLKRGEVlglcgllgsgrteLAL-------------SLFGITHPDSGELFIEGKPVK 329
Cdd:PRK13548 1 AMLEARNLSvRLGGRTlldDVSLTLRPGEV-------------VAIlgpngagkstllrALSGELSPDSGEVRLNGRPLA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 330 lknntdaikrgiGYVSEDRLTLGAILQQSIADNMVISILD--RL-KTPWHLiDEKQCQDIVQEWIADLDIKvtdpnnALS 406
Cdd:PRK13548 68 ------------DWSPAELARRRAVLPQHSSLSFPFTVEEvvAMgRAPHGL-SRAEDDALVAAALAQVDLA------HLA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 407 -----TLSGGNQQKVVLAKwILT-------RPKVLILDSPTVGVDIGAKDSIYKLIHRL---SGVG-ISILliTDEASEA 470
Cdd:PRK13548 129 grdypQLSGGEQQRVQLAR-VLAqlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLaheRGLAvIVVL--HDLNLAA 205
|
250
....*....|....*.
gi 491046221 471 YYnCDRILHMKQGSIV 486
Cdd:PRK13548 206 RY-ADRIVLLHQGRLV 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
281-456 |
3.10e-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: 48.24 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNtDAIKRGIGYVSEDRLTLGAILQQSIA 360
Cdd:cd03248 31 QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEH-KYLHSKVSLVGQEPVLFARSLQDNIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 361 DNMVISILDRLKtpwHLIDEKQCQDIVQEWIADLDikvTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDI 440
Cdd:cd03248 110 YGLQSCSFECVK---EAAQKAHAHSFISELASGYD---TEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
|
170 180
....*....|....*....|....*....
gi 491046221 441 GAKDSIYKLI-------------HRLSGV 456
Cdd:cd03248 184 ESEQQVQQALydwperrtvlviaHRLSTV 212
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
408-488 |
3.31e-06 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 47.91 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEA-YYNCDRILHMKQGSIV 486
Cdd:cd03217 105 FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLdYIKPDRVHVLYDGRIV 184
|
..
gi 491046221 487 KE 488
Cdd:cd03217 185 KS 186
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
408-501 |
3.54e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 48.93 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVK 487
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIK 245
|
90
....*....|....*.
gi 491046221 488 EIVTDSI--NEQQLEE 501
Cdd:PRK13651 246 DGDTYDIlsDNKFLIE 261
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
408-488 |
3.79e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 48.21 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVK 487
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
|
.
gi 491046221 488 E 488
Cdd:PRK11264 225 Q 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
408-488 |
3.93e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 48.43 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVK 487
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEE 232
|
.
gi 491046221 488 E 488
Cdd:PRK10619 233 E 233
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
346-505 |
4.92e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 47.85 E-value: 4.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 346 EDRLTLGAILQQ------SIADNMVISIldRLK--TPWHLIDEKQCQDIVQEWIADlDIKVTDPNNALStLSGGNQQKVV 417
Cdd:PRK14239 83 DLRKEIGMVFQQpnpfpmSIYENVVYGL--RLKgiKDKQVLDEAVEKSLKGASIWD-EVKDRLHDSALG-LSGGQQQRVC 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 418 LAKWILTRPKVLILDSPTVGVD-IGA---KDSIYKLIHRLsgvgiSILLITDEASEAYYNCDRILHMKQGSIV-----KE 488
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDpISAgkiEETLLGLKDDY-----TMLLVTRSMQQASRISDRTGFFLDGDLIeyndtKQ 233
|
170
....*....|....*..
gi 491046221 489 IVTDSINeQQLEEIING 505
Cdd:PRK14239 234 MFMNPKH-KETEDYISG 249
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
269-454 |
5.29e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 48.95 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLSRAgqYR-------DINLNL-KRGEVLGLCGLLGSGRTeLALSLFGITHPDSGELFIEGKPVKLKNNTdAIKRG 340
Cdd:PRK10790 341 IDIDNVSFA--YRddnlvlqNINLSVpSRGFVALVGHTGSGKST-LASLLMGYYPLTEGEIRLDGRPLSSLSHS-VLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 341 IGYVSEDRLTLgailqqsiADNMVISI-LDRLKTP---WHLIDEKQCQDIVQEWIADLDIKVTDPNNalsTLSGGNQQKV 416
Cdd:PRK10790 417 VAMVQQDPVVL--------ADTFLANVtLGRDISEeqvWQALETVQLAELARSLPDGLYTPLGEQGN---NLSVGQKQLL 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491046221 417 VLAKWILTRPKVLILDSPTVGVDIGAKDSIYK----------LI---HRLS 454
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQalaavrehttLVviaHRLS 536
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
281-472 |
5.86e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 47.77 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELaLSLF-GITHPDSGELFIEGKPVKlknnTDAIKRGIGYVSEdrltlGAILQQSI 359
Cdd:PRK11248 18 EDINLTLESGELLVVLGPSGCGKTTL-LNLIaGFVPYQHGSITLDGKPVE----GPGAERGVVFQNE-----GLLPWRNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 360 ADNMVISIldRLKTpwhlIDEKQCQDIVQEWIADLDIKVTDpNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVD 439
Cdd:PRK11248 88 QDNVAFGL--QLAG----VEKMQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190
....*....|....*....|....*....|....
gi 491046221 440 IGAKDSIYKLIHRL-SGVGISILLITDEASEAYY 472
Cdd:PRK11248 161 AFTREQMQTLLLKLwQETGKQVLLITHDIEEAVF 194
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
281-489 |
7.04e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 47.50 E-value: 7.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPV-KLKNNTDAIKRGigyvsedrLTLGAILQQ-- 357
Cdd:PRK11629 26 HNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsKLSSAAKAELRN--------QKLGFIYQFhh 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 358 -----SIADNMVISILDRLKTPwhlideKQCQDIVQEWIADLDIKvTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILD 432
Cdd:PRK11629 98 llpdfTALENVAMPLLIGKKKP------AEINSRALEMLAAVGLE-HRANHRPSELSGGERQRVAIARALVNNPRLVLAD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 433 SPTVGVDIGAKDSIYKLIHRLSGV-GISILLITDEASEAyYNCDRILHMKQGSIVKEI 489
Cdd:PRK11629 171 EPTGNLDARNADSIFQLLGELNRLqGTAFLVVTHDLQLA-KRMSRQLEMRDGRLTAEL 227
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
267-487 |
7.09e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 47.48 E-value: 7.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 267 TVLEIKNLSRAGQYR-------------DINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNn 333
Cdd:PRK15112 3 TLLEVRNLSKTFRYRtgwfrrqtveavkPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 334 tdaikrgIGYVSEdRLTLgaILQQ-SIADNMVISILDRLKTPWHLIDEKQCQDIVQEWIADLDIKVTDPNNAL---STLS 409
Cdd:PRK15112 82 -------YSYRSQ-RIRM--IFQDpSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASyypHMLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 410 GGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGV-GISILLITDEASEAYYNCDRILHMKQGSIVK 487
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
382-486 |
7.75e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 47.49 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 382 QCQDIVQEWIAD---LDIKVTDPNNalstLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVG 457
Cdd:PRK13640 119 EMIKIVRDVLADvgmLDYIDSEPAN----LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkKKNN 194
|
90 100 110
....*....|....*....|....*....|..
gi 491046221 458 ISILLIT---DEASEAyyncDRILHMKQGSIV 486
Cdd:PRK13640 195 LTVISIThdiDEANMA----DQVLVLDDGKLL 222
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
406-486 |
8.84e-06 |
|
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: 46.64 E-value: 8.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 406 STLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGvGISILLITDEASeAYYNCDRILHMKQGSI 485
Cdd:cd03369 124 LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT-NSTILTIAHRLR-TIIDYDKILVMDAGEV 201
|
.
gi 491046221 486 V 486
Cdd:cd03369 202 K 202
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
394-485 |
9.42e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 48.14 E-value: 9.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 394 LDIKVTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIgakDSIYKLIHRLSGVGISILLIT------DEA 467
Cdd:COG0488 139 LGFPEEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL---ESIEWLEEFLKNYPGTVLVVShdryflDRV 215
|
90
....*....|....*...
gi 491046221 468 seayynCDRILHMKQGSI 485
Cdd:COG0488 216 ------ATRILELDRGKL 227
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
408-487 |
9.74e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 47.32 E-value: 9.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVD-IGAK---DSIYKLiHRLSgvGISILLITDEASEAYYNCDRILHMKQG 483
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDpKGRKemmEMFYKL-HKEK--GLTTVLVTHSMEDAARYADQIVVMHKG 222
|
....
gi 491046221 484 SIVK 487
Cdd:PRK13634 223 TVFL 226
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
312-486 |
9.93e-06 |
|
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: 46.72 E-value: 9.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 312 GITHPDSGELFIEG----------KPVKL---KNNTDA---IKRGIGYVSEDRLTLGAILQQSIAdnmviSILDRLKtpw 375
Cdd:cd03298 46 GFETPQSGRVLINGvdvtaappadRPVSMlfqENNLFAhltVEQNVGLGLSPGLKLTAEDRQAIE-----VALARVG--- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 376 hlidekqcqdivqewIADLDIKVTDpnnalsTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL-S 454
Cdd:cd03298 118 ---------------LAGLEKRLPG------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhA 176
|
170 180 190
....*....|....*....|....*....|..
gi 491046221 455 GVGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:cd03298 177 ETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
281-486 |
1.26e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 46.92 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVklknntDAIKRGIGYVSEDRLTLGAILQQSI- 359
Cdd:PRK13638 18 KGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL------DYSKRGLLALRQQVATVFQDPEQQIf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 360 ---ADNMVISILDRLKTPwhlidEKQCQDIVQEWIADLDIKVTDpNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTV 436
Cdd:PRK13638 92 ytdIDSDIAFSLRNLGVP-----EAEITRRVDEALTLVDAQHFR-HQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491046221 437 GVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:PRK13638 166 GLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQIL 215
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
281-497 |
1.28e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 46.90 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKlKNNTDAIKRGIGYVSEDRLTLGAI-LQQSI 359
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQ-HYASKEVARRIGLLAQNATTPGDItVQELV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 360 ADNMVISilDRLKTPWHLIDEKQCQDIVQEW-IADLDIKVTDpnnalsTLSGGNQQKVVLAKWILTRPKVLILDSPTVGV 438
Cdd:PRK10253 103 ARGRYPH--QPLFTRWRKEDEEAVTKAMQATgITHLADQSVD------TLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 439 DIGAKDSIYKLIHRLSGV-GISILLITDEASEAYYNCDRILHMKQGSIV-----KEIVTDSINEQ 497
Cdd:PRK10253 175 DISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVaqgapKEIVTAELIER 239
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
316-486 |
1.39e-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: 46.38 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 316 PDSGELFIEGKPVKlKNNTDAIKRGIGYVSEDRltlgAILQQSIADNMVISILDRlktpwhlIDEKQCQDIVQEWIADLD 395
Cdd:cd03249 55 PTSGEILLDGVDIR-DLNLRWLRSQIGLVSQEP----VLFDGTIAENIRYGKPDA-------TDEEVEEAAKKANIHDFI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 396 IKVTDPNNAL-----STLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSgVGISILLITDEASeA 470
Cdd:cd03249 123 MSLPDGYDTLvgergSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLS-T 200
|
170
....*....|....*.
gi 491046221 471 YYNCDRILHMKQGSIV 486
Cdd:cd03249 201 IRNADLIAVLQNGQVV 216
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
344-494 |
1.44e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 46.63 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 344 VSEDRLTLGAILQQ------SIADNMVISILDRlktpwHLIDEKQCQDIVQEWIADLDI--KVTDP-NNALSTLSGGNQQ 414
Cdd:PRK14271 96 VLEFRRRVGMLFQRpnpfpmSIMDNVLAGVRAH-----KLVPRKEFRGVAQARLTEVGLwdAVKDRlSDSPFRLSGGQQQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 415 KVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGvGISILLITDEASEAYYNCDRILHMKQGSIVKEIVTDSI 494
Cdd:PRK14271 171 LLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLAD-RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
398-488 |
1.78e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 46.66 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 398 VTDPNNALST----LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLS-GVGISILLITDEASEAYY 472
Cdd:PRK11022 140 IPDPASRLDVyphqLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQqKENMALVLITHDLALVAE 219
|
90
....*....|....*.
gi 491046221 473 NCDRILHMKQGSIVKE 488
Cdd:PRK11022 220 AAHKIIVMYAGQVVET 235
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
269-485 |
2.03e-05 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 46.76 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLS--RAGQ--YRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKLKNNTdAIKRGIGYV 344
Cdd:PRK09536 4 IDVSDLSveFGDTtvLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAR-AASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 345 SEDrltlgailqQSIADNM-VISILDRLKTPwHL--IDEKQCQD--IVQEWIADLDI-KVTDpnNALSTLSGGNQQKVVL 418
Cdd:PRK09536 83 PQD---------TSLSFEFdVRQVVEMGRTP-HRsrFDTWTETDraAVERAMERTGVaQFAD--RPVTSLSGGERQRVLL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 419 AKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISIL-LITDEASEAYYnCDRILHMKQGSI 485
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVaAIHDLDLAARY-CDELVLLADGRV 217
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
358-487 |
2.03e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 45.99 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 358 SIADNMVISI-LDRLKTPWHLIDEkqcqdiVQEWI---ADLDIKVTDP-NNALSTLSGGNQQKVVLAKWILTRPKVLILD 432
Cdd:PRK14267 101 TIYDNVAIGVkLNGLVKSKKELDE------RVEWAlkkAALWDEVKDRlNDYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 433 SPTVGVDIGAKDSIYKLIHRLSGvGISILLITDEASEAYYNCDRILHMKQGSIVK 487
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFELKK-EYTIVLVTHSPAQAARVSDYVAFLYLGKLIE 228
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-179 |
2.10e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.43 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 7 ADKSDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGS-KI---EIDgksyhrlt 82
Cdd:NF033858 260 DDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEaWLfgqPVD-------- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 83 pdkARELGV--QVIY--QDLSLFPNLTVAENIafELNLKGYfgwfrkkQL-REKALEILNELA--FTIDP--DTPVQFLP 153
Cdd:NF033858 332 ---AGDIATrrRVGYmsQAFSLYGELTVRQNL--ELHARLF-------HLpAAEIAARVAEMLerFDLADvaDALPDSLP 399
|
170 180
....*....|....*....|....*...
gi 491046221 154 --IAQRQQVAIcrALVADARLVIMDEPT 179
Cdd:NF033858 400 lgIRQRLSLAV--AVIHKPELLILDEPT 425
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
408-477 |
2.14e-05 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 46.44 E-value: 2.14e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGV-GISILLITDEASEAYYNCDRI 477
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLqGTSILLISHDLESISQWADTI 229
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
400-440 |
2.21e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.25 E-value: 2.21e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 491046221 400 DPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDI 440
Cdd:PRK11147 149 DPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI 189
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
408-487 |
2.22e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 46.28 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVK 487
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVL 225
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
316-486 |
2.44e-05 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 46.70 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 316 PDSGELFIEGKPVKlKNNTDAIKRGIGYVSEDrltlGAILQQSIADNMVISILDrlktpwhlIDEKQCQDIVQ-----EW 390
Cdd:COG1132 392 PTSGRILIDGVDIR-DLTLESLRRQIGVVPQD----TFLFSGTIRENIRYGRPD--------ATDEEVEEAAKaaqahEF 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 391 IADLdikvtdPN--NAL-----STLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGA----KDSIYKLI--------- 450
Cdd:COG1132 459 IEAL------PDgyDTVvgergVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETealiQEALERLMkgrttivia 532
|
170 180 190
....*....|....*....|....*....|....*.
gi 491046221 451 HRLSgvgiSILlitdeaseayyNCDRILHMKQGSIV 486
Cdd:COG1132 533 HRLS----TIR-----------NADRILVLDDGRIV 553
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
258-485 |
2.61e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.89 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 258 PPNNAEDRRTVLEIKNLSRAgqYRD-------INLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVKL 330
Cdd:PRK10522 312 PRPQAFPDWQTLELRNVTFA--YQDngfsvgpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 331 kNNTDAIKRGIGYVSEDrltlgailqqsiadnmvISILDRLKTPwhlidEKQCQD--IVQEWIADLDI--KVTDPNNALS 406
Cdd:PRK10522 390 -EQPEDYRKLFSAVFTD-----------------FHLFDQLLGP-----EGKPANpaLVEKWLERLKMahKLELEDGRIS 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 407 T--LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIY-KLIHRLSGVGISILLITDEasEAYY-NCDRILHMKQ 482
Cdd:PRK10522 447 NlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYqVLLPLLQEMGKTIFAISHD--DHYFiHADRLLEMRN 524
|
...
gi 491046221 483 GSI 485
Cdd:PRK10522 525 GQL 527
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
26-221 |
3.71e-05 |
|
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: 44.24 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 26 HRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTisGVYAPddgskieidgksyhrltpdkarelGVQVIYQDLSLFPnlt 105
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNE--GLYAS------------------------GKARLISFLPKFS--- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 106 vaeniafelnlkgyfgwfRKKQLREKALEILNELAFT-IDPDTPVQFLPIAQRQQVAICRALVADAR--LVIMDEPTASL 182
Cdd:cd03238 59 ------------------RNKLIFIDQLQFLIDVGLGyLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGL 120
|
170 180 190
....*....|....*....|....*....|....*....
gi 491046221 183 TRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEiSDRI 221
Cdd:cd03238 121 HQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWI 158
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
408-492 |
3.95e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 45.61 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIVK 487
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
90
....*....|
gi 491046221 488 -----EIVTD 492
Cdd:PRK13631 257 tgtpyEIFTD 266
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
384-486 |
5.01e-05 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 45.00 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 384 QDIVQEWIADLDIkVTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLI 463
Cdd:PRK11231 116 NARVNQAMEQTRI-NHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTV 194
|
90 100
....*....|....*....|...
gi 491046221 464 TDEASEAYYNCDRILHMKQGSIV 486
Cdd:PRK11231 195 LHDLNQASRYCDHLVVLANGHVM 217
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1-241 |
5.25e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.50 E-value: 5.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 1 MTSTSKADKSDPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCG--KSTLIKTISGvyaPDDGSKieidgkSY 78
Cdd:NF000106 1 MTRKTISNGARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRR------PW 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 79 HRLTPDKARelgvQVIYQDLSLFPNLTVAENIAFE----LNLKGYFGWFRKKQLREKALEILNELAFTIDPDTPVQFLPI 154
Cdd:NF000106 72 RF*TWCANR----RALRRTIG*HRPVR*GRRESFSgrenLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 155 AQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWP 234
Cdd:NF000106 148 GMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGK 227
|
....*..
gi 491046221 235 AEGLTTR 241
Cdd:NF000106 228 VDELKTK 234
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
380-493 |
6.02e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 44.82 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 380 EKQCQDIVQEWIADLDIKVTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGIS 459
Cdd:PRK13641 118 EDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHT 197
|
90 100 110
....*....|....*....|....*....|....*....
gi 491046221 460 ILLITDEASEAYYNCDRILHMKQGSIVK-----EIVTDS 493
Cdd:PRK13641 198 VILVTHNMDDVAEYADDVLVLEHGKLIKhaspkEIFSDK 236
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
79-221 |
6.38e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.77 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 79 HRLTPDKareLGVQVIYQDLSLFPNLTVAENIAF--ELNLKGyfgwfRKKQLREKAL-EILNELAFTID-------PDTP 148
Cdd:TIGR00630 414 TRLKPEA---LAVTVGGKSIADVSELSIREAHEFfnQLTLTP-----EEKKIAEEVLkEIRERLGFLIDvgldylsLSRA 485
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491046221 149 VQFLPIAQRQQVAICRALvaDARLV----IMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRlEEVKEISDRI 221
Cdd:TIGR00630 486 AGTLSGGEAQRIRLATQI--GSGLTgvlyVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHD-EDTIRAADYV 559
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
406-488 |
7.47e-05 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 44.79 E-value: 7.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 406 STLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKL---IHRLsgVGISILLITDEASEAYYNCDRILHMKQ 482
Cdd:PRK11153 139 AQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELlkdINRE--LGLTIVLITHEMDVVKRICDRVAVIDA 216
|
....*.
gi 491046221 483 GSIVKE 488
Cdd:PRK11153 217 GRLVEQ 222
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
281-497 |
7.78e-05 |
|
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: 44.56 E-value: 7.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPvklknntdaikrgIGYVSEDRLTlgAILQQSIA 360
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQD-------------IAAMSRKELR--ELRRKKIS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 361 dnMVI---------SILDRLKTPWHL--IDEKQCQDIVQEWIADLDIKvTDPNNALSTLSGGNQQKVVLAKWILTRPKVL 429
Cdd:cd03294 106 --MVFqsfallphrTVLENVAFGLEVqgVPRAEREERAAEALELVGLE-GWEHKYPDELSGGMQQRVGLARALAVDPDIL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491046221 430 ILDSPTVGVDIGAKDSIYKLIHRLSG-VGISILLITDEASEAYYNCDRILHMKQGSIV-----KEIVTDSINEQ 497
Cdd:cd03294 183 LMDEAFSALDPLIRREMQDELLRLQAeLQKTIVFITHDLDEALRLGDRIAIMKDGRLVqvgtpEEILTNPANDY 256
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
404-497 |
7.94e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.73 E-value: 7.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 404 ALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQG 483
Cdd:NF000106 141 AAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRG 220
|
90
....*....|....
gi 491046221 484 SIVKEIVTDSINEQ 497
Cdd:NF000106 221 RVIADGKVDELKTK 234
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
375-486 |
8.25e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 45.22 E-value: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 375 WHLIDEKQCQDIVQEWIADLDIKVTDPNnalSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLS 454
Cdd:PRK11174 456 QQALENAWVSEFLPLLPQGLDTPIGDQA---AGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS 532
|
90 100 110
....*....|....*....|....*....|..
gi 491046221 455 GvGISILLITDEAsEAYYNCDRILHMKQGSIV 486
Cdd:PRK11174 533 R-RQTTLMVTHQL-EDLAQWDQIWVMQDGQIV 562
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
44-260 |
8.56e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.35 E-value: 8.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 44 LAGTNGCGKSTLIKTISGVYAPDDGsKIEIDGKSYHRLTPDKARELgVQVIYQDLSLFPNlTVAENI-AF-ELNLKGYFG 121
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKG-RIMIDDCDVAKFGLTDLRRV-LSIIPQSPVLFSG-TVRFNIdPFsEHNDADLWE 1343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 122 WFRKKQLREkaleILNELAFTIDPDTPV--QFLPIAQRQQVAICRALVADARLVIMDEPTASLTrTEVNQLLSTVNYLKD 199
Cdd:PLN03232 1344 ALERAHIKD----VIDRNPFGLDAEVSEggENFSVGQRQLLSLARALLRRSKILVLDEATASVD-VRTDSLIQRTIREEF 1418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491046221 200 KGITVVFVSHRLEEVKEiSDRITVIRDGQKIGTWPAEGLTTRKITELMTgldIVHERKPPN 260
Cdd:PLN03232 1419 KSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFR---MVHSTGPAN 1475
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
281-481 |
8.92e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 44.49 E-value: 8.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKPVK--LKNNTdaikrgIGYV--SEDRLTLGAILQ 356
Cdd:PRK15056 24 RDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRqaLQKNL------VAYVpqSEEVDWSFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 357 QSIAdnmvisILDRL-KTPWHLIDEKQCQDIVQEWIADLDIkVTDPNNALSTLSGGNQQKVVLAKWILTRPKVLILDSPT 435
Cdd:PRK15056 98 EDVV------MMGRYgHMGWLRRAKKRDRQIVTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491046221 436 VGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMK 481
Cdd:PRK15056 171 TGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
402-488 |
9.37e-05 |
|
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: 43.07 E-value: 9.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 402 NNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLI-------------HRLSGVgisillitdeas 468
Cdd:cd03247 93 NNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIfevlkdktliwitHHLTGI------------ 160
|
90 100
....*....|....*....|
gi 491046221 469 eayYNCDRILHMKQGSIVKE 488
Cdd:cd03247 161 ---EHMDKILFLENGKIIMQ 177
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
401-463 |
1.01e-04 |
|
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: 43.08 E-value: 1.01e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 401 PNNALSTLSGGNQQKVVLAKWILTRPK--VLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLI 463
Cdd:cd03238 81 LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILI 145
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
408-492 |
1.01e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 43.96 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGSIV- 486
Cdd:PRK13647 139 LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLa 218
|
....*....
gi 491046221 487 ---KEIVTD 492
Cdd:PRK13647 219 egdKSLLTD 227
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
29-245 |
1.27e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGvyaPDDGSKIEIDGK--SYHRLTPDKARELGVqvIYQDLSLFPNLTV 106
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG---RKTGGYIEGDIRisGFPKKQETFARISGY--CEQNDIHSPQVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 107 AENIAFE--LNLKGYFGWFRKKQLREKALEI--LNELAFTIDPDTPVQFLPIAQRQQVAICRALVADARLVIMDEPTASL 182
Cdd:PLN03140 971 RESLIYSafLRLPKEVSKEEKMMFVDEVMELveLDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 183 TRTEVNQLLSTVNYLKDKGITVVFVSHRLE-EVKEISDRITVI-RDGQKIGTWPAeGLTTRKITE 245
Cdd:PLN03140 1051 DARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMkRGGQVIYSGPL-GRNSHKIIE 1114
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
408-486 |
1.58e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 43.46 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLS-GVGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNkEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
393-484 |
2.06e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 393 DLDIKVTDPNNALSTLSGGNQQKVVLAKWILTRPK--VLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLIT-DEASE 469
Cdd:PRK00635 462 DLGLPYLTPERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEhDEQMI 541
|
90
....*....|....*
gi 491046221 470 AYynCDRILHMKQGS 484
Cdd:PRK00635 542 SL--ADRIIDIGPGA 554
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
172-215 |
2.34e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.85 E-value: 2.34e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 491046221 172 LVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVK 215
Cdd:TIGR00630 853 LYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIK 896
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
405-483 |
2.49e-04 |
|
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: 41.28 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 405 LSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGvgiSILLIT------DEAseayynCDRIL 478
Cdd:cd03221 68 FEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG---TVILVShdryflDQV------ATKII 138
|
....*
gi 491046221 479 HMKQG 483
Cdd:cd03221 139 ELEDG 143
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
406-455 |
2.57e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.86 E-value: 2.57e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 491046221 406 STLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSG 455
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKG 627
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
316-486 |
2.96e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 43.41 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 316 PDSGELFIEGKPVKlKNNTDAIKRGIGYVSEDRLtlgaILQQSIADNMVISILDRLKTPWHLIDEK-QCQDIVQEWIADL 394
Cdd:PRK13657 387 PQSGRILIDGTDIR-TVTRASLRRNIAVVFQDAG----LFNRSIEDNIRVGRPDATDEEMRAAAERaQAHDFIERKPDGY 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 395 DIKVTDPNNALStlsGGNQQKVVLAKWILTRPKVLILDSPTVGVDI-------GAKDSIYK------LIHRLSGVgisil 461
Cdd:PRK13657 462 DTVVGERGRQLS---GGERQRLAIARALLKDPPILILDEATSALDVeteakvkAALDELMKgrttfiIAHRLSTV----- 533
|
170 180
....*....|....*....|....*
gi 491046221 462 litdeaseayYNCDRILHMKQGSIV 486
Cdd:PRK13657 534 ----------RNADRILVFDNGRVV 548
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
269-486 |
3.38e-04 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 42.76 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 269 LEIKNLS-----RAGQY---RDINLNLKRGEVlglcgllgsgrtelalslFGI---------T---------HPDSGELF 322
Cdd:COG1135 2 IELENLSktfptKGGPVtalDDVSLTIEKGEI------------------FGIigysgagksTlircinlleRPTSGSVL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 323 IEGKPVKLKNNTD--AIKRGIGYvsedrltlgaILQQ-------SIADN----MVISILDRLKtpwhlIDEKqcqdiVQE 389
Cdd:COG1135 64 VDGVDLTALSERElrAARRKIGM----------IFQHfnllssrTVAENvalpLEIAGVPKAE-----IRKR-----VAE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 390 wIADLdikV--TDPNNAL-STLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLI----HRLsgvGISILL 462
Cdd:COG1135 124 -LLEL---VglSDKADAYpSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLkdinREL---GLTIVL 196
|
250 260
....*....|....*....|....*..
gi 491046221 463 ITDEAS---EAyynCDRILHMKQGSIV 486
Cdd:COG1135 197 ITHEMDvvrRI---CDRVAVLENGRIV 220
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
267-469 |
3.60e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 42.44 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 267 TVLEIKNLS-RAGQ---YRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGkpvklkNNTDAIKRGIG 342
Cdd:PRK11831 6 NLVDMRGVSfTRGNrciFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDG------ENIPAMSRSRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 343 YVSEDRLTLgaiLQQSIADNMVISILDRLKtpWHLIDEKQCQDIVQEWIADLDIKVTDPNNAL----STLSGGNQQKVVL 418
Cdd:PRK11831 80 YTVRKRMSM---LFQSGALFTDMNVFDNVA--YPLREHTQLPAPLLHSTVMMKLEAVGLRGAAklmpSELSGGMARRAAL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491046221 419 AKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRL-SGVGISILLITDEASE 469
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELnSALGVTCVVVSHDVPE 206
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
11-68 |
3.78e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.23 E-value: 3.78e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 11 DPLITLRDLSKSFGGHRALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDG 68
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSG 367
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
375-487 |
4.10e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.43 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 375 WHLIDEKQCQDIVQEWIADLDIKVTDPNNALSTlsgGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIhRLS 454
Cdd:PLN03232 1342 WEALERAHIKDVIDRNPFGLDAEVSEGGENFSV---GQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTI-REE 1417
|
90 100 110
....*....|....*....|....*....|...
gi 491046221 455 GVGISILLITDEASeAYYNCDRILHMKQGSIVK 487
Cdd:PLN03232 1418 FKSCTMLVIAHRLN-TIIDCDKILVLSSGQVLE 1449
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
359-468 |
4.24e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 42.81 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 359 IADNMVISILDRLKTPwHLIDEKQCQDIVQEWiadldikvtdpnnaLSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGV 438
Cdd:TIGR00954 549 LSDKDLEQILDNVQLT-HILEREGGWSAVQDW--------------MDVLSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
|
90 100 110
....*....|....*....|....*....|
gi 491046221 439 DIGAKDSIYKLIHRlsgVGISILLITDEAS 468
Cdd:TIGR00954 614 SVDVEGYMYRLCRE---FGITLFSVSHRKS 640
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
409-487 |
4.30e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 41.94 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 409 SGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLIT------DeaseaYYNCDRILHMKQ 482
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILIThyqrllD-----YIKPDYVHVMQN 227
|
....*
gi 491046221 483 GSIVK 487
Cdd:CHL00131 228 GKIIK 232
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
281-488 |
4.87e-04 |
|
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: 41.83 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEG---KPVKLKNntdaIKRGIGYVSEDRLtlgaILQQ 357
Cdd:cd03251 19 RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvRDYTLAS----LRRQIGLVSQDVF----LFND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 358 SIADNMVISILDrlktpwhlIDEKQCQDIVQ-----EWIADL----DIKVTDPNnalSTLSGGNQQKVVLAKWILTRPKV 428
Cdd:cd03251 91 TVAENIAYGRPG--------ATREEVEEAARaanahEFIMELpegyDTVIGERG---VKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 429 LILDSPTVGVDIGAKDSIYKLIHRLSgVGISILLITDEASeAYYNCDRILHMKQGSIVKE 488
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLS-TIENADRIVVLEDGKIVER 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
407-484 |
4.89e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 43.08 E-value: 4.89e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 407 TLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDEASEAYYNCDRILHMKQGS 484
Cdd:TIGR01257 2070 TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGA 2147
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
252-450 |
5.43e-04 |
|
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: 43.01 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 252 IVHERKPPNNAEDRRTVlEIKNLS---RAGQ---YRDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEG 325
Cdd:TIGR00957 1269 QIQETAPPSGWPPRGRV-EFRNYClryREDLdlvLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG 1347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 326 KPVKlKNNTDAIKRGIGYVSEDRLTLGAILQQSIADNMVISILDrlktPWHLIDEKQCQDIVQEWIADLDIKVTDPNNAL 405
Cdd:TIGR00957 1348 LNIA-KIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEE----VWWALELAHLKTFVSALPDKLDHECAEGGENL 1422
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491046221 406 STlsgGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLI 450
Cdd:TIGR00957 1423 SV---GQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTI 1464
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
408-496 |
5.79e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 41.82 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGvGISILLITDEASEAYYNCDRILHMKQGSIV- 486
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK-DMTIVLVTHFPQQAARISDYVAFLYKGQIVe 225
|
90
....*....|....
gi 491046221 487 ----KEIVTDSINE 496
Cdd:PRK14247 226 wgptREVFTNPRHE 239
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
38-227 |
6.40e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.43 E-value: 6.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 38 KGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIEIDGKSYHRLTPDKARELGVQVIYQDLSlfpnltvaeniafelnlk 117
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGS------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 118 gyfgwfrkkqlREKALEILNELAFTIDPDtpvqflpiaqrqqvaicralvadarLVIMDEPTASLTRTEVNQLLSTV--- 194
Cdd:smart00382 63 -----------GELRLRLALALARKLKPD-------------------------VLILDEITSLLDAEQEALLLLLEelr 106
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491046221 195 ---NYLKDKGITVVFVSHRLEEVKE-----ISDRITVIRDG 227
Cdd:smart00382 107 lllLLKSEKNLTVILTTNDEKDLGPallrrRFDRRIVLLLI 147
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
406-486 |
8.92e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 42.02 E-value: 8.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 406 STLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSGVGISILLITDE---ASEAyyncDRILHMKQ 482
Cdd:PRK10535 143 SQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDpqvAAQA----ERVIEIRD 218
|
....
gi 491046221 483 GSIV 486
Cdd:PRK10535 219 GEIV 222
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
29-227 |
9.60e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.03 E-value: 9.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIEIDGKsyhrltpdkarelgVQVIYQdLSLFPNLTVAE 108
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGT--------------VAYVPQ-VSWIFNATVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 109 NIAF--ELNLKGYFGWFRKKQLREKaLEILNELAFTIDPDTPVQfLPIAQRQQVAICRALVADARLVIMDEPTASLTRTE 186
Cdd:PLN03130 698 NILFgsPFDPERYERAIDVTALQHD-LDLLPGGDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHV 775
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491046221 187 VNQLLSTVnyLKD--KGITVVFVSHRLEEVKEIsDRITVIRDG 227
Cdd:PLN03130 776 GRQVFDKC--IKDelRGKTRVLVTNQLHFLSQV-DRIILVHEG 815
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
27-112 |
1.16e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 40.24 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 27 RALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGSKIeidgksYHRLTPDKARELGVQVIYQDLSLFPNLTV 106
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIY------YKNCNINNIAKPYCTYIGHNLGLKLEMTV 87
|
....*.
gi 491046221 107 AENIAF 112
Cdd:PRK13541 88 FENLKF 93
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
309-486 |
1.20e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.65 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 309 SLFGITHPDSGELFIEGkpvklknnTDAIKRGIgyvSEDRLTLGAILQQSIADNMVISI-LDRLKTP-----WHLIDEKQ 382
Cdd:PLN03130 1284 ALFRIVELERGRILIDG--------CDISKFGL---MDLRKVLGIIPQAPVLFSGTVRFnLDPFNEHndadlWESLERAH 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 383 CQDIVQEWIADLDIKVTDpnnALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLI------------ 450
Cdd:PLN03130 1353 LKDVIRRNSLGLDAEVSE---AGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIreefksctmlii 1429
|
170 180 190
....*....|....*....|....*....|....*..
gi 491046221 451 -HRLSgvgisilLITDeaseayynCDRILHMKQGSIV 486
Cdd:PLN03130 1430 aHRLN-------TIID--------CDRILVLDAGRVV 1451
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
377-435 |
1.82e-03 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 40.69 E-value: 1.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 377 LIDEK-QCQDIVQEWIA-DLDIKVTDPNNAL---------STLSGGNQQKVVLAKWILTRPKVLILDSPT 435
Cdd:TIGR03719 120 LAAEQaELQEIIDAADAwDLDSQLEIAMDALrcppwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPT 189
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
406-486 |
1.91e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 40.63 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 406 STLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLSG-VGISILLITDEASEAYYNCDRILHMKQGS 484
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAReINIPILYVSHSLDEILRLADRVVVLEQGK 206
|
..
gi 491046221 485 IV 486
Cdd:PRK11144 207 VK 208
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
407-450 |
2.13e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.78 E-value: 2.13e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 491046221 407 TLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLI 450
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1401
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
24-221 |
2.42e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 38.88 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 24 GGHR-ALRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISGVYapddgskieidGKSYHRLTPDKARELGVQVIYQDLSLFp 102
Cdd:cd03227 5 GRFPsYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLAL-----------GGAQSATRRRSGVKAGCIVAAVSAELI- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 103 nltvaeniafelnlkgyfgwFRKKQLrEKALEILNELAFtidpdtpvqflpiaqrqQVAIcrALVADARLVIMDEPTASL 182
Cdd:cd03227 73 --------------------FTRLQL-SGGEKELSALAL-----------------ILAL--ASLKPRPLYILDEIDRGL 112
|
170 180 190
....*....|....*....|....*....|....*....
gi 491046221 183 TRTEVNQLLSTVNYLKDKGITVVFVSHRlEEVKEISDRI 221
Cdd:cd03227 113 DPRDGQALAEAILEHLVKGAQVIVITHL-PELAELADKL 150
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
154-227 |
3.09e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 39.51 E-value: 3.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 154 IAQRQQVAICRALVADARLVIMDEPTASLTRTEVNQLLSTV-NYLKDKgiTVVFVSHRLEEVKEiSDRITVIRDG 227
Cdd:cd03288 159 VGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVmTAFADR--TVVTIAHRVSTILD-ADLVLVLSRG 230
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
27-56 |
3.58e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 39.53 E-value: 3.58e-03
10 20 30
....*....|....*....|....*....|
gi 491046221 27 RALRNIDLTLnkGEVHCLAGTNGCGKSTLI 56
Cdd:COG4637 11 KSLRDLELPL--GPLTVLIGANGSGKSNLL 38
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
29-247 |
4.06e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.77 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 29 LRNIDLTLNKGEVHCLAGTNGCGKSTLIKTISG-VYAPDDGSKIEIDGKSYHRLTPDKARELGVQVIYQD---LSLfpNL 104
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrSYGRNISGTVFKDGKEVDVSTVSDAIDAGLAYVTEDrkgYGL--NL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 105 --TVAENIAFElNLKGY--FGW------------FRKKqLREKALEIlnelaftidpDTPVQFLPIAQRQQVAICRALVA 168
Cdd:NF040905 354 idDIKRNITLA-NLGKVsrRGVideneeikvaeeYRKK-MNIKTPSV----------FQKVGNLSGGNQQKVVLSKWLFT 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491046221 169 DARLVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVKEISDRITVIRDGQKIGTWPAEGLTTRKITELM 247
Cdd:NF040905 422 DPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGELPREEASQERIMRLI 500
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
113-230 |
4.31e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 113 ELNLKGYFGWFRKKQLREKAL-EIL----NELAFTID-------PDTPVQFLPIAQRQQVAICRALVADARLV--IMDEP 178
Cdd:PRK00635 426 QMSLQELFIFLSQLPSKSLSIeEVLqglkSRLSILIDlglpyltPERALATLSGGEQERTALAKHLGAELIGItyILDEP 505
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 491046221 179 TASLTRTEVNQLLSTVNYLKDKGITVVFVSHRlEEVKEISDRITVIRDGQKI 230
Cdd:PRK00635 506 SIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADRIIDIGPGAGI 556
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
402-483 |
4.36e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 39.86 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 402 NNALSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKdsiYKLIHRLSGV---GISILL-ITDEASEAYYNCDRI 477
Cdd:PLN03211 201 NSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAA---YRLVLTLGSLaqkGKTIVTsMHQPSSRVYQMFDSV 277
|
....*.
gi 491046221 478 LHMKQG 483
Cdd:PLN03211 278 LVLSEG 283
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
408-494 |
4.61e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 39.40 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 408 LSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLS-GVGISILLITDEASEAYYNCDRILHMKQGSIV 486
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNqNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
....*...
gi 491046221 487 KEIVTDSI 494
Cdd:PRK15093 239 ETAPSKEL 246
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
14-75 |
4.65e-03 |
|
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: 38.32 E-value: 4.65e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491046221 14 ITLRDLSKSFGGHRALRNIDlTLNKGEVHCLAGTNGCGKSTLIKTISGVYAPDDGsKIEIDG 75
Cdd:cd03222 1 QLYPDCVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGD-NDEWDG 60
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
407-463 |
4.96e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 4.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491046221 407 TLSGGNQQKVVLAKWILTR---PKVLILDSPTVGVDIgakDSIYKL---IHRLSGVGISILLI 463
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHF---DDIKKLlevLQRLVDKGNTVVVI 888
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
172-215 |
5.04e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 38.75 E-value: 5.04e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 491046221 172 LVIMDEPTASLTRTEVNQLLSTVNYLKDKGITVVFVSHRLEEVK 215
Cdd:cd03271 193 LYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIK 236
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
27-139 |
5.89e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.83 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 27 RALRNIDLTLNKGE-VHCLAGTNGCGKSTLIKTISGVYAPDDGSKIEIDGKSY-------------------HRLTPDKA 86
Cdd:COG3950 12 RGFEDLEIDFDNPPrLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLlirngefgdsaklilyygtSRLLLDGP 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 491046221 87 RELGVQVIYQDLSLFPNLtvAENIAFELNLKGYFGWFR--KKQLREKALEILNEL 139
Cdd:COG3950 92 LKKLERLKEEYFSRLDGY--DSLLDEDSNLREFLEWLReyLEDLENKLSDELDEK 144
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
375-496 |
6.03e-03 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 39.51 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 375 WHLIDEKQCQDIVQEWIADLDIKVTDPNnalSTLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYK-LIHRL 453
Cdd:TIGR01271 1324 WKVAEEVGLKSVIEQFPDKLDFVLVDGG---YVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKtLKQSF 1400
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 491046221 454 SGVGIsilLITDEASEAYYNCDRILhMKQGSIVKEIvtDSINE 496
Cdd:TIGR01271 1401 SNCTV---ILSEHRVEALLECQQFL-VIEGSSVKQY--DSIQK 1437
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
281-484 |
7.37e-03 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 38.30 E-value: 7.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 281 RDINLNLKRGEVLGLCGLLGSGRTELALSLFGITHPDSGELFIEGKpvklknntdaikrgIGYVSEdrltLGAILQQSIA 360
Cdd:cd03291 54 KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------------ISFSSQ----FSWIMPGTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491046221 361 DNMVISIldrlktpwhLIDEKQCQDIVQEWIADLDI-KVTDPNNALS-----TLSGGNQQKVVLAKWILTRPKVLILDSP 434
Cdd:cd03291 116 ENIIFGV---------SYDEYRYKSVVKACQLEEDItKFPEKDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491046221 435 TVGVDIGAKDSIY-KLIHRLSGVGISILLITDeaSEAYYNCDRILHMKQGS 484
Cdd:cd03291 187 FGYLDVFTEKEIFeSCVCKLMANKTRILVTSK--MEHLKKADKILILHEGS 235
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
403-470 |
7.96e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 38.22 E-value: 7.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491046221 403 NALStLSGGNQQKVVLAKWILTRPKVLILDSPTVGVDIGAKDSIYKLIHRLsGVGISILLITDEASEA 470
Cdd:PRK14243 148 SGLS-LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHNMQQA 213
|
|
|