|
Name |
Accession |
Description |
Interval |
E-value |
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-516 |
0e+00 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 613.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYGLGMV 97
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGIGMV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 98 YQHFTLVPSLTGAENLVISRTEVPA-VINWPRERKALAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVL 176
Cdd:COG3845 86 HQHFMLVPNLTVAENIVLGLEPTKGgRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILIL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 177 DEPTSVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELSTAEMAAMMIG-DVkl 255
Cdd:COG3845 166 DEPTAVLTPQEADELFEILRRLAAEG-KSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMVGrEV-- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 256 aELDTRIPVTETAKAVLQIERIKAPDRSGLKTIEIDSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAA 335
Cdd:COG3845 243 -LLRVEKAPAEPGEVVLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGED 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 336 YGATRPETRRNN-VRFIPEEPLQNACAPRMSVSENLAFRTFDLKESGAdAIWLNRNKIKKGATALIADFKVRTASQSSPI 414
Cdd:COG3845 322 ITGLSPRERRRLgVAYIPEDRLGRGLVPDMSVAENLILGRYRRPPFSR-GGFLDRKAIRAFAEELIEEFDVRTPGPDTPA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 415 AALSGGNVQRAVLARELTGEVDLLIVSNPCFGLDFSAVAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMVISEGKL 494
Cdd:COG3845 401 RSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
490 500
....*....|....*....|..
gi 2790395612 495 VYETAARSADISVIGAHMAGHH 516
Cdd:COG3845 481 VGEVPAAEATREEIGLLMAGVK 502
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
22-516 |
7.43e-131 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 389.38 E-value: 7.43e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 22 DMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYGLGMVYQHF 101
Cdd:COG1129 9 GISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGIAIIHQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 102 TLVPSLTGAENLVISRTEVPA-VINWPRERKALAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPT 180
Cdd:COG1129 89 NLVPNLSVAENIFLGREPRRGgLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 181 SVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELSTAEMAAMMIGDvklaELDT 260
Cdd:COG1129 169 ASLTEREVERLFRIIRRLKAQG-VAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVGR----ELED 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 261 RIPVTETAKA--VLQIERIKAPDRsgLKTIeidSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGA 338
Cdd:COG1129 244 LFPKRAAAPGevVLEVEGLSVGGV--VRDV---SFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 339 TRPETR-RNNVRFIPEEPLQNACAPRMSVSENLAFRTFDlkeSGADAIWLNRNKIKKGATALIADFKVRTASQSSPIAAL 417
Cdd:COG1129 319 RSPRDAiRAGIAYVPEDRKGEGLVLDLSIRENITLASLD---RLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 418 SGGNVQRAVLARELTGEVDLLIVSNPCFGLDFSAVAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLVYE 497
Cdd:COG1129 396 SGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGE 475
|
490
....*....|....*....
gi 2790395612 498 TAARSADISVIGAHMAGHH 516
Cdd:COG1129 476 LDREEATEEAIMAAATGGA 494
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-494 |
3.65e-77 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 251.00 E-value: 3.65e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 21 LDM---TMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFY-HQT-SGSLSVDGREVTIASPKDAAAYGLG 95
Cdd:PRK13549 6 LEMkniTKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYpHGTyEGEIIFEGEELQASNIRDTERAGIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 96 MVYQHFTLVPSLTGAENLVISRTEVPA-VINWPRERKALAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFL 174
Cdd:PRK13549 86 IIHQELALVKELSVLENIFLGNEITPGgIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 175 VLDEPTSVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELSTAEMAAMMIGDvK 254
Cdd:PRK13549 166 ILDEPTASLTESETAVLLDIIRDLKAHG-IACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMMVGR-E 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 255 LAELDTRIPvTETAKAVLQIERIKA--PDRSGLKTIEIDSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQ-AGSVTV 331
Cdd:PRK13549 244 LTALYPREP-HTIGEVILEVRNLTAwdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 332 KGAAYGATRP-ETRRNNVRFIPEEPLQNACAPRMSVSENLAFRTFDlKESGADAIwlNRNKIKKGATALIADFKVRTASQ 410
Cdd:PRK13549 323 DGKPVKIRNPqQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALD-RFTGGSRI--DDAAELKTILESIQRLKVKTASP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 411 SSPIAALSGGNVQRAVLARELTGEVDLLIVSNPCFGLDFSAVAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMVIS 490
Cdd:PRK13549 400 ELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMH 479
|
....
gi 2790395612 491 EGKL 494
Cdd:PRK13549 480 EGKL 483
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-503 |
2.79e-74 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 243.92 E-value: 2.79e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYGLGMV 97
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 98 YQHFTLVPSLTGAENLVISRTEVPAV-----INWPRERKALAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRS 172
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGRHLTKKVcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 173 FLVLDEPTSVLTPAEADEMLGLVRGMTERGElTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELSTAEMAAMMIGD 252
Cdd:PRK09700 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGT-AIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVGR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 253 VKLAELDTRIPVTETA--KAVLQIERIKAPDRSGLKTIeidSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVT 330
Cdd:PRK09700 245 ELQNRFNAMKENVSNLahETVFEVRNVTSRDRKKVRDI---SFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 331 VKGAAYGATRP-ETRRNNVRFIPEEPLQNACAPRMSVSENLAFRTFdLKESGADAIW--LNRNKIKKGATALIADFKVRT 407
Cdd:PRK09700 322 LNGKDISPRSPlDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRS-LKDGGYKGAMglFHEVDEQRTAENQRELLALKC 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 408 ASQSSPIAALSGGNVQRAVLARELTGEVDLLIVSNPCFGLDFSAVAEIRaRIMRA-RNAGAAVLLLSEDLDELMEMSDRI 486
Cdd:PRK09700 401 HSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIY-KVMRQlADDGKVILMVSSELPEIITVCDRI 479
|
490
....*....|....*..
gi 2790395612 487 MVISEGKLVYETAARSA 503
Cdd:PRK09700 480 AVFCEGRLTQILTNRDD 496
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
32-504 |
7.42e-74 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 242.12 E-value: 7.42e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 32 ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYGLGMVYQHFTLVPSLTGAE 111
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAIIYQELHLVPEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 112 NLVISRteVPAVINWPRERKALA---AFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTPAEA 188
Cdd:PRK11288 99 NLYLGQ--LPHKGGIVNRRLLNYearEQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 189 DEMLGLVRGMTERGELtVLMISHKFHEVTKFADAVSILRRGKLIGS-GKVGELSTAEMAAMM----IGDVklaeLDTRip 263
Cdd:PRK11288 177 EQLFRVIRELRAEGRV-ILYVSHRMEEIFALCDAITVFKDGRYVATfDDMAQVDRDQLVQAMvgreIGDI----YGYR-- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 264 VTETAKAVLQIERIKAPdrsGLKtiEIDSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRP-E 342
Cdd:PRK11288 250 PRPLGEVRLRLDGLKGP---GLR--EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPrD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 343 TRRNNVRFIPEEPLQNACAPRMSVSENLA------FRTFDLkesgadaiWLNRNKIKKGATALIADFKVRTASQSSPIAA 416
Cdd:PRK11288 325 AIRAGIMLCPEDRKAEGIIPVHSVADNINisarrhHLRAGC--------LINNRWEAENADRFIRSLNIKTPSREQLIMN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 417 LSGGNVQRAVLARELTGEVDLLIVSNPCFGLDFSAVAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLVY 496
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAG 476
|
....*...
gi 2790395612 497 ETAARSAD 504
Cdd:PRK11288 477 ELAREQAT 484
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
32-504 |
2.77e-72 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 238.36 E-value: 2.77e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 32 ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYGLGMVYQHFTLVPSLTGAE 111
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 112 NLVISRTEVPAV--INWPRERKALAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTPAEAD 189
Cdd:PRK10762 99 NIFLGREFVNRFgrIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 190 EMLGLVRGMTERGELTVlMISHKFHEVTKFADAVSILRRGKLIGSGKVGELSTAEMAAMMIGDvKLAELDTRIPVtETAK 269
Cdd:PRK10762 179 SLFRVIRELKSQGRGIV-YISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVGR-KLEDQYPRLDK-APGE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 270 AVLQIERIKAPdrsGLKTIeidSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRP-ETRRNNV 348
Cdd:PRK10762 256 VRLKVDNLSGP---GVNDV---SFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPqDGLANGI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 349 RFIPEEPLQNACAPRMSVSENL---AFRTFDlKESGAdaiwLNRNKIKKGATALIADFKVRTASQSSPIAALSGGNVQRA 425
Cdd:PRK10762 330 VYISEDRKRDGLVLGMSVKENMsltALRYFS-RAGGS----LKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQKV 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790395612 426 VLARELTGEVDLLIVSNPCFGLDFSAVAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLVYETAARSAD 504
Cdd:PRK10762 405 AIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQAT 483
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-494 |
1.20e-68 |
|
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: 228.56 E-value: 1.20e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 23 MTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFY-HQT-SGSLSVDGREVTIASPKDAAAYGLGMVYQH 100
Cdd:TIGR02633 7 IVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYpHGTwDGEIYWSGSPLKASNIRDTERAGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 101 FTLVPSLTGAENLVI--------SRTEVPAVInwpreRKALAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRS 172
Cdd:TIGR02633 87 LTLVPELSVAENIFLgneitlpgGRMAYNAMY-----LRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 173 FLVLDEPTSVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELSTAEMAAMMIGD 252
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAHG-VACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 253 vKLAELDTRIPvTETAKAVLQIERIKA--PDRSGLKTIEIDSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQ-AGSV 329
Cdd:TIGR02633 241 -EITSLYPHEP-HEIGDVILEARNLTCwdVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 330 TVKGAAYGATRP-ETRRNNVRFIPEEPLQNACAPRMSVSENLafrTFDLKESGADAIWLNRNKIKKGATALIADFKVRTA 408
Cdd:TIGR02633 319 FINGKPVDIRNPaQAIRAGIAMVPEDRKRHGIVPILGVGKNI---TLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 409 SQSSPIAALSGGNVQRAVLARELTGEVDLLIVSNPCFGLDFSAVAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMV 488
Cdd:TIGR02633 396 SPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLV 475
|
....*.
gi 2790395612 489 ISEGKL 494
Cdd:TIGR02633 476 IGEGKL 481
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-513 |
1.45e-65 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 220.69 E-value: 1.45e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYGLGMV 97
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 98 YQHFTLVPSLTGAENLVISRTEVPAvinwpRERKaLAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLD 177
Cdd:PRK15439 92 PQEPLLFPNLSVKENILFGLPKRQA-----SMQK-MKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 178 EPTSVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELSTAEMAAMMIGDVKLAE 257
Cdd:PRK15439 166 EPTASLTPAETERLFSRIRELLAQG-VGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAITPAAREKS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 258 L-DTRI---------PVTETAKAVLQIERIkapdrSGLKTIEIdSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAG 327
Cdd:PRK15439 245 LsASQKlwlelpgnrRQQAAGAPVLTVEDL-----TGEGFRNI-SLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 328 SVTVKGAAYGATRPETR-RNNVRFIPEEPLQNACAPRMSVSENLAFRTFDLKesgadAIWLNRNKIKKGATALIADFKVR 406
Cdd:PRK15439 319 RIMLNGKEINALSTAQRlARGLVYLPEDRQSSGLYLDAPLAWNVCALTHNRR-----GFWIKPARENAVLERYRRALNIK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 407 TASQSSPIAALSGGNVQRAVLARELTGEVDLLIVSNPCFGLDFSAVAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRI 486
Cdd:PRK15439 394 FNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRV 473
|
490 500
....*....|....*....|....*..
gi 2790395612 487 MVISEGKLVYETAARSADISVIgAHMA 513
Cdd:PRK15439 474 LVMHQGEISGALTGAAINVDTI-MRLA 499
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-234 |
2.73e-62 |
|
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: 201.12 E-value: 2.73e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYGLGMV 97
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 98 YqhftlvpsltgaenlvisrtevpavinwprerkalaafmehmpfqipldrpvsQLAAGEKQKLEIVKQLYLGRSFLVLD 177
Cdd:cd03216 81 Y-----------------------------------------------------QLSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2790395612 178 EPTSVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGS 234
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQG-VAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
27-494 |
1.13e-61 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 209.97 E-value: 1.13e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 27 FGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYGLGMVYQHFTLVPS 106
Cdd:PRK10982 8 FPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 107 LTGAENLVISRTEVPAV-INWPRERKALAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTP 185
Cdd:PRK10982 88 RSVMDNMWLGRYPTKGMfVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 186 AEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELSTAEMAAMMIGdvklAELDTRIP-V 264
Cdd:PRK10982 168 KEVNHLFTIIRKLKERG-CGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVG----RSLTQRFPdK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 265 TETAKAV-LQIERIKAPDRSGLKTIeidSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRP-E 342
Cdd:PRK10982 243 ENKPGEViLEVRNLTSLRQPSIRDV---SFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNAnE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 343 TRRNNVRFIPEEPLQNACAPRMSVSENLAFRtfDLKESGADAIWLNRNKIKKGATALIADFKVRTASQSSPIAALSGGNV 422
Cdd:PRK10982 320 AINHGFALVTEERRSTGIYAYLDIGFNSLIS--NIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQ 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790395612 423 QRAVLARELTGEVDLLIVSNPCFGLDFSAVAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMVISEGKL 494
Cdd:PRK10982 398 QKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-512 |
1.83e-55 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 193.47 E-value: 1.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 21 LDM---TMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFY-HQT-SGSLSVDGREVTIASPKDAAAYGLG 95
Cdd:NF040905 2 LEMrgiTKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYpHGSyEGEILFDGEVCRFKDIRDSEALGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 96 MVYQHFTLVPSLTGAENLVISRTevPA---VINWPRERKALAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRS 172
Cdd:NF040905 82 IIHQELALIPYLSIAENIFLGNE--RAkrgVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 173 FLVLDEPTSVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGS--GKVGELSTAEMAAMMI 250
Cdd:NF040905 160 LLILDEPTAALNEEDSAALLDLLLELKAQG-ITSIIISHKLNEIRRVADSITVLRDGRTIETldCRADEVTEDRIIRGMV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 251 GdvklAELDTRIP--VTETAKAVLQIE--RIKAPDRSGLKTIEIDSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQ- 325
Cdd:NF040905 239 G----RDLEDRYPerTPKIGEVVFEVKnwTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRn 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 326 -AGSVTVKGAaygatrpETRRNNVrfipeeplqnacapRMSVSENLAFRTFDLKESG-------------------ADAI 385
Cdd:NF040905 315 iSGTVFKDGK-------EVDVSTV--------------SDAIDAGLAYVTEDRKGYGlnliddikrnitlanlgkvSRRG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 386 WLNRNKIKKGATALIADFKVRTASQSSPIAALSGGNVQRAVLARELTGEVDLLIVSNPCFGLDFSAVAEIRARIMRARNA 465
Cdd:NF040905 374 VIDENEEIKVAEEYRKKMNIKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE 453
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2790395612 466 GAAVLLLSEDLDELMEMSDRIMVISEGKLVYETAARSADISVIGAHM 512
Cdd:NF040905 454 GKGVIVISSELPELLGMCDRIYVMNEGRITGELPREEASQERIMRLI 500
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
268-494 |
8.95e-50 |
|
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: 168.76 E-value: 8.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 268 AKAVLQIERIKAPDRsgLKTIeidSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRRNN 347
Cdd:cd03215 1 GEPVLEVRGLSVKGA--VRDV---SFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 348 -VRFIPEEPLQNACAPRMSVSENLAFRTFdlkesgadaiwlnrnkikkgataliadfkvrtasqsspiaaLSGGNVQRAV 426
Cdd:cd03215 76 gIAYVPEDRKREGLVLDLSVAENIALSSL-----------------------------------------LSGGNQQKVV 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790395612 427 LARELTGEVDLLIVSNPCFGLDFSAVAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMVISEGKL 494
Cdd:cd03215 115 LARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
18-501 |
4.82e-48 |
|
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: 173.94 E-value: 4.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQT---SGSLSVDGREVTIASPKDAAAYgL 94
Cdd:COG1123 7 VRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR-I 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 95 GMVYQHFT--LVPSLTGA------ENLVISRTEVPAvinwpRERKALAAF-MEHMpfqipLDRPVSQLAAGEKQKLEIVK 165
Cdd:COG1123 86 GMVFQDPMtqLNPVTVGDqiaealENLGLSRAEARA-----RVLELLEAVgLERR-----LDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 166 QLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELSTAEM 245
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 246 AAMMIGDVKLAELDTRiPVTETAKAVLQIERIKA--PDRSGLKTIEID--SLTVHAGEIVGIAGISGNGQKELAEILAG- 320
Cdd:COG1123 236 ALAAVPRLGAARGRAA-PAAAAAEPLLEVRNLSKryPVRGKGGVRAVDdvSLTLRRGETLGLVGESGSGKSTLARLLLGl 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 321 QRPTqAGSVTVKG---AAYGATRPETRRNNVRFIPeeplQNACA---PRMSVSENLAF--RTFDLkesgadaiwLNRNKI 392
Cdd:COG1123 315 LRPT-SGSILFDGkdlTKLSRRSLRELRRRVQMVF----QDPYSslnPRMTVGDIIAEplRLHGL---------LSRAER 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 393 KKGATALIADFKVRTASQSSPIAALSGGNVQRAVLARELTGEVDLLIVSNPCFGLDFSavaeIRARIMR-----ARNAG- 466
Cdd:COG1123 381 RERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVS----VQAQILNllrdlQRELGl 456
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2790395612 467 ---------AAVLllsedldelmEMSDRIMVISEGKLVYETAAR 501
Cdd:COG1123 457 tylfishdlAVVR----------YIADRVAVMYDGRIVEDGPTE 490
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
18-239 |
2.57e-47 |
|
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: 164.15 E-value: 2.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYGLGMV 97
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 98 YQHFTLVPSLTGAENLVI----SRTEVPAVINWPRERKALAAFMEHMPFQIPL----DRPVSQLAAGEKQKLEIVKQLYL 169
Cdd:cd03219 81 FQIPRLFPELTVLENVMVaaqaRTGSGLLLARARREEREARERAEELLERVGLadlaDRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 170 GRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGE 239
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERG-ITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
18-240 |
1.19e-45 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 159.84 E-value: 1.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTiASPKDAAAYgLGMV 97
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA-RDPAEVRRR-IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 98 YQHFTLVPSLTGAENLV-------ISRTEVPAVINWprerkALAAF-MEHMpfqipLDRPVSQLAAGEKQKLEIVKQLyL 169
Cdd:COG1131 79 PQEPALYPDLTVRENLRffarlygLPRKEARERIDE-----LLELFgLTDA-----ADRKVGTLSGGMKQRLGLALAL-L 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790395612 170 GR-SFLVLDEPTSVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:COG1131 148 HDpELLILDEPTSGLDPEARRELWELLRELAAEG-KTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
19-239 |
3.74e-45 |
|
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: 159.05 E-value: 3.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 19 ETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYGLGMVY 98
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIARTF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 99 QHFTLVPSLTGAENLVI------SRTEVPAVINWPRERKALAAF------------MEHMpfqipLDRPVSQLAAGEKQK 160
Cdd:COG0411 86 QNPRLFPELTVLENVLVaaharlGRGLLAALLRLPRARREEREAreraeellervgLADR-----ADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790395612 161 LEIVKQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGE 239
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
18-231 |
2.59e-40 |
|
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: 143.31 E-value: 2.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGreVTIASPKDAAAYGLGMV 97
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG--KDIKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 98 YQHFTLVPSLTGAENLVISRtevpavinwprerkalaafmehmpfqipldrpvsqlaaGEKQKLEIVKQLYLGRSFLVLD 177
Cdd:cd03230 79 PEEPSLYENLTVRENLKLSG--------------------------------------GMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2790395612 178 EPTSVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKL 231
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEG-KTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
28-240 |
1.01e-37 |
|
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: 138.23 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 28 GSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYgLGMVYQH------- 100
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGLVFQNpddqlfa 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 101 --------FtlvpsltGAENLVISRTEVPAVInwpreRKALAAF-MEHMpfqipLDRPVSQLAAGEKQKLEIVKQLYLGR 171
Cdd:COG1122 91 ptveedvaF-------GPENLGLPREEIRERV-----EEALELVgLEHL-----ADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790395612 172 SFLVLDEPTSVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEG-KTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
28-240 |
2.24e-37 |
|
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: 137.33 E-value: 2.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 28 GSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKD--AAAYGLGMVYQHFTLVP 105
Cdd:cd03258 16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrKARRRIGMIFQHFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 106 SLTGAENLV-------ISRTEVPAVINWPRERKALAAFMEHMPfqipldrpvSQLAAGEKQKLEIVKQLYLGRSFLVLDE 178
Cdd:cd03258 96 SRTVFENVAlpleiagVPKAEIEERVLELLELVGLEDKADAYP---------AQLSGGQKQRVGIARALANNPKVLLCDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790395612 179 PTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:cd03258 167 ATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
18-232 |
3.92e-37 |
|
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: 136.11 E-value: 3.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAaayGLGMV 97
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR---NIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 98 YQHFTLVPSLTGAENLV-------ISRTEVpavinwpRERKALAAFMEHMPfqIPLDRPVSQLAAGEKQKLEIVKQLYLG 170
Cdd:cd03259 78 FQDYALFPHLTVAENIAfglklrgVPKAEI-------RARVRELLELVGLE--GLLNRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790395612 171 RSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLI 232
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
18-240 |
9.16e-36 |
|
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: 132.88 E-value: 9.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTiaspKDAAAY--GLG 95
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVrrRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 96 MVYQHFTLVPSLTGAENLVISrtevPAVINWPRERKA-----LAAFMEHMPFQiplDRPVSQLAAGEKQKLEIVKQLYLG 170
Cdd:cd03265 77 IVFQDLSVDDELTGWENLYIH----ARLYGVPGAERRerideLLDFVGLLEAA---DRLVKTYSGGMRRRLEIARSLVHR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 171 RSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
32-230 |
5.30e-35 |
|
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: 130.28 E-value: 5.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 32 ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYgLGMVYQH-----FTlvPS 106
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGLVFQNpddqfFG--PT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 107 LT-----GAENLVISRTEVPAvinwpRERKALAAF-MEHMpfqipLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPT 180
Cdd:cd03225 93 VEeevafGLENLGLPEEEIEE-----RVEEALELVgLEGL-----RDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2790395612 181 SVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGK 230
Cdd:cd03225 163 AGLDPAGRRELLELLKKLKAEG-KTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
18-241 |
5.81e-35 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 131.13 E-value: 5.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAygLGMV 97
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ--IGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 98 YQHFTLVPSLTGAENLvisRTEVPAVINWPRERKALAA-FMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVL 176
Cdd:COG4555 80 PDERGLYDRLTVRENI---RYFAELYGLFDEELKKRIEeLIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790395612 177 DEPTSVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELS 241
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKEG-KTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELR 220
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
28-240 |
1.12e-34 |
|
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: 129.86 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 28 GSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYGLGMVYQHFTLVPSL 107
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYVPEGRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 108 TGAENLVISRtevpavinWPRERKALAAFMEHMpFQI-P-----LDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTS 181
Cdd:cd03224 91 TVEENLLLGA--------YARRRAKRKARLERV-YELfPrlkerRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2790395612 182 VLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:cd03224 162 GLAPKIVEEIFEAIRELRDEG-VTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
18-235 |
5.14e-34 |
|
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: 127.33 E-value: 5.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTiaspKDAAAYG-LGM 96
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ----KNIEALRrIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 97 VYQHFTLVPSLTGAENLVISRT----------EVPAVINwprerkalaafMEHMPfqiplDRPVSQLAAGEKQKLEIVKQ 166
Cdd:cd03268 77 LIEAPGFYPNLTARENLRLLARllgirkkridEVLDVVG-----------LKDSA-----KKKVKGFSLGMKQRLGIALA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 167 LyLGR-SFLVLDEPTSVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGSG 235
Cdd:cd03268 141 L-LGNpDLLILDEPTNGLDPDGIKELRELILSLRDQG-ITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
18-245 |
6.01e-33 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 125.93 E-value: 6.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYgLGMV 97
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR-IAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 98 YQHFTLVPSLTGAENLVISRTevPAVINWPRERK--------ALAAF-MEHMpfqipLDRPVSQLAAGEKQKLEIVKQLY 168
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRY--PHLGLFGRPSAedreaveeALERTgLEHL-----ADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790395612 169 LGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELSTAEM 245
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPEL 230
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
22-235 |
1.16e-32 |
|
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: 123.80 E-value: 1.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 22 DMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKdaaaygLGMVYQHF 101
Cdd:cd03235 4 DLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR------IGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 102 TLVPS--LTGAENLVISRTEVPAVINWPRE---RKALAAF----MEHMpfqipLDRPVSQLAAGEKQKLEIVKQLYLGRS 172
Cdd:cd03235 78 SIDRDfpISVRDVVLMGLYGHKGLFRRLSKadkAKVDEALervgLSEL-----ADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790395612 173 FLVLDEPTSVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRgKLIGSG 235
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREG-MTILVVTHDLGLVLEYFDRVLLLNR-TVVASG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
29-231 |
2.43e-32 |
|
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: 123.37 E-value: 2.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 29 SFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAY---GLGMVYQHFTLVP 105
Cdd:cd03255 16 KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFrrrHIGFVFQSFNLLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 106 SLTGAENLvisrtEVPAVI----NWPRERKALAAF----MEHMpfqipLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLD 177
Cdd:cd03255 96 DLTALENV-----ELPLLLagvpKKERRERAEELLervgLGDR-----LNHYPSELSGGQQQRVAIARALANDPKIILAD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2790395612 178 EPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKfHEVTKFADAVSILRRGKL 231
Cdd:cd03255 166 EPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
33-181 |
3.43e-32 |
|
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: 120.45 E-value: 3.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 33 LDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAyGLGMVYQHFTLVPSLTGAEN 112
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK-EIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790395612 113 LVISRtEVPAVINWPRERKALAAfMEHMPFQIPLDRPV----SQLAAGEKQKLEIVKQLYLGRSFLVLDEPTS 181
Cdd:pfam00005 80 LRLGL-LLKGLSKREKDARAEEA-LEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
18-245 |
4.97e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 120.58 E-value: 4.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKdaaaygLGMV 97
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR------IGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 98 YQHFTLVPS--LTGAEnLV-------------ISRTEVPAVinwpreRKALAAF-MEHMpfqipLDRPVSQLAAGEKQKl 161
Cdd:COG1121 81 PQRAEVDWDfpITVRD-VVlmgrygrrglfrrPSRADREAV------DEALERVgLEDL-----ADRPIGELSGGQQQR- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 162 eivkqLYLGRSF------LVLDEPTSVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGkLIGSG 235
Cdd:COG1121 148 -----VLLARALaqdpdlLLLDEPFAGVDAATEEALYELLRELRREG-KTILVVTHDLGAVREYFDRVLLLNRG-LVAHG 220
|
250
....*....|
gi 2790395612 236 KVGELSTAEM 245
Cdd:COG1121 221 PPEEVLTPEN 230
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
35-235 |
5.22e-31 |
|
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: 119.52 E-value: 5.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 35 HVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPkdaAAYGLGMVYQHFTLVPSLTGAENLV 114
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPP---ADRPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 115 ISRteVPAVINWPRERKALAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTPAEADEMLGL 194
Cdd:cd03298 93 LGL--SPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2790395612 195 VRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSG 235
Cdd:cd03298 171 VLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
28-240 |
1.22e-30 |
|
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: 125.02 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 28 GSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYG--LGMVYQH-FT-L 103
Cdd:COG1123 276 GGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELRrrVQMVFQDpYSsL 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 104 VPSLTGAENLvisrTEVPAVINW--PRERKALAAFMEHMpFQIP---LDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDE 178
Cdd:COG1123 356 NPRMTVGDII----AEPLRLHGLlsRAERRERVAELLER-VGLPpdlADRYPHELSGGQRQRVAIARALALEPKLLILDE 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790395612 179 PTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:COG1123 431 PTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
26-235 |
1.72e-30 |
|
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: 118.38 E-value: 1.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 26 RFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYG--LGMVYQH--F 101
Cdd:cd03257 14 GGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRRkeIQMVFQDpmS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 102 TLVPSLTGAENLV-ISRTEVPAVINWPRERKALAAFMehmpfQIPLDRPV-----SQLAAGEKQKLEIVKQLYLGRSFLV 175
Cdd:cd03257 94 SLNPRMTIGEQIAePLRIHGKLSKKEARKEAVLLLLV-----GVGLPEEVlnrypHELSGGQRQRVAIARALALNPKLLI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 176 LDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSG 235
Cdd:cd03257 169 ADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
18-230 |
1.83e-30 |
|
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: 116.90 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYG-LGM 96
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRrIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 97 VYQHFTLVPSLTGAENLVISrtevpavinwprerkalaafmehmpfqipldrpvsqLAAGEKQKLEIVKQLYLGRSFLVL 176
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG------------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2790395612 177 DEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGK 230
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
18-240 |
8.62e-30 |
|
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: 116.07 E-value: 8.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREvtIASPKDAAAYGLGMV 97
Cdd:cd03263 3 IRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYS--IRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 98 YQHFTLVPSLTGAENLVI-------SRTEVPAVINWprerkalaaFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLG 170
Cdd:cd03263 81 PQFDALFDELTVREHLRFyarlkglPKSEIKEEVEL---------LLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 171 RSFLVLDEPTSVLTPAEADEMLGLVRGMteRGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
28-240 |
1.71e-29 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 118.64 E-value: 1.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 28 GSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKD--AAAYGLGMVYQHFTLVP 105
Cdd:COG1135 16 GPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElrAARRKIGMIFQHFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 106 SLTGAEN----LVISrtevpaviNWPR-ERKA----------LAAFMEHMPfqipldrpvSQLAAGEKQKLEIVKQLYLG 170
Cdd:COG1135 96 SRTVAENvalpLEIA--------GVPKaEIRKrvaellelvgLSDKADAYP---------SQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 171 RSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:COG1135 159 PKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDV 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
22-230 |
1.98e-29 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 113.11 E-value: 1.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 22 DMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPkdaaayglgmvyqhf 101
Cdd:cd00267 4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPL--------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 102 tlvpsltgaenlvisrtevpavinwPRERKALAAfmehmpfqipldrpVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTS 181
Cdd:cd00267 69 -------------------------EELRRRIGY--------------VPQLSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2790395612 182 VLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGK 230
Cdd:cd00267 110 GLDPASRERLLELLRELAEEG-RTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-240 |
7.25e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 115.98 E-value: 7.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 24 TMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTiASPKDAAAY-----GLgmvY 98
Cdd:COG4152 8 TKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-PEDRRRIGYlpeerGL---Y 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 99 qhftlvPSLTGAENLV-------ISRTEVpavinwpreRKALAAFMEHmpFQIP--LDRPVSQLAAGEKQKLEIVKQLyL 169
Cdd:COG4152 84 ------PKMKVGEQLVylarlkgLSKAEA---------KRRADEWLER--LGLGdrANKKVEELSKGNQQKVQLIAAL-L 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790395612 170 GR-SFLVLDEPTSVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:COG4152 146 HDpELLILDEPFSGLDPVNVELLKDVIRELAAKG-TTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
22-235 |
9.66e-29 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 112.14 E-value: 9.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 22 DMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAayglgmvyQHF 101
Cdd:cd03214 4 NLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA--------RKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 102 TLVP---SLTGAENLvisrtevpavinwprerkalaafmehmpfqipLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDE 178
Cdd:cd03214 76 AYVPqalELLGLAHL--------------------------------ADRPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2790395612 179 PTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSG 235
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
18-231 |
2.71e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 111.83 E-value: 2.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTiasPKDAAAY----- 92
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLS---AMPPPEWrrqva 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 93 --------GLGMVYQHFTLVPSLTGAEnlvisrtevpavINWPRERKALAAFmeHMPfQIPLDRPVSQLAAGEKQKLEIV 164
Cdd:COG4619 78 yvpqepalWGGTVRDNLPFPFQLRERK------------FDRERALELLERL--GLP-PDILDKPVERLSGGERQRLALI 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790395612 165 KQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKL 231
Cdd:COG4619 143 RALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
17-240 |
3.27e-28 |
|
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: 112.43 E-value: 3.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 17 GIETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAaayGLGM 96
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER---NVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 97 VYQHFTLVPSLTGAENL-----VISRTEVPAVINWPRERKALAAFMEHMPFQiplDRPVSQLAAGEKQKLEIVKQLYLGR 171
Cdd:cd03296 79 VFQHYALFRHMTVFDNVafglrVKPRSERPPEAEIRAKVHELLKLVQLDWLA---DRYPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790395612 172 SFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
28-239 |
5.42e-28 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 114.51 E-value: 5.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 28 GSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKD--AAAYGLGMVYQHFTLVP 105
Cdd:PRK11153 16 RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrKARRQIGMIFQHFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 106 SLTGAENLV-------ISRTEVPAVINWPRERKALAAFMEHMPfqipldrpvSQLAAGEKQKLEIVKQLYLGRSFLVLDE 178
Cdd:PRK11153 96 SRTVFDNVAlplelagTPKAEIKARVTELLELVGLSDKADRYP---------AQLSGGQKQRVAIARALASNPKVLLCDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790395612 179 PTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGE 239
Cdd:PRK11153 167 ATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSE 227
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
28-240 |
1.14e-27 |
|
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: 110.84 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 28 GSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYGLGMVYQHFTLVPSL 107
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGYVPEGRRIFPSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 108 TGAENLvisrtEVPAVInwPRERKALAAFMEHMpFQI-P-----LDRPVSQLAAGEKQKLEIvkqlylGR------SFLV 175
Cdd:COG0410 94 TVEENL-----LLGAYA--RRDRAEVRADLERV-YELfPrlkerRRQRAGTLSGGEQQMLAI------GRalmsrpKLLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790395612 176 LDEPTSVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:COG0410 160 LDEPSLGLAPLIVEEIFEIIRRLNREG-VTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
18-231 |
1.63e-27 |
|
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: 109.65 E-value: 1.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAaayGLGMV 97
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR---DIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 98 YQHFTLVPSLTGAENLVI---SRTEVPAVINwprERKALAAFM---EHMpfqipLDRPVSQLAAGEKQKLEIVKQLYLGR 171
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFglkLRKVPKDEID---ERVREVAELlqiEHL-----LDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 172 SFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKL 231
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
28-245 |
1.92e-27 |
|
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: 110.35 E-value: 1.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 28 GSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKD--AAAYGLGMVYQHFTLVP 105
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrQLRRQIGMIFQQFNLIE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 106 SLTGAENLVISR----TEVPAVINW--PRER-KALAAF----MEHMPFQipldrPVSQLAAGEKQKLEIVKQLYLGRSFL 174
Cdd:cd03256 92 RLSVLENVLSGRlgrrSTWRSLFGLfpKEEKqRALAALervgLLDKAYQ-----RADQLSGGQQQRVAIARALMQQPKLI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790395612 175 VLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELsTAEM 245
Cdd:cd03256 167 LADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL-TDEV 236
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
33-239 |
2.41e-27 |
|
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: 109.73 E-value: 2.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 33 LDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDaaaYGLGMVYQHFTLVPSLTGAEN 112
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK---RDISYVPQNYALFPHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 113 L-------VISRTEVPavinwpRERKALAAFM--EHMpfqipLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVL 183
Cdd:cd03299 92 IayglkkrKVDKKEIE------RKVLEIAEMLgiDHL-----LNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2790395612 184 TPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGE 239
Cdd:cd03299 161 DVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-236 |
2.74e-27 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 110.46 E-value: 2.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 22 DMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYGLGMVYQHF 101
Cdd:PRK11300 10 GLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQHV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 102 TLVPSLTGAENLVISRTE------VPAVINWP----RERKAL---AAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLY 168
Cdd:PRK11300 90 RLFREMTVIENLLVAQHQqlktglFSGLLKTPafrrAESEALdraATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMV 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790395612 169 LGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGK 236
Cdd:PRK11300 170 TQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGT 237
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
18-235 |
3.39e-27 |
|
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: 108.91 E-value: 3.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIAsPKDAAAY----- 92
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA-ARNRIGYlpeer 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 93 GLgmvYqhftlvPSLTGAENLV-------ISRTEVPAVINWPRERKALAAFmehmpfqipLDRPVSQLAAGEKQKLEIVK 165
Cdd:cd03269 80 GL---Y------PKMKVIDQLVylaqlkgLKKEEARRRIDEWLERLELSEY---------ANKRVEELSKGNQQKVQFIA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 166 QLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGElTVLMISHKFHEVTKFADAVSILRRGKLIGSG 235
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGK-TVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
18-240 |
3.81e-27 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 109.13 E-value: 3.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKD--AAAYGLG 95
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 96 MVYQHFTLVPSLTGAENL--------VISRTEVPAVINWPRERKALAAFMEHMPfqipldrpvSQLAAGEKQKLEIVKQL 167
Cdd:cd03261 81 MLFQSGALFDSLTVFENVafplrehtRLSEEEIREIVLEKLEAVGLRGAEDLYP---------AELSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790395612 168 YLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
32-257 |
4.31e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 110.49 E-value: 4.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 32 ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYgLGMVYQH----F--TLVP 105
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ-VGMVFQNpdnqFvgATVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 106 S--LTGAENLVISRTEVPAVINWPRERKALAAFMEHMPfqipldrpvSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVL 183
Cdd:PRK13635 101 DdvAFGLENIGVPREEMVERVDQALRQVGMEDFLNREP---------HRLSGGQKQRVAIAGVLALQPDIIILDEATSML 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790395612 184 TPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKfADAVSILRRGKLIGSGKVGELSTAEMAAMMIG-DVKLAE 257
Cdd:PRK13635 172 DPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKSGHMLQEIGlDVPFSV 245
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
18-240 |
4.73e-27 |
|
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: 109.51 E-value: 4.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGS----FTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAyG 93
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRR-R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 94 LGMVYQH--------FTLVPSLtgAENLVISRTevpavinwPRERKALAAFME--HMPFQIpLDRPVSQLAAGEKQKLEI 163
Cdd:COG1124 81 VQMVFQDpyaslhprHTVDRIL--AEPLRIHGL--------PDREERIAELLEqvGLPPSF-LDRYPHQLSGGQRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790395612 164 VKQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
18-231 |
4.56e-26 |
|
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: 105.57 E-value: 4.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRF-GSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTiASPKDAAAY---G 93
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS-DLRGRAIPYlrrK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 94 LGMVYQHFTLVPSLTGAENLVISR--TEVPavinwPRE-RKALAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLG 170
Cdd:cd03292 80 IGVVFQDFRLLPDRNVYENVAFALevTGVP-----PREiRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790395612 171 RSFLVLDEPTSVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKL 231
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKKINKAG-TTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
22-244 |
1.18e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 104.84 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 22 DMTMRFGSFTAldHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPkdaAAYGLGMVYQHF 101
Cdd:COG3840 6 DLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP---AERPVSMLFQEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 102 TLVPSLTGAENLVISRTevpavinwPR------ERKALAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFLV 175
Cdd:COG3840 81 NLFPHLTVAQNIGLGLR--------PGlkltaeQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790395612 176 LDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELSTAE 244
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
18-244 |
3.45e-25 |
|
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: 103.91 E-value: 3.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAY--GLG 95
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrrRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 96 MVYQH---FTlvpSLTGAENLV---ISRTEVPavinwPRERKALAAFM----------EHMPfqipldrpvSQLAAGEKq 159
Cdd:COG1127 86 MLFQGgalFD---SLTVFENVAfplREHTDLS-----EAEIRELVLEKlelvglpgaaDKMP---------SELSGGMR- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 160 kleivKQLYLGRS------FLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIG 233
Cdd:COG1127 148 -----KRVALARAlaldpeILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIA 222
|
250
....*....|.
gi 2790395612 234 SGKVGELSTAE 244
Cdd:COG1127 223 EGTPEELLASD 233
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
18-245 |
5.42e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 103.70 E-value: 5.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYgLGMV 97
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR-RAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 98 YQHFTLVPSLT-------GAENLVISRTEVPAVINWPRERKALAAFmehmpfqipLDRPVSQLAAGEKQKLEIVK---QL 167
Cdd:PRK13548 82 PQHSSLSFPFTveevvamGRAPHGLSRAEDDALVAAALAQVDLAHL---------AGRDYPQLSGGEQQRVQLARvlaQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 168 YL---GRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELSTAE 244
Cdd:PRK13548 153 WEpdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPE 232
|
.
gi 2790395612 245 M 245
Cdd:PRK13548 233 T 233
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
18-245 |
6.03e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 103.66 E-value: 6.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYgLGMV 97
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARR-RAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 98 YQHFTLVPSLT-------GAENLVISRTEVPAVInwpreRKALAAF-MEHMpfqipLDRPVSQLAAGEKQKLeivkQL-- 167
Cdd:COG4559 81 PQHSSLAFPFTveevvalGRAPHGSSAAQDRQIV-----REALALVgLAHL-----AGRSYQTLSGGEQQRV----QLar 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 168 ---------YLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVG 238
Cdd:COG4559 147 vlaqlwepvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRG-GGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPE 225
|
....*..
gi 2790395612 239 ELSTAEM 245
Cdd:COG4559 226 EVLTDEL 232
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
26-211 |
7.80e-25 |
|
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: 101.79 E-value: 7.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 26 RFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREvtIASPKDAAAYGLGMVYQHFTLVP 105
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEP--IRDAREDYRRRLAYLGHADGLKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 106 SLTGAENLVISRtevpAVINWPRERKALAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTP 185
Cdd:COG4133 89 ELTVRENLRFWA----ALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDA 164
|
170 180
....*....|....*....|....*.
gi 2790395612 186 AEADEMLGLVRGMTERGeLTVLMISH 211
Cdd:COG4133 165 AGVALLAELIAAHLARG-GAVLLTTH 189
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
31-241 |
8.06e-25 |
|
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: 107.92 E-value: 8.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 31 TALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDaaayglgmVYQHFTLVP----- 105
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS--------WRRQIAWVPqnpyl 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 106 -SLTGAENLVI-----SRTEVPAVInwprERKALAAFMEHMPFQipLDRPV----SQLAAGEKQKLEIVKQLYLGRSFLV 175
Cdd:COG4988 423 fAGTIRENLRLgrpdaSDEELEAAL----EAAGLDEFVAALPDG--LDTPLgeggRGLSGGQAQRLALARALLRDAPLLL 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790395612 176 LDEPTSVLTPAEADEMLGLVRGMTErgELTVLMISHKFHEVtKFADAVSILRRGKLIGSGKVGELS 241
Cdd:COG4988 497 LDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEELL 559
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
18-233 |
1.16e-24 |
|
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: 101.78 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGS----FTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKdaaayg 93
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 94 LGMVYQHFTLVPSLTGAEN--LVISRTEVPAvinwpRERKA----------LAAFMEHMPfqipldrpvSQLAAGEKQKL 161
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNvaLGLELQGVPK-----AEAREraeellelvgLSGFENAYP---------HQLSGGMRQRV 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790395612 162 EIVKQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSIL--RRGKLIG 233
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVA 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
26-240 |
1.61e-24 |
|
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: 102.72 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 26 RFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAY---GLGMVYQHFT 102
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkKISMVFQSFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 103 LVPSLTGAENLVISrTEVPAVINWPRERKALAAfMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSV 182
Cdd:cd03294 113 LLPHRTVLENVAFG-LEVQGVPRAEREERAAEA-LELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790395612 183 LTP---AE-ADEMLGLVRGMtergELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:cd03294 191 LDPlirREmQDELLRLQAEL----QKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-237 |
2.56e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 101.20 E-value: 2.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 23 MTMRFgsftaldhvSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPkdaAAYGLGMVYQHFT 102
Cdd:PRK10771 14 LPMRF---------DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPP---SRRPVSMLFQENN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 103 LVPSLTGAENlvISRTEVPAVINWPRERKALAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSV 182
Cdd:PRK10771 82 LFSHLTVAQN--IGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2790395612 183 LTPAEADEMLGLVRGMTERGELTVLMISHkfhevtKFADAVSILRRGKLIGSGKV 237
Cdd:PRK10771 160 LDPALRQEMLTLVSQVCQERQLTLLMVSH------SLEDAARIAPRSLVVADGRI 208
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
28-239 |
4.62e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 100.13 E-value: 4.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 28 GSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAY--GLGMVYQHFTLVP 105
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLrrRIGVVFQDFRLLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 106 SLTGAEN----LVIS-------RTEVPAVINWPRerkaLAAFMEHMPfqipldrpvSQLAAGEKQKLEIVKQLyLGR-SF 173
Cdd:COG2884 93 DRTVYENvalpLRVTgksrkeiRRRVREVLDLVG----LSDKAKALP---------HELSGGEQQRVAIARAL-VNRpEL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790395612 174 LVLDEPTSVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGE 239
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEINRRG-TTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
24-232 |
8.68e-24 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 102.48 E-value: 8.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 24 TMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTiaspkDAAAY--GLGMVYQHF 101
Cdd:COG3842 12 SKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT-----GLPPEkrNVGMVFQDY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 102 TLVPSLTGAEN-------LVISRTEVpavinwpRER--KALAAF-MEHMpfqipLDRPVSQLAAGEKQKLEivkqlyLGR 171
Cdd:COG3842 87 ALFPHLTVAENvafglrmRGVPKAEI-------RARvaELLELVgLEGL-----ADRYPHQLSGGQQQRVA------LAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790395612 172 SF------LVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLI 232
Cdd:COG3842 149 ALapeprvLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
26-236 |
1.25e-23 |
|
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: 99.23 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 26 RFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTiasPKDAAAYGLGMVYQHFTLVP 105
Cdd:cd03300 9 FYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT---NLPPHKRPVNTVFQNYALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 106 SLTGAENLV-------ISRTEVPAVINWPRERKALAAFMEHMPfqipldrpvSQLAAGEKQKLEIVKQLYLGRSFLVLDE 178
Cdd:cd03300 86 HLTVFENIAfglrlkkLPKAEIKERVAEALDLVQLEGYANRKP---------SQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 179 PTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKL--IGSGK 236
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIqqIGTPE 216
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
8-257 |
2.46e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 101.45 E-value: 2.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 8 PLPQTGKAVG--IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIAS 85
Cdd:PRK11607 8 PQAKTRKALTplLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 86 PKDAAaygLGMVYQHFTLVPSLTGAENLV-------ISRTEVPAVINwprERKALAafmeHMpfQIPLDRPVSQLAAGEK 158
Cdd:PRK11607 88 PYQRP---INMMFQSYALFPHMTVEQNIAfglkqdkLPKAEIASRVN---EMLGLV----HM--QEFAKRKPHQLSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 159 QKLEIVKQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVG 238
Cdd:PRK11607 156 QRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPE 235
|
250 260
....*....|....*....|..
gi 2790395612 239 EL---STAEMAAMMIGDVKLAE 257
Cdd:PRK11607 236 EIyehPTTRYSAEFIGSVNVFE 257
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
32-230 |
2.50e-23 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 96.68 E-value: 2.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 32 ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDaaayglgmVYQHFTLVP------ 105
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES--------LRKNIAYVPqdpflf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 106 SLTGAENLvisrtevpavinwprerkalaafmehmpfqipldrpvsqLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTP 185
Cdd:cd03228 89 SGTIRENI---------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDP 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2790395612 186 AEADEMLGLVRGMteRGELTVLMISHKFHEVtKFADAVSILRRGK 230
Cdd:cd03228 130 ETEALILEALRAL--AKGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
32-239 |
3.24e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 99.35 E-value: 3.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 32 ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYG-LGMV-----YQHF--TL 103
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKkVGLVfqypeYQLFeeTI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 104 VPSLT-GAENLVISRTEVPAvinwpRERKALAafMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSV 182
Cdd:PRK13637 102 EKDIAfGPINLGLSEEEIEN-----RVKRAMN--IVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2790395612 183 LTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGE 239
Cdd:PRK13637 175 LDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
18-223 |
3.42e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 98.24 E-value: 3.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVtiaspKDAAA------ 91
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV-----NDPKVderlir 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 92 YGLGMVYQHFTLVPSLTGAENLVISRTEVPAVINWPRERKA--------LAAFMEHMPfqipldrpvSQLAAGEKQKLEI 163
Cdd:PRK09493 77 QEAGMVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQArellakvgLAERAHHYP---------SELSGGQQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 164 VKQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGeLTVLMIShkfHEVTkFADAV 223
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEG-MTMVIVT---HEIG-FAEKV 202
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
18-240 |
3.78e-23 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 97.64 E-value: 3.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQ-----TSGSLSVDGREVTiASPKDAAAY 92
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIY-DLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 93 --GLGMVYQHFTLVPsLTGAENLVIsrtevPAVINWPRERKALAAFMEHMPFQIPLDRPVS------QLAAGEKQKLEIV 164
Cdd:cd03260 80 rrRVGMVFQKPNPFP-GSIYDNVAY-----GLRLHGIKLKEELDERVEEALRKAALWDEVKdrlhalGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790395612 165 KQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMteRGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
24-235 |
4.04e-23 |
|
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: 97.26 E-value: 4.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 24 TMRFGSFTALDHVSVSIPAGsFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIAspKDAAAYGLGMVYQHFTL 103
Cdd:cd03264 7 TKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ--PQKLRRRIGYLPQEFGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 104 VPSLTGAENL----VISRtevpavINWPRERKALAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVkQLYLGR-SFLVLDE 178
Cdd:cd03264 84 YPNFTVREFLdyiaWLKG------IPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIA-QALVGDpSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2790395612 179 PTSVLTPAEADEMLGLVRGMTErgELTVLMISHKFHEVTKFADAVSILRRGKLIGSG 235
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
18-245 |
6.05e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.78 E-value: 6.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYgLGMV 97
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARR-LALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 98 YQHFtLVPSLTGAENLViSRTEVPAVINWPR----ERKALAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSF 173
Cdd:PRK11231 82 PQHH-LTPEGITVRELV-AYGRSPWLSLWGRlsaeDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790395612 174 LVLDEPTSVLTPAEADEMLGLVRGMTERGElTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELSTAEM 245
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGL 230
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
32-240 |
6.95e-23 |
|
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: 102.60 E-value: 6.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 32 ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYgLGMVYQHFTLvpsLTG-- 109
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQ-IGVVLQDVFL---FSGti 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 110 AENLVISRTEVP-AVINWPRERKALAAFMEHMPFQipLDRPV----SQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLT 184
Cdd:COG2274 566 RENITLGDPDATdEEIIEAARLAGLHDFIEALPMG--YDTVVgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALD 643
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2790395612 185 PAEADEMLGLVRGMteRGELTVLMISHKfHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:COG2274 644 AETEAIILENLRRL--LKGRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-235 |
7.24e-23 |
|
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: 96.60 E-value: 7.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 21 LDMTMRFGSFTaLDhVSVSIPaGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDG------REVTIASPKDAaayGL 94
Cdd:cd03297 4 VDIEKRLPDFT-LK-IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsRKKINLPPQQR---KI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 95 GMVYQHFTLVPSLTGAENLVIS-RTEVPAVINWpRERKALAAF-MEHMpfqipLDRPVSQLAAGEKQKLEIVKQLYLGRS 172
Cdd:cd03297 78 GLVFQQYALFPHLNVRENLAFGlKRKRNREDRI-SVDELLDLLgLDHL-----LNRYPAQLSGGEKQRVALARALAAQPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790395612 173 FLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSG 235
Cdd:cd03297 152 LLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
18-235 |
1.12e-22 |
|
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: 96.28 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRF----GSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVtIASPKDAAAyG 93
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEARR-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 94 LGMVYQHFTLVPSLTGAENLV-------ISRTEVPAVINWprerkaLAAFMEHMPFqipLDRPVSQLAAGEKQKLEIVKQ 166
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEyfaglygLKGDELTARLEE------LADRLGMEEL---LDRRVGGFSTGMRQKVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790395612 167 LYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGElTVLMISHKFHEVTKFADAVSILRRGKLIGSG 235
Cdd:cd03266 151 LVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
26-246 |
1.20e-22 |
|
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: 96.46 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 26 RFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYGLGMVYQHFTLVP 105
Cdd:cd03218 9 RYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYLPQEASIFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 106 SLTGAENL--VISRTEVPaviNWPRERKALAAFMEhmpFQIP--LDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTS 181
Cdd:cd03218 89 KLTVEENIlaVLEIRGLS---KKEREEKLEELLEE---FHIThlRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790395612 182 VLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELSTAEMA 246
Cdd:cd03218 163 GVDPIAVQDIQKIIKILKDRG-IGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELV 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
32-236 |
1.21e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 97.37 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 32 ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYgLGMVYQH----------- 100
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKK-IGIIFQNpdnqfigatve 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 101 ----FTLvpsltgaENLVISRTEVPAVInwprERKALAAFMEHMpfqipLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVL 176
Cdd:PRK13632 103 ddiaFGL-------ENKKVPPKKMKDII----DDLAKKVGMEDY-----LDKEPQNLSGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 177 DEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKfADAVSILRRGKLIGSGK 236
Cdd:PRK13632 167 DESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGK 225
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-240 |
1.31e-22 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 99.03 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 21 LDMTMRFGSFTaLDhVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGR-----EVTIASPKDAAAygLG 95
Cdd:TIGR02142 3 ARFSKRLGDFS-LD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsRKGIFLPPEKRR--IG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 96 MVYQHFTLVPSLTGAENLV--ISRTEVP-AVINWPRERKALAafMEHMpfqipLDRPVSQLAAGEKQKLEIVKQLYLGRS 172
Cdd:TIGR02142 79 YVFQEARLFPHLSVRGNLRygMKRARPSeRRISFERVIELLG--IGHL-----LGRLPGRLSGGEKQRVAIGRALLSSPR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790395612 173 FLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:TIGR02142 152 LLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
18-231 |
1.82e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 98.62 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAaygLGMV 97
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK---VGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 98 YQHFTLVPSLTGAENL-----VISRTEVP--AVInwpreRKALAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLG 170
Cdd:PRK10851 80 FQHYALFRHMTVFDNIafgltVLPRRERPnaAAI-----KAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790395612 171 RSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKL 231
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
18-224 |
2.25e-22 |
|
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: 95.29 E-value: 2.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTiASPKDAAAY--GLG 95
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT-DDKKNINELrqKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 96 MVYQHFTLVPSLTGAENLvisrTEVP-AVINWPRErKALAAFMEHmpfqipLDR----------PvSQLAAGEKQKLEIV 164
Cdd:cd03262 80 MVFQQFNLFPHLTVLENI----TLAPiKVKGMSKA-EAEERALEL------LEKvgladkadayP-AQLSGGQQQRVAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 165 KQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGeLTVLMIShkfHEVtKFADAVS 224
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEG-MTMVVVT---HEM-GFAREVA 202
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
18-211 |
3.95e-22 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 95.06 E-value: 3.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTiASPKDAAAY--GLG 95
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLrrKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 96 MVYQHFTLVPSLTGAENLvisrTEVP-AVINWPR---ERKA--------LAAFMEHMPfqipldrpvSQLAAGEKQKLEI 163
Cdd:COG1126 81 MVFQQFNLFPHLTVLENV----TLAPiKVKKMSKaeaEERAmellervgLADKADAYP---------AQLSGGQQQRVAI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2790395612 164 VKQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGeLTVLMISH 211
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEG-MTMVVVTH 194
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-240 |
1.33e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 96.05 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 6 DTPLPQTGKAVGIETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGreVTIAS 85
Cdd:PRK13536 30 KASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG--VPVPA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 86 PKDAAAYGLGMVYQHFTLVPSLTGAENLVI-------SRTEVPAVInwprerkalAAFMEHMPFQIPLDRPVSQLAAGEK 158
Cdd:PRK13536 108 RARLARARIGVVPQFDNLDLEFTVRENLLVfgryfgmSTREIEAVI---------PSLLEFARLESKADARVSDLSGGMK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 159 QKLEIVKQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGElTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVG 238
Cdd:PRK13536 179 RRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPH 257
|
..
gi 2790395612 239 EL 240
Cdd:PRK13536 258 AL 259
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
29-281 |
2.18e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 94.10 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 29 SFT-------ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFY--HQTSGS-LSVDGREVTIASPKDAAAYgLGMVY 98
Cdd:PRK13640 12 SFTypdskkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpDDNPNSkITVDGITLTAKTVWDIREK-VGIVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 99 QH-------FTLVPSLT-GAENLVISRTEVPAVINWPRERKALAAFMEHMPfqipldrpvSQLAAGEKQKLEIVKQLYLG 170
Cdd:PRK13640 91 QNpdnqfvgATVGDDVAfGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEP---------ANLSGGQKQRVAIAGILAVE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 171 RSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKfADAVSILRRGKLIGSGKVGEL-STAEMaamm 249
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIfSKVEM---- 236
|
250 260 270
....*....|....*....|....*....|..
gi 2790395612 250 igdVKLAELDtrIPVTETAKAVLQIERIKAPD 281
Cdd:PRK13640 237 ---LKEIGLD--IPFVYKLKNKLKEKGISVPQ 263
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
26-235 |
8.97e-21 |
|
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: 91.24 E-value: 8.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 26 RFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYGLgMVYQHFTLVP 105
Cdd:cd03267 30 KYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGV-VFGQKTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 106 SLTGAENLVISRtevpAVINWP--RERKALAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVL 183
Cdd:cd03267 109 DLPVIDSFYLLA----AIYDLPpaRFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2790395612 184 TPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSG 235
Cdd:cd03267 185 DVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
18-245 |
9.62e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.95 E-value: 9.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKdaAAYGLGMV 97
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH--ARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 98 YQHFTLVPSLTGAENLVI-----------SRTEVPAVINWPR-ERKAlaafmehmpfqiplDRPVSQLAAGEKQKLEIVK 165
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVfgryfglsaaaARALVPPLLEFAKlENKA--------------DAKVGELSGGMKRRLTLAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 166 QLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGElTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELSTAEM 245
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEI 230
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
18-240 |
1.04e-20 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 91.21 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRF-GSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKdAAAYGLGM 96
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPV-ELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 97 VYQHFTLVPSLTGAENLVIsrteVPAVINWPRERKALAAF----MEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRS 172
Cdd:cd03295 80 VIQQIGLFPHMTVEENIAL----VPKLLKWPKEKIRERADellaLVGLDPAEFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790395612 173 FLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
23-251 |
1.06e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 91.97 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 23 MTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYgLGMVYQHFT 102
Cdd:PRK10253 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 103 LVPSLTGAEnlVISRTEVPAVINWPRERK----ALAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDE 178
Cdd:PRK10253 92 TPGDITVQE--LVARGRYPHQPLFTRWRKedeeAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790395612 179 PTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELSTAEMAAMMIG 251
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYG 242
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
22-244 |
1.07e-20 |
|
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: 91.30 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 22 DMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSG-SLSVDGRE---VTIAS--PKdaaaygLG 95
Cdd:COG1119 8 NVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERrggEDVWElrKR------IG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 96 MVYQ--HFTLVPSLTgAENLVIS-------RTEVPAVINWPRERKALAAF-MEHMpfqipLDRPVSQLAAGEKQKLEIvk 165
Cdd:COG1119 82 LVSPalQLRFPRDET-VLDVVLSgffdsigLYREPTDEQRERARELLELLgLAHL-----ADRPFGTLSQGEQRRVLI-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 166 qlylGRSF------LVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGE 239
Cdd:COG1119 154 ----ARALvkdpelLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEE 229
|
....*
gi 2790395612 240 LSTAE 244
Cdd:COG1119 230 VLTSE 234
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
30-235 |
1.24e-20 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 90.67 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 30 FTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGRevtIASPKDAaayGLGMvyqhftlVPSLTG 109
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR---VSSLLGL---GGGF-------NPELTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 110 AENLVI-------SRTEVPAVINWPRERKALAAFMehmpfqiplDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSV 182
Cdd:cd03220 102 RENIYLngrllglSRKEIDEKIDEIIEFSELGDFI---------DLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2790395612 183 LTPAEADEMLGLVRGMTERGElTVLMISHKFHEVTKFADAVSILRRGKLIGSG 235
Cdd:cd03220 173 GDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
31-232 |
2.19e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 90.92 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 31 TALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYgLGMVYQHFTL--VPSLT 108
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY-IGRVFQDPMMgtAPSMT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 109 GAENLVI------SRTEVPAVINWPRE--RKALAAF---MEHMpfqipLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLD 177
Cdd:COG1101 99 IEENLALayrrgkRRGLRRGLTKKRRElfRELLATLglgLENR-----LDTKVGLLSGGQRQALSLLMATLTKPKLLLLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2790395612 178 EPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLI 232
Cdd:COG1101 174 EHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
32-236 |
2.71e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 90.96 E-value: 2.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 32 ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASP-KDAAAY--GLGMVYQ--------H 100
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnKDIKQIrkKVGLVFQfpesqlfeE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 101 FTLVPSLTGAENLVISRTEVPAVinwPRERKALAAFMEHMpfqipLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPT 180
Cdd:PRK13649 102 TVLKDVAFGPQNFGVSQEEAEAL---AREKLALVGISESL-----FEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2790395612 181 SVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGSGK 236
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKLHQSG-MTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
18-240 |
4.69e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 90.29 E-value: 4.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFT-ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGRevtiasPKDAAAYGL-- 94
Cdd:PRK13636 6 LKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK------PIDYSRKGLmk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 95 -----GMVYQ---HFTLVPSLT-----GAENLVISRTEVPAvinwpRERKALA-AFMEHMPfqiplDRPVSQLAAGEKQK 160
Cdd:PRK13636 80 lresvGMVFQdpdNQLFSASVYqdvsfGAVNLKLPEDEVRK-----RVDNALKrTGIEHLK-----DKPTHCLSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 161 LEIVKQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
30-232 |
6.02e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 89.84 E-value: 6.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 30 FTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTiASPKDA----AAYGLGMVYQhftlVP 105
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIT-HKTKDKyirpVRKRIGMVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 106 SLTGAENLVISRTEV-PAVINWPRERKALAAFMEHMPFQIPLD----RPVsQLAAGEKQKLEIVKQLYLGRSFLVLDEPT 180
Cdd:PRK13646 95 ESQLFEDTVEREIIFgPKNFKMNLDEVKNYAHRLLMDLGFSRDvmsqSPF-QMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2790395612 181 SVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLI 232
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIV 225
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
31-232 |
8.64e-20 |
|
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: 87.70 E-value: 8.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 31 TALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYGLGMVYQHFTlvpSLTGA 110
Cdd:cd03226 14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYVMQDVDYQLF---TDSVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 111 ENLVISRTEVPAVINWPRE---RKALAAFMEHMPFqipldrpvsQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTPAE 187
Cdd:cd03226 91 EELLLGLKELDAGNEQAETvlkDLDLYALKERHPL---------SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2790395612 188 ADEMLGLVRGMTERGElTVLMISHKFHEVTKFADAVSILRRGKLI 232
Cdd:cd03226 162 MERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-242 |
1.13e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.43 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKC---IMGFYHQ--TSGSLSVDGREVtIASPKDAAAY 92
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEarVSGEVYLDGQDI-FKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 93 GLGMVYQHFTLVPSLTGAEN---------LVISRTEVPAVINWPRERKALAAFMEHMpfqipLDRPVSQLAAGEKQKLEI 163
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENvalglklnrLVKSKKELQERVRWALEKAQLWDEVKDR-----LDAPAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790395612 164 VKQLYLGRSFLVLDEPTSVLTPAEADEMLGLVrgMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELST 242
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLF--LELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
26-239 |
1.59e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 87.83 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 26 RFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGRevtIASPkdaAAYGLGMvyqhftlVP 105
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR---VSAL---LELGAGF-------HP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 106 SLTGAENLVI-------SRTEVPAVInwprerKALAAFMEHMPFqipLDRPVSQLAAGEKQKL----------EIvkqly 168
Cdd:COG1134 102 ELTGRENIYLngrllglSRKEIDEKF------DEIVEFAELGDF---IDQPVKTYSSGMRARLafavatavdpDI----- 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790395612 169 lgrsfLVLDEPTSVltpaeADEM-----LGLVRGMTERGElTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGE 239
Cdd:COG1134 168 -----LLVDEVLAV-----GDAAfqkkcLARIRELRESGR-TVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
32-240 |
1.66e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 91.76 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 32 ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDG---REVTIASPKDAaaygLGMVYQHFTLVpSLT 108
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdiRDLTLESLRRQ----IGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 109 GAENLV-----ISRTEVPAVInwpreRKALAA-FMEHMPFQipLDRPVSQ----LAAGEKQKLEIVKQLYLGRSFLVLDE 178
Cdd:COG1132 430 IRENIRygrpdATDEEVEEAA-----KAAQAHeFIEALPDG--YDTVVGErgvnLSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790395612 179 PTSVL-TPAEADEMLGLVRGMTERgelTVLMISHKFHEVtKFADAVSILRRGKLIGSGKVGEL 240
Cdd:COG1132 503 ATSALdTETEALIQEALERLMKGR---TTIVIAHRLSTI-RNADRILVLDDGRIVEQGTHEEL 561
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
18-235 |
3.03e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 87.87 E-value: 3.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFT-ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYgLGM 96
Cdd:PRK13647 5 IEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSK-VGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 97 VYQH-FTLVPSLT-------GAENLVISRTEVPAvinwpRERKALAAF-MEHMPfqiplDRPVSQLAAGEKQKLEIVKQL 167
Cdd:PRK13647 84 VFQDpDDQVFSSTvwddvafGPVNMGLDKDEVER-----RVEEALKAVrMWDFR-----DKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790395612 168 YLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGElTVLMISHKFHEVTKFADAVSILRRGKLIGSG 235
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
22-252 |
3.30e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 89.01 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 22 DMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIAS--PKDaaaygLGMVYQ 99
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSiqQRD-----ICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 100 HFTLVPSLTGAEN-------LVISRTEVPAvinwpRERKALA----AFMEhmpfqiplDRPVSQLAAGEKQKLEIVKQLY 168
Cdd:PRK11432 86 SYALFPHMSLGENvgyglkmLGVPKEERKQ-----RVKEALElvdlAGFE--------DRYVDQISGGQQQRVALARALI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 169 LGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL----STAE 244
Cdd:PRK11432 153 LKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELyrqpASRF 232
|
....*...
gi 2790395612 245 MAAMMiGD 252
Cdd:PRK11432 233 MASFM-GD 239
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
32-240 |
7.65e-19 |
|
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: 85.35 E-value: 7.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 32 ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDG---REVTIASPKDaaayGLGMVYQHfTLVPSLT 108
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidiRDISRKSLRS----MIGVVLQD-TFLFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 109 GAENLVISRTEVP-AVINWPRERKALAAFMEHMP--FQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTP 185
Cdd:cd03254 93 IMENIRLGRPNATdEEVIEAAKEAGAHDFIMKLPngYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2790395612 186 aEADEML--GLVRGMTERgelTVLMISHKFhEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:cd03254 173 -ETEKLIqeALEKLMKGR---TSIIIAHRL-STIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
29-251 |
7.67e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 86.34 E-value: 7.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 29 SFTaLDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYgLGMVYQH--FTLVPS 106
Cdd:PRK13648 22 SFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKH-IGIVFQNpdNQFVGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 107 LT------GAENLVISRTEVPAVINWPRERKALAAFMEHMPfqipldrpvSQLAAGEKQKLEIVKQLYLGRSFLVLDEPT 180
Cdd:PRK13648 100 IVkydvafGLENHAVPYDEMHRRVSEALKQVDMLERADYEP---------NALSGGQKQRVAIAGVLALNPSVIILDEAT 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790395612 181 SVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKfADAVSILRRGKLIGSGKVGELSTAEMAAMMIG 251
Cdd:PRK13648 171 SMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEELTRIG 240
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
33-244 |
9.33e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 85.66 E-value: 9.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 33 LDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQtSGSLSVDGREVTIASPKDAA---AY-------GLGM-VYQHF 101
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELArhrAYlsqqqspPFAMpVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 102 TL-VPSLTGAEnlvisrtEVPAVINwprerkALAAFMEHMPFqipLDRPVSQLAAGEKQKLEIVK-------QLYLGRSF 173
Cdd:COG4138 91 ALhQPAGASSE-------AVEQLLA------QLAEALGLEDK---LSRPLTQLSGGEWQRVRLAAvllqvwpTINPEGQL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790395612 174 LVLDEPTSVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELSTAE 244
Cdd:COG4138 155 LLLDEPMNSLDVAQQAALDRLLRELCQQG-ITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPE 224
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-214 |
1.08e-18 |
|
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: 88.88 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 2 SVIRDTPLPQTGKAVGIETLDMTMRF--------GSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGS 73
Cdd:TIGR02857 299 AVLDAAPRPLAGKAPVTAAPASSLEFsgvsvaypGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGS 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 74 LSVDGREVTIASPKDAAAyGLGMVYQHFTLVPSlTGAENLVISRTEV-PAVINWPRERKALAAFMEHMP--FQIPLDRPV 150
Cdd:TIGR02857 379 IAVNGVPLADADADSWRD-QIAWVPQHPFLFAG-TIAENIRLARPDAsDAEIREALERAGLDEFVAALPqgLDTPIGEGG 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790395612 151 SQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGelTVLMISHKFH 214
Cdd:TIGR02857 457 AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHRLA 518
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
33-237 |
1.20e-18 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 85.39 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 33 LDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGF--YHQTSGSLSVDGREVTIASPKDAAAYGLGMVYQHFTLVPSLTGA 110
Cdd:TIGR01978 16 LKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHpsYEVTSGTILFKGQDLLELEPDERARAGLFLAFQYPEEIPGVSNL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 111 ENLvisRTEVPAVINWPRERK-ALAAFMEH---------MPFQIpLDRPVSQ-LAAGEKQKLEIVKQLYLGRSFLVLDEP 179
Cdd:TIGR01978 96 EFL---RSALNARRSARGEEPlDLLDFEKLlkeklalldMDEEF-LNRSVNEgFSGGEKKRNEILQMALLEPKLAILDEI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790395612 180 TSVLtpaEADEMLGLVRGMTE-RGELT-VLMISHkFHEVTKF--ADAVSILRRGKLIGSGKV 237
Cdd:TIGR01978 172 DSGL---DIDALKIVAEGINRlREPDRsFLIITH-YQRLLNYikPDYVHVLLDGRIVKSGDV 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-463 |
3.45e-18 |
|
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: 87.55 E-value: 3.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGF--YHQTSGSL----------------SVDGR 79
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 80 ------------EVTIASPKDAAAYGLG-----MVYQHFTLVPSLTGAENLVISRTEvpavINWPRERKALAAF------ 136
Cdd:TIGR03269 81 pcpvcggtlepeEVDFWNLSDKLRRRIRkriaiMLQRTFALYGDDTVLDNVLEALEE----IGYEGKEAVGRAVdliemv 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 137 -MEHMPFQIPLDrpvsqLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHE 215
Cdd:TIGR03269 157 qLSHRITHIARD-----LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 216 VTKFADAVSILRRGKLIGSGKVGELSTAEMAAmmigdVKLAELDTRIpvtETAKAVLQIERIK----APDRSGLKTIEID 291
Cdd:TIGR03269 232 IEDLSDKAIWLENGEIKEEGTPDEVVAVFMEG-----VSEVEKECEV---EVGEPIIKVRNVSkryiSVDRGVVKAVDNV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVK-GAAY---GATRPETRRNNVRFIPEEPLQNACAPRMSVS 367
Cdd:TIGR03269 304 SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWvdmTKPGPDGRGRAKRYIGILHQEYDLYPHRTVL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 368 ENLafrtfdlkesgADAIWLN-------RNKIKKGATALIADFKVRTASQSSPiAALSGGNVQRAVLARELTGEVDLLIV 440
Cdd:TIGR03269 384 DNL-----------TEAIGLElpdelarMKAVITLKMVGFDEEKAEEILDKYP-DELSEGERHRVALAQVLIKEPRIVIL 451
|
490 500
....*....|....*....|...
gi 2790395612 441 SNPCFGLDFSAVAEIRARIMRAR 463
Cdd:TIGR03269 452 DEPTGTMDPITKVDVTHSILKAR 474
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
22-240 |
4.13e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 84.25 E-value: 4.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 22 DMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAA----------- 90
Cdd:PRK10619 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQlkvadknqlrl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 91 -AYGLGMVYQHFTLVPSLTGAENLVISRTEVPAVINW-PRERK----ALAAFMEHMPFQIPLDrpvsqLAAGEKQKLEIV 164
Cdd:PRK10619 90 lRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQeARERAvkylAKVGIDERAQGKYPVH-----LSGGQQQRVSIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790395612 165 KQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGElTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
22-235 |
4.27e-18 |
|
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: 82.57 E-value: 4.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 22 DMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGF--YHQTSGSLSVDGREVTIASPKDAAAYGLGMVYQ 99
Cdd:cd03217 5 DLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIFLAFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 100 HftlvPSltgaenlvisrtEVPAVinwprerkALAAFMehmpfqipldRPVSQ-LAAGEKQKLEIVKQLYLGRSFLVLDE 178
Cdd:cd03217 85 Y----PP------------EIPGV--------KNADFL----------RYVNEgFSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 179 PTSVLTpAEADEMLG-LVRGMTERGElTVLMISHkFHEVTKF--ADAVSILRRGKLIGSG 235
Cdd:cd03217 131 PDSGLD-IDALRLVAeVINKLREEGK-SVLIITH-YQRLLDYikPDRVHVLYDGRIVKSG 187
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
32-240 |
4.57e-18 |
|
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: 83.43 E-value: 4.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 32 ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDG---REVTIASPKDAaaygLGMVYQHfTLVPSLT 108
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvRDYTLASLRRQ----IGLVSQD-VFLFNDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 109 GAENLVISRTEVpavinwPRERKALAA-------FMEHMP--FQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEP 179
Cdd:cd03251 92 VAENIAYGRPGA------TREEVEEAAraanaheFIMELPegYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790395612 180 TSVL-TPAEADEMLGLVRGMTERgelTVLMISHKFHEVTKfADAVSILRRGKLIGSGKVGEL 240
Cdd:cd03251 166 TSALdTESERLVQAALERLMKNR---TTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEEL 223
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-243 |
5.01e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 83.94 E-value: 5.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 33 LDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPK---DAAAY--GLGMVYQHFTLVPSL 107
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIfqiDAIKLrkEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 108 TGAENLVisrteVPAVINWPRERKALAAFMEHMPFQIPL-----DR---PVSQLAAGEKQKLEIVKQLYLGRSFLVLDEP 179
Cdd:PRK14246 106 SIYDNIA-----YPLKSHGIKEKREIKKIVEECLRKVGLwkevyDRlnsPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790395612 180 TSVLTPAEADEMLGLVRGMteRGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELSTA 243
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
32-231 |
5.29e-18 |
|
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: 81.71 E-value: 5.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 32 ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYGLGMV---YQHFTLVPSLT 108
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVpedRKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 109 GAENLVISRtevpavinwprerkalaafmehmpfqipldrpvsQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTPAEA 188
Cdd:cd03215 95 VAENIALSS----------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2790395612 189 DEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKL 231
Cdd:cd03215 141 AEIYRLIRELADAG-KAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
18-244 |
6.65e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 85.66 E-value: 6.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKdAAAYGLGMV 97
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAR-AASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 98 YQHFTLVPSLTGAENLVISRTevPAVINW----PRERKALAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSF 173
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRT--PHRSRFdtwtETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790395612 174 LVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMIsHKFHEVTKFADAVSILRRGKLIGSGKVGELSTAE 244
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
33-273 |
7.75e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 83.63 E-value: 7.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 33 LDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDaAAYGLGMVYQH-------FTLVP 105
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWD-IRHKIGMVFQNpdnqfvgATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 106 SLT-GAENLVISRTEVPAVINWPRERKALAAFMEHMPfqipldrpvSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLT 184
Cdd:PRK13650 102 DVAfGLENKGIPHEEMKERVNEALELVGMQDFKEREP---------ARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 185 PAEADEMLGLVRGMTERGELTVLMISHKFHEVTkFADAVSILRRgkligsGKVGELSTAEMAAMMIGDvkLAELDTRIPV 264
Cdd:PRK13650 173 PEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKN------GQVESTSTPRELFSRGND--LLQLGLDIPF 243
|
....*....
gi 2790395612 265 TETAKAVLQ 273
Cdd:PRK13650 244 TTSLVQSLR 252
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
18-244 |
1.03e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 83.31 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRF-GSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYgLGM 96
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF-VGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 97 VYQH---FTLVPSLT-----GAENLVISRTEVPAvinwpRERKALAAF-MEHMpfqipLDRPVSQLAAGEKQKLEIVKQL 167
Cdd:PRK13652 83 VFQNpddQIFSPTVEqdiafGPINLGLDEETVAH-----RVSSALHMLgLEEL-----RDRVPHHLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790395612 168 YLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELSTAE 244
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
33-235 |
2.04e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 81.65 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 33 LDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGF--YHQTSGSLSVDGREVTIASPKDAAAYGLGMVYQHFTLVPSLTGA 110
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERARAGIFLAFQYPVEIPGVSVS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 111 ENLVIS----RTEVPAVINWPRERKALAAFMEhMP--FqipLDRPVSQ-LAAGEKQKLEIVKQLYLGRSFLVLDEPTSvl 183
Cdd:COG0396 96 NFLRTAlnarRGEELSAREFLKLLKEKMKELG-LDedF---LDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDS-- 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790395612 184 tpaeademlGL----VRGMTE------RGELTVLMISH--KFHEVTKfADAVSILRRGKLIGSG 235
Cdd:COG0396 170 ---------GLdidaLRIVAEgvnklrSPDRGILIITHyqRILDYIK-PDFVHVLVDGRIVKSG 223
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
32-235 |
2.04e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 82.86 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 32 ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPK---DAAAYGLGMVYQ--------H 100
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeiKPVRKKVGVVFQfpesqlfeE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 101 FTLVPSLTGAENLVISRTEVPAVINWPRERKALAA-FMEHMPFqipldrpvsQLAAGEKQKLEIVKQLYLGRSFLVLDEP 179
Cdd:PRK13643 101 TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPF---------ELSGGQMRRVAIAGILAMEPEVLVLDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2790395612 180 TSVLTPAEADEMLGLVRGMTERGElTVLMISHKFHEVTKFADAVSILRRGKLIGSG 235
Cdd:PRK13643 172 TAGLDPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
18-240 |
4.98e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 81.28 E-value: 4.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFT-ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIaSPKD--AAAYGL 94
Cdd:PRK13639 2 LETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKY-DKKSllEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 95 GMVYQH---FTLVPSLT-----GAENLVISRTEVPAvinwpRERKALAAF-MEHMPfqiplDRPVSQLAAGEKQKLEIVK 165
Cdd:PRK13639 81 GIVFQNpddQLFAPTVEedvafGPLNLGLSKEEVEK-----RVKEALKAVgMEGFE-----NKPPHHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790395612 166 QLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEG-ITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
292-497 |
6.62e-17 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 80.11 E-value: 6.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRRNnVRFIPEEPlqnACAPRMSVSENLA 371
Cdd:COG1131 20 SLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR-IGYVPQEP---ALYPDLTVRENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 372 F--RTFDLkesgadaiwlNRNKIKKGATALIADFKVrTASQSSPIAALSGGNVQRAVLARELTGEVDLLIVSNPCFGLDF 449
Cdd:COG1131 96 FfaRLYGL----------PRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2790395612 450 SAVAEIRARIMRARNAGAAVlllsedldelM----------EMSDRIMVISEGKLVYE 497
Cdd:COG1131 165 EARRELWELLRELAAEGKTV----------LlsthyleeaeRLCDRVAIIDKGRIVAD 212
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
29-240 |
7.23e-17 |
|
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: 79.97 E-value: 7.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 29 SFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDG---REVTIASPKDAaaygLGMVYQHFTLVP 105
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdiREVTLDSLRRA----IGVVPQDTVLFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 106 SlTGAENLVISRtevPAVINWPRERKALAA----FMEHMPFQipLDRPVSQ----LAAGEKQKLEIVKQLYLGRSFLVLD 177
Cdd:cd03253 89 D-TIGYNIRYGR---PDATDEEVIEAAKAAqihdKIMRFPDG--YDTIVGErglkLSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790395612 178 EPTSVL-TPAEADEMLGLVRGMTERgelTVLMISHKFHEVTKfADAVSILRRGKLIGSGKVGEL 240
Cdd:cd03253 163 EATSALdTHTEREIQAALRDVSKGR---TTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
22-439 |
1.09e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.81 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 22 DMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGReVTIaspkdaaayglGMVYQHF 101
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-LRI-----------GYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 102 TLVPSLTGAENLVISRTEVPAVInwpRERKALAAFMEHMPFQI----------------------------------PLD 147
Cdd:COG0488 71 PLDDDLTVLDTVLDGDAELRALE---AELEELEAKLAEPDEDLerlaelqeefealggweaearaeeilsglgfpeeDLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 148 RPVSQLAAGEKQKLEIVKQLyLGRS-FLVLDEPTSVLtpaeaD--------EMLglvrgMTERGelTVLMISHKFHevtk 218
Cdd:COG0488 148 RPVSELSGGWRRRVALARAL-LSEPdLLLLDEPTNHL-----DlesiewleEFL-----KNYPG--TVLVVSHDRY---- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 219 FADAV--SI--LRRGKLIgSGKVG-----ELSTAEMAAMMIG----DVKLAELDT-----RIPVTETAKA---VLQIERI 277
Cdd:COG0488 211 FLDRVatRIleLDRGKLT-LYPGNysaylEQRAERLEQEAAAyakqQKKIAKEEEfirrfRAKARKAKQAqsrIKALEKL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 278 K----------------APDRSGLKTIEID---------------SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQA 326
Cdd:COG0488 290 EreepprrdktveirfpPPERLGKKVLELEglsksygdktllddlSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDS 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 327 GSVTVkgaayGATrpetrrnnVRfipeeplqnacaprmsvsenLAF-----RTFDLKESGADAIW-LNRNKIKKGATALI 400
Cdd:COG0488 370 GTVKL-----GET--------VK--------------------IGYfdqhqEELDPDKTVLDELRdGAPGGTEQEVRGYL 416
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2790395612 401 ADFKVRTASQSSPIAALSGGnvQRA--VLARELTGEVDLLI 439
Cdd:COG0488 417 GRFLFSGDDAFKPVGVLSGG--EKArlALAKLLLSPPNVLL 455
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
27-235 |
1.48e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 79.29 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 27 FGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYGL-----GMVYQHF 101
Cdd:PRK11124 12 YGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKAIRElrrnvGMVFQQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 102 TLVPSLTGAENLVisrtEVPAVINWPRERKALAAFMEHM------PFQiplDRPVSQLAAGEKQKLEIVKQLYLGRSFLV 175
Cdd:PRK11124 92 NLWPHLTVQQNLI----EAPCRVLGLSKDQALARAEKLLerlrlkPYA---DRFPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 176 LDEPTSVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGSG 235
Cdd:PRK11124 165 FDEPTAALDPEITAQIVSIIRELAETG-ITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
31-235 |
2.10e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 79.36 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 31 TALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDG----REVTIASPKDAAayglGMVYQH--FTLV 104
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsDEENLWDIRNKA----GMVFQNpdNQIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 105 PSLT------GAENLVISRTEVPAVINWPRERKALAAFMEHMPfqipldrpvSQLAAGEKQKLEIVKQLYLGRSFLVLDE 178
Cdd:PRK13633 100 ATIVeedvafGPENLGIPPEEIRERVDESLKKVGMYEYRRHAP---------HLLSGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2790395612 179 PTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKfADAVSILRRGKLIGSG 235
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEG 226
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
10-181 |
2.31e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 82.48 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 10 PQTGKAVGIETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTiasPKDA 89
Cdd:NF033858 259 ADDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---AGDI 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 90 AA-YGLGMVYQHFTLVPSLTGAENLV-------ISRTEVPAVINWPRERKALAAFMEHMPFQIPLD-RPVSQLAAGEKQK 160
Cdd:NF033858 336 ATrRRVGYMSQAFSLYGELTVRQNLElharlfhLPAAEIAARVAEMLERFDLADVADALPDSLPLGiRQRLSLAVAVIHK 415
|
170 180
....*....|....*....|.
gi 2790395612 161 LEIvkqlylgrsfLVLDEPTS 181
Cdd:NF033858 416 PEL----------LILDEPTS 426
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
32-251 |
3.44e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 78.91 E-value: 3.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 32 ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIA-SPKDAAAY--GLGMVYQhF------- 101
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGkKNKKLKPLrkKVGIVFQ-Fpehqlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 102 -TLVPSLT-GAENLVISRTEVPAvinwpRERKALA------AFMEHMPFQipldrpvsqLAAGEKQKLEIVKQLYLGRSF 173
Cdd:PRK13634 101 eTVEKDICfGPMNFGVSEEDAKQ-----KAREMIElvglpeELLARSPFE---------LSGGQMRRVAIAGVLAMEPEV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 174 LVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL--STAEMAAMMIG 251
Cdd:PRK13634 167 LVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIfaDPDELEAIGLD 246
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
33-251 |
3.77e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 78.60 E-value: 3.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 33 LDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAyGLGMVYQH-------FTLVP 105
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRR-KIGMVFQNpdnqfvgATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 106 SLT-GAENLVISRTEVPAvinwpRERKALAAfMEHMPFQIpldRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLT 184
Cdd:PRK13642 102 DVAfGMENQGIPREEMIK-----RVDEALLA-VNMLDFKT---REPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790395612 185 PAEADEMLGLVRGMTERGELTVLMISHKFHEVTKfADAVSILRRGKLIGSGKVGELSTAEMAAMMIG 251
Cdd:PRK13642 173 PTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVEIG 238
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-257 |
3.92e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 78.60 E-value: 3.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 15 AVGIETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFY-----HQTSGSLSVDGRevTIASPKDA 89
Cdd:PRK14271 19 APAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdkvsgYRYSGDVLLGGR--SIFNYRDV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 90 AAYG--LGMVYQHFTLVPS------LTGAE-NLVISRTEVPAVinwPRERKALAAFMEHMPFQIPlDRPVsQLAAGEKQK 160
Cdd:PRK14271 97 LEFRrrVGMLFQRPNPFPMsimdnvLAGVRaHKLVPRKEFRGV---AQARLTEVGLWDAVKDRLS-DSPF-RLSGGQQQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 161 LEIVKQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERgeLTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:PRK14271 172 LCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
250 260
....*....|....*....|....
gi 2790395612 241 -------STAEMAAMMIGDVKLAE 257
Cdd:PRK14271 250 fsspkhaETARYVAGLSGDVKDAK 273
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-236 |
4.00e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 77.96 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCI-----MGFYHQTSGSLSVDGRevTIASPK-DAAA 91
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGR--NIYSPDvDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 92 Y--GLGMVYQHFTLVPSLTGAEN---------LVISRTEVPAVINWPRERkalAAFMEHMPFQIPlDRPvSQLAAGEKQK 160
Cdd:PRK14267 83 VrrEVGMVFQYPNPFPHLTIYDNvaigvklngLVKSKKELDERVEWALKK---AALWDEVKDRLN-DYP-SNLSGGQRQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790395612 161 LEIVKQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTErgELTVLMISHKFHEVTKFADAVSILRRGKLIGSGK 236
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKK--EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGP 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
34-233 |
4.02e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 80.74 E-value: 4.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 34 DHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYH-QTSGSLSVDGREVTIASPKDAAAYGLGMV---YQHFTLVPSLTG 109
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIAQGIAMVpedRKRDGIVPVMGV 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 110 AENL---VISRTEVPAVINWPRERKALAAFMEHMPFQIP-LDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTP 185
Cdd:PRK13549 359 GKNItlaALDRFTGGSRIDDAAELKTILESIQRLKVKTAsPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2790395612 186 AEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIG 233
Cdd:PRK13549 439 GAKYEIYKLINQLVQQG-VAIIVISSELPEVLGLSDRVLVMHEGKLKG 485
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
18-266 |
4.66e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 77.82 E-value: 4.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTiASPKDAAAYGLGMV 97
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVA-TTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 98 YQHFTLVPSLTGAEnLVI------SR----TEVPAVINwprerKALaAFMEHMPFQiplDRPVSQLAAGEKQkleivkql 167
Cdd:COG4604 81 RQENHINSRLTVRE-LVAfgrfpySKgrltAEDREIID-----EAI-AYLDLEDLA---DRYLDELSGGQRQ-------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 168 ylgRSF-----------LVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGK 236
Cdd:COG4604 143 ---RAFiamvlaqdtdyVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGT 219
|
250 260 270
....*....|....*....|....*....|.
gi 2790395612 237 VGELSTAEMaammigdvkLAEL-DTRIPVTE 266
Cdd:COG4604 220 PEEIITPEV---------LSDIyDTDIEVEE 241
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
33-234 |
7.75e-16 |
|
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: 79.87 E-value: 7.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 33 LDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYH-QTSGSLSVDGREVTIASPKDAAAYGLGMV---YQHFTLVPSLT 108
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNPAQAIRAGIAMVpedRKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 109 GAENLVIS---RTEVPAVINWPRERKALAAFMEHMPFQI--PlDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVL 183
Cdd:TIGR02633 356 VGKNITLSvlkSFCFKMRIDAAAELQIIGSAIQRLKVKTasP-FLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2790395612 184 TPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGS 234
Cdd:TIGR02633 435 DVGAKYEIYKLINQLAQEG-VAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
32-235 |
8.98e-16 |
|
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: 76.47 E-value: 8.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 32 ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAyGLGMVYQHFTLVpSLTGAE 111
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRR-NIGYVPQDVTLF-YGTLRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 112 NLVISRTEV--PAVINwPRERKALAAFMEHMPFQipLDRPVS----QLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTP 185
Cdd:cd03245 97 NITLGAPLAddERILR-AAELAGVTDFVNKHPNG--LDLQIGergrGLSGGQRQAVALARALLNDPPILLLDEPTSAMDM 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2790395612 186 AEADEMLGLVRGMTerGELTVLMISHKFhEVTKFADAVSILRRGKLIGSG 235
Cdd:cd03245 174 NSEERLKERLRQLL--GDKTLIIITHRP-SLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
32-240 |
1.02e-15 |
|
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: 76.76 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 32 ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYgLGMVYQHFTLVpSLTGAE 111
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQ-VGVVLQENVLF-NRSIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 112 NLVISRTEVpavinwPRERKALAA-------FMEHMPF---QIPLDRPVSqLAAGEKQKLEIVKQLYLGRSFLVLDEPTS 181
Cdd:cd03252 95 NIALADPGM------SMERVIEAAklagahdFISELPEgydTIVGEQGAG-LSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 182 VL-TPAEADEMLGLVRGMTERgelTVLMISHKFHEVtKFADAVSILRRGKLIGSGKVGEL 240
Cdd:cd03252 168 ALdYESEHAIMRNMHDICAGR---TVIIIAHRLSTV-KNADRIIVMEKGRIVEQGSHDEL 223
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
28-235 |
1.06e-15 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 75.67 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 28 GSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMG--FYHQTSGSLSVDGREVTIASPKDAaaygLGMVYQHFTLVP 105
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFRKI----IGYVPQDDILHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 106 SLTGAENLVISrtevpAVInwprerkalaafmehmpfqipldrpvSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTP 185
Cdd:cd03213 96 TLTVRETLMFA-----AKL--------------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2790395612 186 AEADEMLGLVRGMTERGElTVLMISHK-FHEVTKFADAVSILRRGKLIGSG 235
Cdd:cd03213 145 SSALQVMSLLRRLADTGR-TIICSIHQpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
20-240 |
1.08e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 78.02 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 20 TLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGF----YHQTSGSLSVDGREVTIASPKDAAAY--- 92
Cdd:COG4170 10 TIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGItkdnWHVTADRFRWNGIDLLKLSPRERRKIigr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 93 GLGMVYQHFT--LVPSLTGAENL--VISRTEVPAVI-NWPRERKALA-------------AFMEHMPFQIPldrpvsqla 154
Cdd:COG4170 90 EIAMIFQEPSscLDPSAKIGDQLieAIPSWTFKGKWwQRFKWRKKRAiellhrvgikdhkDIMNSYPHELT--------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 155 AGEKQKLEIVKQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGS 234
Cdd:COG4170 161 EGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVES 240
|
....*.
gi 2790395612 235 GKVGEL 240
Cdd:COG4170 241 GPTEQI 246
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
32-235 |
1.14e-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: 80.44 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 32 ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREvtIASPKDAAAYGLGMVYQHFTLVPSLTGAE 111
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKD--IETNLDAVRQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 112 NLVISRTEVPAviNWPRERKALAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTPAEADEM 191
Cdd:TIGR01257 1023 HILFYAQLKGR--SWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2790395612 192 LGLVrgMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSG 235
Cdd:TIGR01257 1101 WDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
31-240 |
1.88e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 77.43 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 31 TALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREvtiasP---KDAAAYGLGMVY-QHFTLVPS 106
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-----PfkrRKEFARRIGVVFgQRSQLWWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 107 LTGAENLVISRT--EVPavinwPRE-RKALAAFMEHM---PFqipLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPT 180
Cdd:COG4586 111 LPAIDSFRLLKAiyRIP-----DAEyKKRLDELVELLdlgEL---LDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPT 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790395612 181 svltpaeademLGL-------VRG----MTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:COG4586 183 -----------IGLdvvskeaIREflkeYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEEL 242
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
28-241 |
2.38e-15 |
|
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: 78.69 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 28 GSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSV----DGREVTIASP--KDAAAYGLGMVYQHF 101
Cdd:TIGR03269 295 GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPdgRGRAKRYIGILHQEY 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 102 TLVPSLTGAENLvisrTEVPAvINWPRE---RKAL-----AAFMEHMPFQIpLDRPVSQLAAGEKQKLEIVKQLYLGRSF 173
Cdd:TIGR03269 375 DLYPHRTVLDNL----TEAIG-LELPDElarMKAVitlkmVGFDEEKAEEI-LDKYPDELSEGERHRVALAQVLIKEPRI 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790395612 174 LVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGK----VGELS 241
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDpeeiVEELT 520
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
33-235 |
2.80e-15 |
|
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: 75.00 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 33 LDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQ---TSGSLSVDGREVTIASPKDAAAYglgmVYQHFTLVPSLTG 109
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPDQFQKCVAY----VRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 110 AENL---VISRTEVPaviNWPRERKALAAF--MEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLT 184
Cdd:cd03234 99 RETLtytAILRLPRK---SSDAIRKKRVEDvlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2790395612 185 PAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSG 235
Cdd:cd03234 176 SFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
33-231 |
3.51e-15 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 73.40 E-value: 3.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 33 LDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDaaaYG--LGMVYQHFTLVPSlTGA 110
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNE---LGdhVGYLPQDDELFSG-SIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 111 ENLvisrtevpavinwprerkalaafmehmpfqipldrpvsqLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTPAEADE 190
Cdd:cd03246 94 ENI---------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERA 134
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2790395612 191 MLGLVRGMTERGElTVLMISHKfHEVTKFADAVSILRRGKL 231
Cdd:cd03246 135 LNQAIAALKAAGA-TRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
10-236 |
3.96e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 78.22 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 10 PQTGKAVGIETLDMTMRFGSfTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASpKDA 89
Cdd:PRK10790 335 PLQSGRIDIDNVSFAYRDDN-LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSV 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 90 AAYGLGMVYQHfTLVPSLTGAENLV----ISRTEVPAVInwprERKALAAFMEHMPFQI--PLDRPVSQLAAGEKQKLEI 163
Cdd:PRK10790 413 LRQGVAMVQQD-PVVLADTFLANVTlgrdISEEQVWQAL----ETVQLAELARSLPDGLytPLGEQGNNLSVGQKQLLAL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790395612 164 VKQLYLGRSFLVLDEPTSVL---TPAEADEMLGLVRGMTergelTVLMISHKFHEVTKfADAVSILRRGKLIGSGK 236
Cdd:PRK10790 488 ARVLVQTPQILILDEATANIdsgTEQAIQQALAAVREHT-----TLVVIAHRLSTIVE-ADTILVLHRGQAVEQGT 557
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
33-232 |
4.58e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 75.64 E-value: 4.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 33 LDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTI-ASPKDAAAY--GLGMVYQ--------HF 101
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPeTGNKNLKKLrkKVSLVFQfpeaqlfeNT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 102 TLVPSLTGAENLVISRTEVP-AVINWPRERKALAAFMEHMPFqipldrpvsQLAAGEKQKLEIVKQLYLGRSFLVLDEPT 180
Cdd:PRK13641 103 VLKDVEFGPKNFGFSEDEAKeKALKWLKKVGLSEDLISKSPF---------ELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2790395612 181 SVLTPAEADEMLGLVRGMTERGElTVLMISHKFHEVTKFADAVSILRRGKLI 232
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
292-497 |
5.80e-15 |
|
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: 74.08 E-value: 5.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKG---AAYGATRPETRRNNVRFIPEEPLqNACAPRMSVSE 368
Cdd:cd03257 25 SFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdlLKLSRRLRKIRRKEIQMVFQDPM-SSLNPRMTIGE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 369 NLAfrtfdlkesgaDAIWLNRNKIKKGATALIADFKVRTASQSSPIA-----ALSGGNVQRAVLARELTGEVDLLIVSNP 443
Cdd:cd03257 104 QIA-----------EPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLnryphELSGGQRQRVAIARALALNPKLLIADEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790395612 444 CFGLDFSAVAEIRARIMRARNAG-----------AAVLllsedldelmEMSDRIMVISEGKLVYE 497
Cdd:cd03257 173 TSALDVSVQAQILDLLKKLQEELgltllfithdlGVVA----------KIADRVAVMYAGKIVEE 227
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
22-262 |
7.27e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 74.33 E-value: 7.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 22 DMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLsvdgreVTIASPKDAAAYGLGMVYQHF 101
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------LAGTAPLAEAREDTRLMFQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 102 TLVPSLTgaenlVISRTEVPAVINW-PRERKALAAF-MEHMPFQIPldrpvSQLAAGEKQKLEIVKQLYLGRSFLVLDEP 179
Cdd:PRK11247 91 RLLPWKK-----VIDNVGLGLKGQWrDAALQALAAVgLADRANEWP-----AALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 180 TSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEvtkfadAVSILRRGKLIGSGKVGELSTAEMA-AMMIGDVKLAEL 258
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSE------AVAMADRVLLIEEGKIGLDLTVDLPrPRRRGSARLAEL 234
|
....
gi 2790395612 259 DTRI 262
Cdd:PRK11247 235 EAEV 238
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
15-244 |
7.61e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.92 E-value: 7.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 15 AVGIETLDMTMRFGSfTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYgl 94
Cdd:PRK15056 6 GIVVNDVTVTWRNGH-TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAY-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 95 gmVYQHFTL---VPSLTgaENLV-ISRTEVPAVINWP--RERKALAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLY 168
Cdd:PRK15056 83 --VPQSEEVdwsFPVLV--EDVVmMGRYGHMGWLRRAkkRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790395612 169 LGRSFLVLDEP-TSVLTPAEAdEMLGLVRGMTERGElTVLMISHKFHEVTKFADaVSILRRGKLIGSGKVGELSTAE 244
Cdd:PRK15056 159 QQGQVILLDEPfTGVDVKTEA-RIISLLRELRDEGK-TMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTFTAE 232
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
22-244 |
8.32e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.44 E-value: 8.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 22 DMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKcIMGFYHQ-TSGSLSVDGREVTIASPKdaaAYGLGMVYqh 100
Cdd:PRK10575 16 NVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHQPpSEGEILLDAQPLESWSSK---AFARKVAY-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 101 ftLVPSLTGAENLVISrtEVPAVINWPRErKALAAF----MEHMPFQIPL-------DRPVSQLAAGEKQKLEIVKQLYL 169
Cdd:PRK10575 90 --LPQQLPAAEGMTVR--ELVAIGRYPWH-GALGRFgaadREKVEEAISLvglkplaHRLVDSLSGGERQRAWIAMLVAQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790395612 170 GRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELSTAE 244
Cdd:PRK10575 165 DSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
33-232 |
9.54e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 77.07 E-value: 9.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 33 LDHVSVSIPAGSFHALLGENGAGKSTLVKcIMGFYHQ-TSGSLSVDGREVTIASPKDAAAY---GLGMVYQHFTLVPSLT 108
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDKpTSGTYRVAGQDVATLDADALAQLrreHFGFIFQRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 109 GAENLvisrtEVPAVINW--PRERKALA-AFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTP 185
Cdd:PRK10535 103 AAQNV-----EVPAVYAGleRKQRLLRAqELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2790395612 186 AEADEMLGLVRGMTERGElTVLMISHKfHEVTKFADAVSILRRGKLI 232
Cdd:PRK10535 178 HSGEEVMAILHQLRDRGH-TVIIVTHD-PQVAAQAERVIEIRDGEIV 222
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
292-439 |
9.92e-15 |
|
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: 71.53 E-value: 9.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRRNNVRFIPEEPLQNacaPRMSVSENLA 371
Cdd:pfam00005 5 SLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLF---PRLTVRENLR 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790395612 372 FR----TFDLKESGADAI-WLNRNKIKkgataLIADFKVRtasqsSPIAALSGGNVQRAVLARELTGEVDLLI 439
Cdd:pfam00005 82 LGlllkGLSKREKDARAEeALEKLGLG-----DLADRPVG-----ERPGTLSGGQRQRVAIARALLTKPKLLL 144
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
37-240 |
1.27e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 75.84 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 37 SVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDG---REVTIASPKDAAAYGLGMVYQHFTLVPSLTGAENL 113
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 114 VISrTEVPAVINWPRERKALAAF----MEHMPFQIPldrpvSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTPAEAD 189
Cdd:PRK10070 128 AFG-MELAGINAEERREKALDALrqvgLENYAHSYP-----DELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2790395612 190 EMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:PRK10070 202 EMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-240 |
1.44e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.89 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGRevtiasPKDAAAYGL--- 94
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK------PLDYSKRGLlal 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 95 ----GMVYQH------FTLVPS--LTGAENLVISRTEVPAvinwpRERKALAaFMEHMPFQiplDRPVSQLAAGEKQKLE 162
Cdd:PRK13638 76 rqqvATVFQDpeqqifYTDIDSdiAFSLRNLGVPEAEITR-----RVDEALT-LVDAQHFR---HQPIQCLSHGQKKRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790395612 163 IVKQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGElTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:PRK13638 147 IAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
30-235 |
1.45e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 74.50 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 30 FTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSV----------DGREVTIASPKDAAAYG-----L 94
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknNHELITNPYSKKIKNFKelrrrV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 95 GMV-----YQHF--TLVPSLT-GAENLVISRTEVpavinwpreRKALAAFMEHMPFQIP-LDRPVSQLAAGEKQKLEIVK 165
Cdd:PRK13631 119 SMVfqfpeYQLFkdTIEKDIMfGPVALGVKKSEA---------KKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAG 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 166 QLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGElTVLMISHKFHEVTKFADAVSILRRGKLIGSG 235
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
292-493 |
1.61e-14 |
|
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: 72.50 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRRNNVRFIpeepLQNA----CAPRmsVS 367
Cdd:cd03225 21 SLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV----FQNPddqfFGPT--VE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 368 ENLAFRTFDLKESGADAiwlnRNKIKKGATAL-IADFKVRtasqssPIAALSGGNVQRAVLARELTGEVDLLIVSNPCFG 446
Cdd:cd03225 95 EEVAFGLENLGLPEEEI----EERVEEALELVgLEGLRDR------SPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2790395612 447 LDFSAVAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMVISEGK 493
Cdd:cd03225 165 LDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-310 |
1.90e-14 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 75.88 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 22 DMTMRFGS----FTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGF----YHQTSGSLSVDGREVTIASPKDAAAY- 92
Cdd:COG4172 11 DLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDLLGLSERELRRIr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 93 --GLGMVYQ--------HFTLvpsltG---AENLVI----SRTEVPA-VINW------PRERKALAAFmehmPFQipldr 148
Cdd:COG4172 91 gnRIAMIFQepmtslnpLHTI-----GkqiAEVLRLhrglSGAAARArALELlervgiPDPERRLDAY----PHQ----- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 149 pvsqLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLtpaeaD-----EMLGLVRGMTERGELTVLMISHKFHEVTKFADAV 223
Cdd:COG4172 157 ----LSGGQRQRVMIAMALANEPDLLIADEPTTAL-----DvtvqaQILDLLKDLQRELGMALLLITHDLGVVRRFADRV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 224 SILRRGKLIGSGKVGELSTAE--------MAAMMIGDVKlaeldtriPVTETAKAVLQIERIKA--PDRSGL--KTIE-- 289
Cdd:COG4172 228 AVMRQGEIVEQGPTAELFAAPqhpytrklLAAEPRGDPR--------PVPPDAPPLLEARDLKVwfPIKRGLfrRTVGhv 299
|
330 340
....*....|....*....|....*
gi 2790395612 290 --ID--SLTVHAGEIVGIAGISGNG 310
Cdd:COG4172 300 kaVDgvSLTLRRGETLGLVGESGSG 324
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
22-240 |
2.11e-14 |
|
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: 73.93 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 22 DMTMRF----GSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFY---HQTSGSLSVDGREVTIASPKDAAAY-- 92
Cdd:COG0444 6 NLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDLLKLSEKELRKIrg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 93 -GLGMVYQH-FT-LVPSLT-G---AENLVI----SRTEvpavinwpRERKALAAfMEHMpfQIP-----LDR-PvSQLAA 155
Cdd:COG0444 86 rEIQMIFQDpMTsLNPVMTvGdqiAEPLRIhgglSKAE--------ARERAIEL-LERV--GLPdperrLDRyP-HELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 156 GEKQKLEIVKQLYLGRSFLVLDEPTSVLtpaeaD-----EMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGK 230
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTAL-----DvtiqaQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGR 228
|
250
....*....|
gi 2790395612 231 LIGSGKVGEL 240
Cdd:COG0444 229 IVEEGPVEEL 238
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
26-226 |
4.19e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 71.67 E-value: 4.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 26 RFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKdaaAYGLGMVYQHFTlvP 105
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE---IYRQQVSYCAQT--P 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 106 SLTGA---ENLVIS---RTEVPavinwprERKALAAFMehMPFQIP---LDRPVSQLAAGEKQKLEIVKQLYLGRSFLVL 176
Cdd:PRK10247 91 TLFGDtvyDNLIFPwqiRNQQP-------DPAIFLDDL--ERFALPdtiLTKNIAELSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2790395612 177 DEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKfADAVSIL 226
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITL 210
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
32-240 |
4.44e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 74.67 E-value: 4.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 32 ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDG---REVTIASPKDAAAyglgMVYQHFTLVPSlT 108
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlRDYTLASLRNQVA----LVSQNVHLFND-T 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 109 GAENLVISRTEvpaviNWPRERKALAAFMEH-MPFQIPLDRPV--------SQLAAGEKQKLEIVKQLYLGRSFLVLDEP 179
Cdd:PRK11176 433 IANNIAYARTE-----QYSREQIEEAARMAYaMDFINKMDNGLdtvigengVLLSGGQRQRIAIARALLRDSPILILDEA 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790395612 180 TSVL-TPAEADEMLGLVRGMTERgelTVLMISHKFHEVTKfADAVSILRRGKLIGSGKVGEL 240
Cdd:PRK11176 508 TSALdTESERAIQAALDELQKNR---TSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAEL 565
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
35-299 |
5.49e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.53 E-value: 5.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 35 HVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAaayGLGMVYQHFTLVPSLTGAENLV 114
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAER---GVGMVFQSYALYPHLSVAENMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 115 -------ISRTEVPAVINWPRERKALAAFmehmpfqipLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTPAE 187
Cdd:PRK11000 98 fglklagAKKEEINQRVNQVAEVLQLAHL---------LDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 188 ADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL---STAEMAAMMIGDVKLAELDTRipV 264
Cdd:PRK11000 169 RVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELyhyPANRFVAGFIGSPKMNFLPVK--V 246
|
250 260 270
....*....|....*....|....*....|....*
gi 2790395612 265 TETAKAVLQIErikAPDRSGLkTIEIDSLTVHAGE 299
Cdd:PRK11000 247 TATAIEQVQVE---LPNRQQV-WLPVEGRGVQVGA 277
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
18-235 |
5.70e-14 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 70.99 E-value: 5.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGRevtiaspkDAAAYGLGMV 97
Cdd:cd03244 5 FKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGV--------DISKIGLHDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 98 YQHFTLVP------SLTGAENL----VISRTEVPAVInwprERKALAAFMEHMPFQipLDRPV----SQLAAGEKQKLEI 163
Cdd:cd03244 77 RSRISIIPqdpvlfSGTIRSNLdpfgEYSDEELWQAL----ERVGLKEFVESLPGG--LDTVVeeggENLSVGQRQLLCL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790395612 164 VKQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRgmTERGELTVLMISHKFHEVTKFaDAVSILRRGKLIGSG 235
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQKTIR--EAFKDCTVLTIAHRLDTIIDS-DRILVLDKGRVVEFD 219
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
18-235 |
5.88e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 71.97 E-value: 5.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTmrFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFY--HQTSGS-LSVDGREVT----IASPKDAA 90
Cdd:PRK09984 7 VEKLAKT--FNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShIELLGRTVQregrLARDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 91 AYGLGMVYQHFTLVPSLTGAENLVI-SRTEVP---AVINW---PRERKALAAF----MEHMPFQipldrPVSQLAAGEKQ 159
Cdd:PRK09984 85 RANTGYIFQQFNLVNRLSVLENVLIgALGSTPfwrTCFSWftrEQKQRALQALtrvgMVHFAHQ-----RVSTLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790395612 160 KLEIVKQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSG 235
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
33-240 |
8.36e-14 |
|
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: 71.03 E-value: 8.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 33 LDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVtiaspKDAAAYGL----GMVYQHFTLVpSLT 108
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI-----RDLNLRWLrsqiGLVSQEPVLF-DGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 109 GAENLVISRTEVPAVinwprERKALAAFMEHMPFQIPL----DRPV----SQLAAGEKQKLEIVKQLYLGRSFLVLDEPT 180
Cdd:cd03249 93 IAENIRYGKPDATDE-----EVEEAAKKANIHDFIMSLpdgyDTLVgergSQLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790395612 181 SVL-TPAEADEMLGLVRGMTERgelTVLMISHKFHEVTKfADAVSILRRGKLIGSGKVGEL 240
Cdd:cd03249 168 SALdAESEKLVQEALDRAMKGR---TTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDEL 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
35-252 |
9.82e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.55 E-value: 9.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 35 HVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYGLgmVY-----QHFTL------ 103
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGL--VYlpedrQSSGLyldapl 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 104 ---VPSLTGAEN-LVISRTEVPAVINwpRERKALAAFMEHmpfqipLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEP 179
Cdd:PRK15439 359 awnVCALTHNRRgFWIKPARENAVLE--RYRRALNIKFNH------AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790395612 180 T-SVLTPAEADeMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELSTAEMAAMMIGD 252
Cdd:PRK15439 431 TrGVDVSARND-IYQLIRSIAAQN-VAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVDTIMRLAFGE 502
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
31-244 |
2.23e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.92 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 31 TALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYGLGMVYQHFTLVPSLTGA 110
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQEASIFRRLSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 111 ENLvISRTEVPAVINWPRERKALAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTPAEADE 190
Cdd:PRK10895 97 DNL-MAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVID 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2790395612 191 MLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELSTAE 244
Cdd:PRK10895 176 IKRIIEHLRDSG-LGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-241 |
2.50e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 72.30 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 4 IRDTP-LPQTGKAVG-IETLDMTMRF-GSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDG-- 78
Cdd:PRK13657 319 VRDPPgAIDLGRVKGaVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtd 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 79 -REVTIASPKDAaaygLGMVYQHFTLVpSLTGAENLVISRTEV-PAVINWPRERKALAAFMEHMP--FQIPLDRPVSQLA 154
Cdd:PRK13657 399 iRTVTRASLRRN----IAVVFQDAGLF-NRSIEDNIRVGRPDAtDEEMRAAAERAQAHDFIERKPdgYDTVVGERGRQLS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 155 AGEKQKLEIVKQLYLGRSFLVLDEPTSVLTPA-EADEMLGLVRGMTERgelTVLMISHKFHEVtKFADAVSILRRGKLIG 233
Cdd:PRK13657 474 GGERQRLAIARALLKDPPILILDEATSALDVEtEAKVKAALDELMKGR---TTFIIAHRLSTV-RNADRILVFDNGRVVE 549
|
....*...
gi 2790395612 234 SGKVGELS 241
Cdd:PRK13657 550 SGSFDELV 557
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
14-211 |
2.61e-13 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 72.01 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 14 KAVGIETLDMTMRF-GSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTiASPKDAAAY 92
Cdd:TIGR02868 331 GKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVS-SLDQDEVRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 93 GLGMVYQHFTLVPSlTGAENLVISRTEVP-AVINWPRERKALAAFMEHMP--FQIPLDRPVSQLAAGEKQKLEIVKQLYL 169
Cdd:TIGR02868 410 RVSVCAQDAHLFDT-TVRENLRLARPDATdEELWAALERVGLADWLRALPdgLDTVLGEGGARLSGGERQRLALARALLA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2790395612 170 GRSFLVLDEPTSVLTPAEADEMLGLVRGMTErgELTVLMISH 211
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITH 528
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
33-240 |
2.68e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 72.45 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 33 LDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGrevtiaspKDAAAYGLGMVYQHFTLVpsltGAEN 112
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDG--------VPLVQYDHHYLHRQVALV----GQEP 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 113 LVISRTeVPAVINW-----PRERKALAAFMEH-----MPFQIPLDRPV----SQLAAGEKQKLEIVKQLYLGRSFLVLDE 178
Cdd:TIGR00958 565 VLFSGS-VRENIAYgltdtPDEEIMAAAKAANahdfiMEFPNGYDTEVgekgSQLSGGQKQRIAIARALVRKPRVLILDE 643
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790395612 179 PTSVLTpAEADEMLGLVRgmtERGELTVLMISHKFHEVTKfADAVSILRRGKLIGSGKVGEL 240
Cdd:TIGR00958 644 ATSALD-AECEQLLQESR---SRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQL 700
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
36-244 |
3.33e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.58 E-value: 3.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 36 VSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQtSGSLSVDGREVTIASPKDAA---AY-------GLGM-VYQHFTL- 103
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELArhrAYlsqqqtpPFAMpVFQYLTLh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 104 VPSLTgaeNLVISRTEVPAVInwprERKALAAFmehmpfqipLDRPVSQLAAGEKQK-------LEIVKQLYLGRSFLVL 176
Cdd:PRK03695 94 QPDKT---RTEAVASALNEVA----EALGLDDK---------LGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790395612 177 DEPTSVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELSTAE 244
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSELCQQG-IAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
292-469 |
3.66e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 68.03 E-value: 3.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGAtrpetrrnnvrFIPEeplqnacapRMSVSENLA 371
Cdd:NF040873 12 DLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVA-----------YVPQ---------RSEVPDSLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 372 FRTFDLKESGADA-----IWLNRNKIKKGATAL----IADFKVRtasqssPIAALSGGNVQRAVLARELTGEVDLLIVSN 442
Cdd:NF040873 72 LTVRDLVAMGRWArrglwRRLTRDDRAAVDDALervgLADLAGR------QLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180
....*....|....*....|....*..
gi 2790395612 443 PCFGLDFSAVAEIRARIMRARNAGAAV 469
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHARGATV 172
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
31-235 |
3.74e-13 |
|
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: 67.72 E-value: 3.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 31 TALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIAspKDAAAYGLGMVYQHFTLVpSLTGA 110
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL--EKALSSLISVLNQRPYLF-DTTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 111 ENLVIsrtevpavinwprerkalaafmehmpfqipldrpvsQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTPAEADE 190
Cdd:cd03247 93 NNLGR------------------------------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQ 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2790395612 191 MLGLVRGMTErgELTVLMISHKFHEVTKFaDAVSILRRGKLIGSG 235
Cdd:cd03247 137 LLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
47-211 |
3.81e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.04 E-value: 3.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 47 ALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAA---AYGLGMVYQHFTLVPSLTGAENLvisrtEVPAV 123
Cdd:PRK10584 40 ALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAklrAKHVGFVFQSFMLIPTLNALENV-----ELPAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 124 INWPRERKA---LAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTE 200
Cdd:PRK10584 115 LRGESSRQSrngAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNR 194
|
170
....*....|.
gi 2790395612 201 RGELTVLMISH 211
Cdd:PRK10584 195 EHGTTLILVTH 205
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
292-495 |
3.81e-13 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 68.80 E-value: 3.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAG-QRPTqAGSVTVKGAAYGATRPETRRNNVRFipeeplQN-ACAPRMSVSEN 369
Cdd:cd03300 20 SLDIKEGEFFTLLGPSGCGKTTLLRLIAGfETPT-SGEILLDGKDITNLPPHKRPVNTVF------QNyALFPHLTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 370 LAFrtfDLKESGadaiwLNRNKIKKGATALIADFKVRTASQSSPiAALSGGNVQRAVLARELTGEVDLLIVSNPCFGLDF 449
Cdd:cd03300 93 IAF---GLRLKK-----LPKAEIKERVAEALDLVQLEGYANRKP-SQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2790395612 450 SAVAEIRARIMR-ARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLV 495
Cdd:cd03300 164 KLRKDMQLELKRlQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQ 210
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
18-183 |
3.96e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 70.75 E-value: 3.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAaygLGMV 97
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRH---VNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 98 YQHFTLVPSLTGAENLV--ISRTEVPAVINWPRERKALAAF-MEHMPfqiplDRPVSQLAAGEKQKLEIVKQLYLGRSFL 174
Cdd:PRK09452 92 FQSYALFPHMTVFENVAfgLRMQKTPAAEITPRVMEALRMVqLEEFA-----QRKPHQLSGGQQQRVAIARAVVNKPKVL 166
|
....*....
gi 2790395612 175 VLDEPTSVL 183
Cdd:PRK09452 167 LLDESLSAL 175
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-221 |
4.67e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 69.30 E-value: 4.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 17 GIETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCiMGFYHQTSGSLSVDG------------------ 78
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGrveffnqniyerrvnlnr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 79 --REVTIASPK---------DAAAYGLGMVYQHftlvpsltgaenlviSRTEVPAVINWPRERKALAAFMEHMPFQIPLD 147
Cdd:PRK14258 86 lrRQVSMVHPKpnlfpmsvyDNVAYGVKIVGWR---------------PKLEIDDIVESALKDADLWDEIKHKIHKSALD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790395612 148 rpvsqLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFAD 221
Cdd:PRK14258 151 -----LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
28-503 |
5.10e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.42 E-value: 5.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 28 GSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDG-------------REVTIASPKDAAAYGL 94
Cdd:PRK10261 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvielSEQSAAQMRHVRGADM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 95 GMVYQH--FTLVPSLTGAENLVISrteVPAVINWPRERKALAAFMEHMPFQIP-----LDRPVSQLAAGEKQKLEIVKQL 167
Cdd:PRK10261 107 AMIFQEpmTSLNPVFTVGEQIAES---IRLHQGASREEAMVEAKRMLDQVRIPeaqtiLSRYPHQLSGGMRQRVMIAMAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 168 YLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELSTA---- 243
Cdd:PRK10261 184 SCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHApqhp 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 244 ----------EMAAMMIGD-------VKLAELDTRIPVTET-----AKAVLQIERI--KAPDRSGL--------KTIEID 291
Cdd:PRK10261 264 ytrallaavpQLGAMKGLDyprrfplISLEHPAKQEPPIEQdtvvdGEPILQVRNLvtRFPLRSGLlnrvtrevHAVEKV 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGA---AYGATRPETRRNNVRFIPEEPLQnACAPRMSVSE 368
Cdd:PRK10261 344 SFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPYA-SLDPRQTVGD 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 369 NL-----AFRTFDLKESGADAIWLNRNkikkgaTALIADFKVRTASQsspiaaLSGGNVQRAVLARELTGEVDLLIVSNP 443
Cdd:PRK10261 423 SImeplrVHGLLPGKAAAARVAWLLER------VGLLPEHAWRYPHE------FSGGQRQRICIARALALNPKVIIADEA 490
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790395612 444 CFGLDFSavaeIRARIMR-----ARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLVyETAARSA 503
Cdd:PRK10261 491 VSALDVS----IRGQIINllldlQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV-EIGPRRA 550
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
292-497 |
5.72e-13 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 68.73 E-value: 5.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYgATRPETRRNNVRFIPEEplqNACAPRMSVSENLA 371
Cdd:COG4555 21 SFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV-RKEPREARRQIGVLPDE---RGLYDRLTVRENIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 372 FrtfdlkesgadAIWLNRNKIKKGATAL-----------IADFKVRTasqsspiaaLSGGNVQRAVLARELTGEVDLLIV 440
Cdd:COG4555 97 Y-----------FAELYGLFDEELKKRIeeliellgleeFLDRRVGE---------LSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2790395612 441 SNPCFGLDFSAVAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLVYE 497
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQ 213
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
26-240 |
7.87e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 68.13 E-value: 7.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 26 RFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYGLGMVYQHftlvP 105
Cdd:COG1137 12 SYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIGYLPQE----A 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 106 S----LTGAENL--VISRTEVPavinwPRERKA-LAAFMEHmpFQIP--LDRPVSQLAAGEKQKLEIVKQLYLGRSFLVL 176
Cdd:COG1137 88 SifrkLTVEDNIlaVLELRKLS-----KKEREErLEELLEE--FGIThlRKSKAYSLSGGERRRVEIARALATNPKFILL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790395612 177 DEPTSVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:COG1137 161 DEPFAGVDPIAVADIQKIIRHLKERG-IGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEI 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
32-236 |
9.15e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 68.48 E-value: 9.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 32 ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYGLGMVYQH-------FTLV 104
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNpetqfvgRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 105 PSLT-GAENLVISRTEVPAVINWPRERKALAAFMEHMPfqipldrpvSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVL 183
Cdd:PRK13644 97 EDLAfGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSP---------KTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2790395612 184 TPAEADEMLGLVRGMTERGElTVLMISHKFHEVtKFADAVSILRRGKLIGSGK 236
Cdd:PRK13644 168 DPDSGIAVLERIKKLHEKGK-TIVYITHNLEEL-HDADRIIVMDRGKIVLEGE 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
28-247 |
1.05e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 68.17 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 28 GSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAY--GLGMVYQhftlvp 105
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFrrDIQMVFQ------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 106 SLTGAENlviSRTEVPAVINWP---------RERKALAAFMEHMPFQIP--LDRPVSQLAAGEKQKLEIVKQLYLGRSFL 174
Cdd:PRK10419 97 DSISAVN---PRKTVREIIREPlrhllsldkAERLARASEMLRAVDLDDsvLDKRPPQLSGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790395612 175 VLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELSTAEMAA 247
Cdd:PRK10419 174 ILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTFSSPA 246
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
18-240 |
1.31e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 67.85 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDgrEVTIASPKD-AAAYGL-- 94
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVG--DITIDTARSlSQQKGLir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 95 ------GMVYQHFTLVPSLTGAENLVisrtEVPAVIN-WPRE------RKALAafmehmpfQIPL----DRPVSQLAAGE 157
Cdd:PRK11264 82 qlrqhvGFVFQNFNLFPHRTVLENII----EGPVIVKgEPKEeataraRELLA--------KVGLagkeTSYPRRLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 158 KQKLEIVKQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERgELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKV 237
Cdd:PRK11264 150 QQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPA 228
|
...
gi 2790395612 238 GEL 240
Cdd:PRK11264 229 KAL 231
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
33-231 |
1.42e-12 |
|
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: 67.11 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 33 LDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIaspkdaaayglgmvYQHFTL--VPSLTGA 110
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ--------------YEHKYLhsKVSLVGQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 111 ENLVISRTeVPAVINW-----PRERKALAA-------FMEHMP--FQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVL 176
Cdd:cd03248 96 EPVLFARS-LQDNIAYglqscSFECVKEAAqkahahsFISELAsgYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2790395612 177 DEPTSVLTpAEADEML-GLVRGMTERGelTVLMISHKFHEVTKfADAVSILRRGKL 231
Cdd:cd03248 175 DEATSALD-AESEQQVqQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
28-240 |
1.85e-12 |
|
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: 69.33 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 28 GSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFyHQTSGSLSVDGREVTIASPKDAAAY--GLGMVYQ--HFTL 103
Cdd:COG4172 297 GHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRALRPLrrRMQVVFQdpFGSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 104 VPSLT-G---AENLVISRTEVPAVinwPRERKALAAFME-HMPFQIpLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDE 178
Cdd:COG4172 376 SPRMTvGqiiAEGLRVHGPGLSAA---ERRARVAEALEEvGLDPAA-RHRYPHEFSGGQRQRIAIARALILEPKLLVLDE 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790395612 179 PTSVLtpaeaD-----EMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:COG4172 452 PTSAL-----DvsvqaQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
33-214 |
2.54e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 66.38 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 33 LDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAA---YGLGMVYQHFTLVPSLTG 109
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAElrnQKLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 110 AEN----LVISRTEvPAVINwPRERKALAAF-MEHMPFQIPldrpvSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLT 184
Cdd:PRK11629 105 LENvampLLIGKKK-PAEIN-SRALEMLAAVgLEHRANHRP-----SELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190
....*....|....*....|....*....|
gi 2790395612 185 PAEADEMLGLVRGMTERGELTVLMISHKFH 214
Cdd:PRK11629 178 ARNADSIFQLLGELNRLQGTAFLVVTHDLQ 207
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
292-495 |
2.63e-12 |
|
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: 66.00 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAG-QRPTQaGSVTVKGAAYGATRPETRrnNVRFIPEEPlqnACAPRMSVSENL 370
Cdd:cd03259 20 SLTVEPGEFLALLGPSGCGKTTLLRLIAGlERPDS-GEILIDGRDVTGVPPERR--NIGMVFQDY---ALFPHLTVAENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 371 AFrtfDLKESGadaiwLNRNKIKKGATALIADFKVRTASQSSPiAALSGGNVQRAVLARELTGEVDLLIVSNPcfgldFS 450
Cdd:cd03259 94 AF---GLKLRG-----VPKAEIRARVRELLELVGLEGLLNRYP-HELSGGQQQRVALARALAREPSLLLLDEP-----LS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2790395612 451 AV-AEIRARIMRA-----RNAGAAVLLLSEDLDELMEMSDRIMVISEGKLV 495
Cdd:cd03259 160 ALdAKLREELREElkelqRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
263-495 |
2.72e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 68.32 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 263 PVTETAKAVLQIERIKAPDRS--GLKTIEIDSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATR 340
Cdd:PRK11607 8 PQAKTRKALTPLLEIRNLTKSfdGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 341 PETRRNNVRFipeeplQN-ACAPRMSVSENLAfrtFDLKESGadaiwLNRNKIKKGATALIA-----DFKVRTASQsspi 414
Cdd:PRK11607 88 PYQRPINMMF------QSyALFPHMTVEQNIA---FGLKQDK-----LPKAEIASRVNEMLGlvhmqEFAKRKPHQ---- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 415 aaLSGGNVQRAVLARELTGEVDLLIVSNPCFGLDFS-------AVAEIRARImrarnaGAAVLLLSEDLDELMEMSDRIM 487
Cdd:PRK11607 150 --LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlrdrmqlEVVDILERV------GVTCVMVTHDQEEAMTMAGRIA 221
|
....*...
gi 2790395612 488 VISEGKLV 495
Cdd:PRK11607 222 IMNRGKFV 229
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
22-243 |
2.86e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 67.91 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 22 DMTMRF----GSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGF----YHQTSGSLSVDGREVTIASPKD---AA 90
Cdd:PRK15093 8 NLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPRErrkLV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 91 AYGLGMVYQ--HFTLVPSLTGAENLVISrteVPA---------VINWpRERKALA-----------AFMEHMPFQipldr 148
Cdd:PRK15093 88 GHNVSMIFQepQSCLDPSERVGRQLMQN---IPGwtykgrwwqRFGW-RKRRAIEllhrvgikdhkDAMRSFPYE----- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 149 pvsqLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRR 228
Cdd:PRK15093 159 ----LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYC 234
|
250
....*....|....*
gi 2790395612 229 GKLIGSGKVGELSTA 243
Cdd:PRK15093 235 GQTVETAPSKELVTT 249
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
292-497 |
3.69e-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: 65.85 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYgATRPETRRNNVRFIPEeplQNACAPRMSVSENLA 371
Cdd:cd03266 25 SFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEARRRLGFVSD---STGLYDRLTARENLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 372 F--RTFDLKESGADAiwlnrnKIKKGATAL-IADFKVRtasqssPIAALSGGNVQRAVLARELTGEVDLLIVSNPCFGLD 448
Cdd:cd03266 101 YfaGLYGLKGDELTA------RLEELADRLgMEELLDR------RVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2790395612 449 FSAVAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLVYE 497
Cdd:cd03266 169 VMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
284-495 |
4.09e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.07 E-value: 4.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 284 GLKTIEIDSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETR-RNNVRFIPEEPlqnACAP 362
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARaRRGIGYLPQEA---SIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 363 RMSVSENLaFRTFDLKESgadaiwLNRNKIKKGATALIADFKVrTASQSSPIAALSGGNVQRAVLARELTGEVDLLIVSN 442
Cdd:PRK10895 92 RLSVYDNL-MAVLQIRDD------LSAEQREDRANELMEEFHI-EHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2790395612 443 PCFGLDFSAVAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLV 495
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLI 216
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
36-244 |
6.69e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 67.95 E-value: 6.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 36 VSVSIPAGSFHALLGENGAGKSTLVKCIMGF--YHqtsGSLSVDGREVTIASPKDAAAYgLGMVYQHFTLvPSLTGAENL 113
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpYQ---GSLKINGIELRELDPESWRKH-LSWVGQNPQL-PHGTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 114 VISRTEV-PAVINWPRERKALAAFMEHMPFQipLDRPVSQLAA----GEKQKLEIVKQLYLGRSFLVLDEPTSVL-TPAE 187
Cdd:PRK11174 444 LLGNPDAsDEQLQQALENAWVSEFLPLLPQG--LDTPIGDQAAglsvGQAQRLALARALLQPCQLLLLDEPTASLdAHSE 521
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2790395612 188 ADEMLGLVRGMTERgelTVLMISHKFHEVTKFaDAVSILRRGKLIGSGKVGELSTAE 244
Cdd:PRK11174 522 QLVMQALNAASRRQ---TTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
292-497 |
8.71e-12 |
|
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: 64.83 E-value: 8.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGA-AYGATRPETR--RNNVRFIPEeplQNACAPRMSVSE 368
Cdd:cd03261 20 DLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdISGLSEAELYrlRRRMGMLFQ---SGALFDSLTVFE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 369 NLAFRtfdLKESGAdaiwLNRNKIKKGATALIADFKVRTASQSSPiAALSGGNVQRAVLARELTGEVDLLIVSNPCFGLD 448
Cdd:cd03261 97 NVAFP---LREHTR----LSEEEIREIVLEKLEAVGLRGAEDLYP-AELSGGMKKRVALARALALDPELLLYDEPTAGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2790395612 449 FSAVAEIRARIMRARNA-GAAVLLLSEDLDELMEMSDRIMVISEGKLVYE 497
Cdd:cd03261 169 PIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAE 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
292-510 |
8.84e-12 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 65.05 E-value: 8.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAG-QRPTqAGSVTVKGAayGATRPETRRNNVRFIpeepLQN-ACAPRMSVSEN 369
Cdd:cd03296 22 SLDIPSGELVALLGPSGSGKTTLLRLIAGlERPD-SGTILFGGE--DATDVPVQERNVGFV----FQHyALFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 370 LAFrtfDLKESGAdAIWLNRNKIKKGATALIADFKVRTASQSSPiAALSGGNVQRAVLARELTGEVDLLIVSNPCFGLDF 449
Cdd:cd03296 95 VAF---GLRVKPR-SERPPEAEIRAKVHELLKLVQLDWLADRYP-AQLSGGQRQRVALARALAVEPKVLLLDEPFGALDA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 450 SAVAEIRARIMRARN-AGAAVLLLSEDLDELMEMSDRIMVISEGKL--------VYETAARSADISVIGA 510
Cdd:cd03296 170 KVRKELRRWLRRLHDeLHVTTVFVTHDQEEALEVADRVVVMNKGRIeqvgtpdeVYDHPASPFVYSFLGE 239
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
33-211 |
9.70e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.12 E-value: 9.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 33 LDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYgLGmvYQHFtLVPSLTGAEN 112
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHY-LG--HRNA-MKPALTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 113 LvisrtEVPAVINWPRERKALAAfMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTPAeADEML 192
Cdd:PRK13539 94 L-----EFWAAFLGGEELDIAAA-LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AVALF 166
|
170 180
....*....|....*....|
gi 2790395612 193 -GLVRGMTERGELtVLMISH 211
Cdd:PRK13539 167 aELIRAHLAQGGI-VIAATH 185
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-180 |
1.45e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 66.63 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 10 PQTGKAVgIETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVdGREVTIAspkda 89
Cdd:COG0488 309 ERLGKKV-LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKIG----- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 90 aayglgmvY--QHF-TLVPSLTGAENLV-----ISRTEVpavinwpreRKALAAFM---EHmpfqipLDRPVSQLAAGEK 158
Cdd:COG0488 382 --------YfdQHQeELDPDKTVLDELRdgapgGTEQEV---------RGYLGRFLfsgDD------AFKPVGVLSGGEK 438
|
170 180
....*....|....*....|..
gi 2790395612 159 QKLEIVKQLYLGRSFLVLDEPT 180
Cdd:COG0488 439 ARLALAKLLLSPPNVLLLDEPT 460
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
22-236 |
1.75e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.83 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 22 DMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTS--GSLSVDGREVTIASPKDAaayglGMVYQ 99
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILKRT-----GFVTQ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 100 HFTLVPSLTGAENLV-ISRTEVPAVINwpRERKALAAfmEHMPFQIPLDRP---------VSQLAAGEKQKLEIVKQLYL 169
Cdd:PLN03211 148 DDILYPHLTVRETLVfCSLLRLPKSLT--KQEKILVA--ESVISELGLTKCentiignsfIRGISGGERKRVSIAHEMLI 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790395612 170 GRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGK 236
Cdd:PLN03211 224 NPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGK 290
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
33-235 |
2.72e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 63.66 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 33 LDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGF--YHQTSGSLSVDGREVTIASPKDAAAYGLGMVYQHFTLVPsltGA 110
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQYPVEIP---GV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 111 ENLVISRTEVPAVINW----PRERKALAAFME------HMPFQIpLDRPVSQ-LAAGEKQKLEIVKQLYLGRSFLVLDEP 179
Cdd:PRK09580 94 SNQFFLQTALNAVRSYrgqePLDRFDFQDLMEekiallKMPEDL-LTRSVNVgFSGGEKKRNDILQMAVLEPELCILDES 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 180 TSVLtpaEADEMLGLVRGMT--ERGELTVLMISHkFHEVTKF--ADAVSILRRGKLIGSG 235
Cdd:PRK09580 173 DSGL---DIDALKIVADGVNslRDGKRSFIIVTH-YQRILDYikPDYVHVLYQGRIVKSG 228
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
30-240 |
3.06e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 64.26 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 30 FTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYGL----GMV-----YQH 100
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVKRLrkeiGLVfqfpeYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 101 F--TLVPSLT-GAENLVISRTE----VPAV---INWPRErkalaaFMEHMPFQipldrpvsqLAAGEKQKLEIVKQLYLG 170
Cdd:PRK13645 104 FqeTIEKDIAfGPVNLGENKQEaykkVPELlklVQLPED------YVKRSPFE---------LSGGQKRRVALAGIIAMD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 171 RSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:PRK13645 169 GNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
292-493 |
4.69e-11 |
|
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: 61.43 E-value: 4.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAG-QRPTQaGSVTVKGAAYGATRPETR--RNNVRFIpeepLQNACA-PRMSVS 367
Cdd:cd03229 20 SLNIEAGEIVALLGPSGSGKSTLLRCIAGlEEPDS-GSILIDGEDLTDLEDELPplRRRIGMV----FQDFALfPHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 368 ENLAFrtfdlkesgadaiwlnrnkikkgataliadfkvrtasqsspiaALSGGNVQRAVLARELTGEVDLLIVSNPCFGL 447
Cdd:cd03229 95 ENIAL-------------------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSAL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2790395612 448 DFSAVAEIRARIMRAR-NAGAAVLLLSEDLDELMEMSDRIMVISEGK 493
Cdd:cd03229 132 DPITRREVRALLKSLQaQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
27-232 |
4.90e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.97 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 27 FGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYGLGMVYQHFTLVPS 106
Cdd:PRK11614 15 YGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRRVFSR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 107 LTGAENLVI-----SRTEVPAVINW-----PR--ERKALAAfmehmpfqipldrpvSQLAAGEKQKLEIVKQLYLGRSFL 174
Cdd:PRK11614 95 MTVEENLAMggffaERDQFQERIKWvyelfPRlhERRIQRA---------------GTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2790395612 175 VLDEPTSVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLI 232
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQLREQG-MTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
280-497 |
5.32e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 63.47 E-value: 5.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 280 PDrsGLKTIEIDSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYG--ATRPETRRnNVRFIPEEPLQ 357
Cdd:PRK13644 12 PD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGdfSKLQGIRK-LVGIVFQNPET 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 358 NACAprMSVSENLAFrtfdlkesGADAIWLNRNKIKKGATALIADFKVRTASQSSPiAALSGGNVQRAVLARELTGEVDL 437
Cdd:PRK13644 89 QFVG--RTVEEDLAF--------GPENLCLPPIEIRKRVDRALAEIGLEKYRHRSP-KTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 438 LIVSNPCFGLDFSAVAEIRARIMRARNAGAAVlLLSEDLDELMEMSDRIMVISEGKLVYE 497
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLHEKGKTI-VYITHNLEELHDADRIIVMDRGKIVLE 216
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
33-223 |
5.50e-11 |
|
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: 61.02 E-value: 5.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 33 LDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGslsvdgrevTIASPKDAAAYglgMVYQHfTLVPSLTGAEN 112
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSG---------RIGMPEGEDLL---FLPQR-PYLPLGTLREQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 113 LVIsrtevpavinwprerkalaafmehmpfqiPLDRpvsQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTPAEADEML 192
Cdd:cd03223 84 LIY-----------------------------PWDD---VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY 131
|
170 180 190
....*....|....*....|....*....|.
gi 2790395612 193 GLVRGMtergELTVLMISHKfHEVTKFADAV 223
Cdd:cd03223 132 QLLKEL----GITVISVGHR-PSLWKFHDRV 157
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
29-242 |
6.78e-11 |
|
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: 65.42 E-value: 6.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 29 SFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGRevTIASPKDAAAYGLGMVYQHFTLVPSLT 108
Cdd:TIGR01257 1951 SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK--SILTNISDVHQNMGYCPQFDAIDDLLT 2028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 109 GAENLV-------ISRTEVPAVINWPRERKALAAFMehmpfqiplDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTS 181
Cdd:TIGR01257 2029 GREHLYlyarlrgVPAEEIEKVANWSIQSLGLSLYA---------DRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTT 2099
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790395612 182 VLTPaEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELST 242
Cdd:TIGR01257 2100 GMDP-QARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKS 2159
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
284-514 |
7.89e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.46 E-value: 7.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 284 GLKTIEIDSLTVHAGEIVGIAGISGNGQKELAEILAGQRP--TQAGSVTVKGAAYGATR-PETRRNNVRFIPEEPlqnAC 360
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNiRDTERAGIVIIHQEL---TL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 361 APRMSVSENLaFRTFDLKESGADaiwLNRNKIKKGATALIADFKVRTASQSSPIAALSGGNVQRAVLARELTGEVDLLIV 440
Cdd:TIGR02633 90 VPELSVAENI-FLGNEITLPGGR---MAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790395612 441 SNPCFGLDFSAVaEIRARIMRARNA-GAAVLLLSEDLDELMEMSDRIMVISEGKLVYETAARSADISVIGAHMAG 514
Cdd:TIGR02633 166 DEPSSSLTEKET-EILLDIIRDLKAhGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVG 239
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
23-228 |
8.46e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.44 E-value: 8.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 23 MTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLsvdgrevtiaspKDAAAYGLGMVYQHFT 102
Cdd:PRK09544 10 VSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGKLRIGYVPQKLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 103 LVPSLTgaenLVISR--TEVPAVinwprERKALAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPT 180
Cdd:PRK09544 78 LDTTLP----LTVNRflRLRPGT-----KKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2790395612 181 SVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRR 228
Cdd:PRK09544 149 QGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
32-244 |
8.92e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 64.08 E-value: 8.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 32 ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTiaspkdaaAYGLGMVYQHFTLVP------ 105
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIA--------DYSEAALRQAISVVSqrvhlf 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 106 SLTGAENLVI-----SRTEVPAVINwpreRKALAAFMEHMPfqiPLD-------RpvsQLAAGEKQKLEIVKQLYLGRSF 173
Cdd:PRK11160 427 SATLRDNLLLaapnaSDEALIEVLQ----QVGLEKLLEDDK---GLNawlgeggR---QLSGGEQRRLGIARALLHDAPL 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790395612 174 LVLDEPTSVLTPAEADEMLGLVRGMTErgELTVLMISHKFHEVTKFaDAVSILRRGKLIGSGKVGELSTAE 244
Cdd:PRK11160 497 LLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQQ 564
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
31-235 |
9.27e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.96 E-value: 9.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 31 TALDHVSVSIPAGSFHALLGENGAGKST----LVKCImgfyhQTSGSLSVDGREVTIASPKDAAAYGLGM--VYQ--HFT 102
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRHRIqvVFQdpNSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 103 LVPSLTG----AENLvisRTEVPAVINWPRERKALAAFMEhmpfqIPLD-----RPVSQLAAGEKQKLEIVKQLYLGRSF 173
Cdd:PRK15134 375 LNPRLNVlqiiEEGL---RVHQPTLSAAQREQQVIAVMEE-----VGLDpetrhRYPAEFSGGQRQRIAIARALILKPSL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790395612 174 LVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSG 235
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-211 |
1.00e-10 |
|
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: 61.35 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVtiASPKDAAAYGLGMV 97
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL--DFQRDSIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 98 YQHFTLVPSLTGAENL-VISRTEVPAVINWPRERKALAAFMehmpfqiplDRPVSQLAAGEKQKLEIVKQLYLGRSFLVL 176
Cdd:cd03231 79 GHAPGIKTTLSVLENLrFWHADHSDEQVEEALARVGLNGFE---------DRPVAQLSAGQQRRVALARLLLSGRPLWIL 149
|
170 180 190
....*....|....*....|....*....|....*
gi 2790395612 177 DEPTSVLTPAEADEMLGLVRGMTERGELtVLMISH 211
Cdd:cd03231 150 DEPTTALDKAGVARFAEAMAGHCARGGM-VVLTTH 183
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-180 |
1.01e-10 |
|
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: 64.19 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 8 PLPQTGKAVgIETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVdGREVTIASpk 87
Cdd:TIGR03719 314 PGPRLGDKV-IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAY-- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 88 daaayglgmVYQ-HFTLVPSLT-------GAENLVISRTEVPAvinwpreRKALAAFMEHMPFQiplDRPVSQLAAGEKQ 159
Cdd:TIGR03719 390 ---------VDQsRDALDPNKTvweeisgGLDIIKLGKREIPS-------RAYVGRFNFKGSDQ---QKKVGQLSGGERN 450
|
170 180
....*....|....*....|.
gi 2790395612 160 KLEIVKQLYLGRSFLVLDEPT 180
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPT 471
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
31-457 |
1.06e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.96 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 31 TALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQ-----TSGSLSVDGREVTIASpkDAAAYGL-----GMVYQH 100
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppvvyPSGDIRFHGESLLHAS--EQTLRGVrgnkiAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 101 fTLVpSLTGAENLVISRTEVPAVINWPRERKALAAFME-------HMPFQIPLDRPvSQLAAGEKQKLEIVKQLYLGRSF 173
Cdd:PRK15134 101 -PMV-SLNPLHTLEKQLYEVLSLHRGMRREAARGEILNcldrvgiRQAAKRLTDYP-HQLSGGERQRVMIAMALLTRPEL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 174 LVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELSTAE--------M 245
Cdd:PRK15134 178 LIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPthpytqklL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 246 AAMMIGDVklaeldtrIPVTETAKAVLQIERIKA--PDRSGLKTIEID--------SLTVHAGEIVGIAGISGNGQKELA 315
Cdd:PRK15134 258 NSEPSGDP--------VPLPEPASPLLDVEQLQVafPIRKGILKRTVDhnvvvkniSFTLRPGETLGLVGESGSGKSTTG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 316 eiLAGQRPTQA-GSVTVKGAA-YGATR----PETRRNNVRFipEEPlQNACAPRMSVSENLA------FRTFDLKESGAD 383
Cdd:PRK15134 330 --LALLRLINSqGEIWFDGQPlHNLNRrqllPVRHRIQVVF--QDP-NSSLNPRLNVLQIIEeglrvhQPTLSAAQREQQ 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790395612 384 AIwlnrnkikkgatALIADFKVRTASQSSPIAALSGGNVQRAVLARELTGEVDLLIVSNPCFGLDFSAVAEIRA 457
Cdd:PRK15134 405 VI------------AVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILA 466
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
292-469 |
1.25e-10 |
|
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: 61.01 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAaygatRPETRRNNVRFIPEEPLQNACAPrMSVsenla 371
Cdd:cd03235 19 SFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGYVPQRRSIDRDFP-ISV----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 372 frtFDLKESGADA-----IWLNRNKIKKGATAL----IADFKVRtasqssPIAALSGGNVQRAVLARELTGEVDLLIVSN 442
Cdd:cd03235 88 ---RDVVLMGLYGhkglfRRLSKADKAKVDEALervgLSELADR------QIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180
....*....|....*....|....*..
gi 2790395612 443 PCFGLDFSAVAEIRARIMRARNAGAAV 469
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELRREGMTI 185
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
33-240 |
1.31e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 63.69 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 33 LDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDG---REVTIASPKDAaaygLGMVYQHfTLVPSLTG 109
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdiRDVTQASLRAA----IGIVPQD-TVLFNDTI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 110 AENLV-----ISRTEVPAVInwprERKALAAFMEHMPFQipLDRPVSQ----LAAGEKQKLEIVKQLYLGRSFLVLDEPT 180
Cdd:COG5265 449 AYNIAygrpdASEEEVEAAA----RAAQIHDFIESLPDG--YDTRVGErglkLSGGEKQRVAIARTLLKNPPILIFDEAT 522
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790395612 181 SVL-TPAEADEMLGLVRGMTERgelTVLMISHKFHEVTKfADAVSILRRGKLIGSGKVGEL 240
Cdd:COG5265 523 SALdSRTERAIQAALREVARGR---TTLVIAHRLSTIVD-ADEILVLEAGRIVERGTHAEL 579
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
26-215 |
1.55e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 61.64 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 26 RFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDaaayglGMVYQHFTLVP 105
Cdd:PRK11248 10 DYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER------GVVFQNEGLLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 106 SLTGAENLVISrTEVPAVINWPRERKALAafmehMPFQIPLD----RPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTS 181
Cdd:PRK11248 84 WRNVQDNVAFG-LQLAGVEKMQRLEIAHQ-----MLKKVGLEgaekRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190
....*....|....*....|....*....|....
gi 2790395612 182 VLTPAEADEMLGLVRGMTERGELTVLMISHKFHE 215
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQETGKQVLLITHDIEE 191
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
10-232 |
2.08e-10 |
|
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: 60.50 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 10 PQTGKavgIETLDMTMRFGSF--TALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGrevtiaspK 87
Cdd:cd03369 2 PEHGE---IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDG--------I 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 88 DAAAYGLGMVYQHFTLVPSltgaENLVISRTevpavinwprERKALAAFMEHMPFQIPLDRPVSQ----LAAGEKQKLEI 163
Cdd:cd03369 71 DISTIPLEDLRSSLTIIPQ----DPTLFSGT----------IRSNLDPFDEYSDEEIYGALRVSEgglnLSQGQRQLLCL 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790395612 164 VKQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRgmTERGELTVLMISHKFHEVTKFaDAVSILRRGKLI 232
Cdd:cd03369 137 ARALLKRPRVLVLDEATASIDYATDALIQKTIR--EEFTNSTILTIAHRLRTIIDY-DKILVMDAGEVK 202
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
33-212 |
2.45e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.96 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 33 LDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTiaspKDAAAY--GLGMVYQHFTLVPSLTGA 110
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK----KDLCTYqkQLCFVGHRSGINPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 111 ENLVISrtevpavINWPRERKALAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTPAEADE 190
Cdd:PRK13540 93 ENCLYD-------IHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180
....*....|....*....|..
gi 2790395612 191 MLGLVRGMTERGElTVLMISHK 212
Cdd:PRK13540 166 IITKIQEHRAKGG-AVLLTSHQ 186
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
292-495 |
2.91e-10 |
|
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: 59.96 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRrnNVRFIpeepLQN-ACAPRMSVSENL 370
Cdd:cd03301 20 NLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR--DIAMV----FQNyALYPHMTVYDNI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 371 AFrtfDLKESGADaiwlnRNKIKKgataliadfKVRTASQSSPI--------AALSGGNVQRAVLARELTGEVDLLIVSN 442
Cdd:cd03301 94 AF---GLKLRKVP-----KDEIDE---------RVREVAELLQIehlldrkpKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2790395612 443 PCFGLDFSAVAEIRARIMR-ARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLV 495
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRlQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
292-495 |
3.32e-10 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 59.99 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRpetrRNNVRFIPEEplqNACAPRMSVSENLA 371
Cdd:cd03269 20 SFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEE---RGLYPKMKVIDQLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 372 FRTfDLKEsgadaiwLNRNKIKKGATALIADFKVrTASQSSPIAALSGGNVQRAVLARELTGEVDLLIVSNPCFGLDFSA 451
Cdd:cd03269 93 YLA-QLKG-------LKKEEARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2790395612 452 VAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLV 495
Cdd:cd03269 164 VELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
32-230 |
3.77e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 61.13 E-value: 3.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 32 ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAY--GLGMVYQ--HFTLVPSL 107
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLrqKIQIVFQnpYGSLNPRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 108 TgaenlVISRTEVPAVINW---PRERKALAAFM--------EHMpfqiplDRPVSQLAAGEKQKLEIVKQLYLGRSFLVL 176
Cdd:PRK11308 110 K-----VGQILEEPLLINTslsAAERREKALAMmakvglrpEHY------DRYPHMFSGGQRQRIAIARALMLDPDVVVA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2790395612 177 DEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGK 230
Cdd:PRK11308 179 DEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGR 232
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
28-183 |
4.59e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 61.40 E-value: 4.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 28 GSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAaayGLGMVYQHFTLVPSL 107
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADR---DIAMVFQNYALYPHM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 108 TGAENLV-------ISRTEVpavinwpRERKALAAFM-EHMPFqipLDRPVSQLAAGEKQKLE----IVKQlylGRSFLv 175
Cdd:PRK11650 92 SVRENMAyglkirgMPKAEI-------EERVAEAARIlELEPL---LDRKPRELSGGQRQRVAmgraIVRE---PAVFL- 157
|
....*...
gi 2790395612 176 LDEPTSVL 183
Cdd:PRK11650 158 FDEPLSNL 165
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
292-494 |
5.20e-10 |
|
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: 59.43 E-value: 5.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAG-QRPTQaGSVTVKG----AAYGATRPETRRNNVRFIPEeplQNACAPRMSV 366
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGlDRPTS-GEVRVDGtdisKLSEKELAAFRRRHIGFVFQ---SFNLLPDLTA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 367 SENLAFRTFDLKESGADAiwlnRNKIKKGATAL-IADFKVRTASQsspiaaLSGGNVQRAVLARELTGEVDLLIVSNPCF 445
Cdd:cd03255 100 LENVELPLLLAGVPKKER----RERAEELLERVgLGDRLNHYPSE------LSGGQQQRVAIARALANDPKIILADEPTG 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790395612 446 GLDfsavAEIRARIMR-----ARNAGAAVlllsedldeLM--------EMSDRIMVISEGKL 494
Cdd:cd03255 170 NLD----SETGKEVMEllrelNKEAGTTI---------VVvthdpelaEYADRIIELRDGKI 218
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
32-211 |
5.53e-10 |
|
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: 59.37 E-value: 5.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 32 ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSV--DGREVTI--ASPKDAAA---YGLGMVYQHFTLV 104
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLaqASPREILAlrrRTIGYVSQFLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 105 PSLTgAENLVISrtevPAV-INWPRER-KALAAFMEHMpFQIPldRPVSQLAA-----GEKQKLEIVKQLYLGRSFLVLD 177
Cdd:COG4778 106 PRVS-ALDVVAE----PLLeRGVDREEaRARARELLAR-LNLP--ERLWDLPPatfsgGEQQRVNIARGFIADPPLLLLD 177
|
170 180 190
....*....|....*....|....*....|....
gi 2790395612 178 EPTSVLTPAEADEMLGLVRGMTERGeLTVLMISH 211
Cdd:COG4778 178 EPTASLDAANRAVVVELIEEAKARG-TAIIGIFH 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
292-497 |
5.90e-10 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 59.04 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRRNNVRFipeepLQNACAPRMSVSENLA 371
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLF-----QENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 372 F-RTFDLKESGADaiwlnRNKIKKGATAL-IADFKVRTASQsspiaaLSGGNVQRAVLARELTGEVDLLIVSNPcfgldF 449
Cdd:cd03298 93 LgLSPGLKLTAED-----RQAIEVALARVgLAGLEKRLPGE------LSGGERQRVALARVLVRDKPVLLLDEP-----F 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2790395612 450 SAVAEIRARIMRA------RNAGAAVLLLSEDLDELMEMSDRIMVISEGKLVYE 497
Cdd:cd03298 157 AALDPALRAEMLDlvldlhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
292-494 |
6.47e-10 |
|
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: 58.18 E-value: 6.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRRNnVRFIPEEPLQNacaPRMSVSENLA 371
Cdd:cd03230 20 SLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR-IGYLPEEPSLY---ENLTVRENLK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 372 frtfdlkesgadaiwlnrnkikkgataliadfkvrtasqsspiaaLSGGNVQRAVLARELTGEVDLLIVSNPCFGLDFSA 451
Cdd:cd03230 96 ---------------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPES 130
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2790395612 452 VAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMVISEGKL 494
Cdd:cd03230 131 RREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
292-494 |
8.27e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 60.48 E-value: 8.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAayGATRPETRRNNVRFIpeepLQNACAPR-MSVSENL 370
Cdd:PRK10851 22 SLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT--DVSRLHARDRKVGFV----FQHYALFRhMTVFDNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 371 AF--RTFDLKESgadaiwLNRNKIKKGATALIADFKVRTASQSSPiAALSGGNVQRAVLARELTGEVDLLIVSNPCFGLD 448
Cdd:PRK10851 96 AFglTVLPRRER------PNAAAIKAKVTQLLEMVQLAHLADRYP-AQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2790395612 449 FSAVAEIRaRIMRA-----RNAGAAVlllSEDLDELMEMSDRIMVISEGKL 494
Cdd:PRK10851 169 AQVRKELR-RWLRQlheelKFTSVFV---THDQEEAMEVADRVVVMSQGNI 215
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
27-239 |
1.08e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 58.73 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 27 FGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAA--AYGLGMVYQHFTLV 104
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflRRQIGMIFQDHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 105 PSLTGAENLVIsrtevPAVINWPRE---RKALAAFMEHMPFqipLDRPVS---QLAAGEKQKLEIVKQLYLGRSFLVLDE 178
Cdd:PRK10908 92 MDRTVYDNVAI-----PLIIAGASGddiRRRVSAALDKVGL---LDKAKNfpiQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790395612 179 PTSVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGsGKVGE 239
Cdd:PRK10908 164 PTGNLDDALSEGILRLFEEFNRVG-VTVLMATHDIGLISRRSYRMLTLSDGHLHG-GVGGE 222
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-180 |
1.17e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.91 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 24 TMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAA----AY---GLGM 96
Cdd:NF033858 8 SHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVcpriAYmpqGLGK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 97 vyqhfTLVPSLTGAENLV-------ISRTEvpavinwpRERK--------ALAAFmehmpfqipLDRPVSQLAAGEKQKL 161
Cdd:NF033858 88 -----NLYPTLSVFENLDffgrlfgQDAAE--------RRRRidellratGLAPF---------ADRPAGKLSGGMKQKL 145
|
170
....*....|....*....
gi 2790395612 162 EIVKQLYLGRSFLVLDEPT 180
Cdd:NF033858 146 GLCCALIHDPDLLILDEPT 164
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
30-236 |
1.23e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 59.33 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 30 FTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSL----------------SVDGREVTIASPK------ 87
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekEKVLEKLVIQKTRfkkikk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 88 -DAAAYGLGMVYQHftlvpsltgAENLVISRTEVPAVINWPR-------ERKALAA-----------FMEHMPFQipldr 148
Cdd:PRK13651 100 iKEIRRRVGVVFQF---------AEYQLFEQTIEKDIIFGPVsmgvskeEAKKRAAkyielvgldesYLQRSPFE----- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 149 pvsqLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGElTVLMISHKFHEVTKFADAVSILRR 228
Cdd:PRK13651 166 ----LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFKD 240
|
....*...
gi 2790395612 229 GKLIGSGK 236
Cdd:PRK13651 241 GKIIKDGD 248
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
33-240 |
1.93e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 60.06 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 33 LDHVSVSIPAGSFHALLGENGAGKSTLVKCIMgFYHQT----SGSLSVDGREVTIASPKDAAAYglgmVYQHFTLVPSLT 108
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPIDAKEMRAISAY----VQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 109 GAENLVIS--------------RTEVPAVINWPRERKAlaafmEHMPFQIPLDrpVSQLAAGEKQKLEIVKQLYLGRSFL 174
Cdd:TIGR00955 116 VREHLMFQahlrmprrvtkkekRERVDEVLQALGLRKC-----ANTRIGVPGR--VKGLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790395612 175 VLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
33-264 |
1.96e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.68 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 33 LDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYH--------QTSGSLSVDGREVTIASPKDAAayglgmvyqHFTLV 104
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEPLAAIDAPRLA---------RLRAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 105 PSLTGAENLVISRTEVPAVINWPRERKALAafMEHMPFQI-----------PLD-RPVSQLAAGEKQKLE---IVKQLY- 168
Cdd:PRK13547 88 LPQAAQPAFAFSAREIVLLGRYPHARRAGA--LTHRDGEIawqalalagatALVgRDVTTLSGGELARVQfarVLAQLWp 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 169 -----LGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELSTA 243
Cdd:PRK13547 166 phdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTP 245
|
250 260
....*....|....*....|...
gi 2790395612 244 EMAAMMIG-DVKLAEL-DTRIPV 264
Cdd:PRK13547 246 AHIARCYGfAVRLVDAgDGVPPV 268
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
282-469 |
2.42e-09 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 57.12 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 282 RSGLKTIEIDSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRRnNVRFIPEeplQNACA 361
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIAR-GLLYLGH---APGIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 362 PRMSVSENLAFRTFDlkeSGADAIWlnrnkikkgaTALiADFKVRtASQSSPIAALSGGNVQRAVLARELTGEVDLLIVS 441
Cdd:cd03231 86 TTLSVLENLRFWHAD---HSDEQVE----------EAL-ARVGLN-GFEDRPVAQLSAGQQRRVALARLLLSGRPLWILD 150
|
170 180
....*....|....*....|....*...
gi 2790395612 442 NPCFGLDFSAVAEIRARIMRARNAGAAV 469
Cdd:cd03231 151 EPTTALDKAGVARFAEAMAGHCARGGMV 178
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
18-237 |
2.73e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.73 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGF--YHQTSGSLSVDGREVTIASPKDAAAYGLG 95
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPEERAHLGIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 96 MVYQHFTLVPSLTGAENLVISRTEVPAVINWPrERKALAAF---MEHMPF----QIPLDRPVSQ-LAAGEKQKLEIVKQL 167
Cdd:CHL00131 88 LAFQYPIEIPGVSNADFLRLAYNSKRKFQGLP-ELDPLEFLeiiNEKLKLvgmdPSFLSRNVNEgFSGGEKKRNEILQMA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790395612 168 YLGRSFLVLDEPTSVL------TPAEADEMLglvrgMTErgELTVLMISH--KFHEVTKfADAVSILRRGKLIGSGKV 237
Cdd:CHL00131 167 LLDSELAILDETDSGLdidalkIIAEGINKL-----MTS--ENSIILITHyqRLLDYIK-PDYVHVMQNGKIIKTGDA 236
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
292-497 |
3.27e-09 |
|
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: 57.06 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETR-RNNVRFIPEEplqNACAPRMSVSENL 370
Cdd:cd03224 20 SLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaRAGIGYVPEG---RRIFPELTVEENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 371 afrtfdlkESGADAiwLNRNKIKKGATALIADFKVRTASQSSPIAALSGGNVQRAVLARELTGEVDLLIVSNPCFGLDFS 450
Cdd:cd03224 97 --------LLGAYA--RRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2790395612 451 AVAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLVYE 497
Cdd:cd03224 167 IVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLE 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
288-495 |
3.38e-09 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 57.35 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 288 IEIDSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRrnNVRFIPeeplQNACA-PRMSV 366
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR--DISYVP----QNYALfPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 367 SENLAFrtfdlkesGADAIWLNRNKIKKGATALIADFKVRTASQSSPiAALSGGNVQRAVLARELTGEVDLLIVSNPCFG 446
Cdd:cd03299 89 YKNIAY--------GLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKP-ETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2790395612 447 LDFSAVAEIRARIMRAR-NAGAAVLLLSEDLDELMEMSDRIMVISEGKLV 495
Cdd:cd03299 160 LDVRTKEKLREELKKIRkEFGVTVLHVTHDFEEAWALADKVAIMLNGKLI 209
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
18-240 |
3.70e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 57.48 E-value: 3.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCI--MGFYH---QTSGSLSVDGREvtIASPKDAAA- 91
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNpevTITGSIVYNGHN--IYSPRTDTVd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 92 --YGLGMVYQHFTLVPsLTGAENLVISRTevpavINWPRERKALAAFMEHMPFQIPL-----DRPVSQ---LAAGEKQKL 161
Cdd:PRK14239 84 lrKEIGMVFQQPNPFP-MSIYENVVYGLR-----LKGIKDKQVLDEAVEKSLKGASIwdevkDRLHDSalgLSGGQQQRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 162 EIVKQLYLGRSFLVLDEPTSVLTPAEA----DEMLGLvrgmteRGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKV 237
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAgkieETLLGL------KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDT 231
|
...
gi 2790395612 238 GEL 240
Cdd:PRK14239 232 KQM 234
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
106-327 |
4.26e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 58.21 E-value: 4.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 106 SLTGAENLVIsrteVPAVINWPRE--RKALAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVL 183
Cdd:NF000106 100 SFSGRENLYM----IGR*LDLSRKdaRARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 184 TPAEADEMLGLVRGMTERGElTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELSTAEMA-AMMIGDVKLAELDTRi 262
Cdd:NF000106 176 DPRTRNEVWDEVRSMVRDGA-TVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGrTLQIRPAHAAELDRM- 253
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790395612 263 pVTETAKAVLQ-IERIKAPDRSGLKTIEIDSlTVHAGEIVGIAG-----ISGNGQ--KELAEI---LAGQRPTQAG 327
Cdd:NF000106 254 -VGAIAQAGLDgIAGATADHEDGVVNVPIVS-DEQLSAVVGMLGergftISGHQHpsAQL*EVflaITGQKTSEAA 327
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
22-235 |
4.72e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 57.24 E-value: 4.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 22 DMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREvtiASPKDAAAYG-------- 93
Cdd:PRK11701 11 GLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD---GQLRDLYALSeaerrrll 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 94 ---LGMVYQHFT--LVPSLTGAENlVISRTEVPAVINWPRERKALAAFMEHMpfQIPLDR----PvSQLAAGEKQKLEIV 164
Cdd:PRK11701 88 rteWGFVHQHPRdgLRMQVSAGGN-IGERLMAVGARHYGDIRATAGDWLERV--EIDAARiddlP-TTFSGGMQQRLQIA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790395612 165 KQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSG 235
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
286-493 |
4.74e-09 |
|
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: 55.33 E-value: 4.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 286 KTIEIDSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRRNNVRFIPEeplqnacaprms 365
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 366 vsenlafrtfdlkesgadaiwlnrnkikkgataliadfkvrtasqsspiaaLSGGNVQRAVLARELTGEVDLLIVSNPCF 445
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2790395612 446 GLDFSAVAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMVISEGK 493
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
298-496 |
4.85e-09 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 56.53 E-value: 4.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 298 GEIVGIAGISGNGQKELAEILAG-QRPTqAGSVTVKGAAYGATR------PETRRNNVRFipeepLQNACAPRMSVSENL 370
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGlEKPD-GGTIVLNGTVLFDSRkkinlpPQQRKIGLVF-----QQYALFPHLNVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 371 AFrtfDLKEsgadaiwLNRNKIKKGATALIADFKVRTASQSSPiAALSGGNVQRAVLARELTGEVDLLIVSNPCFGLDfs 450
Cdd:cd03297 97 AF---GLKR-------KRNREDRISVDELLDLLGLDHLLNRYP-AQLSGGEKQRVALARALAAQPELLLLDEPFSALD-- 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2790395612 451 avAEIRARIM-----RARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLVY 496
Cdd:cd03297 164 --RALRLQLLpelkqIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
286-495 |
5.45e-09 |
|
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: 56.44 E-value: 5.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 286 KTIEIDSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRRNNVRFIPEEP-LQNAcaprm 364
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVtLFYG----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 365 SVSENLAFRtfdlKESGADAIWLNRNKIkKGATALIA------DFKVRTASQSspiaaLSGGNVQRAVLARELTGEVDLL 438
Cdd:cd03245 93 TLRDNITLG----APLADDERILRAAEL-AGVTDFVNkhpnglDLQIGERGRG-----LSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2790395612 439 IVSNPCFGLDFSAVAEIRARImrARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLV 495
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKERL--RQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
29-231 |
5.87e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 57.13 E-value: 5.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 29 SFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGrEVTIaspkdaAAYGLGMVYQhftlvpsLT 108
Cdd:PRK13546 36 TFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSV------IAISAGLSGQ-------LT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 109 GAEN-------LVISRTEVPAVINWPRERKALAAFMEhmpfqipldRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTS 181
Cdd:PRK13546 102 GIENiefkmlcMGFKRKEIKAMTPKIIEFSELGEFIY---------QPVKKYSSGMRAKLGFSINITVNPDILVIDEALS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2790395612 182 VLTPAEADEMLGLVRGMTERGElTVLMISHKFHEVTKFADAVSILRRGKL 231
Cdd:PRK13546 173 VGDQTFAQKCLDKIYEFKEQNK-TIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
20-239 |
7.51e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 57.58 E-value: 7.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 20 TLDMTMRFGSfTALDhVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGR-----EVTIASPKDAAayGL 94
Cdd:PRK11144 3 ELNFKQQLGD-LCLT-VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaEKGICLPPEKR--RI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 95 GMVYQHFTLVPSLTGAENLvisrtevpavinwpreRKALAAFM-------------EHMpfqipLDRPVSQLAAGEKQKL 161
Cdd:PRK11144 79 GYVFQDARLFPHYKVRGNL----------------RYGMAKSMvaqfdkivallgiEPL-----LDRYPGSLSGGEKQRV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790395612 162 EIVKQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGE 239
Cdd:PRK11144 138 AIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
292-464 |
7.98e-09 |
|
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: 58.07 E-value: 7.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRRNNVRFIPEEPLQNAcaprMSVSENLA 371
Cdd:TIGR02857 342 SFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFA----GTIAENIR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 372 FRTfdlkeSGADAIWLNRNKIKKGATALIADfkvRTASQSSPI----AALSGGNVQRAVLARELTGEVDLLIVSNPCFGL 447
Cdd:TIGR02857 418 LAR-----PDASDAEIREALERAGLDEFVAA---LPQGLDTPIgeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
170
....*....|....*..
gi 2790395612 448 DFSAVAEIRARIMRARN 464
Cdd:TIGR02857 490 DAETEAEVLEALRALAQ 506
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
32-239 |
1.12e-08 |
|
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: 54.64 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 32 ALDHVSVSIPAGSFHALLGENGAGKSTLVKciMGFYHQtsgslsvdGREVTIASPKDAAAYGLGMVYQHFTLVPslTGAE 111
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYAS--------GKARLISFLPKFSRNKLIFIDQLQFLID--VGLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 112 NLvisrtevpavinwprerkalaafmehmpfqiPLDRPVSQLAAGEKQKLEIVKQLY--LGRSFLVLDEPTSVLTPAEAD 189
Cdd:cd03238 78 YL-------------------------------TLGQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDIN 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2790395612 190 EMLGLVRGMTERGElTVLMISHKfHEVTKFADavSILRRGKliGSGKVGE 239
Cdd:cd03238 127 QLLEVIKGLIDLGN-TVILIEHN-LDVLSSAD--WIIDFGP--GSGKSGG 170
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
292-501 |
1.79e-08 |
|
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: 55.03 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRRNNVRFIpeepLQNA----CAPrmSVS 367
Cdd:COG1122 21 SLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV----FQNPddqlFAP--TVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 368 ENLAFrtfdlkesGADAIWLNRNKIKKGATALIADFKVRTASQSSPiAALSGGNVQRAVLARELTGEVDLLIVSNPCFGL 447
Cdd:COG1122 95 EDVAF--------GPENLGLPREEIRERVEEALELVGLEHLADRPP-HELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2790395612 448 DFSAVAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLVYETAAR 501
Cdd:COG1122 166 DPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPR 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
292-461 |
2.01e-08 |
|
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: 54.79 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAygATRPETRRnnvRFIPEEPlqnACAPRMSVSENLA 371
Cdd:cd03293 24 SLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP--VTGPGPDR---GYVFQQD---ALLPWLTVLDNVA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 372 FrtfdlkesGADAIWLNRNKIKKGATALIADFKVRTASQSSPiAALSGGNVQRAVLARELTGEVDLLIvsnpcfgLD--F 449
Cdd:cd03293 96 L--------GLELQGVPKAEARERAEELLELVGLSGFENAYP-HQLSGGMRQRVALARALAVDPDVLL-------LDepF 159
|
170
....*....|..
gi 2790395612 450 SAVAEIRARIMR 461
Cdd:cd03293 160 SALDALTREQLQ 171
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
292-514 |
2.11e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 55.46 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAG-QRPTQaGSVTVKGAAYGATRPETR---RNNVRFIPEEPLqNACAPRMSVS 367
Cdd:PRK10419 32 SLSLKSGETVALLGRSGCGKSTLARLLVGlESPSQ-GNVSWRGEPLAKLNRAQRkafRRDIQMVFQDSI-SAVNPRKTVR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 368 ENLA--FRTF-DLKESGADAiwlnrnkiKKGATALIADFKVRTASQSSPiaALSGGNVQRAVLARELTGEVDLLI----V 440
Cdd:PRK10419 110 EIIRepLRHLlSLDKAERLA--------RASEMLRAVDLDDSVLDKRPP--QLSGGQLQRVCLARALAVEPKLLIldeaV 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790395612 441 SNpcfgLDFSAVAEIRARIMRARN-AGAAVLLLSEDLDELMEMSDRIMVISEGKLVyETAARSADISVigAHMAG 514
Cdd:PRK10419 180 SN----LDLVLQAGVIRLLKKLQQqFGTACLFITHDLRLVERFCQRVMVMDNGQIV-ETQPVGDKLTF--SSPAG 247
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
292-451 |
2.16e-08 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 54.76 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETR-------RNNVrFipeeplqnacaPRM 364
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERpvsmlfqENNL-F-----------PHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 365 SVSENLAF-RTFDLKesgadaiwLNRNKIKKGATAL----IADFKVRTasqssPiAALSGGNVQRAVLAReltgevdLLI 439
Cdd:COG3840 87 TVAQNIGLgLRPGLK--------LTAEQRAQVEQALervgLAGLLDRL-----P-GQLSGGQRQRVALAR-------CLV 145
|
170
....*....|....
gi 2790395612 440 VSNPCFGLD--FSA 451
Cdd:COG3840 146 RKRPILLLDepFSA 159
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
292-495 |
2.73e-08 |
|
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: 54.80 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRRNNVRFIpeepLQNACAPRMSVSENLA 371
Cdd:cd03252 22 SLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVV----LQENVLFNRSIRDNIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 372 frtfdLKESGADaiwlnRNKIKKGATALIA-DFKVRTASQSSPI-----AALSGGNVQRAVLARELTGEVDLLIVSNPCF 445
Cdd:cd03252 98 -----LADPGMS-----MERVIEAAKLAGAhDFISELPEGYDTIvgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2790395612 446 GLDFSAVAEIRaRIMRARNAGAAVLLLSEDLDELMEmSDRIMVISEGKLV 495
Cdd:cd03252 168 ALDYESEHAIM-RNMHDICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIV 215
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-180 |
2.74e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.28 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 8 PLPQTGKAVgIETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVdGREVTIASpk 87
Cdd:PRK11819 316 PGPRLGDKV-IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVKLAY-- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 88 daaayglgmVYQ-HFTLVPSLT-------GAENLVISRTEVPAvinwpreRKALAAFMEHMPFQiplDRPVSQLAAGEKQ 159
Cdd:PRK11819 392 ---------VDQsRDALDPNKTvweeisgGLDIIKVGNREIPS-------RAYVGRFNFKGGDQ---QKKVGVLSGGERN 452
|
170 180
....*....|....*....|.
gi 2790395612 160 KLEIVKQLYLGRSFLVLDEPT 180
Cdd:PRK11819 453 RLHLAKTLKQGGNVLLLDEPT 473
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
292-497 |
3.09e-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: 54.65 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAG-QRPTQaGSVTVKGAAYGATRPETRRN-NVRFIPEEPLqnacAPRMSVSEN 369
Cdd:cd03267 41 SFTIEKGEIVGFIGPNGAGKTTTLKILSGlLQPTS-GEVRVAGLVPWKRRKKFLRRiGVVFGQKTQL----WWDLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 370 LAF--RTFDLKESGAdaiwlnRNKIKKGATAL-IADFkvrtasQSSPIAALSGGNVQRAVLARELTGEVDLLIVSNPCFG 446
Cdd:cd03267 116 FYLlaAIYDLPPARF------KKRLDELSELLdLEEL------LDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2790395612 447 LDFSAVAEIRARIMRA-RNAGAAVLLLSEDLDELMEMSDRIMVISEGKLVYE 497
Cdd:cd03267 184 LDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
273-495 |
3.92e-08 |
|
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: 53.80 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 273 QIERIKAPDRSGLKTIEIDSLTVHAGEIVGIAGISGNGQKELAEILAG-QRPTQaGSVTVKGAAYGATRpetRRNNVRFI 351
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGlIKESS-GSILLNGKPIKAKE---RRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 352 PEEPLQNACapRMSVSENLAFRTFDLKESGADAiwlnrNKIKKgaTALIADFKVRtasqsSPiAALSGGNVQRAVLAREL 431
Cdd:cd03226 77 MQDVDYQLF--TDSVREELLLGLKELDAGNEQA-----ETVLK--DLDLYALKER-----HP-LSLSGGQKQRLAIAAAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790395612 432 TGEVDLLIVSNPCFGLDFSAVAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLV 495
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
292-495 |
4.25e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.16 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAA------YGATRPETR---RNNVRFIPEEPLQnacAP 362
Cdd:PRK11701 26 SFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdlYALSEAERRrllRTEWGFVHQHPRD---GL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 363 RMSVSE--NLAFRTF--------DLKESGADaiWLNRNKIkkgATALIADFkvrtasqssPiAALSGGNVQRAVLARELT 432
Cdd:PRK11701 103 RMQVSAggNIGERLMavgarhygDIRATAGD--WLERVEI---DAARIDDL---------P-TTFSGGMQQRLQIARNLV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790395612 433 GEVDLLIVSNPCFGLDFSavaeIRARI---MRA--RNAGAAVLLLSEDLDELMEMSDRIMVISEGKLV 495
Cdd:PRK11701 168 THPRLVFMDEPTGGLDVS----VQARLldlLRGlvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
32-255 |
4.74e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 54.71 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 32 ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKD--AAAYGLGMVYQH--FTLVPSL 107
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEwrAVRSDIQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 108 T-G---AENLVI-----SRTEVpavinwpRER-KALAAFMEHMPFQIplDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLD 177
Cdd:PRK15079 116 TiGeiiAEPLRTyhpklSRQEV-------KDRvKAMMLKVGLLPNLI--NRYPHEFSGGQCQRIGIARALILEPKLIICD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 178 EPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL--------STAEMAAMM 249
Cdd:PRK15079 187 EPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVyhnplhpyTKALMSAVP 266
|
....*.
gi 2790395612 250 IGDVKL 255
Cdd:PRK15079 267 IPDPDL 272
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
10-240 |
5.53e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 54.02 E-value: 5.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 10 PQTGKAVGIETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKC-------IMGFyhQTSGSLSVDGREVT 82
Cdd:PRK14243 3 TLNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndlIPGF--RVEGKVTFHGKNLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 83 iASPKDAAAY--GLGMVYQHFTLVPS--------------LTGAENLVISRTEVPAVInWPRERKAlaafmehmpfqipL 146
Cdd:PRK14243 81 -APDVDPVEVrrRIGMVFQKPNPFPKsiydniaygaringYKGDMDELVERSLRQAAL-WDEVKDK-------------L 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 147 DRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERgeLTVLMISHKFHEVTKFADAVSIL 226
Cdd:PRK14243 146 KQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTAFF 223
|
250
....*....|....
gi 2790395612 227 RRGKLIGSGKVGEL 240
Cdd:PRK14243 224 NVELTEGGGRYGYL 237
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
292-497 |
6.69e-08 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 53.32 E-value: 6.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAG-QRPTQaGSVTVKGAAYGATRPETR-RNNVRFIPEEPlqnACAPRMSVSEN 369
Cdd:cd03218 20 SLSVKQGEIVGLLGPNGAGKTTTFYMIVGlVKPDS-GKILLDGQDITKLPMHKRaRLGIGYLPQEA---SIFRKLTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 370 L--AFRTFDLkesgadaiwlNRNKIKKGATALIADFKVrTASQSSPIAALSGGNVQRAVLARELTGEVDLLIVSNPCFGL 447
Cdd:cd03218 96 IlaVLEIRGL----------SKKEREEKLEELLEEFHI-THLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2790395612 448 DFSAVAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLVYE 497
Cdd:cd03218 165 DPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAE 214
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
292-462 |
6.81e-08 |
|
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: 55.15 E-value: 6.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRRNNVRFIPeeplQNACAPRMSVSENLA 371
Cdd:COG4988 357 SLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVP----QNPYLFAGTIRENLR 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 372 FRTFDLKEsgaDAIW--LNRnkikkgatALIADFkVRTASQ--SSPI----AALSGGNVQRAVLARELTGEVDLLIVSNP 443
Cdd:COG4988 433 LGRPDASD---EELEaaLEA--------AGLDEF-VAALPDglDTPLgeggRGLSGGQAQRLALARALLRDAPLLLLDEP 500
|
170
....*....|....*....
gi 2790395612 444 CFGLDfsavAEIRARIMRA 462
Cdd:COG4988 501 TAHLD----AETEAEILQA 515
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
292-514 |
7.40e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 53.34 E-value: 7.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAygATRPETRRNNVRFIPEEPLQNACAPRMSVSENLA 371
Cdd:PRK11614 25 SLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKD--ITDWQTAKIMREAVAIVPEGRRVFSRMTVEENLA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 372 FRTFdlkesgadaiWLNRNKIKKGATALIADFKVRTASQSSPIAALSGGNVQRAVLARELTGEVDLLIVSNPCFGLDFSA 451
Cdd:PRK11614 103 MGGF----------FAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790395612 452 VAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLVYET--AARSADISVIGAHMAG 514
Cdd:PRK11614 173 IQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDtgDALLANEAVRSAYLGG 237
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
18-230 |
7.61e-08 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 51.30 E-value: 7.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGReVTIaspkdaaAYglgmv 97
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST-VKI-------GY----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 98 yqhftlvpsltgaenlvisrtevpavinwprerkalaafmehmpfqipldrpVSQLAAGEKQKLEIVKQLYLGRSFLVLD 177
Cdd:cd03221 68 ----------------------------------------------------FEQLSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2790395612 178 EPTSVL-TPA-EAdemlgLVRGMTE-RGelTVLMISHKFHEVTKFADAVSILRRGK 230
Cdd:cd03221 96 EPTNHLdLESiEA-----LEEALKEyPG--TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
270-509 |
8.54e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 54.04 E-value: 8.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 270 AVLQIERIKapDRSGLKTIEID-SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYgATRPETRRNNV 348
Cdd:PRK13537 6 APIDFRNVE--KRYGDKLVVDGlSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV-PSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 349 RFIPEepLQNaCAPRMSVSENLAF--RTFDLKESGADAiwlnrnkikkgATALIADFKVRTASQSSPIAALSGGNVQRAV 426
Cdd:PRK13537 83 GVVPQ--FDN-LDPDFTVRENLLVfgRYFGLSAAAARA-----------LVPPLLEFAKLENKADAKVGELSGGMKRRLT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 427 LARELTGEVDLLIVSNPCFGLDFSAVAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLVYETAARSADIS 506
Cdd:PRK13537 149 LARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
...
gi 2790395612 507 VIG 509
Cdd:PRK13537 229 EIG 231
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
31-211 |
1.12e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 31 TALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVdGREVTIAspkdaaayglgmvY--QH-FTLVPSL 107
Cdd:PRK11147 333 QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEVA-------------YfdQHrAELDPEK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 108 TGAENLVISRTEVpaVINwPRERKALAAFMEhmpFQIPLDR---PVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLt 184
Cdd:PRK11147 399 TVMDNLAEGKQEV--MVN-GRPRHVLGYLQD---FLFHPKRamtPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDL- 471
|
170 180
....*....|....*....|....*...
gi 2790395612 185 paeaD-EMLGLVRGMTERGELTVLMISH 211
Cdd:PRK11147 472 ----DvETLELLEELLDSYQGTVLLVSH 495
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
292-497 |
1.14e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 53.68 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGAtRPETRRNNVRFIPEeplQNACAPRMSVSENLA 371
Cdd:PRK13536 61 SFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQ---FDNLDLEFTVRENLL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 372 F--RTFDLKESGADAIwlnrnkikkgaTALIADFKVRTASQSSPIAALSGGNVQRAVLARELTGEVDLLIVSNPCFGLDF 449
Cdd:PRK13536 137 VfgRYFGMSTREIEAV-----------IPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDP 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2790395612 450 SAVAEI--RARIMRARnaGAAVLLLSEDLDELMEMSDRIMVISEGKLVYE 497
Cdd:PRK13536 206 HARHLIweRLRSLLAR--GKTILLTTHFMEEAERLCDRLCVLEAGRKIAE 253
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
292-497 |
1.70e-07 |
|
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: 51.28 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRRNNVRFIPeeplQNacaprmsvsenla 371
Cdd:cd03214 19 SLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP----QA------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 372 frtfdLKESGadaiwlnrnkikkgatalIADFKVRtasqssPIAALSGGNVQRAVLARELTGEVDLLIVSNPCFGLDFSA 451
Cdd:cd03214 82 -----LELLG------------------LAHLADR------PFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAH 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2790395612 452 VAEIRARIMR-ARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLVYE 497
Cdd:cd03214 133 QIELLELLRRlARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
272-448 |
2.24e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 52.01 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 272 LQIERIKApDRSGLKTIEIDSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAygATRPETRRNNVrfi 351
Cdd:PRK11248 2 LQISHLYA-DYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP--VEGPGAERGVV--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 352 peepLQN-ACAPRMSVSENLAfrtFDLKESGADaiwlnrnKIKKGATALIADFKVRTA-SQSSPIAALSGGNVQRAVLAR 429
Cdd:PRK11248 76 ----FQNeGLLPWRNVQDNVA---FGLQLAGVE-------KMQRLEIAHQMLKKVGLEgAEKRYIWQLSGGQRQRVGIAR 141
|
170
....*....|....*....
gi 2790395612 430 ELTGEVDLLIVSNPCFGLD 448
Cdd:PRK11248 142 ALAANPQLLLLDEPFGALD 160
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
146-488 |
2.62e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.27 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 146 LDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTErgELTVLMISHKFHEVTKFADAVSI 225
Cdd:PRK13409 206 LDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 226 LRrGKLIGSGKV---------------GELStAEmaAMMIGDVKLaELDTRIPVTETAKAVLqierIKAPDRS---GLKT 287
Cdd:PRK13409 284 AY-GEPGAYGVVskpkgvrvgineylkGYLP-EE--NMRIRPEPI-EFEERPPRDESERETL----VEYPDLTkklGDFS 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 288 IEIDSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSV--TVKgAAYgatRPEtrrnnvrFIpeEPLQNacaprMS 365
Cdd:PRK13409 355 LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVdpELK-ISY---KPQ-------YI--KPDYD-----GT 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 366 VSENLAFRTFDLKESgadaiWLNRNKIKKGATALIADFKVRTasqsspiaaLSGGNVQRAVLARELTGEVDLLIVSNPCF 445
Cdd:PRK13409 417 VEDLLRSITDDLGSS-----YYKSEIIKPLQLERLLDKNVKD---------LSGGELQRVAIAACLSRDADLYLLDEPSA 482
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2790395612 446 GLDFS---AVAEIRARIMRARNAGAAVlllsedldelME--------MSDRIMV 488
Cdd:PRK13409 483 HLDVEqrlAVAKAIRRIAEEREATALV----------VDhdiymidyISDRLMV 526
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
144-235 |
2.78e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 51.85 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 144 IPLDRPVSQLAAGEKQKLEIVKQLYL---GRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGElTVLMISHKFHeVTKFA 220
Cdd:cd03271 161 IKLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN-TVVVIEHNLD-VIKCA 238
|
90 100
....*....|....*....|.
gi 2790395612 221 DAVSIL------RRGKLIGSG 235
Cdd:cd03271 239 DWIIDLgpeggdGGGQVVASG 259
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
292-500 |
2.81e-07 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 51.22 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGaaYGATR-PETRRNNVRFIPEEPlqnACAPRMSVSENL 370
Cdd:cd03265 20 SFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG--HDVVRePREVRRRIGIVFQDL---SVDDELTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 371 AF--RTFDLKESGAdaiwlnRNKIKKGATAL-IADFKVRtasqssPIAALSGGNVQRAVLARELTGEVDLLIVSNPCFGL 447
Cdd:cd03265 95 YIhaRLYGVPGAER------RERIDELLDFVgLLEAADR------LVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2790395612 448 DFSAVAEIRARI--MRARNaGAAVLLLSEDLDELMEMSDRIMVISEGKLVYETAA 500
Cdd:cd03265 163 DPQTRAHVWEYIekLKEEF-GMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
292-466 |
2.97e-07 |
|
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: 53.13 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRRNNVRFIPEEPLQNACaprmSVSENLA 371
Cdd:TIGR02868 355 SLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDT----TVRENLR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 372 FRTFDLkeSGADAIWLNRnkikkgATALIADFKVRTASQSSPI----AALSGGNVQRAVLARELTGEVDLLIVSNPCFGL 447
Cdd:TIGR02868 431 LARPDA--TDEELWAALE------RVGLADWLRALPDGLDTVLgeggARLSGGERQRLALARALLADAPILLLDEPTEHL 502
|
170
....*....|....*....
gi 2790395612 448 DfsavAEIRARIMRARNAG 466
Cdd:TIGR02868 503 D----AETADELLEDLLAA 517
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
48-231 |
3.04e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.05 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 48 LLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYgLGMVYQHFTLVPSLTGAENlviSRTEVPAVINWp 127
Cdd:PRK10522 354 LIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL-FSAVFTDFHLFDQLLGPEG---KPANPALVEKW- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 128 RERKALAAFMEHMPFQIPLdrpvSQLAAGEKQKLEIVKQLYLGRSFLVLDEptsvlTPAEAD---------EMLGLVRGM 198
Cdd:PRK10522 429 LERLKMAHKLELEDGRISN----LKLSKGQKKRLALLLALAEERDILLLDE-----WAADQDphfrrefyqVLLPLLQEM 499
|
170 180 190
....*....|....*....|....*....|...
gi 2790395612 199 TErgelTVLMISHKFHEVTKfADAVSILRRGKL 231
Cdd:PRK10522 500 GK----TIFAISHDDHYFIH-ADRLLEMRNGQL 527
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
292-469 |
3.54e-07 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 51.24 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGaaygaTRPETRRNNVRFIPeeplQnacapRMSVSENLA 371
Cdd:COG1121 26 SLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG-----KPPRRARRRIGYVP----Q-----RAEVDWDFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 372 FRTFDLKESGADAI-----WLNRNKIKKGATAL----IADFKVRtasqssPIAALSGGNVQRAVLARELTGEVDLLIVSN 442
Cdd:COG1121 92 ITVRDVVLMGRYGRrglfrRPSRADREAVDEALervgLEDLADR------PIGELSGGQQQRVLLARALAQDPDLLLLDE 165
|
170 180
....*....|....*....|....*..
gi 2790395612 443 PCFGLDFSAVAEIRARIMRARNAGAAV 469
Cdd:COG1121 166 PFAGVDAATEEALYELLRELRREGKTI 192
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
33-223 |
4.03e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.91 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 33 LDHVSVSIPAGSFHALLGENGAGKS-----TLVKCIMGFYHQTSGS-LSVDG---------------------------- 78
Cdd:PRK00635 611 LKDLTISLPLGRLTVVTGVSGSGKSslindTLVPAVEEFIEQGFCSnLSIQWgaisrlvhitrdlpgrsqrsipltyika 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 79 ----REVTIASPKDAAaygLGMVYQHFTLVPSL--------TGAENLVISRTEVPA-----------VINWPRERKALAA 135
Cdd:PRK00635 691 fddlRELFAEQPRSKR---LGLTKSHFSFNTPLgacaecqgLGSITTTDNRTSIPCpsclgkrflpqVLEVRYKGKNIAD 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 136 FMEHMPFQ-------------------------IPLDRPVSQLAAGEKQKLEIVKQLYLG---RSFLVLDEPTSVLTPAE 187
Cdd:PRK00635 768 ILEMTAYEaekffldepsihekihalcslgldyLPLGRPLSSLSGGEIQRLKLAYELLAPskkPTLYVLDEPTTGLHTHD 847
|
250 260 270
....*....|....*....|....*....|....*.
gi 2790395612 188 ADEMLGLVRGMTERGElTVLMISHKFHeVTKFADAV 223
Cdd:PRK00635 848 IKALIYVLQSLTHQGH-TVVIIEHNMH-VVKVADYV 881
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
26-222 |
4.21e-07 |
|
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: 49.67 E-value: 4.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 26 RFGSFtaLDHVSVSIPAGSFHALLGENGAGKSTLVKCImgfyhqtsgslsvdgrevtiaspkdaaAYGLGMVYQHftlvp 105
Cdd:cd03227 6 RFPSY--FVPNDVTFGEGSLTIITGPNGSGKSTILDAI---------------------------GLALGGAQSA----- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 106 slTGAENLVISRTEVPAVinwprerKALAAFMehmpfqipldrpVSQLAAGEKQKLEIVKQL----YLGRSFLVLDEPTS 181
Cdd:cd03227 52 --TRRRSGVKAGCIVAAV-------SAELIFT------------RLQLSGGEKELSALALILalasLKPRPLYILDEIDR 110
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2790395612 182 VLTPAEADEMLGLVRGMTERGeLTVLMISHkFHEVTKFADA 222
Cdd:cd03227 111 GLDPRDGQALAEAILEHLVKG-AQVIVITH-LPELAELADK 149
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
32-242 |
4.53e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.59 E-value: 4.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 32 ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIaspkdaaAYGLGMVYQhftlvpsLTGAE 111
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALI-------AISSGLNGQ-------LTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 112 NLV-------ISRTEVPAVINWPRERKALAAFMehmpfqiplDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLT 184
Cdd:PRK13545 105 NIElkglmmgLTKEKIKEIIPEIIEFADIGKFI---------YQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2790395612 185 PAEADEMLGLVRGMTERGElTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGELST 242
Cdd:PRK13545 176 QTFTKKCLDKMNEFKEQGK-TIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-240 |
7.09e-07 |
|
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: 52.26 E-value: 7.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 3 VIRDTPLPQTGKAVG-IETLDMTMRF--GSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGR 79
Cdd:TIGR00957 1269 QIQETAPPSGWPPRGrVEFRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGL 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 80 EVtiaspkdaAAYGLGMVYQHFTLVP------SLTGAENLVISRTEVPAVINWPRERKALAAFMEHMPFQipLDRPVSQ- 152
Cdd:TIGR00957 1349 NI--------AKIGLHDLRFKITIIPqdpvlfSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDK--LDHECAEg 1418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 153 ---LAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRgmTERGELTVLMISHKFHEVTKFAdAVSILRRG 229
Cdd:TIGR00957 1419 genLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKG 1495
|
250
....*....|.
gi 2790395612 230 KLIGSGKVGEL 240
Cdd:TIGR00957 1496 EVAEFGAPSNL 1506
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-211 |
7.53e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 49.96 E-value: 7.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVD------GREVTI------AS 85
Cdd:COG2401 31 LEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDvpdnqfGREASLidaigrKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 86 PKDAAAYGLGMVyqhftlvpSLTGAENLVisrtevpavinwprerkalaafmehmpfqipldRPVSQLAAGEKQKLEIVK 165
Cdd:COG2401 111 DFKDAVELLNAV--------GLSDAVLWL---------------------------------RRFKELSTGQKFRFRLAL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2790395612 166 QLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISH 211
Cdd:COG2401 150 LLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
292-494 |
7.85e-07 |
|
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: 49.14 E-value: 7.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRRNNVRFIPEEplqnacaprmsvsENLa 371
Cdd:cd03246 22 SFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQD-------------DEL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 372 frtfdLKESGADAIwlnrnkikkgataliadfkvrtasqsspiaaLSGGNVQRAVLARELTGEVDLLIVSNPCFGLDFSA 451
Cdd:cd03246 88 -----FSGSIAENI-------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEG 131
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2790395612 452 VAEIRARIMRARNAGAAVlLLSEDLDELMEMSDRIMVISEGKL 494
Cdd:cd03246 132 ERALNQAIAALKAAGATR-IVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
33-229 |
7.94e-07 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 50.02 E-value: 7.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 33 LDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSL---SVDGREVTIASPKDAAAYGLGMVYQHFTLVpSLTG 109
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsNKNESEPSFEATRSRNRYSVAYAAQKPWLL-NATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 110 AENLV----ISRTEVPAVInwprERKALAAFMEHMPF--QIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVL 183
Cdd:cd03290 96 EENITfgspFNKQRYKAVT----DACSLQPDIDLLPFgdQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2790395612 184 TPAEADEML--GLVRGMTErGELTVLMISHKFHEVTKfADAVSILRRG 229
Cdd:cd03290 172 DIHLSDHLMqeGILKFLQD-DKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
18-240 |
8.10e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 50.53 E-value: 8.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKD--AAAYGLG 95
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlyTVRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 96 MVYQHFTLVPSLTGAENlvisrtevpavINWP-RERKALAAFMEHMPFQIPLD----------RPvSQLAAGEKQKLEIV 164
Cdd:PRK11831 88 MLFQSGALFTDMNVFDN-----------VAYPlREHTQLPAPLLHSTVMMKLEavglrgaaklMP-SELSGGMARRAALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790395612 165 KQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
292-497 |
1.00e-06 |
|
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: 49.50 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGeIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRRNnVRFIPEEPLqnaCAPRMSVSENLA 371
Cdd:cd03264 20 SLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRR-IGYLPQEFG---VYPNFTVREFLD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 372 FrtfdlkesgadAIWLNR---NKIKKGATALIADFKVrTASQSSPIAALSGGNVQRAVLARELTGEVDLLIVSNPCFGLD 448
Cdd:cd03264 95 Y-----------IAWLKGipsKEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2790395612 449 fsavaeIRARImRARN------AGAAVLLLSEDLDELMEMSDRIMVISEGKLVYE 497
Cdd:cd03264 163 ------PEERI-RFRNllselgEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
267-431 |
1.01e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 49.71 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 267 TAKAVLQIERI--KAPDRSGLKTIeidSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETR 344
Cdd:PRK10247 3 ENSPLLQLQNVgyLAGDAKILNNI---SFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 345 RNNVRFIPEEPLQNAcaprMSVSENLAFRtfdlkesgadaiWLNRNKiKKGATALIAD---FKVRTASQSSPIAALSGGN 421
Cdd:PRK10247 80 RQQVSYCAQTPTLFG----DTVYDNLIFP------------WQIRNQ-QPDPAIFLDDlerFALPDTILTKNIAELSGGE 142
|
170
....*....|
gi 2790395612 422 VQRAVLAREL 431
Cdd:PRK10247 143 KQRISLIRNL 152
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
292-469 |
1.07e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.42 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRRNnvrfipeepL-----QNACAPRMSV 366
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQD---------LlylghQPGIKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 367 SENLAFRTFDLKESGADAIWlnrnkikkgaTAL----IADFkvrtasQSSPIAALSGGNVQRAVLARELTGEVDLLIVSN 442
Cdd:PRK13538 92 LENLRFYQRLHGPGDDEALW----------EALaqvgLAGF------EDVPVRQLSAGQQRRVALARLWLTRAPLWILDE 155
|
170 180
....*....|....*....|....*...
gi 2790395612 443 PCFGLDFSAVAEIRARIMR-ARNAGAAV 469
Cdd:PRK13538 156 PFTAIDKQGVARLEALLAQhAEQGGMVI 183
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
298-503 |
1.18e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 51.42 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 298 GEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRRNNvrFIPEEPLqnaCAPRMSVSENLAFRTF-D 376
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKRTG--FVTQDDI---LYPHLTVRETLVFCSLlR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 377 LKESgadaiwLNRNKIKKGATALIADFKV----RTASQSSPIAALSGGNVQRAVLARELTGEVDLLIVSNPCFGLDFSAV 452
Cdd:PLN03211 169 LPKS------LTKQEKILVAESVISELGLtkceNTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAA 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2790395612 453 AEIRARIMRARNAGAA-VLLLSEDLDELMEMSDRIMVISEGKLVYETAARSA 503
Cdd:PLN03211 243 YRLVLTLGSLAQKGKTiVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDA 294
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
282-462 |
1.55e-06 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 48.89 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 282 RSGLKTIEIDSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRRnNVRFIPEeplQNACA 361
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE-NILYLGH---LPGLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 362 PRMSVSENLAFRTFDLkeSGAD-AIWlnrnkikkgatALIADFKVRTASQsSPIAALSGGNVQRAVLARELTGEVDLLIV 440
Cdd:TIGR01189 86 PELSALENLHFWAAIH--GGAQrTIE-----------DALAAVGLTGFED-LPAAQLSAGQQRRLALARLWLSRRPLWIL 151
|
170 180
....*....|....*....|..
gi 2790395612 441 SNPCFGLDFSAVAEIrARIMRA 462
Cdd:TIGR01189 152 DEPTTALDKAGVALL-AGLLRA 172
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
32-79 |
2.51e-06 |
|
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: 48.23 E-value: 2.51e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2790395612 32 ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGR 79
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS 67
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
292-497 |
3.24e-06 |
|
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: 48.20 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAyGATRPETRRNN---VR-FipeeplQN-ACAPRMSV 366
Cdd:cd03219 20 SFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGED-ITGLPPHEIARlgiGRtF------QIpRLFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 367 SENLAF-RTFDLKESGADAIWLNRNK-IKKGATALIADFKVrTASQSSPIAALSGGNVQRAVLARELTGEVDLLIVSNPC 444
Cdd:cd03219 93 LENVMVaAQARTGSGLLLARARREEReARERAEELLERVGL-ADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2790395612 445 FGLDFSAVAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLVYE 497
Cdd:cd03219 172 AGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAE 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
298-496 |
3.31e-06 |
|
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: 47.93 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 298 GEIVGIAGISGNGQKELAEILAGQRPTQA--GSVTVKGAAygaTRPETRRNNVRFIPEEplqNACAPRMSVSENLAFrtf 375
Cdd:cd03213 35 GELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRP---LDKRSFRKIIGYVPQD---DILHPTLTVRETLMF--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 376 dlkesgadaiwlnrnkikkgataliadfkvrtasqSSPIAALSGGNVQRAVLARELTGEVDLLIVSNPCFGLDfSAVAEI 455
Cdd:cd03213 106 -----------------------------------AAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLD-SSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2790395612 456 RARIMRA-RNAGAAVLLLSEDLDELM-EMSDRIMVISEGKLVY 496
Cdd:cd03213 150 VMSLLRRlADTGRTIICSIHQPSSEIfELFDKLLLLSQGRVIY 192
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
33-207 |
3.39e-06 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 47.62 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 33 LDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQ--TSGSLSVDGREVTIASPKdaaayGLGMVYQHFTLVPSLTGA 110
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLDKNFQR-----STGYVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 111 ENLVISRtevpavinWPRErkalaafmehmpfqipldrpvsqLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTPAEADE 190
Cdd:cd03232 98 EALRFSA--------LLRG-----------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
170
....*....|....*..
gi 2790395612 191 MLGLVRGMTERGeLTVL 207
Cdd:cd03232 147 IVRFLKKLADSG-QAIL 162
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
292-496 |
5.06e-06 |
|
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: 47.50 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAaYGATRPETRRNNVRFIPEEplqNACAPRMSVSENLA 371
Cdd:cd03263 22 SLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGY-SIRTDRKAARQSLGYCPQF---DALFDELTVREHLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 372 F--RtfdLKesGadaiwLNRNKIKKGATALIADFKVrTASQSSPIAALSGGNVQRAVLARELTGEVDLLIVSNPCFGLDF 449
Cdd:cd03263 98 FyaR---LK--G-----LPKSEIKEEVELLLRVLGL-TDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790395612 450 ----------SAVAEIRARIMRARNagaavlllsedldelME----MSDRIMVISEGKLVY 496
Cdd:cd03263 167 asrraiwdliLEVRKGRSIILTTHS---------------MDeaeaLCDRIAIMSDGKLRC 212
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
292-496 |
6.61e-06 |
|
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: 47.27 E-value: 6.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQ---RPTQAGSVTVKGAAygaTRPETRRNNVRFIPEeplQNACAPRMSVSE 368
Cdd:cd03234 27 SLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQP---RKPDQFQKCVAYVRQ---DDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 369 NLAFRtfdlkesgadAIWLNRNKIKKGATALIADFKVRTASQSSPIA-----ALSGGNVQRAVLARELTGEVDLLIVSNP 443
Cdd:cd03234 101 TLTYT----------AILRLPRKSSDAIRKKRVEDVLLRDLALTRIGgnlvkGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2790395612 444 CFGLD-FSA--VAEIRARImrARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLVY 496
Cdd:cd03234 171 TSGLDsFTAlnLVSTLSQL--ARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVY 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
34-229 |
7.13e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 47.11 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 34 DHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTiaspKDAAAYGLGMVY-QHFTLV-PSLTGAE 111
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRDEYHQDLLYlGHQPGIkTELTALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 112 NLVISrtevpAVINWPRERKALAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKqLYLGRSFL-VLDEPTSVLTPAEADE 190
Cdd:PRK13538 94 NLRFY-----QRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALAR-LWLTRAPLwILDEPFTAIDKQGVAR 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 2790395612 191 MLGLVRGMTERGELtVLMISHkfHEVTKFADAVSILRRG 229
Cdd:PRK13538 168 LEALLAQHAEQGGM-VILTTH--QDLPVASDKVRKLRLG 203
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
33-448 |
7.58e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 48.39 E-value: 7.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 33 LDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSlsvdgrevtiASPkdAAAYGLGMVYQHFTLVPSLTGAEN 112
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE----------ARP--QPGIKVGYLPQEPQLDPTKTVREN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 113 LVISRTEVPAVINW-----------PRERKALAAFMEHMPFQI----------------------PLDRPVSQLAAGEKQ 159
Cdd:TIGR03719 89 VEEGVAEIKDALDRfneisakyaepDADFDKLAAEQAELQEIIdaadawdldsqleiamdalrcpPWDADVTKLSGGERR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 160 KLEIVKQLYLGRSFLVLDEPTSVLtpaEADEMLGLVRGMTE-RGelTVLMISHKFHevtkFADAVS--ILR--RGKLIG- 233
Cdd:TIGR03719 169 RVALCRLLLSKPDMLLLDEPTNHL---DAESVAWLERHLQEyPG--TVVAVTHDRY----FLDNVAgwILEldRGRGIPw 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 234 ----SGKVgELSTAEMAAMMIGDVKLA-----ELD--------------TRIPVTETAKAVLQIER-------IKAPDRS 283
Cdd:TIGR03719 240 egnySSWL-EQKQKRLEQEEKEESARQktlkrELEwvrqspkgrqakskARLARYEELLSQEFQKRnetaeiyIPPGPRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 284 GLKTIEIDSLT---------------VHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSV----TVKGAAYGATRpetr 344
Cdd:TIGR03719 319 GDKVIEAENLTkafgdklliddlsfkLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIeigeTVKLAYVDQSR---- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 345 rnnvrfipeeplqNACAPRMSVSENLAfrtfdlkeSGADAIWLNRNKIKkgATALIADFKVRTASQSSPIAALSGGNVQR 424
Cdd:TIGR03719 395 -------------DALDPNKTVWEEIS--------GGLDIIKLGKREIP--SRAYVGRFNFKGSDQQKKVGQLSGGERNR 451
|
490 500
....*....|....*....|....
gi 2790395612 425 AVLARELTGEVDLLIVSNPCFGLD 448
Cdd:TIGR03719 452 VHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
34-240 |
7.59e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 47.39 E-value: 7.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 34 DHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFY----HQTSGSLSVDGREVtiaSPKDAAAYGLGMVYQH----FTlvP 105
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDGKPV---APCALRGRKIATIMQNprsaFN--P 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 106 SLTGAENLVisrtEVPAVINWPRERKALAAFMEHMPFQIP---LDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSV 182
Cdd:PRK10418 95 LHTMHTHAR----ETCLALGKPADDATLTAALEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2790395612 183 LTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGKVGEL 240
Cdd:PRK10418 171 LDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
283-514 |
8.96e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.39 E-value: 8.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 283 SGLKTIEIDSLTVHAGEIVGIAGISGNGQKELAEILAGQRP--TQAGSVTVKGAAYGATR-PETRRNNVRFIPEEPlqnA 359
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQASNiRDTERAGIAIIHQEL---A 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 360 CAPRMSVSENLaFRTFDLKESGAdaiwLNRNKIKKGATALIADFKVrTASQSSPIAALSGGNVQRAVLARELTGEVDLLI 439
Cdd:PRK13549 93 LVKELSVLENI-FLGNEITPGGI----MDYDAMYLRAQKLLAQLKL-DINPATPVGNLGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790395612 440 VSNPCFGLDFSAVAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLVYETAARSADISVIGAHMAG 514
Cdd:PRK13549 167 LDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMMVG 241
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
144-235 |
1.12e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.09 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 144 IPLDRPVSQLAAGEKQKLEIVKQLY---LGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGElTVLMISHKFHeVTKFA 220
Cdd:TIGR00630 821 IRLGQPATTLSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGN-TVVVIEHNLD-VIKTA 898
|
90 100
....*....|....*....|.
gi 2790395612 221 DAVSIL------RRGKLIGSG 235
Cdd:TIGR00630 899 DYIIDLgpeggdGGGTVVASG 919
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
292-494 |
1.16e-05 |
|
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: 46.63 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAG-QRPTqAGSVTVKGAAYGATR----PETRRN-NVRFipeepLQNACAPRMS 365
Cdd:cd03292 21 NISISAGEFVFLVGPSGAGKSTLLKLIYKeELPT-SGTIRVNGQDVSDLRgraiPYLRRKiGVVF-----QDFRLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 366 VSENLAFrtfdlkesGADAIWLNRNKIKKGATALIADFKVRTASQSSPiAALSGGNVQRAVLARELTGEVDLLIVSNPCF 445
Cdd:cd03292 95 VYENVAF--------ALEVTGVPPREIRKRVPAALELVGLSHKHRALP-AELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2790395612 446 GLDFSAVAEIrARIMRARN-AGAAVLLLSEDLDELMEMSDRIMVISEGKL 494
Cdd:cd03292 166 NLDPDTTWEI-MNLLKKINkAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
292-497 |
1.53e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 47.03 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGisGNGqkelaeilAG-----------QRPTqAGSVTVKGAAYGatrPETRRNnVRFIPEEP-LQna 359
Cdd:COG4152 21 SFTVPKGEIFGLLG--PNG--------AGktttiriilgiLAPD-SGEVLWDGEPLD---PEDRRR-IGYLPEERgLY-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 360 caPRMSVSENLAFrtF-DLKesGadaiwLNRNKIKKGATALIADFKVrTASQSSPIAALSGGNVQRAVLARELTGEVDLL 438
Cdd:COG4152 84 --PKMKVGEQLVY--LaRLK--G-----LSKAEAKRRADEWLERLGL-GDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2790395612 439 IVSNPCFGLDFSAVAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLVYE 497
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLS 210
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
292-495 |
2.05e-05 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 46.63 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAG-QRPTqAGSVTVKGAAYGATRPETRRNNVRFipeeplQN-ACAPRMSVSEN 369
Cdd:COG3842 25 SLSIEPGEFVALLGPSGCGKTTLLRMIAGfETPD-SGRILLDGRDVTGLPPEKRNVGMVF------QDyALFPHLTVAEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 370 LAFrtfDLKESGadaiwLNRNKIKKGATAL-----IADFKVRTASQsspiaaLSGGNVQRAVLARELTGEVDLLIvsnpc 444
Cdd:COG3842 98 VAF---GLRMRG-----VPKAEIRARVAELlelvgLEGLADRYPHQ------LSGGQQQRVALARALAPEPRVLL----- 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790395612 445 fgLD--FSAV---------AEIRaRIMRARNAGA---------AvlllsedldelMEMSDRIMVISEGKLV 495
Cdd:COG3842 159 --LDepLSALdaklreemrEELR-RLQRELGITFiyvthdqeeA-----------LALADRIAVMNDGRIE 215
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
32-247 |
2.08e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 46.32 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 32 ALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASpkdaaaYG-----LGMVYQHftlvPS 106
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD------YSyrsqrIRMIFQD----PS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 107 LTGAENLVISRT-EVPAVINW---PRER-KAL-------------AAFMEHMpfqipldrpvsqLAAGEKQKLEIVKQLY 168
Cdd:PRK15112 98 TSLNPRQRISQIlDFPLRLNTdlePEQReKQIietlrqvgllpdhASYYPHM------------LAPGQKQRLGLARALI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790395612 169 LGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRRGKLIGSGkvgelSTAEMAA 247
Cdd:PRK15112 166 LRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERG-----STADVLA 239
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
292-462 |
2.55e-05 |
|
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: 44.68 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRRNNVRFIPEEP-LQNacaprMSVSENL 370
Cdd:cd03228 22 SLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQDPfLFS-----GTIRENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 371 afrtfdlkesgadaiwlnrnkikkgataliadfkvrtasqsspiaaLSGGNVQRAVLARELTGEVDLLIvsnpcfgLD-- 448
Cdd:cd03228 97 ----------------------------------------------LSGGQRQRIAIARALLRDPPILI-------LDea 123
|
170
....*....|....*
gi 2790395612 449 FSAV-AEIRARIMRA 462
Cdd:cd03228 124 TSALdPETEALILEA 138
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
11-219 |
3.27e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.70 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 11 QTGKAVgIETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVtiaspkdaA 90
Cdd:PTZ00243 1305 QAGSLV-FEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREI--------G 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 91 AYGLGMVYQHFTLVPS------LTGAEN----LVISRTEVPAVINWPRERKALAAFMEHmpfqipLDRPV----SQLAAG 156
Cdd:PTZ00243 1376 AYGLRELRRQFSMIPQdpvlfdGTVRQNvdpfLEASSAEVWAALELVGLRERVASESEG------IDSRVleggSNYSVG 1449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2790395612 157 EKQKLEIVKQLY-LGRSFLVLDEPTSVLTPAEADEMLGLVrgMTERGELTVLMISHKFHEVTKF 219
Cdd:PTZ00243 1450 QRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQATV--MSAFSAYTVITIAHRLHTVAQY 1511
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
272-495 |
3.47e-05 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 45.91 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 272 LQIERIKA--PDRSGLKTIeidSLTVHAGEIVGIAGISGNGQKELAEILAG-QRPTqAGSVTVKGAAYGATRPeTRRNNV 348
Cdd:COG1118 3 IEVRNISKrfGSFTLLDDV---SLEIASGELVALLGPSGSGKTTLLRIIAGlETPD-SGRIVLNGRDLFTNLP-PRERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 349 RFIPeeplQN-ACAPRMSVSENLAFrtfdlkesGADAIWLNRNKIKKGATALIADFKV-----RTASQsspiaaLSGGNV 422
Cdd:COG1118 78 GFVF----QHyALFPHMTVAENIAF--------GLRVRPPSKAEIRARVEELLELVQLegladRYPSQ------LSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 423 QRAVLARELTGEVDLLIVSNPCFGLDFSAVAEIRARIMR------------------ArnagaavlllsedldelMEMSD 484
Cdd:COG1118 140 QRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRlhdelggttvfvthdqeeA-----------------LELAD 202
|
250
....*....|.
gi 2790395612 485 RIMVISEGKLV 495
Cdd:COG1118 203 RVVVMNQGRIE 213
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
18-77 |
4.15e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.04 E-value: 4.15e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVD 77
Cdd:PRK15064 2 LSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD 61
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
292-466 |
4.49e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 44.48 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRrnnVRFIPEeplQNACAPRMSVSENLA 371
Cdd:PRK13539 22 SFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA---CHYLGH---RNAMKPALTVAENLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 372 FrtfdlkesgadaiWLN-RNKIKKGATALIADFKVrtasqsSPIA-----ALSGGNVQRAVLARELTGEVDLLIVSNPCF 445
Cdd:PRK13539 96 F-------------WAAfLGGEELDIAAALEAVGL------APLAhlpfgYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180
....*....|....*....|.
gi 2790395612 446 GLDFSAVAEIrARIMRARNAG 466
Cdd:PRK13539 157 ALDAAAVALF-AELIRAHLAQ 176
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
15-73 |
5.11e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.65 E-value: 5.11e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2790395612 15 AVGIEtlDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGS 73
Cdd:PRK15064 319 ALEVE--NLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT 375
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
292-495 |
5.71e-05 |
|
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: 45.91 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRRNNVRFIPEEP-LQNAcaprmSVSENL 370
Cdd:COG4987 355 SLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPhLFDT-----TLRENL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 371 AFRTFDLKEsgaDAIWlnrnkikkgaTAL----IADFkVRTASQ--SSPI----AALSGGNVQRAVLARELTGEVDLLIV 440
Cdd:COG4987 430 RLARPDATD---EELW----------AALervgLGDW-LAALPDglDTWLgeggRRLSGGERRRLALARALLRDAPILLL 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2790395612 441 SNPCFGLDFSAVAEIRARIMRARnAGAAVlLLSEDLDELMEMSDRIMVISEGKLV 495
Cdd:COG4987 496 DEPTEGLDAATEQALLADLLEAL-AGRTV-LLITHRLAGLERMDRILVLEDGRIV 548
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
292-499 |
5.78e-05 |
|
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: 45.04 E-value: 5.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAG--QRPTQ-AGSVTVKG----AAYGATRPETRRNNVRFIPEEPLqNACAPRM 364
Cdd:COG0444 25 SFDVRRGETLGLVGESGSGKSTLARAILGllPPPGItSGEILFDGedllKLSEKELRKIRGREIQMIFQDPM-TSLNPVM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 365 SVSENLAfrtfdlkesgaDAIWLNRNKIKKGATALIADF--KVRTASQSSPIAA----LSGGNVQRAVLARELTGEVDLL 438
Cdd:COG0444 104 TVGDQIA-----------EPLRIHGGLSKAEARERAIELleRVGLPDPERRLDRypheLSGGMRQRVMIARALALEPKLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 439 I----VSnpcfGLDFSavaeIRARIM-------RARNAG--------AAVLllsedldelmEMSDRIMVISEGKLVyETA 499
Cdd:COG0444 173 IadepTT----ALDVT----IQAQILnllkdlqRELGLAilfithdlGVVA----------EIADRVAVMYAGRIV-EEG 233
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
292-451 |
5.95e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 44.57 E-value: 5.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRRNNVRFipeepLQNACAPRMSVSENLA 371
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLF-----QENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 372 FRTF-DLKESGAdaiwlNRNKIKKGATAL-IADFKVRTASQsspiaaLSGGNVQRAVLARELTGEVDLLIVSNPcfgldF 449
Cdd:PRK10771 94 LGLNpGLKLNAA-----QREKLHAIARQMgIEDLLARLPGQ------LSGGQRQRVALARCLVREQPILLLDEP-----F 157
|
..
gi 2790395612 450 SA 451
Cdd:PRK10771 158 SA 159
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
287-461 |
8.13e-05 |
|
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: 43.61 E-value: 8.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 287 TIEIDSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGaaygatrpetrrnNVRFIPEEP-LQNAcaprmS 365
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------SIAYVSQEPwIQNG-----T 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 366 VSENLAF-RTFDlKEsgadaiWLNRnKIKkgATALIADFKVRTASQSSPI----AALSGGNVQRAVLARELTGEVDLLIv 440
Cdd:cd03250 82 IRENILFgKPFD-EE------RYEK-VIK--ACALEPDLEILPDGDLTEIgekgINLSGGQKQRISLARAVYSDADIYL- 150
|
170 180
....*....|....*....|....
gi 2790395612 441 snpcfgLD--FSAV-AEIRARIMR 461
Cdd:cd03250 151 ------LDdpLSAVdAHVGRHIFE 168
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
292-448 |
1.26e-04 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 44.45 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRRNNVRFIPEEplqnacaprMSVSENLA 371
Cdd:PRK09536 23 DLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQD---------TSLSFEFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 372 FRT------------FDLKESGADAIWlnRNKIKKGATALIADfkvrtasqsSPIAALSGGNVQRAVLARELTGEVDLLI 439
Cdd:PRK09536 94 VRQvvemgrtphrsrFDTWTETDRAAV--ERAMERTGVAQFAD---------RPVTSLSGGERQRVLLARALAQATPVLL 162
|
....*....
gi 2790395612 440 VSNPCFGLD 448
Cdd:PRK09536 163 LDEPTASLD 171
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
292-448 |
1.40e-04 |
|
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: 42.69 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYgATRPETRRNNVRFIPEEP-LQNAcaprmSVSENL 370
Cdd:cd03247 22 SLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV-SDLEKALSSLISVLNQRPyLFDT-----TLRNNL 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790395612 371 AFRtfdlkesgadaiwlnrnkikkgataliadfkvrtasqsspiaaLSGGNVQRAVLARELTGEVDLLIVSNPCFGLD 448
Cdd:cd03247 96 GRR-------------------------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
292-497 |
1.41e-04 |
|
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: 43.43 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRpETRRNNVR------FipeeplQNAca-prM 364
Cdd:COG1127 25 SLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLS-EKELYELRrrigmlF------QGGalfdsL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 365 SVSENLAFRtfdLKESGAdaiwLNRNKIKKGATALIADFKVRTASQSSPiAALSGGNVQRAVLARELTGEVDLLIVSNPC 444
Cdd:COG1127 98 TVFENVAFP---LREHTD----LSEAEIRELVLEKLELVGLPGAADKMP-SELSGGMRKRVALARALALDPEILLYDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2790395612 445 FGLDFSAVAEIRARIMRARNA-GAAVLLLSEDLDELMEMSDRIMVISEGKLVYE 497
Cdd:COG1127 170 AGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
286-463 |
1.45e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 43.49 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 286 KTIEIDSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQaGSVTVKGAA--YGATRPETR------RNNVRFIPEEPlq 357
Cdd:PRK14258 21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRVefFNQNIYERRvnlnrlRRQVSMVHPKP-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 358 nACAPrMSVSENLAF-----------RTFDLKESGADA--IWLN-RNKIKKGATALiadfkvrtasqsspiaalSGGNVQ 423
Cdd:PRK14258 98 -NLFP-MSVYDNVAYgvkivgwrpklEIDDIVESALKDadLWDEiKHKIHKSALDL------------------SGGQQQ 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2790395612 424 RAVLARELTGEVDLLIVSNPCFGLDFSAVAEIRARIMRAR 463
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLR 197
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
282-494 |
1.47e-04 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 43.51 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 282 RSGLKTI--EIDsLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRrnnVRFipeeplQNA 359
Cdd:PRK11247 21 RYGERTVlnQLD-LHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR---LMF------QDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 360 -CAPRMSVSENLAFrtfdlkesGADAIWLNRnkikkgatALIADFKVRTASQSS--PiAALSGGNVQRAVLARELTGEVD 436
Cdd:PRK11247 91 rLLPWKKVIDNVGL--------GLKGQWRDA--------ALQALAAVGLADRANewP-AALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2790395612 437 LLIVSNPCFGLDFSAVAEIRARIMRA-RNAGAAVLLLSEDLDELMEMSDRIMVISEGKL 494
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
292-461 |
1.49e-04 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 43.42 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRpeTRRNNVRFIPEEPLQnacapRMSVSENLA 371
Cdd:PRK10619 25 SLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVR--DKDGQLKVADKNQLR-----LLRTRLTMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 372 FRTFDL----------KESGADAIWLNRNKIKKGATALIADFKVRTASQSSPIAALSGGNVQRAVLARELTGEVDLLIVS 441
Cdd:PRK10619 98 FQHFNLwshmtvlenvMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFD 177
|
170 180
....*....|....*....|
gi 2790395612 442 NPCFGLDFSAVAEIrARIMR 461
Cdd:PRK10619 178 EPTSALDPELVGEV-LRIMQ 196
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
293-504 |
1.50e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 43.46 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 293 LTVHAGEIVGIAGISGNGQKELAEILAGqrptqagsvTVKGAAYGATRPETRRNNV-------RFIPEEPLQNAC----- 360
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRHLSG---------LITGDKSAGSHIELLGRTVqregrlaRDIRKSRANTGYifqqf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 361 --APRMSVSENLAFRTFDLKESGADAI-WLNRNKIKKGATALIADFKVRTASQSspIAALSGGNVQRAVLARELTGEVDL 437
Cdd:PRK09984 96 nlVNRLSVLENVLIGALGSTPFWRTCFsWFTREQKQRALQALTRVGMVHFAHQR--VSTLSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790395612 438 LIVSNPCFGLDFSAvAEIRARIMR--ARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLVYETAARSAD 504
Cdd:PRK09984 174 ILADEPIASLDPES-ARIVMDTLRdiNQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFD 241
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-181 |
1.50e-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: 44.55 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 2 SVIRDTPLPQTGKAVGIETLDMTMRFGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGrev 81
Cdd:TIGR00957 623 SIERRTIKPGEGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 82 tiaspkdAAAYglgmVYQHfTLVPSLTGAENLVISRTEVPAVINWPRERKALAAFMEHMPF--QIPLDRPVSQLAAGEKQ 159
Cdd:TIGR00957 700 -------SVAY----VPQQ-AWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSgdRTEIGEKGVNLSGGQKQ 767
|
170 180
....*....|....*....|..
gi 2790395612 160 KLEIVKQLYLGRSFLVLDEPTS 181
Cdd:TIGR00957 768 RVSLARAVYSNADIYLFDDPLS 789
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
129-488 |
1.70e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 44.39 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 129 ERKALAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGElTVLM 208
Cdd:COG1245 189 ERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGK-YVLV 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 209 ISHKFHEVTKFADAVSILrRGKLIGSGKV-GELST-------------AEmaAMMIGDVKLaELDTRIPVTETAKAVLqi 274
Cdd:COG1245 268 VEHDLAILDYLADYVHIL-YGEPGVYGVVsKPKSVrvginqyldgylpEE--NVRIRDEPI-EFEVHAPRREKEEETL-- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 275 erIKAPDRSglKT-----IEIDSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSV--TVKgAAYgatRPETRRNN 347
Cdd:COG1245 342 --VEYPDLT--KSyggfsLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVdeDLK-ISY---KPQYISPD 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 348 VRFIPEEPLQNACAPRMSVS--ENLAFRTFDLKEsgadaiwlnrnkikkgatalIADFKVRTasqsspiaaLSGGNVQRA 425
Cdd:COG1245 414 YDGTVEEFLRSANTDDFGSSyyKTEIIKPLGLEK--------------------LLDKNVKD---------LSGGELQRV 464
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790395612 426 VLARELTGEVDLLIVSNPCFGLDFS---AVAEIRARIMRARNAGAAVlllSEDLDELMEM-SDRIMV 488
Cdd:COG1245 465 AIAACLSRDADLYLLDEPSAHLDVEqrlAVAKAIRRFAENRGKTAMV---VDHDIYLIDYiSDRLMV 528
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
40-185 |
1.73e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 42.91 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 40 IPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASPKDAAAYgLGmvyqHF-TLVPSLTGAENL-VISR 117
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAY-LG----HLpGLKADLSTLENLhFLCG 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790395612 118 TEVPAVINWPRERKALAAFMEHMpfqiplDRPVSQLAAGEKQKLEIVkQLYLGRSFL-VLDEPTSVLTP 185
Cdd:PRK13543 109 LHGRRAKQMPGSALAIVGLAGYE------DTLVRQLSAGQKKRLALA-RLWLSPAPLwLLDEPYANLDL 170
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
284-495 |
1.84e-04 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 43.08 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 284 GLKTIEID-SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRRNNVRFIPEEPLqnacap 362
Cdd:PRK11231 13 GTKRILNDlSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHL------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 363 rmsVSENLAFRtfDLKESGAD---AIW--LNRNKIKKGATAL----IADFKVRtasqssPIAALSGGNVQRAVLARELTG 433
Cdd:PRK11231 87 ---TPEGITVR--ELVAYGRSpwlSLWgrLSAEDNARVNQAMeqtrINHLADR------RLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790395612 434 EVDLLIVSNPCFGLDFSAVAEIrARIMRARNA-GAAVLLLSEDLDELMEMSDRIMVISEGKLV 495
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVEL-MRLMRELNTqGKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
50-211 |
2.14e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.59 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 50 GENGAGKSTLVKCI-MGFYHQTSGSLSVDGREVTIASPKDAAAYglgmVYQHFtlvpSLTGAENLVISRTevPAVINWpr 128
Cdd:cd03240 29 GQNGAGKTTIIEALkYALTGELPPNSKGGAHDPKLIREGEVRAQ----VKLAF----ENANGKKYTITRS--LAILEN-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 129 erkalAAFMEHMPFQIPLDRPVSQLAAGEKQKLEIVKQLYLGRSF------LVLDEPTSVLTPAEADEML-GLVRGMTER 201
Cdd:cd03240 97 -----VIFCHQGESNWPLLDMRGRCSGGEKVLASLIIRLALAETFgsncgiLALDEPTTNLDEENIEESLaEIIEERKSQ 171
|
170
....*....|
gi 2790395612 202 GELTVLMISH 211
Cdd:cd03240 172 KNFQLIVITH 181
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
43-241 |
2.31e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.07 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 43 GSFHALLGENGAGKSTLVKCIMGfyHQTSGSLSVDGREVTIASPKDAAAYGLGMVYQHFTLVPSLTGAENLVISrtevpA 122
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIRISGFPKKQETFARISGYCEQNDIHSPQVTVRESLIYS-----A 978
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 123 VINWPRE--RKALAAFMEHMPFQIPLDR---------PVSQLAAGEKQKLEIVKQLYLGRSFLVLDEPTSVLTPAEADEM 191
Cdd:PLN03140 979 FLRLPKEvsKEEKMMFVDEVMELVELDNlkdaivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIV 1058
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2790395612 192 LGLVRGMTERGELTVLMISHKFHEVTKFADAVSILRR-GKLIGSGKVGELS 241
Cdd:PLN03140 1059 MRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRgGQVIYSGPLGRNS 1109
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
293-448 |
2.35e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 42.84 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 293 LTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGA----TRPETRRNNVRFIPEEPLqnaCAPRMSVSE 368
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeeARAKLRAKHVGFVFQSFM---LIPTLNALE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 369 NLAFRTFDLKESGADAiwlnrnkiKKGATALIADFKVRTASQSSPiAALSGGNVQRAVLARELTGEVDLLIVSNPCFGLD 448
Cdd:PRK10584 108 NVELPALLRGESSRQS--------RNGAKALLEQLGLGKRLDHLP-AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
292-448 |
2.38e-04 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 42.88 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAY----GATRPETRRNNVRFIPEeplQNACAPRMSVS 367
Cdd:PRK11629 29 SFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklsSAAKAELRNQKLGFIYQ---FHHLLPDFTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 368 ENLAFRTFDLKEsgadaiwlNRNKIKKGATALIADFKVRTASQSSPiAALSGGNVQRAVLARELTGEVDLLIVSNPCFGL 447
Cdd:PRK11629 106 ENVAMPLLIGKK--------KPAEINSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
.
gi 2790395612 448 D 448
Cdd:PRK11629 177 D 177
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
292-448 |
2.97e-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: 43.78 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAaygatrpetrrnnVRFIPEEP-LQNAcaprmSVSENL 370
Cdd:TIGR00957 658 TFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAwIQND-----SLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 371 AFrtfdlkesgADAIWLNRNKIKKGATALIADFKVRTASQSSPIAA----LSGGNVQRAVLARELTGEVDLLIVSNPCFG 446
Cdd:TIGR00957 720 LF---------GKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSA 790
|
..
gi 2790395612 447 LD 448
Cdd:TIGR00957 791 VD 792
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
280-494 |
3.47e-04 |
|
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: 42.07 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 280 PDRSGLKTIeidSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRRNNVRFIPEEPLQNA 359
Cdd:cd03248 25 PDTLVLQDV---SFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 360 CAPRMSVSENLAFRTFDLKESGADaiwlnrnkiKKGATALIADFKVRTASQSSPIAA-LSGGNVQRAVLARELTGEVDLL 438
Cdd:cd03248 102 RSLQDNIAYGLQSCSFECVKEAAQ---------KAHAHSFISELASGYDTEVGEKGSqLSGGQKQRVAIARALIRNPQVL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2790395612 439 IVSNPCFGLDfsavAEIRARIMRARNAGAAVLLLSEDL--DELMEMSDRIMVISEGKL 494
Cdd:cd03248 173 ILDEATSALD----AESEQQVQQALYDWPERRTVLVIAhrLSTVERADQILVLDGGRI 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
281-495 |
4.99e-04 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 41.92 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 281 DRSGLKTIEIDsLTVHAgeIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAA--YGATRPETRRNNVRFIPEEPLQN 358
Cdd:PRK13638 13 DEPVLKGLNLD-FSLSP--VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPldYSKRGLLALRQQVATVFQDPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 359 ACapRMSVSENLAFrtfDLKESGADAIWLNRnKIKKGATALIADfkvrtASQSSPIAALSGGNVQRAVLARELTGEVDLL 438
Cdd:PRK13638 90 IF--YTDIDSDIAF---SLRNLGVPEAEITR-RVDEALTLVDAQ-----HFRHQPIQCLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2790395612 439 IVSNPCFGLDFSAVAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLV 495
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQIL 215
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
292-335 |
5.44e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.57 E-value: 5.44e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAA 335
Cdd:PRK13545 44 SFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA 87
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
28-323 |
5.79e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.31 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 28 GSFTALDHVSVSIP-----AGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSVDGREVTIASpkdaaayglgmvyqhFT 102
Cdd:PRK10938 9 GTFRLSDTKTLQLPsltlnAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLS---------------FE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 103 LVPSLTGAE-----NLVISRTE------VPAVINWPRERKALAAFMEhMPFQIP--LDRPVSQLAAGEKQKLEIVKQLYL 169
Cdd:PRK10938 74 QLQKLVSDEwqrnnTDMLSPGEddtgrtTAEIIQDEVKDPARCEQLA-QQFGITalLDRRFKYLSTGETRKTLLCQALMS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 170 GRSFLVLDEPTSVLTPAEADEMLGLVRGMTERGeLTVLMISHKFHEVTKFADAVSILRRGKLIGSGK---------VGEL 240
Cdd:PRK10938 153 EPDLLILDEPFDGLDVASRQQLAELLASLHQSG-ITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEreeilqqalVAQL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 241 STAEMAAmmigDVKLAELD-----TRIPvTETAKAVLQIERIKAPDRSGLKTIeidSLTVHAGEIVGIAGISGNGQKELA 315
Cdd:PRK10938 232 AHSEQLE----GVQLPEPDepsarHALP-ANEPRIVLNNGVVSYNDRPILHNL---SWQVNPGEHWQIVGPNGAGKSTLL 303
|
....*...
gi 2790395612 316 EILAGQRP 323
Cdd:PRK10938 304 SLITGDHP 311
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
292-495 |
6.54e-04 |
|
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: 41.48 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKG-----AAYGATRpETRRNNVRFIpeepLQN-ACAPRMS 365
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaaMSRKELR-ELRRKKISMV----FQSfALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 366 VSENLAFrtfDLKESGADAiwlnRNKIKKGATAL----IADFKVRTASQsspiaaLSGGNVQRAVLARELTGEVDLLIVS 441
Cdd:cd03294 119 VLENVAF---GLEVQGVPR----AEREERAAEALelvgLEGWEHKYPDE------LSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 442 NPcfgldFSAVAEIRARIMR------ARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLV 495
Cdd:cd03294 186 EA-----FSALDPLIRREMQdellrlQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
292-493 |
6.62e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 41.51 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAG-QRPTqAGSVTVKG-----------AAYGATRPetrRNNVRFIPEeplqna 359
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGfYKPT-GGTILLRGqhieglpghqiARMGVVRT---FQHVRLFRE------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 360 caprMSVSENLA---------------FRTFDLKESGADAI-----WLNRNKIKkgataliaDFKVRTASQsspiaaLSG 419
Cdd:PRK11300 95 ----MTVIENLLvaqhqqlktglfsglLKTPAFRRAESEALdraatWLERVGLL--------EHANRQAGN------LAY 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2790395612 420 GNVQRAVLARELTGEVDLLIVSNPCFGLDFSAVAEIRARIMRARNA-GAAVLLLSEDLDELMEMSDRIMVISEGK 493
Cdd:PRK11300 157 GQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
281-495 |
7.43e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 41.94 E-value: 7.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 281 DRSGLKT-IEIDSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYG----ATRPETRRNNVRFIPEep 355
Cdd:PRK10070 36 EKTGLSLgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdAELREVRRKKIAMVFQ-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 356 lQNACAPRMSVSENLAFrtfdlkesGADAIWLNRNKIKKGATALIADFKVRTASQSSPiAALSGGNVQRAVLARELTGEV 435
Cdd:PRK10070 114 -SFALMPHMTVLDNTAF--------GMELAGINAEERREKALDALRQVGLENYAHSYP-DELSGGMRQRVGLARALAINP 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2790395612 436 DLLIVSNPCFGLDFSAVAEIRARIMRAR-NAGAAVLLLSEDLDELMEMSDRIMVISEGKLV 495
Cdd:PRK10070 184 DILLMDEAFSALDPLIRTEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
27-92 |
9.21e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 40.56 E-value: 9.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790395612 27 FGSFtalDHVSVSIPAGSFhALLGENGAGKSTLVKCI-MGFYHQTSGSLSVDGR-----EVTIASPKDAAAY 92
Cdd:pfam13476 6 FRSF---RDQTIDFSKGLT-LITGPNGSGKTTILDAIkLALYGKTSRLKRKSGGgfvkgDIRIGLEGKGKAY 73
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
292-448 |
1.22e-03 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 40.90 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKG---AAYGATRPETRRNNVRFIPEeplQNACAPRMSVSE 368
Cdd:PRK11831 27 SLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGeniPAMSRSRLYTVRKRMSMLFQ---SGALFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 369 NLAFrtfDLKESGA--DAIWLNRNKIKKGATALiadfkvRTASQSSPiAALSGGNVQRAVLARELTGEVDLLIVSNPCFG 446
Cdd:PRK11831 104 NVAY---PLREHTQlpAPLLHSTVMMKLEAVGL------RGAAKLMP-SELSGGMARRAALARAIALEPDLIMFDEPFVG 173
|
..
gi 2790395612 447 LD 448
Cdd:PRK11831 174 QD 175
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
292-495 |
1.23e-03 |
|
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: 41.27 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRRNNVRFIPEEP-LQNAcaprmSVSENL 370
Cdd:COG4618 352 SFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVeLFDG-----TIAENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 371 AfRtFDlkesGADAiwlnrNKIKK-----GATALIA------DFKVRTASqsspiAALSGGNVQRAVLARELTGEVDLLI 439
Cdd:COG4618 427 A-R-FG----DADP-----EKVVAaaklaGVHEMILrlpdgyDTRIGEGG-----ARLSGGQRQRIGLARALYGDPRLVV 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 440 V----SNpcfgLDFSAVAEIRARIMRARNAGAAVlLLSEDLDELMEMSDRIMVISEGKLV 495
Cdd:COG4618 491 LdepnSN----LDDEGEAALAAAIRALKARGATV-VVITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
293-494 |
1.29e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 41.17 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 293 LTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKgaaygatrpETRRNNVrfipeEPLQN---------ACAPR 363
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIG---------EKRMNDV-----PPAERgvgmvfqsyALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 364 MSVSENLAFrtfDLKESGADaiwlnRNKIKKgataliadfKVRTASQSSPIA--------ALSGGNVQRAVLARELTGEV 435
Cdd:PRK11000 90 LSVAENMSF---GLKLAGAK-----KEEINQ---------RVNQVAEVLQLAhlldrkpkALSGGQRQRVAIGRTLVAEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 436 DLLIVSNPCFGLDFSAVAEIRARIMRA-RNAGAAVLLLSEDLDELMEMSDRIMVISEGKL 494
Cdd:PRK11000 153 SVFLLDEPLSNLDAALRVQMRIEISRLhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
417-495 |
1.31e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 40.99 E-value: 1.31e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2790395612 417 LSGGNVQRAVLARELTGEVDLLIVSNPCFGLDFSAVAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLV 495
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
292-351 |
1.35e-03 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 40.21 E-value: 1.35e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKG------AAYGATRPE-TRRNNVRFI 351
Cdd:cd03220 42 SFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvssllGLGGGFNPElTGRENIYLN 108
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
290-502 |
1.61e-03 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 40.12 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 290 IDsLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETR--------RNNVRFIpeepLQN-AC 360
Cdd:PRK11264 22 ID-LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQqkglirqlRQHVGFV----FQNfNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 361 APRMSVSENLAFRTFDLK-ESGADAIWLNRnkikkgatALIADFKVRTASQSSPiAALSGGNVQRAVLARELTGEVDLLI 439
Cdd:PRK11264 97 FPHRTVLENIIEGPVIVKgEPKEEATARAR--------ELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2790395612 440 VSNPCFGLDFSAVAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLVYETAARS 502
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKA 230
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
146-223 |
2.03e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 39.93 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 146 LDRPVSQLAAGEKQKLEIVKQLYLGRSFL--VLDEPTSVLTPAEADEMLGLVRGMTERGElTVLMISHKfHEVTKFADAV 223
Cdd:cd03270 131 LSRSAPTLSGGEAQRIRLATQIGSGLTGVlyVLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHD-EDTIRAADHV 208
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
292-465 |
2.21e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 40.60 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQaGSVTVKGAAYGATRPETRRNNVRFIPEEPLqnacAPRMSVSENLA 371
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESWRKHLSWVGQNPQ----LPHGTLRDNVL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 372 FRTFDLKEsgaDAIWLNRNKikkgatALIADFkVRTASQ--SSPI----AALSGGNVQRAVLARELTGEVDLLIVSNPCF 445
Cdd:PRK11174 445 LGNPDASD---EQLQQALEN------AWVSEF-LPLLPQglDTPIgdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTA 514
|
170 180
....*....|....*....|
gi 2790395612 446 GLDfsAVAEirARIMRARNA 465
Cdd:PRK11174 515 SLD--AHSE--QLVMQALNA 530
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
292-495 |
2.22e-03 |
|
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: 40.59 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRRNNVRFIPEEP-LQNAcaprmSVSENL 370
Cdd:COG2274 495 SLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVfLFSG-----TIRENI 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 371 AFrtfdlkesGADAIwlNRNKIKKGA-TALIADFKVRTASQ-SSPI----AALSGGNVQRAVLARELTGEVDLLIVSNPC 444
Cdd:COG2274 570 TL--------GDPDA--TDEEIIEAArLAGLHDFIEALPMGyDTVVgeggSNLSGGQRQRLAIARALLRNPRILILDEAT 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790395612 445 FGLDFSAVAEIRARIMRA-----------RNAgaavlllsedldeLMEMSDRIMVISEGKLV 495
Cdd:COG2274 640 SALDAETEAIILENLRRLlkgrtviiiahRLS-------------TIRLADRIIVLDKGRIV 688
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
298-496 |
2.51e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 40.42 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 298 GEIVGIAGISGNGQKELAEILAGQRPT---QAGSVTVKGAAygATRPETRRNNVrFIPEEPLqnaCAPRMSVSENLAFR- 373
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMP--IDAKEMRAISA-YVQQDDL---FIPTLTVREHLMFQa 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 374 TFDLKESGADAIWLNRNKikkgatALIADFKVRTASQS-----SPIAALSGGNVQRAVLARELTGEVDLLIVSNPCFGLD 448
Cdd:TIGR00955 125 HLRMPRRVTKKEKRERVD------EVLQALGLRKCANTrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2790395612 449 -FSAVAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLVY 496
Cdd:TIGR00955 199 sFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAY 247
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
271-497 |
2.55e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 39.72 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 271 VLQIERIKAPDRSGLKTIEIDSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPETRRNNVRF 350
Cdd:PRK13647 4 IIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 351 IPEEPLQNACAprMSVSENLAFrtfdlkesGADAIWLNRNKIKKGA-TALIA----DFKVRtasqssPIAALSGGNVQRA 425
Cdd:PRK13647 84 VFQDPDDQVFS--STVWDDVAF--------GPVNMGLDKDEVERRVeEALKAvrmwDFRDK------PPYHLSYGQKKRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790395612 426 VLARELTGEVDLLIVSNPCFGLDFSAVAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLVYE 497
Cdd:PRK13647 148 AIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAE 219
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
289-495 |
3.56e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 39.33 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 289 EIDsLTVHAGEIVGIAGISGNGQKELAEILAGQ-RPTQaGSVTVKGAAYGAT------RPETRRNNVRF-IPEEPLQNAc 360
Cdd:PRK13643 24 DID-LEVKKGSYTALIGHTGSGKSTLLQHLNGLlQPTE-GKVTVGDIVVSSTskqkeiKPVRKKVGVVFqFPESQLFEE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 361 aprmSVSENLAF--RTFDLKESGADAIWLNRNKIkkgaTALIADFkvrtaSQSSPIAaLSGGNVQRAVLARELTGEVDLL 438
Cdd:PRK13643 101 ----TVLKDVAFgpQNFGIPKEKAEKIAAEKLEM----VGLADEF-----WEKSPFE-LSGGQMRRVAIAGILAMEPEVL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2790395612 439 IVSNPCFGLDFSAVAEIRARIMRARNAGAAVLLLSEDLDELMEMSDRIMVISEGKLV 495
Cdd:PRK13643 167 VLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
33-74 |
4.70e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 39.76 E-value: 4.70e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2790395612 33 LDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSL 74
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV 717
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
277-494 |
4.84e-03 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 40.00 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 277 IKAPDRSGLKTIEIDSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYgATRPETRRNNVRFIPEepl 356
Cdd:TIGR01257 935 VKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQ--- 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 357 QNACAPRMSVSENLAFRTfDLKESGADAIWLNRNkikkgatALIADFKVRtASQSSPIAALSGGNVQRAVLARELTGEVD 436
Cdd:TIGR01257 1011 HNILFHHLTVAEHILFYA-QLKGRSWEEAQLEME-------AMLEDTGLH-HKRNEEAQDLSGGMQRKLSVAIAFVGDAK 1081
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2790395612 437 LLIVSNPCFGLDFSAVAEIRARIMRARnAGAAVLLLSEDLDELMEMSDRIMVISEGKL 494
Cdd:TIGR01257 1082 VVVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
292-461 |
5.36e-03 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 38.54 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPetrrnNVRFIPEEP----LQNACAPRMSVS 367
Cdd:PRK09493 21 DLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKV-----DERLIRQEAgmvfQQFYLFPHLTAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 368 ENLAFRTFDLKESG-ADAiwlnrnkiKKGATALIAdfKVRTASQSSPIAA-LSGGNVQRAVLARELTGEVDLLIVSNPCF 445
Cdd:PRK09493 96 ENVMFGPLRVRGASkEEA--------EKQARELLA--KVGLAERAHHYPSeLSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170
....*....|....*.
gi 2790395612 446 GLDfsavAEIRARIMR 461
Cdd:PRK09493 166 ALD----PELRHEVLK 177
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
266-495 |
5.54e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 38.87 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 266 ETAKAVLQIERIK--APDRSGLKTIEIdslTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSVTVKGAAYGATRPET 343
Cdd:PRK14246 5 KSAEDVFNISRLYlyINDKAILKDITI---KIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 344 RRNNVRFIPEEPL---QNACAPRMSVSENLAFrtfDLKESGADaiwlNRNKIKK---GATALIADFKVRTASQSSPIAAL 417
Cdd:PRK14246 82 QIDAIKLRKEVGMvfqQPNPFPHLSIYDNIAY---PLKSHGIK----EKREIKKiveECLRKVGLWKEVYDRLNSPASQL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2790395612 418 SGGNVQRAVLARELTGEVDLLIVSNPCFGLDFSAVAEIRARIMRARNAgAAVLLLSEDLDELMEMSDRIMVISEGKLV 495
Cdd:PRK14246 155 SGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
292-497 |
6.15e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 39.57 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 292 SLTVHAGEIVGIAGISGNGQKELAEILAGQ-RPTQAGSVTVKGAaygatrpetrrnnVRFIPEEP-LQNAcaprmSVSEN 369
Cdd:PLN03232 637 NLEIPVGSLVAIVGGTGEGKTSLISAMLGElSHAETSSVVIRGS-------------VAYVPQVSwIFNA-----TVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 370 LAFRTFDLKESGADAIwlnrnkikkGATALIADFKVRTASQSSPIAA----LSGGNVQRAVLARELTGEVDLLIVSNPCF 445
Cdd:PLN03232 699 ILFGSDFESERYWRAI---------DVTALQHDLDLLPGRDLTEIGErgvnISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2790395612 446 GLDFSAVAEIRARIMRARNAGAAvLLLSEDLDELMEMSDRIMVISEGKLVYE 497
Cdd:PLN03232 770 ALDAHVAHQVFDSCMKDELKGKT-RVLVTNQLHFLPLMDRIILVSEGMIKEE 820
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
281-495 |
6.47e-03 |
|
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: 38.32 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 281 DRSGLKTIEIDsltVHAGEIVGIAGISGNGQKELAEILAG------QRPTqAGSVTVKGAAYGA--TRPETRRNNVRFIp 352
Cdd:cd03260 12 DKHALKDISLD---IPKGEITALIGPSGCGKSTLLRLLNRlndlipGAPD-EGEVLLDGKDIYDldVDVLELRRRVGMV- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 353 eepLQNACAPRMSVSENLAFrtfdlkesgadAIWLNRNKIKKGATALIADFKVRTA-----SQSSPIAALSGGNVQRAVL 427
Cdd:cd03260 87 ---FQKPNPFPGSIYDNVAY-----------GLRLHGIKLKEELDERVEEALRKAAlwdevKDRLHALGLSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2790395612 428 ARELTGEVDLLIVSNPCFGLDFSAVAEIRARIMRARNAGAAVlllseDLDELME----MSDRIMVISEGKLV 495
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIV-----IVTHNMQqaarVADRTAFLLNGRLV 219
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
27-76 |
7.07e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.00 E-value: 7.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2790395612 27 FGSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHQTSGSLSV 76
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL 371
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
286-459 |
7.86e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 38.84 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 286 KTIEIDSLTVHAGEIVGIAGISGNGQKELAEILAGQRPTQAGSvtvkgaaygatrpetRRNNVRFIPE---EPLQNAcap 362
Cdd:PRK10938 17 KTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE---------------RQSQFSHITRlsfEQLQKL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 363 rmsVSENLAFRTFDLKESGAD-------AIWLNRNKIKKGATALIADFKVrTASQSSPIAALSGGNVQRAVLARELTGEV 435
Cdd:PRK10938 79 ---VSDEWQRNNTDMLSPGEDdtgrttaEIIQDEVKDPARCEQLAQQFGI-TALLDRRFKYLSTGETRKTLLCQALMSEP 154
|
170 180
....*....|....*....|....
gi 2790395612 436 DLLIVSNPCFGLDFSAVAEIRARI 459
Cdd:PRK10938 155 DLLILDEPFDGLDVASRQQLAELL 178
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
18-185 |
8.26e-03 |
|
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: 38.30 E-value: 8.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 18 IETLDMTMRF--GSFTALDHVSVSIPAGSFHALLGENGAGKSTLVKCIMGFYHqTSGSLSVDG---REVTIASPKDAaay 92
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGvswNSVPLQKWRKA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790395612 93 gLGMVYQHfTLVPSLTGAENL----VISRTEVPAVInwprERKALAAFMEHMPFQIP--LDRPVSQLAAGEKQKLEIVKQ 166
Cdd:cd03289 79 -FGVIPQK-VFIFSGTFRKNLdpygKWSDEEIWKVA----EEVGLKSVIEQFPGQLDfvLVDGGCVLSHGHKQLMCLARS 152
|
170
....*....|....*....
gi 2790395612 167 LYLGRSFLVLDEPTSVLTP 185
Cdd:cd03289 153 VLSKAKILLLDEPSAHLDP 171
|
|
| |
