|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-510 |
0e+00 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 1030.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL 80
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 81 GIGIIYQELSVIDELTVLENLYIGRHLTKKICGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
Cdd:PRK09700 81 GIGIIYQELSVIDELTVLENLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRL 240
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 241 MVGRELQNRFNAMKENVSNLAHETVFEVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEI 320
Cdd:PRK09700 241 MVGRELQNRFNAMKENVSNLAHETVFEVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 321 RLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKC 400
Cdd:PRK09700 321 RLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKC 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 401 HSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIA 480
Cdd:PRK09700 401 HSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIA 480
|
490 500 510
....*....|....*....|....*....|
gi 16131913 481 VFCEGRLTQILTNRDDMSEEEIMAWALPQE 510
Cdd:PRK09700 481 VFCEGRLTQILTNRDDMSEEEIMAWALPQE 510
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-507 |
0e+00 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 729.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLG 81
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 82 IGIIYQELSVIDELTVLENLYIGRHLTKKicgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREPRRG----GLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRLM 241
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 242 VGRELQNRFNAMKENvsnlAHETVFEVRNVTSRDRkkVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIR 321
Cdd:COG1129 237 VGRELEDLFPKRAAA----PGEVVLEVEGLSVGGV--VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 322 LNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISrSLKDGgykGAMGLFHEVDEQRTAENQRELLALKCH 401
Cdd:COG1129 311 LDGKPVRIRSPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLA-SLDRL---SRGGLLDRRRERALAEEYIKRLRIKTP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 402 SVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAV 481
Cdd:COG1129 387 SPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILV 466
|
490 500
....*....|....*....|....*.
gi 16131913 482 FCEGRLTQILTnRDDMSEEEIMAWAL 507
Cdd:COG1129 467 MREGRIVGELD-REEATEEAIMAAAT 491
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-504 |
3.95e-180 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 514.96 E-value: 3.95e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL 80
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 81 GIGIIYQELSVIDELTVLENLYIGRHLTKKIcgvnIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIVLGLEPTKGG----RLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRL 240
Cdd:COG3845 157 YRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 241 MVGRELqnRFNAMKENVSnlAHETVFEVRNVTSRDRK---KVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAG 317
Cdd:COG3845 237 MVGREV--LLRVEKAPAE--PGEVVLEVENLSVRDDRgvpALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPAS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 318 GEIRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSLKDGGYKGAMglfheVDEQRTAENQRELLA 397
Cdd:COG3845 313 GSIRLDGEDITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGRYRRPPFSRGGF-----LDRKAIRAFAEELIE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 398 ---LKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIIT 474
Cdd:COG3845 388 efdVRTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILA 467
|
490 500 510
....*....|....*....|....*....|...
gi 16131913 475 VCDRIAVFCEGRLTQILtNRDDMSEEEI---MA 504
Cdd:COG3845 468 LSDRIAVMYEGRIVGEV-PAAEATREEIgllMA 499
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-510 |
4.11e-176 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 504.85 E-value: 4.11e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGI--HEPTKGTITINnisynklDHKLAA 78
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFE-------GEELQA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 79 -------QLGIGIIYQELSVIDELTVLENLYIGRHLTKKicgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHK 151
Cdd:PRK13549 74 snirdteRAGIAIIHQELALVKELSVLENIFLGNEITPG----GIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 152 QMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSD 231
Cdd:PRK13549 150 QLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 232 VSNDDIVRLMVGRELQNRFNAMKENVSnlahETVFEVRNVTSRD-----RKKVRDISFSVCRGEILGFAGLVGSGRTELM 306
Cdd:PRK13549 230 MTEDDIITMMVGRELTALYPREPHTIG----EVILEVRNLTAWDpvnphIKRVDDVSFSLRRGEILGIAGLVGAGRTELV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 307 NCLFGVDK-RAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISrSLKDggYKGaMGLFHEVDE 385
Cdd:PRK13549 306 QCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLA-ALDR--FTG-GSRIDDAAE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 386 QRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMV 465
Cdd:PRK13549 382 LKTILESIQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVI 461
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 16131913 466 SSELPEIITVCDRIAVFCEGRLTQILTNrDDMSEEEIMAWALPQE 510
Cdd:PRK13549 462 SSELPEVLGLSDRVLVMHEGKLKGDLIN-HNLTQEQVMEAALRSE 505
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-509 |
1.15e-175 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 503.67 E-value: 1.15e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLG 81
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 82 IGIIYQELSVIDELTVLENLYIGRHLTKkicgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLYLGQLPHK----GGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCS-GIVSDVSNDDIVRL 240
Cdd:PRK11288 157 RNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATfDDMAQVDRDQLVQA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 241 MVGRELQNRFNAMKENVSnlahETVFEVRNVTSRdrkKVR-DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGE 319
Cdd:PRK11288 237 MVGREIGDIYGYRPRPLG----EVRLRLDGLKGP---GLRePISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 320 IRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAIS---RSLKDGgykgamGLFHEVDEQRTAENQRELL 396
Cdd:PRK11288 310 VYLDGKPIDIRSPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINISarrHHLRAG------CLINNRWEAENADRFIRSL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 397 ALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVC 476
Cdd:PRK11288 384 NIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVA 463
|
490 500 510
....*....|....*....|....*....|...
gi 16131913 477 DRIAVFCEGRLTQILTnRDDMSEEEIMAWALPQ 509
Cdd:PRK11288 464 DRIVVMREGRIAGELA-REQATERQALSLALPR 495
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
8-503 |
8.30e-164 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 473.51 E-value: 8.30e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 8 MAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHePT---KGTITINNISYNKLDHKLAAQLGIGI 84
Cdd:NF040905 4 MRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCRFKDIRDSEALGIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 85 IYQELSVIDELTVLENLYIGRHLTKKicgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
Cdd:NF040905 83 IHQELALIPYLSIAENIFLGNERAKR----GVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVS--DVSNDDIVRLMV 242
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRadEVTEDRIIRGMV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 243 GRELQNRFNAMKENVSnlahETVFEVRNVT-----SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFG--VDKR 315
Cdd:NF040905 239 GRDLEDRYPERTPKIG----EVVFEVKNWTvyhplHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrsYGRN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 316 AGGEIRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNM------AISRSlkdggykgamGLFHEVDEQRTA 389
Cdd:NF040905 315 ISGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNItlanlgKVSRR----------GVIDENEEIKVA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 390 ENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSEL 469
Cdd:NF040905 385 EEYRKKMNIKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSEL 464
|
490 500 510
....*....|....*....|....*....|....
gi 16131913 470 PEIITVCDRIAVFCEGRLTQILTnRDDMSEEEIM 503
Cdd:NF040905 465 PELLGMCDRIYVMNEGRITGELP-REEASQERIM 497
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-507 |
3.59e-163 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 471.80 E-value: 3.59e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 3 TPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLGI 82
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 83 GIIYQELSVIDELTVLENLYIGRHLTKKICGvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIFLGREFVNRFGR---IDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRLMV 242
Cdd:PRK10762 159 ESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 243 GRELQNRFNAMkenvsNLAH-ETVFEVRNVTSRDrkkVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIR 321
Cdd:PRK10762 239 GRKLEDQYPRL-----DKAPgEVRLKVDNLSGPG---VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 322 LNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISrSLKDGGYKGamGLFHEVDEQRTAENQRELLALKCH 401
Cdd:PRK10762 311 LDGHEVVTRSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLT-ALRYFSRAG--GSLKHADEQQAVSDFIRLFNIKTP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 402 SVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAV 481
Cdd:PRK10762 388 SMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILV 467
|
490 500
....*....|....*....|....*.
gi 16131913 482 FCEGRLTQILtNRDDMSEEEIMAWAL 507
Cdd:PRK10762 468 MHEGRISGEF-TREQATQEKLMAAAV 492
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-506 |
1.28e-152 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 444.56 E-value: 1.28e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 8 MAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLGIGIIYQ 87
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 88 ELSVIDELTVLENLYIGRHLTKKIcgvnIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVI 167
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGRYPTKGM----FVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 168 IMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRLMVGRELQ 247
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSLT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 248 NRFnamkENVSNLAHETVFEVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDI 327
Cdd:PRK10982 237 QRF----PDKENKPGEVILEVRNLTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 328 SPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSLKdggYKGAMGLFHEVDEQRTAENQRELLALKCHSVNQNI 407
Cdd:PRK10982 313 NNHNANEAINHGFALVTEERRSTGIYAYLDIGFNSLISNIRN---YKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 408 TELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
490
....*....|....*....
gi 16131913 488 TQILtNRDDMSEEEIMAWA 506
Cdd:PRK10982 470 AGIV-DTKTTTQNEILRLA 487
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-506 |
6.53e-137 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 405.20 E-value: 6.53e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLG 81
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 82 IGIIYQELSVIDELTVLENLYIGrhLTKKicgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
Cdd:PRK15439 88 IYLVPQEPLLFPNLSVKENILFG--LPKR---------QASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRLM 241
Cdd:PRK15439 157 RDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 242 VG-------RELQNRFNAMKENVSNLAHET-VFEVRNVTSrdrKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVD 313
Cdd:PRK15439 237 TPaarekslSASQKLWLELPGNRRQQAAGApVLTVEDLTG---EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 314 KRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAisrSLKdggyKGAMGLF-HEVDEQRTAENQ 392
Cdd:PRK15439 314 PARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWNVC---ALT----HNRRGFWiKPARENAVLERY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 393 RELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEI 472
Cdd:PRK15439 387 RRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEI 466
|
490 500 510
....*....|....*....|....*....|....
gi 16131913 473 ITVCDRIAVFCEGRLTQILTnRDDMSEEEIMAWA 506
Cdd:PRK15439 467 EQMADRVLVMHQGEISGALT-GAAINVDTIMRLA 499
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-507 |
7.24e-133 |
|
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: 394.58 E-value: 7.24e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGI--HEPTKGTITINNISYNKLDHKLAAQLGIG 83
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 84 IIYQELSVIDELTVLENLYIGRHLTKKicgVNIIDWREMRVRAAMMLLRVGLKVDLDEK-VANLSISHKQMLEIAKTLML 162
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGNEITLP---GGRMAYNAMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRLMV 242
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 243 GRELQNRFnamkenvSNLAHET---VFEVRNVTSRD-----RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGV-D 313
Cdd:TIGR02633 239 GREITSLY-------PHEPHEIgdvILEARNLTCWDvinphRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 314 KRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISrSLKDGGYKGAMglfHEVDEQRTAENQR 393
Cdd:TIGR02633 312 GKFEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLS-VLKSFCFKMRI---DAAAELQIIGSAI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 394 ELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEII 473
Cdd:TIGR02633 388 QRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVL 467
|
490 500 510
....*....|....*....|....*....|....
gi 16131913 474 TVCDRIAVFCEGRLTQILTNrDDMSEEEIMAWAL 507
Cdd:TIGR02633 468 GLSDRVLVIGEGKLKGDFVN-HALTQEQVLAAAL 500
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
263-487 |
3.22e-92 |
|
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: 278.55 E-value: 3.22e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 263 ETVFEVRNVTSRDRkkVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAY 342
Cdd:cd03215 2 EPVLEVRGLSVKGA--VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 ITESRRDNGFFPNFSIAQNMAISRSLkdggykgamglfhevdeqrtaenqrellalkchsvnqnitelSGGNQQKVLISK 422
Cdd:cd03215 80 VPEDRKREGLVLDLSVAENIALSSLL------------------------------------------SGGNQQKVVLAR 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:cd03215 118 WLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-224 |
3.96e-74 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 231.55 E-value: 3.96e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLGIGII 85
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 86 YQelsvideltvlenlyigrhltkkicgvniidwremrvraammllrvglkvdldekvanLSISHKQMLEIAKTLMLDAK 165
Cdd:cd03216 81 YQ----------------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
16-487 |
4.96e-71 |
|
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: 235.18 E-value: 4.96e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPT---KGTITINNISYNKLDHKLAAQLgIGIIYQE---- 88
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR-IGMVFQDpmtq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 89 ---LSVIDELT-VLENLYIGRhltkkicgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
Cdd:COG1123 96 lnpVTVGDQIAeALENLGLSR--------------AEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 165 KVIIMDEPTSSL---TNKEVdyLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRLM 241
Cdd:COG1123 162 DLLIADEPTTALdvtTQAEI--LDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 242 VGRELQNRFNAMKENVSNlahETVFEVRNVT-------SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK 314
Cdd:COG1123 240 VPRLGAARGRAAPAAAAA---EPLLEVRNLSkrypvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 315 RAGGEIRLNGKDISPRSPLDavkkgmayITESRRDNG---------FFPNFSIAQnmAISRSLKdggykgamgLFHEVDE 385
Cdd:COG1123 317 PTSGSILFDGKDLTKLSRRS--------LRELRRRVQmvfqdpyssLNPRMTVGD--IIAEPLR---------LHGLLSR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 386 QRTAENQRELLA---LKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKV 461
Cdd:COG1123 378 AERRERVAELLErvgLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLT 457
|
490 500
....*....|....*....|....*.
gi 16131913 462 ILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:COG1123 458 YLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
10-238 |
2.57e-58 |
|
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: 193.04 E-value: 2.57e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN--NISyNKLDHKLAaQLGIGIIYQ 87
Cdd:cd03219 5 GLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDgeDIT-GLPPHEIA-RLGIGRTFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 88 ELSVIDELTVLENLYIGRHLTKkicGVNIIDWR------EMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
Cdd:cd03219 83 IPRLFPELTVLENVMVAAQART---GSGLLLARarreerEARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIV 238
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
10-239 |
7.20e-57 |
|
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: 189.86 E-value: 7.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLD-HKLaAQLGIGIIYQE 88
Cdd:COG0411 9 GLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPpHRI-ARLGIARTFQN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 89 LSVIDELTVLENLYIGRHLTKKICGVNII--------DWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
Cdd:COG0411 88 PRLFPELTVLENVLVAAHARLGRGLLAALlrlprarrEEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVR 239
Cdd:COG0411 168 ATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADPRVI 247
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-247 |
9.73e-56 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 186.42 E-value: 9.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQlgIGII 85
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR--IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 86 YQELSVIDELTVLENL-YIGRhltkkICGvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
Cdd:COG1131 79 PQEPALYPDLTVRENLrFFAR-----LYG---LPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSN---DDIVRLM 241
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKArllEDVFLEL 230
|
....*.
gi 16131913 242 VGRELQ 247
Cdd:COG1131 231 TGEEAR 236
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-221 |
3.50e-47 |
|
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: 161.41 E-value: 3.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKldHKLAAQLGIGII 85
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK--EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 86 YQELSVIDELTVLENLYigrhltkkicgvniidwremrvraammllrvglkvdldekvanLSISHKQMLEIAKTLMLDAK 165
Cdd:cd03230 79 PEEPSLYENLTVRENLK-------------------------------------------LSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-221 |
1.09e-44 |
|
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: 156.50 E-value: 1.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKL-DHKLAAQL 80
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLsEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 81 G--IGIIYQELSVIDELTVLENLYIGRHLTKKicgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
Cdd:cd03255 81 RrhIGFVFQSFNLLPDLTALENVELPLLLAGV-------PKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 159 TLMLDAKVIIMDEPTSSL---TNKEVdyLFLIMNQLRKEGTAIVYISHKLaEIRRICDRYTVMKDG 221
Cdd:cd03255 154 ALANDPKIILADEPTGNLdseTGKEV--MELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDG 216
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-233 |
5.66e-44 |
|
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: 155.40 E-value: 5.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQlgIGII 85
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ--IGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 86 YQELSVIDELTVLENL-YIGRhltkkicgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
Cdd:COG4555 80 PDERGLYDRLTVRENIrYFAE--------LYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 165 KVIIMDEPTSSL--TNKEvdyLFL-IMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVS 233
Cdd:COG4555 152 KVLLLDEPTNGLdvMARR---LLReILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELR 220
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
20-221 |
7.91e-44 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 153.78 E-value: 7.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLgIGIIYQ-------ELSVI 92
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGLVFQnpddqffGPTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 93 DELT-VLENLYIGRHltkkicgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
Cdd:cd03225 95 EEVAfGLENLGLPEE--------------EIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16131913 172 PTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-232 |
2.12e-41 |
|
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: 155.45 E-value: 2.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 1 MATPYISMAGIGKSF-----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHK 75
Cdd:COG1123 256 AAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 76 LAAQLG--IGIIYQ--------ELSVIDELTvlENLYIGRHLTKKicgvniidwrEMRVRAAMMLLRVGlkvdLDEKVAN 145
Cdd:COG1123 336 SLRELRrrVQMVFQdpysslnpRMTVGDIIA--EPLRLHGLLSRA----------ERRERVAELLERVG----LPPDLAD 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 146 -----LSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtnkevDYL--FLIMNQL----RKEGTAIVYISHKLAEIRRICDR 214
Cdd:COG1123 400 rypheLSGGQRQRVAIARALALEPKLLILDEPTSAL-----DVSvqAQILNLLrdlqRELGLTYLFISHDLAVVRYIADR 474
|
250
....*....|....*...
gi 16131913 215 YTVMKDGSSVCSGIVSDV 232
Cdd:COG1123 475 VAVMYDGRIVEDGPTEEV 492
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-174 |
4.09e-41 |
|
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: 144.71 E-value: 4.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQlGIGIIYQELSVIDELTVLEN 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK-EIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 101 LYIGRHLTKkicgvniIDWREMRVRAAMMLLRVGLKVDLDEKV----ANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
Cdd:pfam00005 80 LRLGLLLKG-------LSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
16-232 |
5.15e-41 |
|
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: 147.09 E-value: 5.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLgIGIIYQ-------E 88
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGLVFQnpddqlfA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 89 LSVIDELT-VLENLYIGRhltkkicgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVI 167
Cdd:COG1122 91 PTVEEDVAfGPENLGLPR--------------EEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 168 IMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-221 |
8.69e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 146.34 E-value: 8.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 3 TPYISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAA 78
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 79 QL---GIGIIYQELSVIDELTVLENLYIGRHLTKkicgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLE 155
Cdd:COG1136 82 RLrrrHIGFVFQFFNLLPELTALENVALPLLLAG-------VSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 156 IAKTLMLDAKVIIMDEPTSSL---TNKEVdylFLIMNQLRKE-GTAIVYISHKLaEIRRICDRYTVMKDG 221
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLdskTGEEV---LELLRELNRElGTTIVMVTHDP-ELAARADRVIRLRDG 220
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
16-235 |
1.50e-40 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 145.65 E-value: 1.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN--NISyNKLDHKLAAqLGIGIIYQELSVID 93
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgrDIT-GLPPHERAR-AGIGYVPEGRRIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 94 ELTVLENLYIGRHLTKKICGVNIIDW--------REMRVRAAmmllrvglkvdldekvANLSISHKQMLEIAKTLMLDAK 165
Cdd:cd03224 89 ELTVEENLLLGAYARRRAKRKARLERvyelfprlKERRKQLA----------------GTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSND 235
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-227 |
2.38e-40 |
|
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: 144.96 E-value: 2.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFG--PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINniSYNKLDHKLAAQLGIG 83
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN--GYSIRTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 84 IIYQELSVIDELTVLENLYIgrhltkkICGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
Cdd:cd03263 79 YCPQFDALFDELTVREHLRF-------YARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRKeGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
10-240 |
5.96e-40 |
|
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: 144.63 E-value: 5.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 10 GIGKSFG-PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL--GIGIIY 86
Cdd:cd03256 5 NLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrQIGMIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 87 QELSVIDELTVLENLYIGRHLTKKIcgvniidWREM--------RVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
Cdd:cd03256 85 QQFNLIERLSVLENVLSGRLGRRST-------WRSLfglfpkeeKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 159 TLMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNQlRKEGTAIVYIsHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSND 235
Cdd:cd03256 158 ALMQQPKLILADEPVASLdpaSSRQVMDLLKRINR-EEGITVIVSL-HQVDLAREYADRIVGLKDGRIVFDGPPAELTDE 235
|
....*
gi 16131913 236 DIVRL 240
Cdd:cd03256 236 VLDEI 240
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-227 |
9.45e-39 |
|
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: 140.43 E-value: 9.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLdHKLAAQLGIGII 85
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN-IEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 86 YQELsvIDELTVLENLYIGRhltkkicgvNIIDWREMRVRAAmmLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
Cdd:cd03268 80 APGF--YPNLTARENLRLLA---------RLLGIRKKRIDEV--LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
267-487 |
1.13e-38 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 140.97 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldAVKKGMAYIT 344
Cdd:COG1131 2 EVRGLTKRygDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA--EVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 EsrrDNGFFPNFSIAQNMAIsrslkdggYKGAMGLFHEVDEQRTAEnQRELLALKcHSVNQNITELSGGNQQKVLISKWL 424
Cdd:COG1131 80 Q---EPALYPDLTVRENLRF--------FARLYGLPRKEARERIDE-LLELFGLT-DAADRKVGTLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131913 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
16-239 |
1.91e-38 |
|
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: 140.12 E-value: 1.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLD-HKLAAqLGIGIIYQELSVIDE 94
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRIAR-LGIGYVPEGRRIFPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 95 LTVLENLYIGRHLTKKICGVN-IIDW--------REMRVRAAmmllrvglkvdldekvANLSISHKQMLEIAKTLMLDAK 165
Cdd:COG0410 93 LTVEENLLLGAYARRDRAEVRaDLERvyelfprlKERRRQRA----------------GTLSGGEQQMLAIGRALMSRPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVR 239
Cdd:COG0410 157 LLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVR 230
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-239 |
3.08e-36 |
|
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: 134.79 E-value: 3.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLgIGII 85
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR-IAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 86 YQELSVIDELTVLENLYIGRH--------LTKKicgvniiDWRemRVRAAMmlLRVGLKvDL-DEKVANLSISHKQMLEI 156
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYphlglfgrPSAE-------DRE--AVEEAL--ERTGLE-HLaDRPVDELSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 157 AKTLMLDAKVIIMDEPTSSLtnkevD--YLFLIMNQLRK----EGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVS 230
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHL-----DlaHQLEVLELLRRlareRGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
....*....
gi 16131913 231 DVSNDDIVR 239
Cdd:COG1120 224 EVLTPELLE 232
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-227 |
3.39e-36 |
|
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: 133.65 E-value: 3.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKldHKLAAQLG 81
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK--EPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 82 IGIIYQELSVIDELTVLENL-YIGRhltkkICGVNiidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLeYFAG-----LYGLK---GDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-227 |
4.39e-36 |
|
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: 133.17 E-value: 4.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNisyNKLDhkLAAQLGIGII 85
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLD--IAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 86 YQELSVIDELTVLENL-YIGRhltkkICGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
Cdd:cd03269 76 PEERGLYPKMKVIDQLvYLAQ-----LKGLKK---EEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131913 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-239 |
4.46e-36 |
|
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: 133.95 E-value: 4.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHK--LAA 78
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 79 QLGIGIIYQELSVIDELTVLEN----LYIGRHLTKKicgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLS------I 148
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENvafpLREHTDLSEA----------EIRELVLEKLELVGLPGAADKMPSELSggmrkrV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 149 ShkqmleIAKTLMLDAKVIIMDEPTSSL---TNKEVDYLfliMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
Cdd:COG1127 151 A------LARALALDPEILLYDEPTAGLdpiTSAVIDEL---IRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKII 221
|
250
....*....|....*..
gi 16131913 225 CSGIVSDV--SNDDIVR 239
Cdd:COG1127 222 AEGTPEELlaSDDPWVR 238
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
10-221 |
6.94e-36 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 133.01 E-value: 6.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 10 GIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLG--IG 83
Cdd:cd03257 6 NLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRRkeIQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 84 IIYQelsviDELTVLENLY-IGRHLTKKIcGVNIIDWREMRVRAAMMLLRVGlkVDLDEKVAN-----LSISHKQMLEIA 157
Cdd:cd03257 86 MVFQ-----DPMSSLNPRMtIGEQIAEPL-RIHGKLSKKEARKEAVLLLLVG--VGLPEEVLNrypheLSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 158 KTLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRKE----GTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:cd03257 158 RALALNPKLLIADEPTSAL---DVSVQAQILDLLKKLqeelGLTLLFITHDLGVVAKIADRVAVMYAG 222
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-232 |
1.82e-35 |
|
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: 132.32 E-value: 1.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGP----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHK--LAAQ 79
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKelRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 80 LGIGIIYQELSVIDELTVLENLyigrHLTKKICGVniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENV----ALPLEIAGV---PKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 160 LMLDAKVIIMDEPTSSL---TNKEVdyLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:cd03258 155 LANNPKVLLCDEATSALdpeTTQSI--LALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-221 |
3.11e-35 |
|
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: 130.72 E-value: 3.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDhklAAQLGIGII 85
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP---PERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 86 YQELSVIDELTVLENLYIGrhltkkiCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
Cdd:cd03259 78 FQDYALFPHLTVAENIAFG-------LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913 166 VIIMDEPTSSLtnkevDYlfLIMNQLRKE--------GTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:cd03259 151 LLLLDEPLSAL-----DA--KLREELREElkelqrelGITTIYVTHDQEEALALADRIAVMNEG 207
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-248 |
4.95e-35 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 131.46 E-value: 4.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGP----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHK-LAAQl 80
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKaFRRR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 81 gIGIIYQ--ELSV-----IDElTVLENLyigrhltkKICGVniidwREMRVRAAMMLLRVGLKVD-LDEKVANLSISHKQ 152
Cdd:COG1124 81 -VQMVFQdpYASLhprhtVDR-ILAEPL--------RIHGL-----PDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 153 MLEIAKTLMLDAKVIIMDEPTSSL---TNKEVdyLFLImNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSsvcsgI 228
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSALdvsVQAEI--LNLL-KDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGR-----I 217
|
250 260
....*....|....*....|...
gi 16131913 229 VSDVSNDDIVRLM---VGRELQN 248
Cdd:COG1124 218 VEELTVADLLAGPkhpYTRELLA 240
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-247 |
2.14e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 129.44 E-value: 2.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAaql 80
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIG--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 81 gigiiY--QELSvIDE---LTVLE----NLYIGRHLTKKICgvniidwREMRVRAAMMLLRVGLkvdldEKVANLSISH- 150
Cdd:COG1121 79 -----YvpQRAE-VDWdfpITVRDvvlmGRYGRRGLFRRPS-------RADREAVDEALERVGL-----EDLADRPIGEl 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 151 ----KQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGsSVCS 226
Cdd:COG1121 141 sggqQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAH 219
|
250 260
....*....|....*....|.
gi 16131913 227 GIVSDVSNDDIVRLMVGRELQ 247
Cdd:COG1121 220 GPPEEVLTPENLSRAYGGPVA 240
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-239 |
3.82e-34 |
|
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: 128.77 E-value: 3.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN--NISYNKLDHKLAAQLGIG 83
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDgeDISGLSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 84 IIYQELSVIDELTVLEN--LYIGRHLTKkicgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
Cdd:cd03261 81 MLFQSGALFDSLTVFENvaFPLREHTRL--------SEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 162 LDAKVIIMDEPTSSL----TNKEVDylfLIMNqLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV--SN 234
Cdd:cd03261 153 LDPELLLYDEPTAGLdpiaSGVIDD---LIRS-LKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELraSD 228
|
....*
gi 16131913 235 DDIVR 239
Cdd:cd03261 229 DPLVR 233
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-221 |
9.85e-34 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 128.28 E-value: 9.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 1 MATPYISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKl 76
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 77 aaqlgIGIIYQELSVIDELTVLENLYIGRHLTKkicgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEI 156
Cdd:COG1116 82 -----RGVVFQEPALLPWLTVLDNVALGLELRG-------VPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913 157 AKTLMLDAKVIIMDEPTSSLtnkevDYL------FLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:COG1116 150 ARALANDPEVLLMDEPFGAL-----DALtrerlqDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
267-487 |
1.18e-33 |
|
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: 125.20 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldAVKKGMAYIT 344
Cdd:cd03230 2 EVRNLSKRygKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE--EVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 EsrrDNGFFPNFSIAQNMaisrslkdggykgamglfhevdeqrtaenqrellalkchsvnqnitELSGGNQQKVLISKWL 424
Cdd:cd03230 80 E---EPSLYENLTVRENL----------------------------------------------KLSGGMKQRLALAQAL 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131913 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:cd03230 111 LHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-221 |
1.33e-33 |
|
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: 126.49 E-value: 1.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKlDHKLAAQL--GIG 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELrqKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 84 IIYQELSVIDELTVLENLYIG----RHLTKKicgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLApikvKGMSKA----------EAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-245 |
2.71e-33 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 127.03 E-value: 2.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 81 GIGIIYQELSVIDELTVLENLYIGRHLTKKicgVNIIDW-----------REMRVRAAMMLLRVGLKVDLDEKVANLSIS 149
Cdd:PRK11300 81 GVVRTFQHVRLFREMTVIENLLVAQHQQLK---TGLFSGllktpafrraeSEALDRAATWLERVGLLEHANRQAGNLAYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 150 HKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGI 228
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGT 237
|
250
....*....|....*...
gi 16131913 229 VSDVSND-DIVRLMVGRE 245
Cdd:PRK11300 238 PEEIRNNpDVIKAYLGEA 255
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-227 |
4.25e-33 |
|
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: 125.17 E-value: 4.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQlgIGII 85
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRR--IGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 86 YQELSVIDELTVLENLYIgrhlTKKICGVNiidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
Cdd:cd03265 79 FQDLSVDDELTGWENLYI----HARLYGVP---GAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131913 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-232 |
2.25e-32 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 126.73 E-value: 2.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHK--LAAQ 79
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERelRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 80 LGIGIIYQELSVIDELTVLENlyIGRHLtkKICGVniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAEN--VALPL--EIAGV---PKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 160 LMLDAKVIIMDEPTSSL---TNKEVdyLFLImNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:COG1135 155 LANNPKVLLCDEATSALdpeTTRSI--LDLL-KDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDV 228
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
10-203 |
3.15e-32 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 122.59 E-value: 3.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLgiGIIYQEL 89
Cdd:COG4133 7 NLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRL--AYLGHAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 90 SVIDELTVLENLyigRHLtkkiCGVNIIDWREMRVRAAmmLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
Cdd:COG4133 85 GLKPELTVRENL---RFW----AALYGLRADREAIDEA--LEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190
....*....|....*....|....*....|....
gi 16131913 170 DEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISH 203
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
14-219 |
6.84e-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: 121.87 E-value: 6.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 14 SFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKlaaqlgIGIIYQELSvID 93
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR------IGYVPQRRS-ID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 94 E---LTVLENLYIGRhlTKKICGVNII---DWRemRVRAAmmLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVI 167
Cdd:cd03235 81 RdfpISVRDVVLMGL--YGHKGLFRRLskaDKA--KVDEA--LERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16131913 168 IMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMK 219
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-221 |
8.13e-32 |
|
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: 120.37 E-value: 8.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLG-IGI 84
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRrIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 85 IYQELSVIDELTVLENLYIGrhltkkicgvniidwremrvraammllrvglkvdldekvanLSISHKQMLEIAKTLMLDA 164
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-----------------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-218 |
8.23e-32 |
|
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: 121.81 E-value: 8.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKlaaqlg 81
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 82 IGIIYQELSVIDELTVLENLYIGRhltkKICGVniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGL----ELQGV---PKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131913 162 LDAKVIIMDEPTSSLtnkevDYLF------LIMNQLRKEGTAIVYISHKLAEIRRICDRYTVM 218
Cdd:cd03293 148 VDPDVLLLDEPFSAL-----DALTreqlqeELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-232 |
4.08e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 122.14 E-value: 4.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNisyNKLDHKLAAQLGI-----Gi 84
Cdd:COG4152 6 GLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLDPEDRRRIGYlpeerG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 85 IYQELSVIDELtvlenLYIGR--HLTKKicgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
Cdd:COG4152 82 LYPKMKVGEQL-----VYLARlkGLSKA----------EAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLH 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 163 DAKVIIMDEPTSSL--TNkeVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:COG4152 147 DPELLILDEPFSGLdpVN--VELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
20-227 |
5.38e-31 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 127.26 E-value: 5.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHK-LAAQlgIGIIYQElsviDEL--- 95
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAsLRRQ--IGVVLQD----VFLfsg 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 96 TVLENLYIGRHLtkkicgvniIDWREMrVRAAMML--------LRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVI 167
Cdd:COG2274 564 TIRENITLGDPD---------ATDEEI-IEAARLAglhdfieaLPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRIL 633
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 168 IMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSG 227
Cdd:COG2274 634 ILDEATSALDAETEAIILENLRRLLKGRTVII-IAHRLSTIRL-ADRIIVLDKGRIVEDG 691
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
261-492 |
6.58e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 119.81 E-value: 6.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 261 AHETVFEVRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprsPLDAVKK 338
Cdd:COG1121 2 MMMPAIELENLTvSYGGRPVlEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK------PPRRARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 339 GMAYITESRRDNGFFPnFSIAQNMAISRSlkdgGYKGAMGLFHEVDEQRTAE--NQRELLALKchsvNQNITELSGGNQQ 416
Cdd:COG1121 76 RIGYVPQRAEVDWDFP-ITVRDVVLMGRY----GRRGLFRRPSRADREAVDEalERVGLEDLA----DRPIGELSGGQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIA-----VFCEGRLTQIL 491
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLllnrgLVAHGPPEEVL 226
|
.
gi 16131913 492 T 492
Cdd:COG1121 227 T 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
10-221 |
1.22e-30 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 116.58 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQlGIGIIYQel 89
Cdd:cd00267 4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR-RIGYVPQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 90 svideltvlenlyigrhltkkicgvniidwremrvraammllrvglkvdldekvanLSISHKQMLEIAKTLMLDAKVIIM 169
Cdd:cd00267 81 --------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16131913 170 DEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
11-235 |
1.35e-30 |
|
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: 119.67 E-value: 1.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 11 IGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL---GIGIIYQ 87
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 88 ELSVIDELTVLENLYIGRhltkKICGVNiidwREMRVRAAMMLL-RVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKV 166
Cdd:cd03294 110 SFALLPHRTVLENVAFGL----EVQGVP----RAEREERAAEALeLVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDI 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 167 IIMDEPTSSL---TNKEVDYLFLimnQL-RKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG----IVSDVSND 235
Cdd:cd03294 182 LLMDEAFSALdplIRREMQDELL---RLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGtpeeILTNPAND 255
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-234 |
2.87e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 117.46 E-value: 2.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVH-ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL--GI 82
Cdd:COG2884 2 IRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLrrRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 83 GIIYQELSVIDELTVLENLYigrhLTKKICGVniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVA----LPLRVTGK---SRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 163 DAKVIIMDEPTSSL---TNKEVDYLFLimnQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSsvcsgIVSDVSN 234
Cdd:COG2884 155 RPELLLADEPTGNLdpeTSWEIMELLE---EINRRGTTVLIATHDLELVDRMPKRVLELEDGR-----LVRDEAR 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
267-482 |
3.63e-30 |
|
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: 116.86 E-value: 3.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprspldavkkgmayiT 344
Cdd:cd03235 1 EVEDLTvSYGGHPVlEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL----------------E 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 ESRRDNGFFP-NFSIAQNMAIS--RSLKDGGYkGAMGLFHEVdeqRTAENQRELLALK----CHSVNQNITELSGGNQQK 417
Cdd:cd03235 65 KERKRIGYVPqRRSIDRDFPISvrDVVLMGLY-GHKGLFRRL---SKADKAKVDEALErvglSELADRQIGELSGGQQQR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 418 VLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVF 482
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
16-221 |
4.63e-30 |
|
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: 115.17 E-value: 4.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLgIGIIYQElSVIDEL 95
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IAYVPQD-PFLFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 96 TVLENLyigrhltkkicgvniidwremrvraammllrvglkvdldekvanLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
Cdd:cd03228 91 TIRENI--------------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSA 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16131913 176 L---TNKEVdylFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDG 221
Cdd:cd03228 127 LdpeTEALI---LEALRALAKGKTVIV-IAHRLSTIRD-ADRIIVLDDG 170
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-486 |
8.62e-30 |
|
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: 122.49 E-value: 8.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 11 IGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKS----TLMKVLSGIHEPTKGTITINNISYNKLDhklAAQL------ 80
Cdd:COG4172 16 FGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLS---ERELrrirgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 81 GIGIIYQE--------LSVIDELTvlENLYIGRHLTKkicgvniidwREMRVRAAMMLLRVGLKvDLDEKVA----NLSI 148
Cdd:COG4172 93 RIAMIFQEpmtslnplHTIGKQIA--EVLRLHRGLSG----------AAARARALELLERVGIP-DPERRLDayphQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 149 SHKQMLEIAKTLMLDAKVIIMDEPTSSL---TNKEVdyLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVC 225
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALdvtVQAQI--LDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 226 SGIVSDV-SN--DDIVRLMVGRELQNRFNAMKENVsnlahETVFEVRNV-------------TSRDRKKVRDISFSVCRG 289
Cdd:COG4172 238 QGPTAELfAApqHPYTRKLLAAEPRGDPRPVPPDA-----PPLLEARDLkvwfpikrglfrrTVGHVKAVDGVSLTLRRG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 290 EILGFAGLVGSGRTELMNCLFGVDkRAGGEIRLNGKDISPRSPldavKKGMAYitesRRD--------NGFF-PNFSIAQ 360
Cdd:COG4172 313 ETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSR----RALRPL----RRRmqvvfqdpFGSLsPRMTVGQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 361 nmAISRSLKdggykgamglFHEVDEQRTAENQR--ELLA---LKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
Cdd:COG4172 384 --IIAEGLR----------VHGPGLSAAERRARvaEALEevgLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDE 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 16131913 436 PTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGR 486
Cdd:COG4172 452 PTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGK 503
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
20-241 |
1.31e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 117.01 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKlDHKLAAQLGIGIIYQE-------LSVI 92
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK-ENLKEIRKKIGIIFQNpdnqfigATVE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 93 DELTV-LENLYIGRHLTKKIcgvnIIDWREmrvraammllRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
Cdd:PRK13632 103 DDIAFgLENKKVPPKKMKDI----IDDLAK----------KVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 172 PTSSLTNKEVDYLFLIMNQLRKEGT-AIVYISHKLAEIrRICDRYTVMKDGSSVCSGIVSDVSND-DIVRLM 241
Cdd:PRK13632 169 STSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILNNkEILEKA 239
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-221 |
2.04e-29 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 118.66 E-value: 2.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNisyNKLDHKLAAQL 80
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG---RDVTGLPPEKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 81 GIGIIYQELSVIDELTVLENlyIG-----RHLTKkicgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLE 155
Cdd:COG3842 78 NVGMVFQDYALFPHLTVAEN--VAfglrmRGVPK----------AEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 156 IAKTLMLDAKVIIMDEPTSSLTNKEVDYL-FLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLREEMrEELRRLQRELGITFIYVTHDQEEALALADRIAVMNDG 212
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
10-227 |
5.98e-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: 112.53 E-value: 5.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLgIGIIYQel 89
Cdd:cd03214 4 NLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVPQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 90 svideltVLEnlyigrhltkkicgvniidwremrvraammllRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
Cdd:cd03214 81 -------ALE--------------------------------LLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 170 DEPTSSL-TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:cd03214 122 DEPTSHLdIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
267-486 |
9.06e-29 |
|
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: 113.30 E-value: 9.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYIT 344
Cdd:cd03224 2 EVENLNAGYGKSqiLFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 ESRRdngFFPNFSIAQN--MAISRsLKDGGYKGAM----GLFHEVDEQRtaenqrellalkchsvNQNITELSGGNQQKV 418
Cdd:cd03224 82 EGRR---IFPELTVEENllLGAYA-RRRAKRKARLervyELFPRLKERR----------------KQLAGTLSGGEQQML 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 419 LISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
Cdd:cd03224 142 AIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-239 |
1.13e-28 |
|
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: 113.41 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLGIGII 85
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 86 YQELSVIDELTVLENLYIGRHLTKKicgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGL-------SKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVR 239
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-232 |
1.25e-28 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 116.05 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHK--LAAQ 79
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKelRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 80 LGIGIIYQELSVIDELTVLENLYigrhLTKKICGVniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVA----LPLELAGT---PKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 160 LMLDAKVIIMDEPTSSL---TNKEVdyLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:PRK11153 155 LASNPKVLLCDEATSALdpaTTRSI--LELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEV 228
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-227 |
1.82e-28 |
|
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: 112.29 E-value: 1.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGeIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLGigii 85
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIG---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 86 Y--QELSVIDELTVLENL-YIGRhltkkicgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
Cdd:cd03264 76 YlpQEFGVYPNFTVREFLdYIAW--------LKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEgtAIVYIS-HKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGED--RIVILStHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-227 |
2.18e-28 |
|
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: 112.66 E-value: 2.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE-----PTKGTITIN--NIsYNKLDHKLAA 78
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDgkDI-YDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 79 QLGIGIIYQELSVIDeLTVLENLYIGrhltKKICGVNIIDWREMRVRAAmmLLRVGL--KVDLDEKVANLSISHKQMLEI 156
Cdd:cd03260 80 RRRVGMVFQKPNPFP-GSIYDNVAYG----LRLHGIKLKEELDERVEEA--LRKAALwdEVKDRLHALGLSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 157 AKTLMLDAKVIIMDEPTSSL----TNKEVDylfLIMnQLRKEgTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALdpisTAKIEE---LIA-ELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFG 222
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
267-495 |
2.66e-28 |
|
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: 112.53 E-value: 2.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAY-- 342
Cdd:cd03219 2 EVRGLTKRfgGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRtf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 -ITESrrdngfFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQR-TAENQRELLALKcHSVNQNITELSGGNQQKVLI 420
Cdd:cd03219 82 qIPRL------FPELTVLENVMVAAQARTGSGLLLARARREEREAReRAEELLERVGLA-DLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVF------CEGRLTQILTNR 494
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLdqgrviAEGTPDEVRNNP 234
|
.
gi 16131913 495 D 495
Cdd:cd03219 235 R 235
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-222 |
6.39e-28 |
|
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: 111.17 E-value: 6.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDhklAAQLGIGII 85
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP---PHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 86 YQELSVIDELTVLENLYIGRHLTKkicgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLKK-------LPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGS 222
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGK 208
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
265-487 |
6.76e-28 |
|
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: 111.67 E-value: 6.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 265 VFEVRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgMAY 342
Cdd:COG1120 1 MLEAENLSvGYGGRPVlDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR-IAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 ITESRRDNGffpNFSIAQNMAISRSlkdgGYKGAMGLFHEVDEQRTAE--NQRELLALKchsvNQNITELSGGNQQKVLI 420
Cdd:COG1120 80 VPQEPPAPF---GLTVRELVALGRY----PHLGLFGRPSAEDREAVEEalERTGLEHLA----DRPVDELSGGERQRVLI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
266-486 |
1.13e-27 |
|
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: 108.81 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 266 FEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprspldavkKGMAYI 343
Cdd:cd03229 1 LELKNVSKRygQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLT---------DLEDEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 344 TESRRDNGF-FPNFSIAQNMaisrslkdggykgamglfhevdeqrtaenqrellalkchSVNQNITE-LSGGNQQKVLIS 421
Cdd:cd03229 72 PPLRRRIGMvFQDFALFPHL---------------------------------------TVLENIALgLSGGQQQRVALA 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVCDRIAVFCEGR 486
Cdd:cd03229 113 RALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAqLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-221 |
1.22e-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: 110.04 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDhklAAQLGIGII 85
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLP---PKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 86 YQELSVIDELTVLENLYIGrhLTKKICGVNIIDwreMRVRAAMMLLRVGLKvdLDEKVANLSISHKQMLEIAKTLMLDAK 165
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFG--LKLRKVPKDEID---ERVREVAELLQIEHL--LDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 166 VIIMDEPTSSLTNK-EVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:cd03301 151 VFLMDEPLSNLDAKlRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDG 207
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-231 |
2.64e-27 |
|
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: 109.22 E-value: 2.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 17 PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQlGIGIIYQELSVIDElT 96
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRR-NIGYVPQDVTLFYG-T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 97 VLENLYIGRhltkkicgVNIIDWREMRvraAMMLLRV---------GLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVI 167
Cdd:cd03245 94 LRDNITLGA--------PLADDERILR---AAELAGVtdfvnkhpnGLDLQIGERGRGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913 168 IMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAeIRRICDRYTVMKDGssvcsGIVSD 231
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKERLRQLLGDKTLII-ITHRPS-LLDLVDRIIVMDSG-----RIVAD 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
16-218 |
2.87e-27 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 111.68 E-value: 2.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEP---TKGTITINNISYNKLDHKLAAQL---GIGIIYQE- 88
Cdd:COG0444 16 GVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKIrgrEIQMIFQDp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 89 -------LSVIDELTvlENLYIGRHLTKKicgvniidwrEMRVRAAMMLLRVGLkvDLDEKVAN-----LSISHKQMLEI 156
Cdd:COG0444 96 mtslnpvMTVGDQIA--EPLRIHGGLSKA----------EARERAIELLERVGL--PDPERRLDrypheLSGGMRQRVMI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 157 AKTLMLDAKVIIMDEPTSSL---TNKEVDYLfliMNQLRKE-GTAIVYISHKLAEIRRICDRYTVM 218
Cdd:COG0444 162 ARALALEPKLLIADEPTTALdvtIQAQILNL---LKDLQRElGLAILFITHDLGVVAEIADRVAVM 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
267-486 |
3.24e-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: 3.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPrspldAVKKGMAYIT 344
Cdd:cd03269 2 EVENVTKRfgRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI-----AARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 ESRrdnGFFPNFSIAQNMAISRSLKdggykgamGLFHEvDEQRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWL 424
Cdd:cd03269 77 EER---GLYPKMKVIDQLVYLAQLK--------GLKKE-EARRRIDEWLERLELSEYA-NKRVEELSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
267-487 |
3.36e-27 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 109.13 E-value: 3.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT------SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSP--LDAVKK 338
Cdd:cd03257 3 EVKNLSvsfptgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlRKIRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 339 GMAYItesrrdngfF--PNFSIAQNMAISRSLKDggykgAMgLFHEVDEQRTAENQRELLALKchSVNQNIT-------E 409
Cdd:cd03257 83 EIQMV---------FqdPMSSLNPRMTIGEQIAE-----PL-RIHGKLSKKEARKEAVLLLLV--GVGLPEEvlnryphE 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:cd03257 146 LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
267-488 |
8.19e-27 |
|
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: 106.75 E-value: 8.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgMAYIt 344
Cdd:cd03214 1 EVENLSVGygGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 esrrdngffpnfsiAQNMAisrslkdggykgAMGLFHevdeqrtaenqrelLAlkchsvNQNITELSGGNQQKVLISKWL 424
Cdd:cd03214 79 --------------PQALE------------LLGLAH--------------LA------DRPFNELSGGERQRVLLARAL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLT 488
Cdd:cd03214 113 AQEPPILLLDEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
21-224 |
8.41e-27 |
|
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: 107.34 E-value: 8.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNisynKLDHKLAAQLGIGIIYQEL-------SVID 93
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG----KPIKAKERRKSIGYVMQDVdyqlftdSVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 94 ELTVlenlyigrhltkkicGVNIIDWREMRVRAAMMLLRV-GLKvdlDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
Cdd:cd03226 92 ELLL---------------GLKELDAGNEQAETVLKDLDLyALK---ERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16131913 173 TSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-222 |
2.11e-26 |
|
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: 106.61 E-value: 2.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 30 PGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKL---AAQLGIGIIYQELSVIDELTVLENLyigrh 106
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInlpPQQRKIGLVFQQYALFPHLNVRENL----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 107 ltkkICGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFL 186
Cdd:cd03297 97 ----AFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 16131913 187 IMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGS 222
Cdd:cd03297 173 ELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-227 |
2.45e-26 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 107.08 E-value: 2.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGI--HEPTKGTITINNISYNKLDHKLAAQLGIGIIYQELSVIDELTVL 98
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERARAGIFLAFQYPVEIPGVSVS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 99 ENLYIgrhltkkicGVNIIDWREMRVRAAMMLLRVGLK-VDLDEKVAN------LSISHKQMLEIAKTLMLDAKVIIMDE 171
Cdd:COG0396 96 NFLRT---------ALNARRGEELSAREFLKLLKEKMKeLGLDEDFLDryvnegFSGGEKKRNEILQMLLLEPKLAILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 172 PTSSLtnkEVDYLFLI---MNQLRKEGTAIVYISHK---LAEIRriCDRYTVMKDGSSVCSG 227
Cdd:COG0396 167 TDSGL---DIDALRIVaegVNKLRSPDRGILIITHYqriLDYIK--PDFVHVLVDGRIVKSG 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-490 |
2.94e-26 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 111.82 E-value: 2.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGI--HEPTKG----------------------- 60
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGriiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 61 -------TITINNISYNKLDHKLAAQLG--IGIIYQE-LSVIDELTVLENLyigrhltkkICGVNIIDW--REMRVRAAM 128
Cdd:TIGR03269 81 pcpvcggTLEPEEVDFWNLSDKLRRRIRkrIAIMLQRtFALYGDDTVLDNV---------LEALEEIGYegKEAVGRAVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 129 MLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDylfLIMNQLRK----EGTAIVYISHK 204
Cdd:TIGR03269 152 LIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAK---LVHNALEEavkaSGISMVLTSHW 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 205 LAEIRRICDRYTVMKDGSSVCSGIVSDVSNddivRLMvgrelqnrfnamkENVSNLAHETVFEV-------RNVTSR--- 274
Cdd:TIGR03269 229 PEVIEDLSDKAIWLENGEIKEEGTPDEVVA----VFM-------------EGVSEVEKECEVEVgepiikvRNVSKRyis 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 275 -DR---KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGE--IRLNGK--DISPRSPLDavkKGMA--YIT 344
Cdd:TIGR03269 292 vDRgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEwvDMTKPGPDG---RGRAkrYIG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 ESRRDNGFFPNFSIAQNM--AISRSLKDggykgAMGLFHEVDEQRTA----ENQRELLalkchsvNQNITELSGGNQQKV 418
Cdd:TIGR03269 369 ILHQEYDLYPHRTVLDNLteAIGLELPD-----ELARMKAVITLKMVgfdeEKAEEIL-------DKYPDELSEGERHRV 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 419 LISKWLCCCPEVIIFDEPTRGID----VGAKAEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEM---EQTFIIVSHDMDFVLDVCDRAALMRDGKIVKI 509
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-215 |
3.01e-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: 106.34 E-value: 3.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGP-VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL--GI 82
Cdd:cd03292 1 IEFINVTKTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLrrKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 83 GIIYQELSVIDELTVLENLYIGRHLTKKicgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGV-------PPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVN 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131913 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKlaeiRRICDRY 215
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHA----KELVDTT 202
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
19-227 |
3.11e-26 |
|
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: 106.54 E-value: 3.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLgIGIIYQElSVIDELTVL 98
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM-IGVVLQD-TFLFSGTIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 99 ENLYIGRHLTKKicGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTN 178
Cdd:cd03254 95 ENIRLGRPNATD--EEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16131913 179 KEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSG 227
Cdd:cd03254 173 ETEKLIQEALEKLMKGRTSII-IAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-227 |
5.16e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 108.76 E-value: 5.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITInnISYNKLDHKLAAQL 80
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV--LGVPVPARARLARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 81 GIGIIYQELSVIDELTVLENLYI-GRHltkkiCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
Cdd:PRK13536 115 RIGVVPQFDNLDLEFTVRENLLVfGRY-----FGMST---REIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARA 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913 160 LMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRK---EGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:PRK13536 187 LINDPQLLILDEPTTGL---DPHARHLIWERLRSllaRGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
12-232 |
7.02e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 105.93 E-value: 7.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 12 GKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNisynkldhKLAAQLGIGIIYQElsv 91
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG--------RVSALLELGAGFHP--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 92 idELTVLENLY-IGRhltkkICGVNIidwREMRVRAAmmllRV----GLKVDLDEKVANLSISHKQMLEIAKTLMLDAKV 166
Cdd:COG1134 102 --ELTGRENIYlNGR-----LLGLSR---KEIDEKFD----EIvefaELGDFIDQPVKTYSSGMRARLAFAVATAVDPDI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 167 IIMDEPTSsltnkeV-DYLFL-----IMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:COG1134 168 LLVDEVLA------VgDAAFQkkclaRIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
263-487 |
7.70e-26 |
|
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: 110.76 E-value: 7.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 263 ETVFEVRNVT----SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGV---DKRAGGEIRLNGKDISPRSPLDA 335
Cdd:COG1123 2 TPLLEVRDLSvrypGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 336 VKKgMAYITESRrDNGFFPNFSIAQnmaISRSLKDGGykgamglfheVDEQRTAENQRELLALK--CHSVNQNITELSGG 413
Cdd:COG1123 82 GRR-IGMVFQDP-MTQLNPVTVGDQ---IAEALENLG----------LSRAEARARVLELLEAVglERRLDRYPHQLSGG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 414 NQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:COG1123 147 QRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
267-487 |
1.30e-25 |
|
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: 104.51 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT----SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIspRSPLDAVKKGMAY 342
Cdd:cd03263 2 QIRNLTktykKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI--RTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 ITesrRDNGFFPNFSIAQNMAISRSLKdggykgamGLFHEvDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISK 422
Cdd:cd03263 80 CP---QFDALFDELTVREHLRFYARLK--------GLPKS-EIKEEVELLLRVLGLT-DKANKRARTLSGGMKRKLSLAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
279-487 |
1.36e-25 |
|
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: 104.49 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprspldavKKGMAYITESRRDN-GF-F--- 353
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIS--------KLSEKELAAFRRRHiGFvFqsf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 354 ---PNFSIAQNMAISRSLKdggykgamGLFHEVDEQRtAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEV 430
Cdd:cd03255 92 nllPDLTALENVELPLLLA--------GVPKKERRER-AEELLERVGLG-DRLNHYPSELSGGQQQRVAIARALANDPKI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 431 IIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSElPEIITVCDRIAVFCEGRL 487
Cdd:cd03255 162 ILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
20-227 |
1.72e-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: 109.85 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHK-LAAQlgIGIIYQElSVIDELTVL 98
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAsWRRQ--IAWVPQN-PYLFAGTIR 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 99 ENLYIGRHLtkkicgvniIDWREMR--VRAAMML-----LRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
Cdd:COG4988 429 ENLRLGRPD---------ASDEELEaaLEAAGLDefvaaLPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDE 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 172 PTSSL---TNKEVdylFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSG 227
Cdd:COG4988 500 PTAHLdaeTEAEI---LQALRRLAKGRTVIL-ITHRLALLAQ-ADRILVLDDGRIVEQG 553
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-221 |
2.11e-25 |
|
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: 102.90 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLGIGII---YQELSVIDELT 96
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVpedRKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 97 VLENLYIGRHLTkkicGVNIidwremrvraammllrvglkvdldEKVAnlsishkqmleIAKTLMLDAKVIIMDEPTssl 176
Cdd:cd03215 95 VAENIALSSLLS----GGNQ------------------------QKVV-----------LARWLARDPRVLILDEPT--- 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16131913 177 tnKEVD-----YLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:cd03215 133 --RGVDvgakaEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
263-504 |
2.50e-25 |
|
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: 104.29 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 263 ETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGM 340
Cdd:COG0410 1 MPMLEVENLHAGygGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 341 AYITESRRdngFFPNFSIAQNMAisrslkdggykgaMGLFHEVDEQRTAENQRELLAL-------KchsvNQNITELSGG 413
Cdd:COG0410 81 GYVPEGRR---IFPSLTVEENLL-------------LGAYARRDRAEVRADLERVYELfprlkerR----RQRAGTLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 414 NQQKVLISKWLCCCPEVIIFDEPTRGIdvgakA-----EIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLT 488
Cdd:COG0410 141 EQQMLAIGRALMSRPKLLLLDEPSLGL-----ApliveEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIV 215
|
250
....*....|....*.
gi 16131913 489 QILTNRDDMSEEEIMA 504
Cdd:COG0410 216 LEGTAAELLADPEVRE 231
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
267-495 |
3.45e-25 |
|
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: 104.11 E-value: 3.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT------SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgM 340
Cdd:COG1124 3 EVRNLSvsygqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR-V 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 341 AYItesrrdngfF--------PNFSIAQnmAISRSLKdggykgamgLFHEVDEQRTAENQRELLALKCHSVNQNITELSG 412
Cdd:COG1124 82 QMV---------FqdpyaslhPRHTVDR--ILAEPLR---------IHGLPDREERIAELLEQVGLPPSFLDRYPHQLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 413 GNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQIL 491
Cdd:COG1124 142 GQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEEL 221
|
....
gi 16131913 492 TNRD 495
Cdd:COG1124 222 TVAD 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-238 |
3.69e-25 |
|
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: 104.01 E-value: 3.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 3 TPYISMAGIGKSFGPVHALKSVNLTVYPGEiH-ALLGENGAGKSTLMKVLSGIHEPTKG-TITInnisynkLDHKlaaqL 80
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGE-HwAILGPNGAGKSTLLSLITGDLPPTYGnDVRL-------FGER----R 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 81 G----------IGI--------IYQELSVIDelTVLENLY--IGRhltkkicgvniidWR----EMRVRAAMMLLRVGLK 136
Cdd:COG1119 69 GgedvwelrkrIGLvspalqlrFPRDETVLD--VVLSGFFdsIGL-------------YReptdEQRERARELLELLGLA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 137 VDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL--TNKEvdyLFL-IMNQLRKEG-TAIVYISHKLAEIRRIC 212
Cdd:COG1119 134 HLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLdlGARE---LLLaLLDKLAAEGaPTLVLVTHHVEEIPPGI 210
|
250 260
....*....|....*....|....*.
gi 16131913 213 DRYTVMKDGSSVCSGIVSDVSNDDIV 238
Cdd:COG1119 211 THVLLLKDGRVVAAGPKEEVLTSENL 236
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
267-492 |
3.84e-25 |
|
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: 103.92 E-value: 3.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR---DRKKVRDISFSVCRGEILGFAGLVGSGRTELM---NCLFGVDKragGEIRLNGKDISPRSPLdAVKKGM 340
Cdd:cd03295 2 EFENVTKRyggGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMkmiNRLIEPTS---GEIFIDGEDIREQDPV-ELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 341 AYITESRrdnGFFPNFSIAQNMAISRSLKdggykgamglfhEVDEQRTAENQRELLAL----KCHSVNQNITELSGGNQQ 416
Cdd:cd03295 78 GYVIQQI---GLFPHMTVEENIALVPKLL------------KWPKEKIRERADELLALvgldPAEFADRYPHELSGGQQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILT 492
Cdd:cd03295 143 RVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
267-486 |
6.58e-25 |
|
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: 100.78 E-value: 6.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYIT 344
Cdd:cd00267 1 EIENLSFRygGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA-KLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 EsrrdngffpnfsiaqnmaisrslkdggykgamglfhevdeqrtaenqrellalkchsvnqniteLSGGNQQKVLISKWL 424
Cdd:cd00267 80 Q----------------------------------------------------------------LSGGQRQRVALARAL 95
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
Cdd:cd00267 96 LLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
21-227 |
8.60e-25 |
|
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: 101.45 E-value: 8.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIH--EPTKGTITINNISYNKLDHKLAAQLGIGIIYQELSVIDeltvl 98
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLGIFLAFQYPPEIP----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 99 enlyigrhltkkicGVNIIDwremrvraammLLRvglkvDLDEkvaNLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtn 178
Cdd:cd03217 91 --------------GVKNAD-----------FLR-----YVNE---GFSGGEKKRNEILQLLLLEPDLAILDEPDSGL-- 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131913 179 kEVDYLFLI---MNQLRKEGTAIVYISH--KLAEIRRIcDRYTVMKDGSSVCSG 227
Cdd:cd03217 136 -DIDALRLVaevINKLREEGKSVLIITHyqRLLDYIKP-DRVHVLYDGRIVKSG 187
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
267-490 |
8.97e-25 |
|
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: 102.41 E-value: 8.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVtSRDRK--KVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldaVKKGMAYIT 344
Cdd:cd03299 2 KVENL-SKDWKefKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP---EKRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 EsrrDNGFFPNFSIAQNMAisrslkdggYKGAMGLFHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWL 424
Cdd:cd03299 78 Q---NYALFPHMTVYKNIA---------YGLKKRKVDKKEIERKVLEIAEMLGID-HLLNRKPETLSGGEQQRVAIARAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIITVCDRIAVFCEGRLTQI 490
Cdd:cd03299 145 VVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVtVLHVTHDFEEAWALADKVAIMLNGKLIQV 211
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-221 |
9.04e-25 |
|
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: 102.23 E-value: 9.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNisynkldhKLAAQLGIGIIYQElsvidEL 95
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG--------RVSSLLGLGGGFNP-----EL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 96 TVLENLYIgrhltkkICGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
Cdd:cd03220 100 TGRENIYL-------NGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16131913 176 ltnkeVDYLFLI-----MNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:cd03220 173 -----GDAAFQEkcqrrLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKG 218
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-235 |
1.05e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 103.17 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIheptkgtITINNISYNKLD---------HKL 76
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL-------ITGDKSAGSHIEllgrtvqreGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 77 A-----AQLGIGIIYQELSVIDELTVLENLYIGRhLTKKICGVNIIDW--REMRVRAAMMLLRVGLKVDLDEKVANLSIS 149
Cdd:PRK09984 78 ArdirkSRANTGYIFQQFNLVNRLSVLENVLIGA-LGSTPFWRTCFSWftREQKQRALQALTRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 150 HKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDylfLIMNQLR----KEGTAIVYISHKLAEIRRICDRYTVMKDGSSVC 225
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESAR---IVMDTLRdinqNDGITVVVTLHQVDYALRYCERIVALRQGHVFY 233
|
250
....*....|
gi 16131913 226 SGIVSDVSND 235
Cdd:PRK09984 234 DGSSQQFDNE 243
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
21-221 |
2.66e-24 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 101.05 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL---GIGIIYQELSVIDELTV 97
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqKLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 98 LEN----LYIGRHLTKkicgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
Cdd:PRK11629 105 LENvampLLIGKKKPA-----------EINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16131913 174 SSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRIcDRYTVMKDG 221
Cdd:PRK11629 174 GNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRM-SRQLEMRDG 221
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
266-488 |
2.71e-24 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 99.04 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 266 FEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYI 343
Cdd:cd03216 1 LELRGITKRfgGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 344 TEsrrdngffpnfsiaqnmaisrslkdggykgamglfhevdeqrtaenqrellalkchsvnqniteLSGGNQQKVLISKW 423
Cdd:cd03216 81 YQ----------------------------------------------------------------LSVGERQMVEIARA 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLT 488
Cdd:cd03216 97 LARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
266-499 |
3.08e-24 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 100.87 E-value: 3.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 266 FEVRNVT---SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAvkkgmay 342
Cdd:COG1122 1 IELENLSfsyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLREL------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 itesRRDNGF-FPN-----FS------IA---QNMAISRSlkdggykgamglfhEVDEqRTAE--NQRELLALKchsvNQ 405
Cdd:COG1122 74 ----RRKVGLvFQNpddqlFAptveedVAfgpENLGLPRE--------------EIRE-RVEEalELVGLEHLA----DR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 406 NITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEG 485
Cdd:COG1122 131 PPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDG 210
|
250 260
....*....|....*....|
gi 16131913 486 RLT------QILTNRDDMSE 499
Cdd:COG1122 211 RIVadgtprEVFSDYELLEE 230
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
267-487 |
4.07e-24 |
|
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: 100.65 E-value: 4.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSP--LDAVKKGMAY 342
Cdd:cd03261 2 ELRGLTkSFGGRTVlKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaeLYRLRRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 ITESrrdNGFFPNFSIAQNMAisrslkdggykgamgLFHEVDEQRTAENQRELLALKCHSV------NQNITELSGGNQQ 416
Cdd:cd03261 82 LFQS---GALFDSLTVFENVA---------------FPLREHTRLSEEEIREIVLEKLEAVglrgaeDLYPAELSGGMKK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
274-479 |
4.96e-24 |
|
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: 99.64 E-value: 4.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 274 RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldavkkgmayitesRRDNGFF 353
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---------------RRKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 354 pnfsIAQNMA---ISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKchsvNQNITELSGGNQQKVLISKWLCCCPEV 430
Cdd:cd03226 76 ----VMQDVDyqlFTDSVREELLLGLKELDAGNEQAETVLKDLDLYALK----ERHPLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16131913 431 IIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRI 479
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRV 196
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-224 |
6.11e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 103.38 E-value: 6.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISynkLDHKLAAQL 80
Cdd:PRK11607 15 ALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD---LSHVPPYQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 81 GIGIIYQELSVIDELTVLENLYIGRHLTKKICGvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
Cdd:PRK11607 92 PINMMFQSYALFPHMTVEQNIAFGLKQDKLPKA-------EIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 161 MLDAKVIIMDEPTSSLTNKEVDYLFL-IMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
Cdd:PRK11607 165 AKRPKLLLLDEPMGALDKKLRDRMQLeVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-221 |
7.97e-24 |
|
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: 100.10 E-value: 7.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLGIgIIYQELSVIDELTV 97
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGV-VFGQKTQLWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 98 LENLYIGRHltkkICGVNIIDWREMRVRAAMMLlrvGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL- 176
Cdd:cd03267 113 IDSFYLLAA----IYDLPPARFKKRLDELSELL---DLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLd 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16131913 177 -TNKEVDYLFLIMNQlRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:cd03267 186 vVAQENIRNFLKEYN-RERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
20-221 |
8.67e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 104.86 E-value: 8.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHK-LAAQlgIGIIYQELSVIDElTVL 98
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLEsLRRQ--IGVVPQDTFLFSG-TIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 99 ENLYIGRhltkkicgvniIDWREMRVRAAMMLLRV---------GLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
Cdd:COG1132 432 ENIRYGR-----------PDATDEEVEEAAKAAQAhefiealpdGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILIL 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 170 DEPTSSLtnkevDYL--FLI---MNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDG 221
Cdd:COG1132 501 DEATSAL-----DTEteALIqeaLERLMKGRTTIV-IAHRLSTIRN-ADRILVLDDG 550
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
21-232 |
1.00e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.09 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKL-DHKLAAQLgiGIIYQELSVIDELTVLE 99
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLsSRQLARRL--ALLPQHHLTPEGITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 100 NLYIGR--HLTKkicgvniidW------REMRVRAAMMLLRVglkVDL-DEKVANLSISHKQMLEIAKTLMLDAKVIIMD 170
Cdd:PRK11231 96 LVAYGRspWLSL---------WgrlsaeDNARVNQAMEQTRI---NHLaDRRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131913 171 EPTSSL-TNKEVDyLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:PRK11231 164 EPTTYLdINHQVE-LMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-227 |
1.35e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 99.32 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYN---KLDHKLAAQL-- 80
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfskTPSDKAIRELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 81 GIGIIYQELSVIDELTVLENlyigrhLTKKICGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQN------LIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913 161 MLDAKVIIMDEPTSSL----TNKEVDylflIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:PRK11124 157 MMEPQVLLFDEPTAALdpeiTAQIVS----IIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
267-486 |
1.57e-23 |
|
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: 98.31 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT----SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKK-GMA 341
Cdd:cd03225 1 ELKNLSfsypDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 342 YiteSRRDNGFFpNFSIAQNMAISRslkdggykGAMGLFHEVDEQRTAE--NQRELLALKchsvNQNITELSGGNQQKVL 419
Cdd:cd03225 81 F---QNPDDQFF-GPTVEEEVAFGL--------ENLGLPEEEIEERVEEalELVGLEGLR----DRSPFTLSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 420 ISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-227 |
1.85e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 100.65 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKlaAQL 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH--ARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 81 GIGIIYQELSVIDELTVLENLYI-GRHLTkkicgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
Cdd:PRK13537 81 RVGVVPQFDNLDPDFTVRENLLVfGRYFG--------LSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:PRK13537 153 LVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
281-490 |
2.52e-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: 97.75 E-value: 2.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 281 DISFsVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGkdisprSPLDAVKKGMAYITESRR------DNGFFP 354
Cdd:cd03297 16 KIDF-DLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG------TVLFDSRKKINLPPQQRKiglvfqQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 355 NFSIAQNMAIsrslkdgGYKgamglFHEVDEQRTAENQR-ELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIF 433
Cdd:cd03297 89 HLNVRENLAF-------GLK-----RKRNREDRISVDELlDLLGLD-HLLNRYPAQLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 434 DEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
267-487 |
2.58e-23 |
|
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: 97.82 E-value: 2.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSRDRKK------VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLdAVKKGM 340
Cdd:cd03266 3 TADALTKRFRDVkktvqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV-KEPA-EARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 341 AYITESRrdnGFFPNFSIAQNMAIsrslkdggYKGAMGLfhevdeQRTAENQR-----ELLALKcHSVNQNITELSGGNQ 415
Cdd:cd03266 81 GFVSDST---GLYDRLTARENLEY--------FAGLYGL------KGDELTARleelaDRLGME-ELLDRRVGGFSTGMR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 416 QKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:cd03266 143 QKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
267-495 |
2.69e-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: 98.46 E-value: 2.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprSPLDAVKKGMAYIT 344
Cdd:cd03300 2 ELENVSKFygGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI---TNLPPHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 ESRrdnGFFPNFSIAQNMAISRSLKdggykgamGLFHEVDEQRTAEnQRELLALKCHSvNQNITELSGGNQQKVLISKWL 424
Cdd:cd03300 79 QNY---ALFPHLTVFENIAFGLRLK--------KLPKAEIKERVAE-ALDLVQLEGYA-NRKPSQLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEE 217
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
21-248 |
3.42e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 98.99 E-value: 3.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLD--HKLAAQLGIGIIYQE-LSVID-ELT 96
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraQRKAFRRDIQMVFQDsISAVNpRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 97 VLEnlYIG---RHLTKkicgvniIDWREMRVRAAMMLLRVGLKV-DLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
Cdd:PRK10419 108 VRE--IIReplRHLLS-------LDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 173 TSSLTnkevdyLFL---IMNQLRK----EGTAIVYISHKLAEIRRICDRYTVMKDGssvcsGIVSD--VSNDDIVRLMVG 243
Cdd:PRK10419 179 VSNLD------LVLqagVIRLLKKlqqqFGTACLFITHDLRLVERFCQRVMVMDNG-----QIVETqpVGDKLTFSSPAG 247
|
....*
gi 16131913 244 RELQN 248
Cdd:PRK10419 248 RVLQN 252
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-437 |
3.57e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.45 E-value: 3.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 8 MAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNisynkldhklaaQLGIGIIYQ 87
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------------GLRIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 88 ELSVIDELTVLENLYIG-----------RHLTKKICGVNIIDWR--------------EMRVRAAMMLLRVGLK-VDLDE 141
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGdaelraleaelEELEAKLAEPDEDLERlaelqeefealggwEAEARAEEILSGLGFPeEDLDR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 142 KVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYL--FLimnqLRKEGTAIVyISHklaeirricDRYTVmk 219
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLeeFL----KNYPGTVLV-VSH---------DRYFL-- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 220 DgsSVCSGIVsDVSNDDIvRLMVG------------RELQNRFNAMKENVsnLAHE------------------------ 263
Cdd:COG0488 213 D--RVATRIL-ELDRGKL-TLYPGnysayleqraerLEQEAAAYAKQQKK--IAKEeefirrfrakarkakqaqsrikal 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 264 ---------------------------TVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK 314
Cdd:COG0488 287 eklereepprrdktveirfppperlgkKVLELEGLSKSygDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 315 RAGGEIRLnGKDISprspldavkkgMAYITESRRDngFFPNFSIAQNMaisRSLKDGGYK-------GAMgLFHEvDEQR 387
Cdd:COG0488 367 PDSGTVKL-GETVK-----------IGYFDQHQEE--LDPDKTVLDEL---RDGAPGGTEqevrgylGRF-LFSG-DDAF 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 16131913 388 TAenqrellalkchsvnqnITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
Cdd:COG0488 428 KP-----------------VGVLSGGEKARLALAKLLLSPPNVLLLDEPT 460
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
279-492 |
3.61e-23 |
|
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: 98.87 E-value: 3.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS--PRSPLDAV-KKGMAYITESRrdnGFFPN 355
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAamSRKELRELrRKKISMVFQSF---ALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 356 FSIAQNMAISRSLKdggykgamGLFHEVDEQRtAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
Cdd:cd03294 117 RTVLENVAFGLEVQ--------GVPRAEREER-AAEALELVGLE-GWEHKYPDELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 436 PTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILT 492
Cdd:cd03294 187 AFSALDPLIRREMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGT 244
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
19-221 |
4.23e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 97.90 E-value: 4.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISynkLDHKLAAQLGIGIIYQELSVIDELTVL 98
Cdd:COG3840 13 DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD---LTALPPAERPVSMLFQENNLFPHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 99 ENLYIGRH----LTkkicgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
Cdd:COG3840 90 QNIGLGLRpglkLT-----------AEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16131913 175 SL-TNKEVDYLFLImNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:COG3840 159 ALdPALRQEMLDLV-DELCRErGLTVLMVTHDPEDAARIADRVLLVADG 206
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
10-239 |
4.83e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 97.79 E-value: 4.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLD-HKlAAQLGIGIIYQE 88
Cdd:COG1137 8 NLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmHK-RARLGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 89 LSVIDELTVLENLYIGRHLTKKicgvniiDWREMRVRaammllrvglkvdLDEKVANLSISH--KQM-----------LE 155
Cdd:COG1137 87 ASIFRKLTVEDNILAVLELRKL-------SKKEREER-------------LEELLEEFGITHlrKSKayslsggerrrVE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 156 IAKTLMLDAKVIIMDEPtssltnkevdylF------------LIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSS 223
Cdd:COG1137 147 IARALATNPKFILLDEP------------FagvdpiavadiqKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKV 214
|
250
....*....|....*.
gi 16131913 224 VCSGIVSDVSNDDIVR 239
Cdd:COG1137 215 LAEGTPEEILNNPLVR 230
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
279-437 |
6.89e-23 |
|
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: 94.64 E-value: 6.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRsPLDAVKKGMAYITEsrrDNGFFPNFSI 358
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDD-ERKSLRKEIGYVFQ---DPQLFPRLTV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 359 AQNMAISRSLKdggykgamGLFHEVDEQRTAENQREL--LALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
Cdd:pfam00005 77 RENLRLGLLLK--------GLSKREKDARAEEALEKLglGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
.
gi 16131913 437 T 437
Cdd:pfam00005 149 T 149
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-221 |
7.30e-23 |
|
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: 97.37 E-value: 7.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVH-ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDhklAAQL--GI 82
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQD---PVELrrKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 83 GIIYQELSVIDELTVLENlyIGrhLTKKICGvniidWREMRVRA-AMMLLRVglkVDLDEKV------ANLSISHKQMLE 155
Cdd:cd03295 78 GYVIQQIGLFPHMTVEEN--IA--LVPKLLK-----WPKEKIRErADELLAL---VGLDPAEfadrypHELSGGQQQRVG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 156 IAKTLMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNQlrKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALdpiTRDQLQEEFKRLQQ--ELGKTIVFVTHDIDEAFRLADRIAIMKNG 212
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
4-239 |
7.38e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 100.69 E-value: 7.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLgIG 83
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-VA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 84 IIYQELSVIDELTVLENLYIGR--HLTkKICGVNIIDWREmrVRAAMMllRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGRtpHRS-RFDTWTETDRAA--VERAME--RTGVAQFADRPVTSLSGGERQRVLLARALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 162 LDAKVIIMDEPTSSL-TNKEVDYLFLImNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVR 239
Cdd:PRK09536 156 QATPVLLLDEPTASLdINHQVRTLELV-RRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLR 233
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
10-224 |
1.01e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 98.88 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL--GIGIIYQ 87
Cdd:PRK11308 20 GLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLrqKIQIVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 88 --------ELSVIDELTvlENLYIGRHLTKKicgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANL-SISHKQMLEIAK 158
Cdd:PRK11308 100 npygslnpRKKVGQILE--EPLLINTSLSAA----------ERREKALAMMAKVGLRPEHYDRYPHMfSGGQRQRIAIAR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 159 TLMLDAKVIIMDEPTSSL-TNKEVDYLFLIMNqLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALdVSVQAQVLNLMMD-LQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCV 234
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-231 |
1.02e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 101.72 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 3 TPYISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAA 78
Cdd:PRK10535 2 TALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 79 QL---GIGIIYQELSVIDELTVLEN-----LYIGrhltkkicgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISH 150
Cdd:PRK10535 82 QLrreHFGFIFQRYHLLSHLTAAQNvevpaVYAG------------LERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 151 KQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKlAEIRRICDRYTVMKDGSsvcsgIVS 230
Cdd:PRK10535 150 QQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGE-----IVR 223
|
.
gi 16131913 231 D 231
Cdd:PRK10535 224 N 224
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-222 |
1.57e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 98.24 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQlgIGII-------YQELS 90
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARR--IGVVfgqrsqlWWDLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 91 VIDELTVLenlyigrhltKKICGvniIDWREMRVRAAMM--LLRVGLKvdLDEKVANLSISHKQMLEIAKTLMLDAKVII 168
Cdd:COG4586 113 AIDSFRLL----------KAIYR---IPDAEYKKRLDELveLLDLGEL--LDTPVRQLSLGQRMRCELAAALLHRPKILF 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 169 MDEPTSSL--TNKEVDYLFLI-MNqlRKEGTAIVYISHKLAEIRRICDRYTVMKDGS 222
Cdd:COG4586 178 LDEPTIGLdvVSKEAIREFLKeYN--RERGTTILLTSHDMDDIEALCDRVIVIDHGR 232
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
6-227 |
2.06e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 96.36 E-value: 2.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKlDHKLAAQLG---- 81
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDT-ARSLSQQKGlirq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 82 ----IGIIYQELSVIDELTVLENLYIGRHLTKKIcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIA 157
Cdd:PRK11264 83 lrqhVGFVFQNFNLFPHRTVLENIIEGPVIVKGE------PKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 158 KTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-221 |
2.80e-22 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 95.54 E-value: 2.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYN--KLDHKLAAQLGiG 83
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEA-G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 84 IIYQELSVIDELTVLENLYIG----RHLTKKicgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGplrvRGASKE----------EAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131913 160 LMLDAKVIIMDEPTSSLtNKEVDYLFL-IMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:PRK09493 151 LAVKPKLMLFDEPTSAL-DPELRHEVLkVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKG 212
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-232 |
2.96e-22 |
|
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: 95.48 E-value: 2.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKlaaQLGIGIIYQELSVIDELTVLEN 100
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE---KRDISYVPQNYALFPHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 101 LYIGRHLtKKICGVNIidwrEMRVR--AAMMllrvGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTN 178
Cdd:cd03299 92 IAYGLKK-RKVDKKEI----ERKVLeiAEML----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 179 KEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:cd03299 163 RTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV 217
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-232 |
4.04e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 96.27 E-value: 4.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLA---AQLGIGIIYQELSVIDElT 96
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSdirKKVGLVFQYPEYQLFEE-T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 97 VLENLYIG---RHLTKkicgvniiDWREMRVRAAMMLlrVGLKVD--LDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
Cdd:PRK13637 101 IEKDIAFGpinLGLSE--------EEIENRVKRAMNI--VGLDYEdyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 172 PTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:PRK13637 171 PTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
16-233 |
4.51e-22 |
|
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: 99.49 E-value: 4.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN------NISYNKLDHKLAAQLGIGIIYQEL 89
Cdd:TIGR03269 295 GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvDMTKPGPDGRGRAKRYIGILHQEY 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 90 SVIDELTVLENlyigrhLTKKIcGVNIIDwrEMRVRAAMMLLRVglkVDLDEKVA---------NLSISHKQMLEIAKTL 160
Cdd:TIGR03269 375 DLYPHRTVLDN------LTEAI-GLELPD--ELARMKAVITLKM---VGFDEEKAeeildkypdELSEGERHRVALAQVL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 161 MLDAKVIIMDEPTSSLTN-KEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG----IVSDVS 233
Cdd:TIGR03269 443 IKEPRIVILDEPTGTMDPiTKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGdpeeIVEELT 520
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
20-205 |
4.90e-22 |
|
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: 99.36 E-value: 4.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLgIGIIYQELSVIDElTVLE 99
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR-VSVCAQDAHLFDT-TVRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 100 NLYIGR------HLTKKICGVNIIDWremrVRAammlLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
Cdd:TIGR02868 428 NLRLARpdatdeELWAALERVGLADW----LRA----LPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|..
gi 16131913 174 SSLTNKEVDYLFLIMNQLrKEGTAIVYISHKL 205
Cdd:TIGR02868 500 EHLDAETADELLEDLLAA-LSGRTVVLITHHL 530
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-227 |
5.80e-22 |
|
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: 94.10 E-value: 5.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 26 LTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDhklAAQLGIGIIYQELSVIDELTVLENLYIGR 105
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP---PADRPVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 106 ----HLTKkicgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEV 181
Cdd:cd03298 96 spglKLTA-----------EDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16131913 182 DYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:cd03298 165 AEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
267-487 |
6.25e-22 |
|
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: 93.82 E-value: 6.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprSPLDAVKKgMAYIT 344
Cdd:cd03268 2 KTNDLTKTygKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRR-IGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 ESrrdNGFFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQrtaenqrellalkcHSVNQNITELSGGNQQKVLISKWL 424
Cdd:cd03268 79 EA---PGFYPNLTARENLRLLARLLGIRKKRIDEVLDVVGLK--------------DSAKKKVKGFSLGMKQRLGIALAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131913 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:cd03268 142 LGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
16-227 |
6.71e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 96.51 E-value: 6.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPtKGTITINNISYNKLD-HKLAAQ-----LG--IGIIYQ 87
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKD-NWHVTADRFRWNGIDlLKLSPRerrkiIGreIAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 88 E-LSVIDeltvlENLYIGRHLTKKI----CGVNIIDWREMRVRAAMMLL-RVGLKvdlDEKVANLSISHK------QMLE 155
Cdd:COG4170 97 EpSSCLD-----PSAKIGDQLIEAIpswtFKGKWWQRFKWRKKRAIELLhRVGIK---DHKDIMNSYPHEltegecQKVM 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 156 IAKTLMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNQLRkeGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:COG4170 169 IAMAIANQPRLLIADEPTNAMestTQAQIFRLLARLNQLQ--GTSILLISHDLESISQWADTITVLYCGQTVESG 241
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-227 |
9.05e-22 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 94.14 E-value: 9.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLD-HKLAAQlgIGIIYQElSVIDELT 96
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNlRWLRSQ--IGLVSQE-PVLFDGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 97 VLENLYIGRHLTKkicgvniidwREMRVRAA--------MMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVII 168
Cdd:cd03249 93 IAENIRYGKPDAT----------DEEVEEAAkkanihdfIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 169 MDEPTSSLTN---KEVDYLFlimNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSG 227
Cdd:cd03249 163 LDEATSALDAeseKLVQEAL---DRAMKGRTTIV-IAHRLSTIRN-ADLIAVLQNGQVVEQG 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-221 |
1.21e-21 |
|
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: 93.94 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDhklAAQLGIGII 85
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP---VQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 86 YQELSVIDELTVLENLYIGRHLTKKicgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVKPR---SERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKG 213
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
20-221 |
1.37e-21 |
|
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: 93.45 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN--NISYNKLdHKLAAQlgIGIIYQELSVIDElTV 97
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDghDVRDYTL-ASLRRQ--IGLVSQDVFLFND-TV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 98 LENLYIGRHltkkicgvniiDWREMRVRAA---------MMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVII 168
Cdd:cd03251 93 AENIAYGRP-----------GATREEVEEAaraanahefIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131913 169 MDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRIcDRYTVMKDG 221
Cdd:cd03251 162 LDEATSALDTESERLVQAALERLMKNRTTFV-IAHRLSTIENA-DRIVVLEDG 212
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-490 |
1.68e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 98.00 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 16 GPVHALKSVNLTVYPGEIHALLGENGAGKS----TLMKVL--SG---------IHEPTKGTITINNISYNKLDHKLAAQl 80
Cdd:PRK10261 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGglvqcdkmlLRRRSRQVIELSEQSAAQMRHVRGAD- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 81 gIGIIYQElsvidELTVLENLY-IGRHLTKKICGVNIIDWREMRVRAAMMLLRVGL---KVDLDEKVANLSISHKQMLEI 156
Cdd:PRK10261 106 -MAMIFQE-----PMTSLNPVFtVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 157 AKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSND 235
Cdd:PRK10261 180 AMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 236 D-----------IVRL--MVGRELQNRF-----------NAMKENVSNLAHETVFEVRNVTSR--------DRKK----- 278
Cdd:PRK10261 260 PqhpytrallaaVPQLgaMKGLDYPRRFplislehpakqEPPIEQDTVVDGEPILQVRNLVTRfplrsgllNRVTrevha 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK--DISPRSPLDAVKKGMAYITESrrdngffPNF 356
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQriDTLSPGKLQALRRDIQFIFQD-------PYA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 357 SIAQNMAISRSLKDGgyKGAMGLFHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
Cdd:PRK10261 413 SLDPRQTVGDSIMEP--LRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEA 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 437 TRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEI 545
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
263-488 |
1.95e-21 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 92.80 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 263 ETVFEVRNVT------SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS--PRSPLD 334
Cdd:COG1136 2 SPLLELRNLTksygtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISslSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 335 AVkkgmayitesRRDN-GF-------FPNFSIAQNMAISRSLKdggykgamGLFHEVDEQRTaenqRELLA---LKcHSV 403
Cdd:COG1136 82 RL----------RRRHiGFvfqffnlLPELTALENVALPLLLA--------GVSRKERRERA----RELLErvgLG-DRL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 404 NQNITELSGGNQQKV-----LISKwlcccPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSElPEIITVCD 477
Cdd:COG1136 139 DHRPSQLSGGQQQRVaiaraLVNR-----PKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHD-PELAARAD 212
|
250
....*....|.
gi 16131913 478 RIAVFCEGRLT 488
Cdd:COG1136 213 RVIRLRDGRIV 223
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-235 |
2.58e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 93.45 E-value: 2.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTitinnISYNKLDHKLA--A 78
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGE-----VHYRMRDGQLRdlY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 79 QLG-----------IGIIYQE------LSVIDELTVLENLY-IG-RHltkkicgvniidWREMRVRAAMMLLRVGLKVD- 138
Cdd:PRK11701 77 ALSeaerrrllrteWGFVHQHprdglrMQVSAGGNIGERLMaVGaRH------------YGDIRATAGDWLERVEIDAAr 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 139 LDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL-TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTV 217
Cdd:PRK11701 145 IDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLdVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLV 224
|
250
....*....|....*...
gi 16131913 218 MKDGSSVCSGIVSDVSND 235
Cdd:PRK11701 225 MKQGRVVESGLTDQVLDD 242
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-238 |
3.04e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 93.65 E-value: 3.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLgIGIIYQELSviDEL--- 95
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSK-VGLVFQDPD--DQVfss 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 96 TVLENLYIGRhltkkicgVNI-IDWREMRVRAAMMLLRVGLKvDLDEKVA-NLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
Cdd:PRK13647 96 TVWDDVAFGP--------VNMgLDKDEVERRVEEALKAVRMW-DFRDKPPyHLSYGQKKRVAIAGVLAMDPDVIVLDEPM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 174 SSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIV 238
Cdd:PRK13647 167 AYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIV 231
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
266-490 |
3.15e-21 |
|
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: 92.24 E-value: 3.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 266 FEVRNVT--SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCL-----FGVDKRAGGEIRLNGKDI-SPRSPLDAVK 337
Cdd:cd03260 1 IELRDLNvyYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIyDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 338 K--GMAYitesRRDNGFfpNFSIAQNMAISrsLKDGGYKGAMGLfHEVDEQ--RTAENQRELLAlkchsvNQNITELSGG 413
Cdd:cd03260 81 RrvGMVF----QKPNPF--PGSIYDNVAYG--LRLHGIKLKEEL-DERVEEalRKAALWDEVKD------RLHALGLSGG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 414 NQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEF 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-221 |
3.16e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 96.67 E-value: 3.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTItinnisynkldhKLAAQLGIGII 85
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV------------KLGETVKIGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 86 YQELSVID-ELTVLENLyigRHLTKkicgvniiDWREMRVRAamMLLRVGLKVD-LDEKVANLSISHKQMLEIAKTLMLD 163
Cdd:COG0488 384 DQHQEELDpDKTVLDEL---RDGAP--------GGTEQEVRG--YLGRFLFSGDdAFKPVGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913 164 AKVIIMDEPT-----SSLTnkevdylfLIMNQLRK-EGTAIVyISHKLAEIRRICDRYTVMKDG 221
Cdd:COG0488 451 PNVLLLDEPTnhldiETLE--------ALEEALDDfPGTVLL-VSHDRYFLDRVATRILEFEDG 505
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
24-485 |
4.18e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 96.31 E-value: 4.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 24 VNLTVYPGEIHALLGENGAGKS-TLMKVLSGIHEP----TKGTITINNISYNKLDHKLAAQL---GIGIIYQELSVidEL 95
Cdd:PRK15134 28 VSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVrgnKIAMIFQEPMV--SL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 96 TVLENlyigrhLTKKICGVNIIDwREMRVRAAM-----MLLRVGL---KVDLDEKVANLSISHKQMLEIAKTLMLDAKVI 167
Cdd:PRK15134 106 NPLHT------LEKQLYEVLSLH-RGMRREAARgeilnCLDRVGIrqaAKRLTDYPHQLSGGERQRVMIAMALLTRPELL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 168 IMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSV----CSGIVSDVSNDDIVRLM- 241
Cdd:PRK15134 179 IADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVeqnrAATLFSAPTHPYTQKLLn 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 242 ---VGRELQ-NRFNAMKENVSNLahETVFEVRNVTSR---DRKKV-RDISFSVCRGEILGFAGLVGSGRT----ELMNCL 309
Cdd:PRK15134 259 sepSGDPVPlPEPASPLLDVEQL--QVAFPIRKGILKrtvDHNVVvKNISFTLRPGETLGLVGESGSGKSttglALLRLI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 310 fgvdkRAGGEIRLNGKdisprsPLDAV-KKGMayITESRRDNGFF--PNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQ 386
Cdd:PRK15134 337 -----NSQGEIWFDGQ------PLHNLnRRQL--LPVRHRIQVVFqdPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQREQ 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 387 RTAENQRElLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMV 465
Cdd:PRK15134 404 QVIAVMEE-VGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLaYLFI 482
|
490 500
....*....|....*....|
gi 16131913 466 SSELPEIITVCDRIAVFCEG 485
Cdd:PRK15134 483 SHDLHVVRALCHQVIVLRQG 502
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
20-239 |
6.11e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 92.45 E-value: 6.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI--NNISYNKLDhKLAAQLGIGIIYQELSviDEL-- 95
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkgEPIKYDKKS-LLEVRKTVGIVFQNPD--DQLfa 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 96 -TVLENLYIG---RHLTKkicgvniiDWREMRVRAAmmLLRVGLKvDLDEKVA-NLSISHKQMLEIAKTLMLDAKVIIMD 170
Cdd:PRK13639 94 pTVEEDVAFGplnLGLSK--------EEVEKRVKEA--LKAVGME-GFENKPPhHLSGGQKKRVAIAGILAMKPEIIVLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 171 EPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV-SNDDIVR 239
Cdd:PRK13639 163 EPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVfSDIETIR 232
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
20-218 |
1.15e-20 |
|
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: 95.05 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIsynKLDHKLAAQLGIGIIY-QELSVIDELTVL 98
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGV---PLADADADSWRDQIAWvPQHPFLFAGTIA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 99 ENLYIGRHltkkicgvniiDWREMRVRAAMML---------LRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
Cdd:TIGR02857 414 ENIRLARP-----------DASDAEIREALERagldefvaaLPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLL 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16131913 170 DEPTSSL---TNKEVDYlflIMNQLRkEGTAIVYISHKLAEIRRiCDRYTVM 218
Cdd:TIGR02857 483 DEPTAHLdaeTEAEVLE---ALRALA-QGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
21-243 |
1.34e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 91.39 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQlGIGIIYQELSVIDELTVLEN 100
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR-KVAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 101 LYIGRHLTKKICGVNIIDWREmRVRAAMMLlrVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL-TNK 179
Cdd:PRK10575 106 VAIGRYPWHGALGRFGAADRE-KVEEAISL--VGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALdIAH 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913 180 EVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRLMVG 243
Cdd:PRK10575 183 QVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYG 246
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
267-487 |
1.65e-20 |
|
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: 90.12 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSplDAVKKGMAYIT 344
Cdd:cd03265 2 EVENLVKKygDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP--REVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 ESRR-DNGffpnFSIAQNMAISRSLKdgGYKGAmglfheVDEQRTAENQR--ELLALKchsvNQNITELSGGNQQKVLIS 421
Cdd:cd03265 80 QDLSvDDE----LTGWENLYIHARLY--GVPGA------ERRERIDELLDfvGLLEAA----DRLVKTYSGGMRRRLEIA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:cd03265 144 RSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-232 |
1.68e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 91.45 E-value: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN--ISYNKlDHKLAAQLGIGIIYQEL-SVIDEL 95
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSR-KGLMKLRESVGMVFQDPdNQLFSA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 96 TVLENLYIGrhltkkicGVNI-IDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
Cdd:PRK13636 99 SVYQDVSFG--------AVNLkLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 175 SLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:PRK13636 171 GLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
266-487 |
2.11e-20 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 89.49 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 266 FEVRNVTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgMAYI 343
Cdd:COG4619 1 LELEGLSFRVGGKPilSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQ-VAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 344 tesRRDNGFFPNfSIAQNMAISRSLKDggykgamglfhevdEQRTAENQRELLA---LKCHSVNQNITELSGGNQQKVLI 420
Cdd:COG4619 80 ---PQEPALWGG-TVRDNLPFPFQLRE--------------RKFDRERALELLErlgLPPDILDKPVERLSGGERQRLAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:COG4619 142 IRALLLQPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
20-235 |
2.49e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 90.96 E-value: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTIT-----INNISYNKLDHKLAAQLGIGIIYQELSVIDE 94
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRvddtlITSTSKNKDIKQIRKKVGLVFQFPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 95 lTVLENLYIGrhltKKICGVNIIdwrEMRVRAAMMLLRVGLKVDLDEKvANLSISHKQM--LEIAKTLMLDAKVIIMDEP 172
Cdd:PRK13649 102 -TVLKDVAFG----PQNFGVSQE---EAEALAREKLALVGISESLFEK-NPFELSGGQMrrVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131913 173 TSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSND 235
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-240 |
2.70e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 90.84 E-value: 2.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIsynKLDHKLAAQL--GIGIIYQE-------LS 90
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWDVrrQVGMVFQNpdnqfvgAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 91 VIDELTV-LENLYIGRHltkkicgvniidwrEM--RVRAAmmLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVI 167
Cdd:PRK13635 99 VQDDVAFgLENIGVPRE--------------EMveRVDQA--LRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 168 IMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVY-ISHKLAEIRRiCDRYTVMKDGSSVCSGIVSDV--SNDDIVRL 240
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLKEQKGITVLsITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIfkSGHMLQEI 237
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-221 |
3.20e-20 |
|
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: 89.09 E-value: 3.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLD-HKLAAQlgIGIIYQElSVIDELTVL 98
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGlHDLRSR--ISIIPQD-PVLFSGTIR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 99 ENL-YIGRHLTKKIcgvniidWR---EMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
Cdd:cd03244 96 SNLdPFGEYSDEEL-------WQaleRVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16131913 175 SltnkeVDYLF--LIMNQLRKE--GTAIVYISHKLAEIrrI-CDRYTVMKDG 221
Cdd:cd03244 169 S-----VDPETdaLIQKTIREAfkDCTVLTIAHRLDTI--IdSDRILVLDKG 213
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-224 |
4.05e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 90.61 E-value: 4.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIS-YNKLDHKLAAQL--GIGIIYQ-ELSVIDEL 95
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITiTHKTKDKYIRPVrkRIGMVFQfPESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 96 TVLENLYIGrhltKKICGVNIidwREMRVRAAMMLLRVGLKVDLDEKvANLSISHKQMLEIAKT--LMLDAKVIIMDEPT 173
Cdd:PRK13646 102 TVEREIIFG----PKNFKMNL---DEVKNYAHRLLMDLGFSRDVMSQ-SPFQMSGGQMRKIAIVsiLAMNPDIIVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16131913 174 SSLTNKEVDYLFLIMNQLR-KEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIV 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-221 |
4.21e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 89.64 E-value: 4.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYN---------K 71
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 72 LDHKLAAQL---GIGIIYQELSVIDELTVLENLYigrHLTKKICGVNIIDWREmrvRAAMMLLRVGLKVDLDEKV-ANLS 147
Cdd:PRK10619 81 VADKNQLRLlrtRLTMVFQHFNLWSHMTVLENVM---EAPIQVLGLSKQEARE---RAVKYLAKVGIDERAQGKYpVHLS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913 148 ISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:PRK10619 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQG 228
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-227 |
4.22e-20 |
|
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: 94.70 E-value: 4.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 4 PYISMAGIGKSFGPVH--ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI--NNISYNkLDhklAAQ 79
Cdd:TIGR01257 927 PGVCVKNLVKIFEPSGrpAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVggKDIETN-LD---AVR 1002
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 80 LGIGIIYQELSVIDELTVLENLYIGRHLTKKicgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
Cdd:TIGR01257 1003 QSLGMCPQHNILFHHLTVAEHILFYAQLKGR-------SWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIA 1075
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRkEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:TIGR01257 1076 FVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
20-233 |
5.53e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.05 E-value: 5.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLGIGIIYQ--ELSVIDElTV 97
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQnpETQFVGR-TV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 98 LENLYIGrhlTKKICGVNIidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLT 177
Cdd:PRK13644 96 EEDLAFG---PENLCLPPI----EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 178 NKEVDYLFLIMNQLRKEGTAIVYISHKLAEIrRICDRYTVMKDGSSVCSG----IVSDVS 233
Cdd:PRK13644 169 PDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGepenVLSDVS 227
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
267-486 |
5.89e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 90.17 E-value: 5.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPrspldAVKKGMAYIT 344
Cdd:COG4152 3 ELKGLTKRfgDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP-----EDRRRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 ESRrdnGFFPNFSIAQNMAisrslkdggYkgaMGLFHEVDEQRTAENQRELLA---LKcHSVNQNITELSGGNQQKV--- 418
Cdd:COG4152 78 EER---GLYPKMKVGEQLV---------Y---LARLKGLSKAEAKRRADEWLErlgLG-DRANKKVEELSKGNQQKVqli 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 419 --LISKwlcccPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
Cdd:COG4152 142 aaLLHD-----PELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGR 206
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
267-487 |
5.91e-20 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 88.79 E-value: 5.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT------SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSP--LDAVKK 338
Cdd:cd03258 3 ELKNVSkvfgdtGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGkeLRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 339 GMAYItesrrdngfFPNF------SIAQNMAIsrSLKDGGYKGAmglfhEVDEQrtaenQRELLALK--CHSVNQNITEL 410
Cdd:cd03258 83 RIGMI---------FQHFnllssrTVFENVAL--PLEIAGVPKA-----EIEER-----VLELLELVglEDKADAYPAQL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 411 SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:cd03258 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
281-490 |
5.96e-20 |
|
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: 91.33 E-value: 5.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK---DISPRSPLDAVKKGMAYITESRRdngFFPNFS 357
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfDSRKGIFLPPEKRRIGYVFQEAR---LFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 358 IAQNMAIsrslkdgGYKGAMGLFHEVDEQRTAEnqreLLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
Cdd:TIGR02142 92 VRGNLRY-------GMKRARPSERRISFERVIE----LLGIG-HLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131913 438 RGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIITVCDRIAVFCEGRLTQI 490
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAEFGIpILYVSHSLQEVLRLADRVVVLEDGRVAAA 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
261-487 |
6.68e-20 |
|
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: 88.88 E-value: 6.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 261 AHETVFEVRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS--PRSPLDAV 336
Cdd:COG1127 1 MSEPMIEVRNLTkSFGDRVVlDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 337 KK--GMAYitesrRDNGFFPNFSIAQNMA--------ISRSLKdggykgamglfhevdeqrtaenqRELLALKCHSV--- 403
Cdd:COG1127 81 RRriGMLF-----QGGALFDSLTVFENVAfplrehtdLSEAEI-----------------------RELVLEKLELVglp 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 404 ---NQNITELSGGNQQKV-----LISKwlcccPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIIT 474
Cdd:COG1127 133 gaaDKMPSELSGGMRKRValaraLALD-----PEILLYDEPTAGLDPITSAVIDELIRELRDELGLtSVVVTHDLDSAFA 207
|
250
....*....|...
gi 16131913 475 VCDRIAVFCEGRL 487
Cdd:COG1127 208 IADRVAVLADGKI 220
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-221 |
8.18e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 91.16 E-value: 8.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDhklAAQL 80
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP---AENR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 81 GIGIIYQELSVIDELTVLENLYIGRHLtKKICGVNIidwrEMRVRAAMMLLRvgLKVDLDEKVANLSISHKQMLEIAKTL 160
Cdd:PRK09452 87 HVNTVFQSYALFPHMTVFENVAFGLRM-QKTPAAEI----TPRVMEALRMVQ--LEEFAQRKPHQLSGGQQQRVAIARAV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 161 MLDAKVIIMDEPTSSLtnkevDY-LFLIM-NQL----RKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:PRK09452 160 VNKPKVLLLDESLSAL-----DYkLRKQMqNELkalqRKLGITFVFVTHDQEEALTMSDRIVVMRDG 221
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-222 |
8.61e-20 |
|
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: 88.26 E-value: 8.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 3 TPYISMAGIGKSF-----GPV--HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNiSYNKLDhk 75
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqGGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRH-DGGWVD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 76 LAA----------QLGIGIIYQELSVIDELT----VLENLyigRHLtkkicGVniiDWREMRVRAAMMLLRVGLKvdldE 141
Cdd:COG4778 79 LAQaspreilalrRRTIGYVSQFLRVIPRVSaldvVAEPL---LER-----GV---DREEARARARELLARLNLP----E 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 142 KVANLSIS-----HKQMLEIAKTLMLDAKVIIMDEPTSSL--TNKEV--DylflIMNQLRKEGTAIVYISHKLAEIRRIC 212
Cdd:COG4778 144 RLWDLPPAtfsggEQQRVNIARGFIADPPLLLLDEPTASLdaANRAVvvE----LIEEAKARGTAIIGIFHDEEVREAVA 219
|
250
....*....|
gi 16131913 213 DRYTVMKDGS 222
Cdd:COG4778 220 DRVVDVTPFS 229
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-224 |
1.03e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 88.40 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 81 GIGIIYQELSVIDELTVLENLYIGRHLTKKicgvniIDWREMRVRAAMMLLRvgLKVDLDEKVANLSISHKQMLEIAKTL 160
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEENLAMGGFFAER------DQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
266-487 |
1.49e-19 |
|
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: 87.20 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 266 FEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSP-LDAVKKGMAY 342
Cdd:cd03262 1 IEIKNLHKSfgDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKnINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 ITESrrdngF--FPNFSIAQNMAIsrslkdggykgAMGLFHEVDEQRTAENQRELLA---LKcHSVNQNITELSGGNQQK 417
Cdd:cd03262 81 VFQQ-----FnlFPHLTVLENITL-----------APIKVKGMSKAEAEERALELLEkvgLA-DKADAYPAQLSGGQQQR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 418 VLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:cd03262 144 VAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-232 |
2.04e-19 |
|
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: 91.28 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 12 GKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHePTKGTITINNISYNKLDHK--LAAQLGIGIIYQE- 88
Cdd:COG4172 293 RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRalRPLRRRMQVVFQDp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 89 -------LSVidELTVLENLYI-GRHLTKkicgvniidwREMRVRAAMMLLRVGlkvdLDEKVAN-----LSISHKQMLE 155
Cdd:COG4172 372 fgslsprMTV--GQIIAEGLRVhGPGLSA----------AERRARVAEALEEVG----LDPAARHrypheFSGGQRQRIA 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 156 IAKTLMLDAKVIIMDEPTSSL---TNKEVdyLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:COG4172 436 IARALILEPKLLVLDEPTSALdvsVQAQI--LDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-227 |
3.44e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 90.94 E-value: 3.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHK-LAAQlgIGIIYQElSVIDELTVLE 99
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHyLHRQ--VALVGQE-PVLFSGSVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 100 NlyIGRHLTKKicgvniiDWREMRVRAAM-------MLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
Cdd:TIGR00958 574 N--IAYGLTDT-------PDEEIMAAAKAanahdfiMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEA 644
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 173 TSSLtNKEVDYLFLIMNQlRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSG 227
Cdd:TIGR00958 645 TSAL-DAECEQLLQESRS-RASRTVLL-IAHRLSTVER-ADQILVLKKGSVVEMG 695
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
267-490 |
3.85e-19 |
|
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: 85.77 E-value: 3.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkKGMAYIT 344
Cdd:cd03301 2 ELENVTKRfgNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD---RDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 ESRrdnGFFPNFSIAQNMAISRSLKDGGYKgamglfhEVDEQ--RTAenqrELLALKcHSVNQNITELSGGNQQKVLISK 422
Cdd:cd03301 79 QNY---ALYPHMTVYDNIAFGLKLRKVPKD-------EIDERvrEVA----ELLQIE-HLLDRKPKQLSGGQRQRVALGR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 423 WLCCCPEVIIFDEPTRGID----VGAKAEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMNDGQIQQI 212
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
271-490 |
4.04e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.52 E-value: 4.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 271 VTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgmayITESRRDN 350
Cdd:PRK09536 11 VEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR----VASVPQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 351 GFFPNFSIAQNMAISRSlkdgGYKGAMGLFHEVDEQ--RTAENQRELLALkchsVNQNITELSGGNQQKVLISKWLCCCP 428
Cdd:PRK09536 87 SLSFEFDVRQVVEMGRT----PHRSRFDTWTETDRAavERAMERTGVAQF----ADRPVTSLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 429 EVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
Cdd:PRK09536 159 PVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAA 220
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-232 |
5.26e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 86.77 E-value: 5.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLgIGIIYQelsviDELTV 97
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQR-IRMIFQ-----DPSTS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 98 LE-NLYIGRHLTKKICGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN-LSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
Cdd:PRK15112 100 LNpRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHmLAPGQKQRLGLARALILRPKVIIADEALAS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 176 LTNKEVDYLFLIMNQLR-KEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:PRK15112 180 LDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADV 237
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-247 |
5.27e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 86.10 E-value: 5.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 1 MATpyISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL 80
Cdd:PRK10895 1 MAT--LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 81 GIGIIYQELSVIDELTVLENLY----IGRHLTKKicgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEI 156
Cdd:PRK10895 79 GIGYLPQEASIFRRLSVYDNLMavlqIRDDLSAE----------QREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 157 AKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDD 236
Cdd:PRK10895 149 ARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
250
....*....|..
gi 16131913 237 IV-RLMVGRELQ 247
Cdd:PRK10895 229 HVkRVYLGEDFR 240
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
266-487 |
5.72e-19 |
|
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: 84.91 E-value: 5.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 266 FEVRNVTSRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAG--GEIRLNGKDISPRSPldavKKGMAY 342
Cdd:cd03213 11 VTVKSSPSKSGKQLlKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSF----RKIIGY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 ItesRRDNGFFPNFSIAQNMAISrslkdggykgamglfhevdeqrtaenqrelLALKChsvnqniteLSGGNQQKVLISK 422
Cdd:cd03213 87 V---PQDDILHPTLTVRETLMFA------------------------------AKLRG---------LSGGERKRVSIAL 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMV----SSelpEIITVCDRIAVFCEGRL 487
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSihqpSS---EIFELFDKLLLLSQGRV 190
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
263-486 |
6.19e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 87.55 E-value: 6.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 263 ETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGM 340
Cdd:PRK13537 5 VAPIDFRNVEKRygDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 341 AyiteSRRDNgFFPNFSIAQNMAISrslkdGGYKGAmglfhevdeqrTAENQRELL------ALKCHSVNQNITELSGGN 414
Cdd:PRK13537 85 V----PQFDN-LDPDFTVRENLLVF-----GRYFGL-----------SAAAARALVppllefAKLENKADAKVGELSGGM 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 415 QQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
Cdd:PRK13537 144 KRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
267-495 |
6.94e-19 |
|
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: 85.85 E-value: 6.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkkgmayit 344
Cdd:cd03296 4 EVRNVSKRfgDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 esrRDNGF-FPNFSIAQNMAISRSLkdggykgAMGLFHEVDEQRTAENQ-----RELLALKCHS--VNQNITELSGGNQQ 416
Cdd:cd03296 74 ---RNVGFvFQHYALFRHMTVFDNV-------AFGLRVKPRSERPPEAEirakvHELLKLVQLDwlADRYPAQLSGGQRQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
Cdd:cd03296 144 RVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDE 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
267-489 |
6.98e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 85.91 E-value: 6.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDisprspldaVKKGMAYIT 344
Cdd:PRK09493 3 EFKNVSKHfgPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLK---------VNDPKVDER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 ESRRDNG-------FFPNFSIAQNMAISRSLKDGGYKGAmglfhevdeqrtAENQ-RELLA---LKCHSvNQNITELSGG 413
Cdd:PRK09493 74 LIRQEAGmvfqqfyLFPHLTALENVMFGPLRVRGASKEE------------AEKQaRELLAkvgLAERA-HHYPSELSGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 414 NQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
Cdd:PRK09493 141 QQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAE 216
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-243 |
7.85e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 89.34 E-value: 7.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 22 KSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLdhKLAAQLGIGIIYqelsvIDELTVLENL 101
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINAL--STAQRLARGLVY-----LPEDRQSSGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 102 YIGRHLTKKICGVNIID---W----REMRV----RAAMmllrvGLKV-DLDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
Cdd:PRK15439 353 YLDAPLAWNVCALTHNRrgfWikpaRENAVleryRRAL-----NIKFnHAEQAARTLSGGNQQKVLIAKCLEASPQLLIV 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 170 DEPTssltnKEVDY-----LFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRLMVG 243
Cdd:PRK15439 428 DEPT-----RGVDVsarndIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVDTIMRLAFG 501
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-232 |
8.42e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 85.73 E-value: 8.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE-----PTKGTITINNISYNKLDHKLAAQL 80
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 81 gIGIIYQELSVIDELTVLENLYIGRHLTKKicgVNIIDWREMRVRAAM--MLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
Cdd:PRK14247 84 -VQMVFQIPNPIPNLSIFENVALGLKLNRL---VKSKKELQERVRWALekAQLWDEVKDRLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 159 TLMLDAKVIIMDEPTSSL---TNKEVDYLFLimnQLRKEGTaIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLdpeNTAKIESLFL---ELKKDMT-IVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
19-227 |
1.40e-18 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 83.52 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQlgIGIIYQELSVIDElTVL 98
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSL--ISVLNQRPYLFDT-TLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 99 ENLyiGRHltkkicgvniidwremrvraammllrvglkvdldekvanLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTN 178
Cdd:cd03247 93 NNL--GRR---------------------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16131913 179 K-EVDYLFLIMNQLrkEGTAIVYISHKLAEIRRIcDRYTVMKDGSSVCSG 227
Cdd:cd03247 132 ItERQLLSLIFEVL--KDKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
267-493 |
1.45e-18 |
|
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: 84.45 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT------SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavkkGM 340
Cdd:cd03293 2 EVRNVSktygggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP------DR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 341 AYITEsrrDNGFFPNFSIAQNMAIsrSLKDGGYKGAmglfhevDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLI 420
Cdd:cd03293 76 GYVFQ---QDALLPWLTVLDNVAL--GLELQGVPKA-------EARERAEELLELVGLS-GFENAYPHQLSGGMRQRVAL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYK-VMRQLADDGKVILMVSSELPEIITVCDRIAVF--CEGRLTQILTN 493
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEeLLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEVEV 218
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-227 |
1.63e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 85.84 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN--ISYNKLDHKLAA-QLGIGIIYQ--ELSVIDE 94
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErvITAGKKNKKLKPlRKKVGIVFQfpEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 95 lTVLenlyigrhltKKIC------GVNIIDWREmrvRAAMMLLRVGLKVDLDEKvANLSISHKQM--LEIAKTLMLDAKV 166
Cdd:PRK13634 102 -TVE----------KDICfgpmnfGVSEEDAKQ---KAREMIELVGLPEELLAR-SPFELSGGQMrrVAIAGVLAMEPEV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 167 IIMDEPTSSLT---NKEVDYLFlimNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:PRK13634 167 LVLDEPTAGLDpkgRKEMMEMF---YKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQG 228
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
267-489 |
1.96e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 84.80 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKkgmAYIT 344
Cdd:PRK11264 5 EVKNLVKKfhGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQK---GLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 ESRRDNGF-FPNFsiaqNMAISRSLKDGGYKGAMGLFHEVDEQRTAENqRELLALKCHSVNQNI--TELSGGNQQKVLIS 421
Cdd:PRK11264 82 QLRQHVGFvFQNF----NLFPHRTVLENIIEGPVIVKGEPKEEATARA-RELLAKVGLAGKETSypRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
10-239 |
2.01e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 84.82 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLD-HKLAAQLgiGIIYQE 88
Cdd:PRK13548 7 NLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSpAELARRR--AVLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 89 LSVIDELTVLENLYIGRhltkkicgvniIDWREMRVRAAMMLLRVGLKVDLDE----KVANLSISHKQMLEIAKTLM--- 161
Cdd:PRK13548 85 SSLSFPFTVEEVVAMGR-----------APHGLSRAEDDALVAAALAQVDLAHlagrDYPQLSGGEQQRVQLARVLAqlw 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 162 ---LDAKVIIMDEPTSSLtnkevDylflIMNQL----------RKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGI 228
Cdd:PRK13548 154 epdGPPRWLLLDEPTSAL-----D----LAHQHhvlrlarqlaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGT 224
|
250
....*....|.
gi 16131913 229 VSDVSNDDIVR 239
Cdd:PRK13548 225 PAEVLTPETLR 235
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
21-221 |
2.58e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 84.06 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL---GIGIIYQELSVIDELTV 97
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 98 LENLyigrHLTKKICGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLT 177
Cdd:PRK10584 106 LENV----ELPALLRGESS---RQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16131913 178 NKE----VDYLFlIMNqlRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
Cdd:PRK10584 179 RQTgdkiADLLF-SLN--REHGTTLILVTHDLQLAAR-CDRRLRLVNG 222
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
266-495 |
3.74e-18 |
|
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: 83.36 E-value: 3.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 266 FEVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDA-VKKGMAY 342
Cdd:cd03218 1 LRAENLSKRYGKRkvVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDIT-KLPMHKrARLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 ITEsrrDNGFFPNFSIAQN-MAISRslkdggykgamglFHEVDEQRTAENQRELLAL--KCHSVNQNITELSGGNQQKVL 419
Cdd:cd03218 80 LPQ---EASIFRKLTVEENiLAVLE-------------IRGLSKKEREEKLEELLEEfhITHLRKSKASSLSGGERRRVE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 420 ISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRI------AVFCEGRLTQILTN 493
Cdd:cd03218 144 IARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAyiiyegKVLAEGTPEEIAAN 223
|
..
gi 16131913 494 RD 495
Cdd:cd03218 224 EL 225
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
21-239 |
4.26e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 84.01 E-value: 4.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHK-LAAQLgiGIIYQELSVIDELTVLE 99
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWeLARRR--AVLPQHSSLAFPFTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 100 NLYIGR--HLTKKicgvniiDWREMRVRAAMMLlrvglkVDLDEKVAN----LSISHKQMLEIAKTL-------MLDAKV 166
Cdd:COG4559 95 VVALGRapHGSSA-------AQDRQIVREALAL------VGLAHLAGRsyqtLSGGEQQRVQLARVLaqlwepvDGGPRW 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 167 IIMDEPTSSLtnkevD--YLFLIMNQLRK---EGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVR 239
Cdd:COG4559 162 LFLDEPTSAL-----DlaHQHAVLRLARQlarRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLE 234
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
267-464 |
5.20e-18 |
|
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: 82.84 E-value: 5.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR---DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS----PRSPLDAVKKG 339
Cdd:cd03292 2 EFINVTKTypnGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgRAIPYLRRKIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 340 MAYitesrRDNGFFPNFSIAQNMAISRSLKDGGYKgamglfhevDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVL 419
Cdd:cd03292 82 VVF-----QDFRLLPDRNVYENVAFALEVTGVPPR---------EIRKRVPAALELVGLS-HKHRALPAELSGGEQQRVA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16131913 420 ISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILM 464
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVV 191
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
274-502 |
6.18e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 83.02 E-value: 6.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 274 RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITEsrrDNGFF 353
Cdd:PRK10895 14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQ---EASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 354 PNFSIAQN-MAISRSLKDggykgamgLFHEVDEQRTAENQRELLAlkCHSVNQNITELSGGNQQKVLISKWLCCCPEVII 432
Cdd:PRK10895 91 RRLSVYDNlMAVLQIRDD--------LSAEQREDRANELMEEFHI--EHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 433 FDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEEEI 502
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
274-488 |
1.01e-17 |
|
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: 82.38 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 274 RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldAVKKGMAYITESRrdNGFF 353
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRK--KFLRRIGVVFGQK--TQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 354 PNFSIAQNMAISRSLKDggykgamglfheVDEQRTAENQRELL-ALKC-HSVNQNITELSGGNQQKVLISKWLCCCPEVI 431
Cdd:cd03267 108 WDLPVIDSFYLLAAIYD------------LPPARFKKRLDELSeLLDLeELLDTPVRQLSLGQRMRAEIAAALLHEPEIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 432 IFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRLT 488
Cdd:cd03267 176 FLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
16-239 |
1.14e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 83.31 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLgIGIIYQEL-SVIDE 94
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF-VGLVFQNPdDQIFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 95 LTVLENLYIGRhltkkicgVNI-IDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
Cdd:PRK13652 94 PTVEQDIAFGP--------INLgLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 174 SSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV-SNDDIVR 239
Cdd:PRK13652 166 AGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIfLQPDLLA 233
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-251 |
1.44e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 82.44 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGP-----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKL-DHKLAAQ 79
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLpEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 80 lgIGIIYQelsviD-------ELTVLENLYI----------GRHLTKKicgvniidwREMRVRAAMMLLRVGLKVDLDEK 142
Cdd:COG1101 82 --IGRVFQ-----DpmmgtapSMTIEENLALayrrgkrrglRRGLTKK---------RRELFRELLATLGLGLENRLDTK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 143 VANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDylfLIM---NQLRKEG--TAIVyISHKLAEIRRICDRYTV 217
Cdd:COG1101 146 VGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAA---LVLeltEKIVEENnlTTLM-VTHNMEQALDYGNRLIM 221
|
250 260 270
....*....|....*....|....*....|....
gi 16131913 218 MKDGSsvcsgIVSDVSNDDIVRLMVgRELQNRFN 251
Cdd:COG1101 222 MHEGR-----IILDVSGEEKKKLTV-EDLLELFE 249
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-232 |
1.46e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 83.24 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNI---SYNKLDHKLAAQLGIGIIYQ-ELSVIDEL 95
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIvvsSTSKQKEIKPVRKKVGVVFQfPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 96 TVLENLYIGRHltkkicgvNI-IDWREMRVRAAMMLLRVGLKVDLDEKvANLSISHKQM--LEIAKTLMLDAKVIIMDEP 172
Cdd:PRK13643 101 TVLKDVAFGPQ--------NFgIPKEKAEKIAAEKLEMVGLADEFWEK-SPFELSGGQMrrVAIAGILAMEPEVLVLDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 173 TSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:PRK13643 172 TAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
21-230 |
1.58e-17 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 82.00 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSG--IHEPTKGTITINNISYNKLDHKLAAQLGIGIIYQ---ELSVIDEL 95
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLGIFLAFQypiEIPGVSNA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 96 TVLENLYIGRHLTKKICGVNIIDWREmrvraammLLRVGLK-VDLDEKVAN------LSISHKQMLEIAKTLMLDAKVII 168
Cdd:CHL00131 103 DFLRLAYNSKRKFQGLPELDPLEFLE--------IINEKLKlVGMDPSFLSrnvnegFSGGEKKRNEILQMALLDSELAI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 169 MDEPTSSLtnkEVDYLFLI---MNQLRKEGTAIVYISH--KLAE-IrrICDRYTVMKDGSSVCSGIVS 230
Cdd:CHL00131 175 LDETDSGL---DIDALKIIaegINKLMTSENSIILITHyqRLLDyI--KPDYVHVMQNGKIIKTGDAE 237
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-252 |
1.83e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 84.31 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKL-DHKL--AAQLGIGIIYQELSVIDELT 96
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsDAELreVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 97 VLENLYIGRHLTKkicgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
Cdd:PRK10070 123 VLDNTAFGMELAG-------INAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 177 TNkevdylfLIMNQLR--------KEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG----IVSDVSNDDIVRLMVGR 244
Cdd:PRK10070 196 DP-------LIRTEMQdelvklqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGtpdeILNNPANDYVRTFFRGV 268
|
....*...
gi 16131913 245 ELQNRFNA 252
Cdd:PRK10070 269 DISQVFSA 276
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
267-490 |
2.07e-17 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 83.61 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavkkgmayit 344
Cdd:COG3842 7 ELENVSKRygDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP------------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 eSRRDNGF-------FPNFSIAQNMAISrsLKDGGYKGAmglfhEVDEqRTAEnqreLLALkchsV------NQNITELS 411
Cdd:COG3842 75 -EKRNVGMvfqdyalFPHLTVAENVAFG--LRMRGVPKA-----EIRA-RVAE----LLEL----VgleglaDRYPHQLS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 412 GGNQQKV-----LISKwlcccPEVIIFDEPTRGIDVGAK----AEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVF 482
Cdd:COG3842 138 GGQQQRValaraLAPE-----PRVLLLDEPLSALDAKLReemrEELRRLQREL---GITFIYVTHDQEEALALADRIAVM 209
|
....*...
gi 16131913 483 CEGRLTQI 490
Cdd:COG3842 210 NDGRIEQV 217
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
21-227 |
2.25e-17 |
|
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: 81.16 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSG---IHEPTKGTITINNISYNKldHKLaaQLGIGIIYQELSVIDELTV 97
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRKP--DQF--QKCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 98 LENLY------IGRHLTKKIcgvniidwREMRVrAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
Cdd:cd03234 99 RETLTytailrLPRKSSDAI--------RKKRV-EDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 172 PTSSLTNKEVDYLFLIMNQLRKEG-TAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNrIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-221 |
2.73e-17 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 79.90 E-value: 2.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSG--IHEPTKGTITINNISynklDHKLAAQLGIGIIYQELSVIDELTVL 98
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRP----LDKRSFRKIIGYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 99 ENLYIgrhltkkicgvniidwremrvrAAmmLLRvglkvdldekvanlSISHKQM--LEIAKTLMLDAKVIIMDEPTSSL 176
Cdd:cd03213 101 ETLMF----------------------AA--KLR--------------GLSGGERkrVSIALELVSNPSLLFLDEPTSGL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16131913 177 -TNKEVDYLFLIMnQLRKEGTAIVYISHKL-AEIRRICDRYTVMKDG 221
Cdd:cd03213 143 dSSSALQVMSLLR-RLADTGRTIICSIHQPsSEIFELFDKLLLLSQG 188
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
271-477 |
3.31e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.85 E-value: 3.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 271 VTSRD-RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprsplDAVKKGM-AYITESRR 348
Cdd:PRK15056 14 VTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR-----QALQKNLvAYVPQSEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 349 DNGFFPnfsiaqnMAISRSLKDGGYkGAMGLFhevdeQRTAENQRELLALKCHSVN------QNITELSGGNQQKVLISK 422
Cdd:PRK15056 89 VDWSFP-------VLVEDVVMMGRY-GHMGWL-----RRAKKRDRQIVTAALARVDmvefrhRQIGELSGGQKKRVFLAR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCD 477
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD 210
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
261-481 |
3.62e-17 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 84.26 E-value: 3.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 261 AHETVFEVRNVTSRD---RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVK 337
Cdd:TIGR02857 317 APASSLEFSGVSVAYpgrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADA-DSWR 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 338 KGMAYITEsrrdNGFFPNFSIAQNMAISRslkdggyKGAMGlfHEVDE--QRTAENQ-----RELLALKchsVNQNITEL 410
Cdd:TIGR02857 396 DQIAWVPQ----HPFLFAGTIAENIRLAR-------PDASD--AEIREalERAGLDEfvaalPQGLDTP---IGEGGAGL 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913 411 SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSElPEIITVCDRIAV 481
Cdd:TIGR02857 460 SGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHR-LALAALADRIVV 528
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
21-227 |
4.16e-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: 80.74 E-value: 4.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLD-HKLAAQlgIGIIYQElSVIDELTVLE 99
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTlDSLRRA--IGVVPQD-TVLFNDTIGY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 100 NLYIGRhltkkicgvniIDWREMRVRAA---------MMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMD 170
Cdd:cd03253 94 NIRYGR-----------PDATDEEVIEAakaaqihdkIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 171 EPTSSL-TNKEVdylfLIMNQLRK--EGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
Cdd:cd03253 163 EATSALdTHTER----EIQAALRDvsKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
267-486 |
4.27e-17 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 80.42 E-value: 4.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldavkkgmAYIT 344
Cdd:COG1126 3 EIENLHkSFGDLEVlKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSK---------KDIN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 ESRRDNGF-------FPNFSIAQNMAIS--RSLKdggykgamglfheVDEQRTAENQRELLA---LKcHSVNQNITELSG 412
Cdd:COG1126 74 KLRRKVGMvfqqfnlFPHLTVLENVTLApiKVKK-------------MSKAEAEERAMELLErvgLA-DKADAYPAQLSG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 413 GNQQKVLISKWLCCCPEVIIFDEPTRGID---VGakaEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
Cdd:COG1126 140 GQQQRVAIARALAMEPKVMLFDEPTSALDpelVG---EVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGR 213
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
267-481 |
4.73e-17 |
|
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: 82.02 E-value: 4.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT------SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK---RAGGEIRLNGKDISPRSP--LDA 335
Cdd:COG0444 3 EVRNLKvyfptrRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEkeLRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 336 VK-KGMAYItesrrdngffpnFsiaQN--------MAISRSLKDggykgAMGLFHEVDEQRTAENQRELLALkchsVNqn 406
Cdd:COG0444 83 IRgREIQMI------------F---QDpmtslnpvMTVGDQIAE-----PLRIHGGLSKAEARERAIELLER----VG-- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 407 IT-----------ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIIT 474
Cdd:COG0444 137 LPdperrldryphELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAE 216
|
....*..
gi 16131913 475 VCDRIAV 481
Cdd:COG0444 217 IADRVAV 223
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-224 |
6.86e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 81.68 E-value: 6.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHK--LAAQLGIGIIYQelsviDELTV 97
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDewRAVRSDIQMIFQ-----DPLAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 98 LE-NLYIGR-----------HLTKKicgvniidwrEMRVRAAMMLLRVGLKVDLDEKVAN-LSISHKQMLEIAKTLMLDA 164
Cdd:PRK15079 111 LNpRMTIGEiiaeplrtyhpKLSRQ----------EVKDRVKAMMLKVGLLPNLINRYPHeFSGGQCQRIGIARALILEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913 165 KVIIMDEPTSSLtnkEVDYLFLIMN---QLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
Cdd:PRK15079 181 KLIICDEPVSAL---DVSIQAQVVNllqQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 241
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
20-239 |
7.04e-17 |
|
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: 79.84 E-value: 7.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHK-LAAQlgIGIIYQElSVIDELTVL 98
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwLRRQ--VGVVLQE-NVLFNRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 99 ENLYIGR---HLTKKICGVNIIDWREMrvraaMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
Cdd:cd03252 94 DNIALADpgmSMERVIEAAKLAGAHDF-----ISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 176 LtnkevDYL--FLIMNQLRK--EGTAIVYISHKLAEIRRiCDRYTVMKDGSsvcsgIVSDVSNDDIVR 239
Cdd:cd03252 169 L-----DYEseHAIMRNMHDicAGRTVIIIAHRLSTVKN-ADRIIVMEKGR-----IVEQGSHDELLA 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
21-221 |
7.12e-17 |
|
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: 78.41 E-value: 7.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDhklAAQLG--IGIIYQElsviDEL--- 95
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD---PNELGdhVGYLPQD----DELfsg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 96 TVLENLyigrhltkkicgvniidwremrvraammllrvglkvdldekvanLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
Cdd:cd03246 91 SIAENI--------------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSH 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16131913 176 LTNK-EVDYLFLIMnQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
Cdd:cd03246 127 LDVEgERALNQAIA-ALKAAGATRIVIAHRPETLAS-ADRILVLEDG 171
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
267-486 |
1.04e-16 |
|
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: 77.81 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT----SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAY 342
Cdd:cd03228 2 EFKNVSfsypGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLR-DLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 ITesrrdngffpnfsiaQNMAI-SRSLKDggykgamglfhevdeqrtaenqrellalkchsvnqNIteLSGGNQQKV--- 418
Cdd:cd03228 81 VP---------------QDPFLfSGTIRE-----------------------------------NI--LSGGQRQRIaia 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 419 --LISKwlcccPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELpEIITVCDRIAVFCEGR 486
Cdd:cd03228 109 raLLRD-----PPILILDEATSALDPETEALILEALRALA-KGKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
15-214 |
1.51e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 79.31 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 15 FGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE--P---TKGTITIN--NISYNKLD-HKLAAQlgIGIIY 86
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDgeDIYDPDVDvVELRRR--VGMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 87 QE-----LSVIDeltvleNLYIGrhltKKICGVNiiDWREM--RVRAAmmLLRVGL----KVDLDEKVANLSISHKQMLE 155
Cdd:COG1117 99 QKpnpfpKSIYD------NVAYG----LRLHGIK--SKSELdeIVEES--LRKAALwdevKDRLKKSALGLSGGQQQRLC 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 156 IAKTLMLDAKVIIMDEPTSSL----TNKevdylflI---MNQLRKEGTaIVYISHKLAEIRRICDR 214
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALdpisTAK-------IeelILELKKDYT-IVIVTHNMQQAARVSDY 222
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-442 |
1.67e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 82.29 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 5 YI-SMAGIGKSFGP-VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGtitinnisynklDHKLAAQLGI 82
Cdd:TIGR03719 3 YIyTMNRVSKVVPPkKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG------------EARPQPGIKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 83 GIIYQELSVIDELTVLENLYIG----RHLTKKICGVN----------------------IID----WR-EMRVRAAMMLL 131
Cdd:TIGR03719 71 GYLPQEPQLDPTKTVRENVEEGvaeiKDALDRFNEISakyaepdadfdklaaeqaelqeIIDaadaWDlDSQLEIAMDAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 132 RVGlkvDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYL--FLImnqlRKEGTaIVYISHklaeir 209
Cdd:TIGR03719 151 RCP---PWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLerHLQ----EYPGT-VVAVTH------ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 210 ricDRYTVmkdgSSVCSGIVS--------------------------DVSNDDIVRLMVGRELQ---------------- 247
Cdd:TIGR03719 217 ---DRYFL----DNVAGWILEldrgrgipwegnysswleqkqkrleqEEKEESARQKTLKRELEwvrqspkgrqakskar 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 248 -NRFNAMKENVSNLAHET--------------VFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLF 310
Cdd:TIGR03719 290 lARYEELLSQEFQKRNETaeiyippgprlgdkVIEAENLTKAfgDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMIT 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 311 GVDKRAGGEIRLNgkdisprsplDAVKkgMAYITESRrdNGFFPNFSIAQnmAIS----------RSLKDGGYKGAMGlF 380
Cdd:TIGR03719 370 GQEQPDSGTIEIG----------ETVK--LAYVDQSR--DALDPNKTVWE--EISggldiiklgkREIPSRAYVGRFN-F 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 381 HEVDEQrtaenqrellalkchsvnQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDV 442
Cdd:TIGR03719 433 KGSDQQ------------------KKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
21-221 |
1.91e-16 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 78.28 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLaaqlgigiIYQELSVIDELTVLen 100
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY--------LHSKVSLVGQEPVL-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 101 lyIGRHLTKKIcGVNIIDWREMRVRAA---------MMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
Cdd:cd03248 100 --FARSLQDNI-AYGLQSCSFECVKEAaqkahahsfISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131913 172 PTSSL-TNKEvdylfLIMNQLRKEG---TAIVYISHKLAEIRRiCDRYTVMKDG 221
Cdd:cd03248 177 ATSALdAESE-----QQVQQALYDWperRTVLVIAHRLSTVER-ADQILVLDGG 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
21-176 |
2.04e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 77.91 E-value: 2.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEP---TKGTITINNISynkLDHKLAAQLGIGIIYQELSVIDELTV 97
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRR---LTALPAEQRRIGILFQDDLLFPHLSV 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 98 LENLYIGrhLTKKICGvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
Cdd:COG4136 94 GENLAFA--LPPTIGR------AQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKL 164
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
266-479 |
2.70e-16 |
|
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: 78.38 E-value: 2.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 266 FEVRNVT---SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS--PRSPLDAVKKGM 340
Cdd:cd03256 1 IEVENLSktyPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 341 AYITEsrrDNGFFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRtaenqrellALKC-------HSVNQNITELSGG 413
Cdd:cd03256 81 GMIFQ---QFNLIERLSVLENVLSGRLGRRSTWRSLFGLFPKEEKQR---------ALAAlervgllDKAYQRADQLSGG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 414 NQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLA-DDGKVILMVSSELPEIITVCDRI 479
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREYADRI 215
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
267-490 |
2.94e-16 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 80.19 E-value: 2.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKD----ISPRspldavkkgm 340
Cdd:COG1118 4 EVRNISKRfgSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlftnLPPR---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 341 ayitesRRDNGF-------FPNFSIAQNMAIsrslkdggykgamGLfhEVDEQRTAENQR---ELLALkchsV------N 404
Cdd:COG1118 74 ------ERRVGFvfqhyalFPHMTVAENIAF-------------GL--RVRPPSKAEIRArveELLEL----VqleglaD 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 405 QNITELSGGNQQKV-----LISKwlcccPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDR 478
Cdd:COG1118 129 RYPSQLSGGQRQRValaraLAVE-----PEVLLLDEPFGALDAKVRKELRRWLRRLHDElGGTTVFVTHDQEEALELADR 203
|
250
....*....|..
gi 16131913 479 IAVFCEGRLTQI 490
Cdd:COG1118 204 VVVMNQGRIEQV 215
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
275-500 |
4.01e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 78.13 E-value: 4.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavkKGMAyitesrRDNGFFP 354
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS-----RQLA------RRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 355 N-------FSIAQNMAISRSlkdgGYKGAMGLFHEVDEQRT--AENQRELLALkchsVNQNITELSGGNQQKVLISKWLC 425
Cdd:PRK11231 83 QhhltpegITVRELVAYGRS----PWLSLWGRLSAEDNARVnqAMEQTRINHL----ADRRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 426 CCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEE 500
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
16-262 |
4.38e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 79.46 E-value: 4.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIhepTKGT--ITINNISYNKLD---------HKLAAQlGIGI 84
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV---TKDNwrVTADRMRFDDIDllrlsprerRKLVGH-NVSM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 85 IYQE-LSVIDELTvlenlYIGRHLTKKICGVNI-------IDWRemRVRAAMMLLRVGLKvdlDEKVANLSISHK----- 151
Cdd:PRK15093 94 IFQEpQSCLDPSE-----RVGRQLMQNIPGWTYkgrwwqrFGWR--KRRAIELLHRVGIK---DHKDAMRSFPYEltege 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 152 -QMLEIAKTLMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNQlrKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:PRK15093 164 cQKVMIAIALANQPRLLIADEPTNAMeptTQAQIFRLLTRLNQ--NNNTTILLISHDLQMLSQWADKINVLYCGQTVETA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 16131913 228 IVSDVSN-------DDIVRLM--VGREL--QNRFNAMKENVSNLAH 262
Cdd:PRK15093 242 PSKELVTtphhpytQALIRAIpdFGSAMphKSRLNTLPGAIPLLEH 287
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-176 |
4.66e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 79.69 E-value: 4.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 1 MATpyISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDhklAAQL 80
Cdd:PRK11000 1 MAS--VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVP---PAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 81 GIGIIYQELSVIDELTVLENLYIGRhltkKICGVNIIDwREMRVRAAMMLLRVG-LkvdLDEKVANLSISHKQMLEIAKT 159
Cdd:PRK11000 76 GVGMVFQSYALYPHLSVAENMSFGL----KLAGAKKEE-INQRVNQVAEVLQLAhL---LDRKPKALSGGQRQRVAIGRT 147
|
170
....*....|....*..
gi 16131913 160 LMLDAKVIIMDEPTSSL 176
Cdd:PRK11000 148 LVAEPSVFLLDEPLSNL 164
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
279-495 |
5.22e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 79.00 E-value: 5.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 279 VRDISFSVCRGEILGFAGLVGSGRTE----LMNcLFGVDKRAGGEIRLNGKDIS--PRSPLDAVK-KGMAYITESrrdng 351
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSQtafaLMG-LLAANGRIGGSATFNGREILnlPEKELNKLRaEQISMIFQD----- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 352 ffPNFSIAQNMAISRSLKDggykgaMGLFHEVDEQRTA--ENQRELLALKCHSVNQNIT----ELSGGNQQKVLISKWLC 425
Cdd:PRK09473 106 --PMTSLNPYMRVGEQLME------VLMLHKGMSKAEAfeESVRMLDAVKMPEARKRMKmyphEFSGGMRQRVMIAMALL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913 426 CCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
Cdd:PRK09473 178 CRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARD 248
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-221 |
6.93e-16 |
|
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: 76.30 E-value: 6.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLD-HKLAAQLGIgiIYQELSVIDElTVL 98
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPlEDLRSSLTI--IPQDPTLFSG-TIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 99 ENLYIGRHLTkkicgvniidwrEMRVRAAmmlLRVglkvdlDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSltn 178
Cdd:cd03369 100 SNLDPFDEYS------------DEEIYGA---LRV------SEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATAS--- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16131913 179 keVDYL--FLIMNQLRKE--GTAIVYISHKLAEIRRiCDRYTVMKDG 221
Cdd:cd03369 156 --IDYAtdALIQKTIREEftNSTILTIAHRLRTIID-YDKILVMDAG 199
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
267-489 |
7.63e-16 |
|
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: 76.46 E-value: 7.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSRDRKK--VRDISFSVCRGeILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsPRSPlDAVKKGMAYIT 344
Cdd:cd03264 2 QLENLTKRYGKKraLDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV-LKQP-QKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 EsrrDNGFFPNFSIAQNMAisrslkdggYKGAMGLFHEVDEQRTAENQRELLALKCHsVNQNITELSGGNQQKVLISKWL 424
Cdd:cd03264 79 Q---EFGVYPNFTVREFLD---------YIAWLKGIPSKEVKARVDEVLELVNLGDR-AKKKIGSLSGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgkVILMVSSELPE-IITVCDRIAVFCEGRLTQ 489
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEdVESLCNQVAVLNKGKLVF 209
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
275-487 |
9.68e-16 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 76.54 E-value: 9.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMN---CLFGVDKRAGGEIRLNGKDISPrsplDAVKKGMAYItesRRDNG 351
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDaisGRVEGGGTTSGQILFNGQPRKP----DQFQKCVAYV---RQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 352 FFPNFSIAQN---MAISRSLKdggykgamglfHEVDEQRTAENQRELLALKCHSV--NQNITELSGGNQQKVLISKWLCC 426
Cdd:cd03234 92 LLPGLTVRETltyTAILRLPR-----------KSSDAIRKKRVEDVLLRDLALTRigGNLVKGISGGERRRVSIAVQLLW 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 427 CPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGK-VILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:cd03234 161 DPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRiVILTIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
20-227 |
1.34e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 79.62 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKlAAQLGIGIIYQELSVIDElTVLE 99
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRA-SLRRNIAVVFQDAGLFNR-SIED 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 100 NLYIGRHltkkicGVNIIDWREMRVRAAMM--LLR--VGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
Cdd:PRK13657 428 NIRVGRP------DATDEEMRAAAERAQAHdfIERkpDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSA 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16131913 176 LTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSG 227
Cdd:PRK13657 502 LDVETEAKVKAALDELMKGRTTFI-IAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
266-487 |
1.36e-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: 74.56 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 266 FEVRNVTSR----DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavkkgma 341
Cdd:cd03246 1 LEVENVSFRypgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDP--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 342 yiTESRRDNGFFPnfsiaQNMaisrslkdggykgamglfhevdeqrtaenqrELLAlkcHSVNQNIteLSGGNQQKVLIS 421
Cdd:cd03246 72 --NELGDHVGYLP-----QDD-------------------------------ELFS---GSIAENI--LSGGQRQRLGLA 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSElPEIITVCDRIAVFCEGRL 487
Cdd:cd03246 109 RALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-227 |
1.54e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.98 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 16 GPVHALKSVNLTVYPGEIHALLGENGAGKST----LMKVLsgihePTKGTITINNISYNKLDHK--LAAQLGIGIIYQE- 88
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRqlLPVRHRIQVVFQDp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 89 -LSVIDELTVLENLYIG-----RHLTKKicgvniidWREMRVRAAMMllRVGLKVDLDEKV-ANLSISHKQMLEIAKTLM 161
Cdd:PRK15134 372 nSSLNPRLNVLQIIEEGlrvhqPTLSAA--------QREQQVIAVME--EVGLDPETRHRYpAEFSGGQRQRIAIARALI 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 162 LDAKVIIMDEPTSSLtNKEV--DYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:PRK15134 442 LKPSLIILDEPTSSL-DKTVqaQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
15-221 |
1.74e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 75.68 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 15 FGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL--GIGIIYQELSVI 92
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLrrQIGMIFQDHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 93 DELTVLENLYIgrhlTKKICGVNIIDWREmRVRAAMMllrvglKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVII 168
Cdd:PRK10908 92 MDRTVYDNVAI----PLIIAGASGDDIRR-RVSAALD------KVGLLDKAKNfpiqLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131913 169 MDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-221 |
2.15e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 75.39 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 25 NLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIsynklDHKLA--AQLGIGIIYQELSVIDELTVLENLY 102
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ-----DHTTTppSRRPVSMLFQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 103 IGRHLTKKICGvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLT---NK 179
Cdd:PRK10771 94 LGLNPGLKLNA-------AQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalRQ 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16131913 180 EVdyLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:PRK10771 167 EM--LTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADG 206
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-233 |
2.88e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 76.28 E-value: 2.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLGIGIIYQE-----LSVIDE 94
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNpdnqiVATIVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 95 LTVL---ENLYigrhltkkicgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
Cdd:PRK13633 105 EDVAfgpENLG--------------IPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 172 PTSSLT---NKEVdyLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG----IVSDVS 233
Cdd:PRK13633 171 PTAMLDpsgRREV--VNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGtpkeIFKEVE 236
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
244-502 |
2.94e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.79 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 244 RELQNRFNAMKENVSNLAhETVFEVRNVTS--RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIR 321
Cdd:PRK13536 21 RKHQGISEAKASIPGSMS-TVAIDLAGVSKsyGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKIT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 322 LNGKDISPRSPLDAVKKGMAyiteSRRDNgFFPNFSIAQNMAISrslkdGGYKGamglFHEVDEQRTAENQRELLALKcH 401
Cdd:PRK13536 100 VLGVPVPARARLARARIGVV----PQFDN-LDLEFTVRENLLVF-----GRYFG----MSTREIEAVIPSLLEFARLE-S 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 402 SVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAV 481
Cdd:PRK13536 165 KADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCV 244
|
250 260
....*....|....*....|..
gi 16131913 482 FCEGRltQILTNR-DDMSEEEI 502
Cdd:PRK13536 245 LEAGR--KIAEGRpHALIDEHI 264
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
10-207 |
3.06e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 75.51 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIsynKLDHKLAAQlgiGIIYQEL 89
Cdd:PRK11248 6 HLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK---PVEGPGAER---GVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 90 SVIDELTVLENLYIGRHLTkkicGVniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
Cdd:PRK11248 80 GLLPWRNVQDNVAFGLQLA----GV---EKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16131913 170 DEPTSSL---TNKEVDYLFLimnQL-RKEGTAIVYISHKLAE 207
Cdd:PRK11248 153 DEPFGALdafTREQMQTLLL---KLwQETGKQVLLITHDIEE 191
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
279-490 |
3.24e-15 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 74.81 E-value: 3.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVkkgmayiteSRRDNGFFPNFSI 358
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV---------VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 359 AQNMAISrslkdggYKGAMGLFHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
Cdd:TIGR01184 72 RENIALA-------VDRVLPDLSKSERRAIVEEHIALVGLT-EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131913 439 GIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIITVCDRIAVFCEGRLTQI 490
Cdd:TIGR01184 144 ALDALTRGNLQEELMQIWEEHRVtVLMVTHDVDEALLLSDRVVMLTNGPAANI 196
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
21-208 |
3.25e-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: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQlGIGIIYQELSVIDElTVLEN 100
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ-GVAMVQQDPVVLAD-TFLAN 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 101 LYIGRHLTKKICgvniidWREMRVRAAMMLLRV---GLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL- 176
Cdd:PRK10790 435 VTLGRDISEEQV------WQALETVQLAELARSlpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANId 508
|
170 180 190
....*....|....*....|....*....|....
gi 16131913 177 --TNKEVDYLFlimnQLRKEGTAIVYISHKLAEI 208
Cdd:PRK10790 509 sgTEQAIQQAL----AAVREHTTLVVIAHRLSTI 538
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-205 |
3.57e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.15 E-value: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 3 TPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTItinnisynkldhKLAAQLGI 82
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGKLRI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 83 GIIYQELSVIDELTvlenLYIGRHLTKKiCGVNIIDWREM--RVRAAMMllrvglkvdLDEKVANLSISHKQMLEIAKTL 160
Cdd:PRK09544 70 GYVPQKLYLDTTLP----LTVNRFLRLR-PGTKKEDILPAlkRVQAGHL---------IDAPMQKLSGGETQRVLLARAL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16131913 161 MLDAKVIIMDEPTSSL-TNKEVDyLFLIMNQLRKE-GTAIVYISHKL 205
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVdVNGQVA-LYDLIDQLRRElDCAVLMVSHDL 181
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
279-469 |
3.85e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 75.39 E-value: 3.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS----PRSPLDAVKKGMAYITESRRdNGFFP 354
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdKDGQLKVADKNQLRLLRTRL-TMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 355 NFSIAQNMAISRSLKDGGYKgAMGLFHEVDEQRtAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFD 434
Cdd:PRK10619 100 HFNLWSHMTVLENVMEAPIQ-VLGLSKQEARER-AVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFD 177
|
170 180 190
....*....|....*....|....*....|....*
gi 16131913 435 EPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSEL 469
Cdd:PRK10619 178 EPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEM 212
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
15-243 |
4.80e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.02 E-value: 4.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 15 FGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLgIGIIYQELSVIDE 94
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 95 LTVLENLYIGRHLTKKIcgvnIIDWREMRVRAAMMLLRVGLKVDL-DEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
Cdd:PRK10253 96 ITVQELVARGRYPHQPL----FTRWRKEDEEAVTKAMQATGITHLaDQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913 174 SSL-TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRLMVG 243
Cdd:PRK10253 172 TWLdISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYG 242
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
265-490 |
5.65e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 76.41 E-value: 5.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 265 VFEVRNVT-SRD-RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLdavKKGMAY 342
Cdd:PRK11607 19 LLEIRNLTkSFDgQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY---QRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 ITESRrdnGFFPNFSIAQNMAIsrSLK-DGGYKGAMGLfhEVDEQRTAENQRELLALKCHsvnqnitELSGGNQQKVLIS 421
Cdd:PRK11607 96 MFQSY---ALFPHMTVEQNIAF--GLKqDKLPKAEIAS--RVNEMLGLVHMQEFAKRKPH-------QLSGGQRQRVALA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 422 KWLCCCPEVIIFDEPTRGIDVGAKAEI-YKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQI 231
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
266-487 |
5.75e-15 |
|
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: 74.16 E-value: 5.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 266 FEVRNVTSR----DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDaVKKGMA 341
Cdd:cd03245 3 IEFRNVSFSypnqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD-LRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 342 YITEsrrDNGFFpNFSIAQNMAISRSlkdggykgamglfhEVDEQRTAENQR-----ELLALKCHSVNQNITE----LSG 412
Cdd:cd03245 82 YVPQ---DVTLF-YGTLRDNITLGAP--------------LADDERILRAAElagvtDFVNKHPNGLDLQIGErgrgLSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 413 GNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPeIITVCDRIAVFCEGRL 487
Cdd:cd03245 144 GQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGD-KTLIIITHRPS-LLDLVDRIIVMDSGRI 216
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
20-246 |
5.87e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 75.17 E-value: 5.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQlGIGIIYQElsvideltvLE 99
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRK-HIGIVFQN---------PD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 100 NLYIGRHLTKKIC-GV--NIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
Cdd:PRK13648 94 NQFVGSIVKYDVAfGLenHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913 177 TNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGIVSDVSNDDIVRLMVGREL 246
Cdd:PRK13648 174 DPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEELTRIGLDL 243
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-236 |
7.55e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 77.19 E-value: 7.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHePTKGTITINNISYNKLDH----KLAAQLGigiiyQELSVIdELT 96
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPeswrKHLSWVG-----QNPQLP-HGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 97 VLENLYIGRHltkkicgvniiDWREMRVRAAMML---------LRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVI 167
Cdd:PRK11174 439 LRDNVLLGNP-----------DASDEQLQQALENawvseflplLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 168 IMDEPTSSL-TNKEVdylfLIMNQLRK--EGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGIVSDVSNDD 236
Cdd:PRK11174 508 LLDEPTASLdAHSEQ----LVMQALNAasRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-227 |
7.76e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.53 E-value: 7.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 1 MATPYISMAGIGKSFGPVH-ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNK-LDHKLAA 78
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHtALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQaLQKNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 79 qlgigIIYQELSVIDELTVL--ENLYIGR--HLtkkicGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQML 154
Cdd:PRK15056 82 -----YVPQSEEVDWSFPVLveDVVMMGRygHM-----GWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131913 155 EIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDrYTVMKDGSSVCSG 227
Cdd:PRK15056 152 FLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASG 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-222 |
8.93e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 75.51 E-value: 8.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLdHklAAQLGIGII 85
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL-H--ARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 86 YQELSVIDELTVLENLYIgrhltkkicGVNIIDWREMRVRAA-----MMLLR-VGLKVDLDEKVANLSISHKQMLEIAKT 159
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAF---------GLTVLPRRERPNAAAikakvTQLLEmVQLAHLADRYPAQLSGGQKQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE--GTAiVYISHKLAEIRRICDRYTVMKDGS 222
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElkFTS-VFVTHDQEEAMEVADRVVVMSQGN 214
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-213 |
8.98e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 74.11 E-value: 8.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 15 FGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE-----PTKGTITI--NNISYNKLDhKLAAQLGIGIIYQ 87
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLfgRNIYSPDVD-PIEVRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 88 ELSVIDELTVLENLYIGRHLTKKICGVNIIDWR-EMRVRAAMMLLRVglKVDLDEKVANLSISHKQMLEIAKTLMLDAKV 166
Cdd:PRK14267 93 YPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERvEWALKKAALWDEV--KDRLNDYPSNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16131913 167 IIMDEPTSSL----TNKEVDYLFlimnQLRKEGTaIVYISHKLAEIRRICD 213
Cdd:PRK14267 171 LLMDEPTANIdpvgTAKIEELLF----ELKKEYT-IVLVTHSPAQAARVSD 216
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
263-503 |
1.24e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 73.87 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 263 ETVFEVRNV----TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKK 338
Cdd:PRK13632 5 SVMIKVENVsfsyPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS-KENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 339 GMAYITESRrDNGFFPN-------FSIaQNMAISRS-LKDggykgamglfhEVDEQRTAENQRELLALKCHSvnqniteL 410
Cdd:PRK13632 84 KIGIIFQNP-DNQFIGAtveddiaFGL-ENKKVPPKkMKD-----------IIDDLAKKVGMEDYLDKEPQN-------L 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 411 SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDG-KVILMVSSELPEIItVCDRIAVFCEGRLTQ 489
Cdd:PRK13632 144 SGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAI-LADKVIVFSEGKLIA 222
|
250
....*....|....
gi 16131913 490 ILTNRDDMSEEEIM 503
Cdd:PRK13632 223 QGKPKEILNNKEIL 236
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-221 |
1.89e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 73.27 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE-----PTKGTITIN--NISYNKLD 73
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNghNIYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 74 hklAAQL--GIGIIYQELSVIdELTVLENLYIGRHLT-------------KKICGVNIidWREMRVRaammllrvglkvd 138
Cdd:PRK14239 81 ---TVDLrkEIGMVFQQPNPF-PMSIYENVVYGLRLKgikdkqvldeaveKSLKGASI--WDEVKDR------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 139 LDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTaIVYISHKLAEIRRICDRYTVM 218
Cdd:PRK14239 142 LHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYT-MLLVTRSMQQASRISDRTGFF 220
|
...
gi 16131913 219 KDG 221
Cdd:PRK14239 221 LDG 223
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-211 |
2.14e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 71.62 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNisynKLDHKLAAQLGIGIIYqeLSVID----EL 95
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNG----TPLAEQRDEPHENILY--LGHLPglkpEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 96 TVLENLYIGRHltkkicgvnIIDWREMRVRAAmmLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
Cdd:TIGR01189 89 SALENLHFWAA---------IHGGAQRTIEDA--LAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 16131913 176 LTNKEVDYLFLIMNQLRKEGTAIVYISHK---LAEIRRI 211
Cdd:TIGR01189 158 LDKAGVALLAGLLRAHLARGGIVLLTTHQdlgLVEAREL 196
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
250-502 |
2.49e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 73.73 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 250 FNAMKENVSNLAHETVFEVRNV-------TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRL 322
Cdd:PRK13631 6 MKKKLKVPNPLSDDIILRVKNLycvfdekQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 323 -----NGKDISPRSPLDAVKKGMAYITESRRDNGF---FPNFSIAQNmAISRSLKDGGYkgAMGLfHEVDEQRTAENQRE 394
Cdd:PRK13631 86 gdiyiGDKKNNHELITNPYSKKIKNFKELRRRVSMvfqFPEYQLFKD-TIEKDIMFGPV--ALGV-KKSEAKKLAKFYLN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 395 LLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIIT 474
Cdd:PRK13631 162 KMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLE 241
|
250 260 270
....*....|....*....|....*....|....
gi 16131913 475 VCDRIAVFCEGRLT------QILTNRDDMSEEEI 502
Cdd:PRK13631 242 VADEVIVMDKGKILktgtpyEIFTDQHIINSTSI 275
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-239 |
2.66e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 72.81 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN-----NISYNKLDHKLAaql 80
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDgldvaTTPSRELAKRLA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 81 gigIIYQELSVIDELTVLENLYIGR------HLTKKicgvniiDWRemRVRAAMMLLrvGLKvD-----LDEkvanLSIS 149
Cdd:COG4604 79 ---ILRQENHINSRLTVRELVAFGRfpyskgRLTAE-------DRE--IIDEAIAYL--DLE-DladryLDE----LSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 150 HKQMLEIAKTLMLDAKVIIMDEPTSSLTNK-EVDylflIMNQLRK----EGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
Cdd:COG4604 140 QRQRAFIAMVLAQDTDYVLLDEPLNNLDMKhSVQ----MMKLLRRladeLGKTVVIVLHDINFASCYADHIVAMKDGRVV 215
|
250
....*....|....*
gi 16131913 225 CSGIVSDVSNDDIVR 239
Cdd:COG4604 216 AQGTPEEIITPEVLS 230
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
276-487 |
2.68e-14 |
|
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: 76.21 E-value: 2.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 276 RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIspRSPLDAVKKGMAYITESrrdNGFFPN 355
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI--ETNLDAVRQSLGMCPQH---NILFHH 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 356 FSIAQNMAISRSLKDGGYKGAmglfhevdeQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
Cdd:TIGR01257 1018 LTVAEHILFYAQLKGRSWEEA---------QLEMEAMLEDTGLH-HKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDE 1087
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16131913 436 PTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:TIGR01257 1088 PTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
266-504 |
3.05e-14 |
|
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: 75.26 E-value: 3.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 266 FEVRNVT---SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMA 341
Cdd:COG2274 474 IELENVSfryPGDSPPVlDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLR-QIDPASLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 342 YITEsrrDNGFFpNFSIAQNMAISRSLKDggykgamglfhevDEQ-----RTAENQRELLALKcHSVNQNITE----LSG 412
Cdd:COG2274 553 VVLQ---DVFLF-SGTIRENITLGDPDAT-------------DEEiieaaRLAGLHDFIEALP-MGYDTVVGEggsnLSG 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 413 GNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELpEIITVCDRIAVFCEGRLTQilt 492
Cdd:COG2274 615 GQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRL-STIRLADRIIVLDKGRIVE--- 689
|
250
....*....|..
gi 16131913 493 nrdDMSEEEIMA 504
Cdd:COG2274 690 ---DGTHEELLA 698
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-221 |
3.44e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 72.94 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTIT-----INNISYNKLDHKLAAQLGIGIIYQELSVIDEl 95
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITiagyhITPETGNKNLKKLRKKVSLVFQFPEAQLFEN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 96 TVLENLYIGrhltKKICGVNIidwREMRVRAAMMLLRVGLKVDLDEKvANLSISHKQM--LEIAKTLMLDAKVIIMDEPT 173
Cdd:PRK13641 102 TVLKDVEFG----PKNFGFSE---DEAKEKALKWLKKVGLSEDLISK-SPFELSGGQMrrVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16131913 174 SSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHG 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-229 |
3.79e-14 |
|
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: 75.82 E-value: 3.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYnkldhklaaQLGIGIIYQELSVIDELTVLE 99
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI---------LTNISDVHQNMGYCPQFDAID 2024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 100 NLYIGR---HLTKKICGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
Cdd:TIGR01257 2025 DLLTGRehlYLYARLRGVPA---EEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 2101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131913 177 TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIV 229
Cdd:TIGR01257 2102 DPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTI 2154
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
268-496 |
5.06e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 71.88 E-value: 5.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 268 VRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldavkkgMAYITE 345
Cdd:PRK11701 9 VRGLTKLygPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRD--------LYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 346 SRR------DNGFfpnfsIAQN------MAISRslkdGGYKG----AMGLFHEVDEQRTAENQRELLALKCHSVNQNITE 409
Cdd:PRK11701 81 AERrrllrtEWGF-----VHQHprdglrMQVSA----GGNIGerlmAVGARHYGDIRATAGDWLERVEIDAARIDDLPTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGR-- 486
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRvv 231
|
250
....*....|....
gi 16131913 487 ---LT-QILtnrDD 496
Cdd:PRK11701 232 esgLTdQVL---DD 242
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
267-495 |
5.23e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 73.19 E-value: 5.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkkgmayit 344
Cdd:PRK10851 4 EIANIKkSFGRTQVlNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 esrRDNGF-FPNFSIAQNMAISRSLkdggykgAMGLFHEVDEQR---TAENQR-----ELLALKcHSVNQNITELSGGNQ 415
Cdd:PRK10851 74 ---RKVGFvFQHYALFRHMTVFDNI-------AFGLTVLPRRERpnaAAIKAKvtqllEMVQLA-HLADRYPAQLSGGQK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 416 QKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVI-LMVSSELPEIITVCDRIAVFCEGRLTQILTNR 494
Cdd:PRK10851 143 QRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTsVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
.
gi 16131913 495 D 495
Cdd:PRK10851 223 Q 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
263-503 |
7.33e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 71.80 E-value: 7.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 263 ETVFEVRNVTSR---DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprsPLDAVKKG 339
Cdd:PRK13636 3 DYILKVEELNYNysdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK------PIDYSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 340 mayITESRRDNGFFpnFSIAQNMAISRSLKDGGYKGAMGLFHEVDE-QRTAENQRELLALKcHSVNQNITELSGGNQQKV 418
Cdd:PRK13636 77 ---LMKLRESVGMV--FQDPDNQLFSASVYQDVSFGAVNLKLPEDEvRKRVDNALKRTGIE-HLKDKPTHCLSFGQKKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 419 LISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDM 497
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
....*.
gi 16131913 498 SEEEIM 503
Cdd:PRK13636 231 AEKEML 236
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
17-235 |
9.44e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 71.75 E-value: 9.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 17 PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGI---HEPTKGTITINNISYNKlDHKLAAQLGIGIIYQE----- 88
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTA-KTVWDIREKVGIVFQNpdnqf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 89 --LSVIDELTV-LENLYIGRHLTKKIcgvniidwremrVRAAmmLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
Cdd:PRK13640 98 vgATVGDDVAFgLENRAVPRPEMIKI------------VRDV--LADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIrRICDRYTVMKDGSSVCSGIVSDVSND 235
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-221 |
9.68e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 72.44 E-value: 9.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNisyNKLDHKLAAQLGIGI 84
Cdd:PRK11432 6 FVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG---EDVTHRSIQQRDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 85 IYQELSVIDELTVLENlyIGRHLtkKICGVNIIDWREmRVRAAMMLlrvglkVDL----DEKVANLSISHKQMLEIAKTL 160
Cdd:PRK11432 83 VFQSYALFPHMSLGEN--VGYGL--KMLGVPKEERKQ-RVKEALEL------VDLagfeDRYVDQISGGQQQRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 161 MLDAKVIIMDEPTSSLTNKevdyLFLIMNQLRKE-----GTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDAN----LRRSMREKIRElqqqfNITSLYVTHDQSEAFAVSDTVIVMNKG 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
281-495 |
1.05e-13 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 72.44 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK---DISPRSPLDAVKKGMAYI-TESRrdngFFPNF 356
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqDSARGIFLPPHRRRIGYVfQEAR----LFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 357 SIAQNMaisrslkDGGYKgamglfhevdeqRTAENQR--------ELLALKcHSVNQNITELSGGNQQKVLISKWLCCCP 428
Cdd:COG4148 93 SVRGNL-------LYGRK------------RAPRAERrisfdevvELLGIG-HLLDRRPATLSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913 429 EVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIITVCDRIAVFCEGR------LTQILTNRD 495
Cdd:COG4148 153 RLLLMDEPLAALDLARKAEILPYLERLRDELDIpILYVSHSLDEVARLADHVVLLEQGRvvasgpLAEVLSRPD 226
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
279-492 |
1.31e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 70.23 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisPRSPLDAVKKGMAyiteSRRDNGF------ 352
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ---PMSKLSSAAKAEL----RNQKLGFiyqfhh 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 353 -FPNFSIAQNMAIsrSLKDGGYKGAmglfhevDEQRTAenqRELLA---LKcHSVNQNITELSGGNQQKVLISKWLCCCP 428
Cdd:PRK11629 98 lLPDFTALENVAM--PLLIGKKKPA-------EINSRA---LEMLAavgLE-HRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 429 EVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELpEIITVCDRIAVFCEGRLTQILT 492
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDL-QLAKRMSRQLEMRDGRLTAELS 228
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
282-487 |
1.35e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 70.29 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRdngFFPNFSIAQN 361
Cdd:PRK11614 24 VSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRR---VFSRMTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 362 MAI-----SRSLKDGGYKGAMGLFHEVDEQRTaenqrellalkchsvnQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
Cdd:PRK11614 101 LAMggffaERDQFQERIKWVYELFPRLHERRI----------------QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16131913 437 TRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:PRK11614 165 SLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
281-503 |
1.94e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 70.92 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNG---KDISPRSPLDAVKKGMAYITEsrrdngfFPNFS 357
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvSSTSKQKEIKPVRKKVGVVFQ-------FPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 358 IAQNMAisrsLKDGGY-KGAMGLFHEVDEQRTAEnQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
Cdd:PRK13643 97 LFEETV----LKDVAFgPQNFGIPKEKAEKIAAE-KLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 437 TRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEEEIM 503
Cdd:PRK13643 172 TAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFL 238
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
253-509 |
2.00e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 70.85 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 253 MKENVSNLAH----ETVFEvrnvtsrdRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS 328
Cdd:PRK13637 1 MSIKIENLTHiymeGTPFE--------KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDIT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 329 PRSpldaVKkgmayITESRRDNGF---FPNF-----SIAQNMAISRSlkdggykgAMGLFHEVDEQRTAENQrELLALKC 400
Cdd:PRK13637 73 DKK----VK-----LSDIRKKVGLvfqYPEYqlfeeTIEKDIAFGPI--------NLGLSEEEIENRVKRAM-NIVGLDY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 401 HSV-NQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIITVCDR 478
Cdd:PRK13637 135 EDYkDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMtIILVSHSMEDVAKLADR 214
|
250 260 270
....*....|....*....|....*....|....
gi 16131913 479 IAVFCEGRLTQILTNRDDMSEEEI---MAWALPQ 509
Cdd:PRK13637 215 IIVMNKGKCELQGTPREVFKEVETlesIGLAVPQ 248
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
280-487 |
2.34e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 72.45 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAvkkgmayITESRRDN-GF------ 352
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDA-DA-------LAQLRREHfGFifqryh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 353 -FPNFSIAQNMAISrslkdGGYKGAMglfhevDEQRTAENQRELLALKC-HSVNQNITELSGGNQQKVLISKWLCCCPEV 430
Cdd:PRK10535 97 lLSHLTAAQNVEVP-----AVYAGLE------RKQRLLRAQELLQRLGLeDRVEYQPSQLSGGQQQRVSIARALMNGGQV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 431 IIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSElPEIITVCDRIAVFCEGRL 487
Cdd:PRK10535 166 ILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEI 221
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-209 |
2.46e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.14 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNiSYNKLDHKLA-AQLGIGIIYQE-------- 88
Cdd:PTZ00265 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND-SHNLKDINLKwWRSKIGVVSQDpllfsnsi 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 89 -------LSVIDELTVLENLY-----------IGRHLTKKICGVNIIDWRE-------MRVRAAMMLLRVGLKVDLDEKV 143
Cdd:PTZ00265 477 knnikysLYSLKDLEALSNYYnedgndsqenkNKRNSCRAKCAGDLNDMSNttdsnelIEMRKNYQTIKDSEVVDVSKKV 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 144 ---------------------ANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEvDYLFL-IMNQLR-KEGTAIVY 200
Cdd:PTZ00265 557 lihdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS-EYLVQkTINNLKgNENRITII 635
|
....*....
gi 16131913 201 ISHKLAEIR 209
Cdd:PTZ00265 636 IAHRLSTIR 644
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-244 |
3.89e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 69.31 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN--ISYNKLDHKLAA---QLGIGIIYQELSVIDEL 95
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGkvLYFGKDIFQIDAiklRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 96 TVLENLyigrhlTKKICGVNIIDWREMRVRAAMMLLRVGLKVD----LDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
Cdd:PRK14246 106 SIYDNI------AYPLKSHGIKEKREIKKIVEECLRKVGLWKEvydrLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 172 PTSSLTNKEVDYLFLIMNQLRKEgTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG----IVSDVSNDDIVRLMVGR 244
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGssneIFTSPKNELTEKYVIGR 255
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-230 |
4.49e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 71.62 E-value: 4.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEP---TKGTITINNISYNKLDHKLAAqlgiGIIYQELSVIDEL 95
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAIS----AYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 96 TVLENLYI------GRHLTKKIcgvniidwREMRVRAamMLLRVGL------KVDLDEKVANLSISHKQMLEIAKTLMLD 163
Cdd:TIGR00955 115 TVREHLMFqahlrmPRRVTKKE--------KRERVDE--VLQALGLrkcantRIGVPGRVKGLSGGERKRLAFASELLTD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEG-TAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVS 230
Cdd:TIGR00955 185 PPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGkTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPD 252
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
280-490 |
5.90e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 70.06 E-value: 5.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK---DISPRspldavKKGMAYITESRrdnGFFPNF 356
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPA------ERGVGMVFQSY---ALYPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 357 SIAQNMaiSRSLKDGGYKGAmglfhevDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
Cdd:PRK11000 91 SVAENM--SFGLKLAGAKKE-------EINQRVNQVAEVLQLA-HLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 437 TRGID----VGAKAEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
Cdd:PRK11000 161 LSNLDaalrVQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQV 215
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
24-247 |
5.92e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.90 E-value: 5.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 24 VNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKL---AAQLGIGIIYQELSVIDELTVLEN 100
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIclpPEKRRIGYVFQDARLFPHYKVRGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 101 L-YigrhltkkicGVNiidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLT-- 177
Cdd:PRK11144 97 LrY----------GMA----KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlp 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131913 178 -NKEV-DYLflimNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRLMVGRELQ 247
Cdd:PRK11144 163 rKRELlPYL----ERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMRPWLPKEEQ 231
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-221 |
1.71e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.40 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 3 TPyISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNkldhklAAQLGI 82
Cdd:PRK11247 11 TP-LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLA------EAREDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 83 GIIYQELSVIDELTVLENLYIGrhltkkICGvniiDWREMRVRAammLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
Cdd:PRK11247 84 RLMFQDARLLPWKKVIDNVGLG------LKG----QWRDAALQA---LAAVGLADRANEWPAALSGGQKQRVALARALIH 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 163 DAKVIIMDEPTSSLtnkevDYLFLI-MNQL-----RKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:PRK11247 151 RPGLLLLDEPLGAL-----DALTRIeMQDLieslwQQHGFTVLLVTHDVSEAVAMADRVLLIEEG 210
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
263-487 |
1.77e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 67.49 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 263 ETVFEVRN--VTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLfgvdKRAG---------GEIRLNGKDI-SPR 330
Cdd:PRK14239 3 EPILQVSDlsVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSI----NRMNdlnpevtitGSIVYNGHNIySPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 331 SPLDAVKK--GMAYitesRRDNGFfPnFSIAQNMAISRSLKdgGYKGAMGLFHEVDEQRTAENQRELLALKCHSvnqNIT 408
Cdd:PRK14239 79 TDTVDLRKeiGMVF----QQPNPF-P-MSIYENVVYGLRLK--GIKDKQVLDEAVEKSLKGASIWDEVKDRLHD---SAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:PRK14239 148 GLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
275-489 |
1.92e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 67.38 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCL------FGVDKRAGGEIRLNGKDISPrspLDAVK----KGMAYit 344
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLnrlieiYDSKIKVDGKVLYFGKDIFQ---IDAIKlrkeVGMVF-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 esrRDNGFFPNFSIAQNMAISrsLKDGGYKGAMGLFHEVDEQ-RTAENQRELLalkcHSVNQNITELSGGNQQKVLISKW 423
Cdd:PRK14246 97 ---QQPNPFPHLSIYDNIAYP--LKSHGIKEKREIKKIVEEClRKVGLWKEVY----DRLNSPASQLSGGQQQRLTIARA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVE 232
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
20-236 |
2.31e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.80 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTIT--INNISYNKLDHKLAAQLG---------------- 81
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwiFKDEKNKKKTKEKEKVLEklviqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 82 -----IGIIYQ--ELSVIDElTVLENLYIGrhltKKICGVniiDWREMRVRAAMMLLRVGLKVD-LDEKVANLSISHKQM 153
Cdd:PRK13651 102 eirrrVGVVFQfaEYQLFEQ-TIEKDIIFG----PVSMGV---SKEEAKKRAAKYIELVGLDESyLQRSPFELSGGQKRR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVS 233
Cdd:PRK13651 174 VALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDIL 253
|
...
gi 16131913 234 NDD 236
Cdd:PRK13651 254 SDN 256
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
267-466 |
2.67e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 66.23 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT---SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldavKKGMAYI 343
Cdd:COG2884 3 RFENVSkryPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLK-----RREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 344 tesRR-------DNGFFPNFSIAQNMAISrsLKdggykgAMGLFHEVDEQRTaenqRELLA---LKcHSVNQNITELSGG 413
Cdd:COG2884 78 ---RRrigvvfqDFRLLPDRTVYENVALP--LR------VTGKSRKEIRRRV----REVLDlvgLS-DKAKALPHELSGG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 414 NQQKV-----LISKwlcccPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVS 466
Cdd:COG2884 142 EQQRVaiaraLVNR-----PELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAT 194
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
261-492 |
2.85e-12 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 66.65 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 261 AHETVFEVRNV-----TSRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPld 334
Cdd:COG1116 3 AAAPALELRGVskrfpTGGGGVTAlDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 335 avkkGMAYItesrrdngF-----FPNFSIAQNMAISrsLKdggykgAMGLFHEVDEQRTaenqRELLAL---------KC 400
Cdd:COG1116 81 ----DRGVV--------FqepalLPWLTVLDNVALG--LE------LRGVPKAERRERA----RELLELvglagfedaYP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 401 HsvnqnitELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRI 479
Cdd:COG1116 137 H-------QLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADRV 209
|
250
....*....|....*
gi 16131913 480 AVFCE--GRLTQILT 492
Cdd:COG1116 210 VVLSArpGRIVEEID 224
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
267-490 |
2.87e-12 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 65.90 E-value: 2.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSRDR----KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAY 342
Cdd:cd03369 8 EVENLSVRYApdlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIS-TIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 ITESrrdngffPnfsiaqnmaisrSLKDGGYKGAMGLFHEVDEQRTAEnqrellALKCHSVNQNiteLSGGNQQKVLISK 422
Cdd:cd03369 87 IPQD-------P------------TLFSGTIRSNLDPFDEYSDEEIYG------ALRVSEGGLN---LSQGQRQLLCLAR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGkVILMVSSELPEIITvCDRIAVFCEGRLTQI 490
Cdd:cd03369 139 ALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNS-TILTIAHRLRTIID-YDKILVMDAGEVKEY 204
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-203 |
3.64e-12 |
|
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: 65.59 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINnisyNKLDHKLAAQLGIGIIY--QELSVIDELTVL 98
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLN----GGPLDFQRDSIARGLLYlgHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 99 ENLYIgrhltkkicgvniidWREMRVRAAMM--LLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
Cdd:cd03231 92 ENLRF---------------WHADHSDEQVEeaLARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180
....*....|....*....|....*..
gi 16131913 177 TNKEVDYLFLIMNQLRKEGTAIVYISH 203
Cdd:cd03231 157 DKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-199 |
3.67e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 65.67 E-value: 3.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN-----------ISYnkLDHKLAaqlgigiiyqel 89
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddpdvaeaCHY--LGHRNA------------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 90 sVIDELTVLENLYIGRhltkkicgvNIIDWREMRVRAAmmLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
Cdd:PRK13539 84 -MKPALTVAENLEFWA---------AFLGGEELDIAAA--LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWIL 151
|
170 180 190
....*....|....*....|....*....|..
gi 16131913 170 DEPTSSLtNKEVDYLF--LIMNQLRKEGTAIV 199
Cdd:PRK13539 152 DEPTAAL-DAAAVALFaeLIRAHLAQGGIVIA 182
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
13-227 |
4.01e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 67.18 E-value: 4.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 13 KSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIsYNKLDHKLAAQLG----------- 81
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDI-YIGDKKNNHELITnpyskkiknfk 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 82 -----IGIIYQ--ELSVIDElTVLENLYIGrhltKKICGVNIIDWREmrvRAAMMLLRVGLKVD-LDEKVANLSISHKQM 153
Cdd:PRK13631 113 elrrrVSMVFQfpEYQLFKD-TIEKDIMFG----PVALGVKKSEAKK---LAKFYLNKMGLDDSyLERSPFGLSGGQKRR 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 154 LEIAKTLMLDAKVIIMDEPTSSLTNK-EVDYLFLIMNQlRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:PRK13631 185 VAIAGILAIQPEILIFDEPTAGLDPKgEHEMMQLILDA-KANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-227 |
4.16e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 66.66 E-value: 4.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKG-----TITINNISYNKLDHKL 76
Cdd:PRK14271 18 AAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 77 AAQLGIGIIYQELSVIdELTVLENLYIGRHLTKkicgvnIIDWREMRVRAAMMLLRVGL----KVDLDEKVANLSISHKQ 152
Cdd:PRK14271 98 EFRRRVGMLFQRPNPF-PMSIMDNVLAGVRAHK------LVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQ 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 153 MLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:PRK14271 171 LLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVII-VTHNLAQAARISDRAALFFDGRLVEEG 244
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
13-218 |
4.77e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 68.61 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 13 KSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNisyNKLD-HKLAAQLGIGIIYQELSV 91
Cdd:NF033858 274 MRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFG---QPVDaGDIATRRRVGYMSQAFSL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 92 IDELTVLENLYI-GR--HLTKKicgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVII 168
Cdd:NF033858 351 YGELTVRQNLELhARlfHLPAA----------EIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLI 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 169 MDEPTSSltnkeVD-------YLFLImnQL-RKEGTAIvYIS-HKLAEIRRiCDRYTVM 218
Cdd:NF033858 421 LDEPTSG-----VDpvardmfWRLLI--ELsREDGVTI-FIStHFMNEAER-CDRISLM 470
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-222 |
4.86e-12 |
|
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: 65.18 E-value: 4.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN-ISYnkldhklAAQlgigiiyqeLSVIDELTVL 98
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGsIAY-------VSQ---------EPWIQNGTIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 99 ENLYIGRhltkkicgvniiDWREMRVRAAmmlLRV-GLKVDLD-----------EKVANLSISHKQMLEIAKTLMLDAKV 166
Cdd:cd03250 84 ENILFGK------------PFDEERYEKV---IKAcALEPDLEilpdgdlteigEKGINLSGGQKQRISLARAVYSDADI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 167 IIMDEPTSSLTNKEVDYLF--LIMNQLRKEGTAIVyISHKLaEIRRICDRYTVMKDGS 222
Cdd:cd03250 149 YLLDDPLSAVDAHVGRHIFenCILGLLLNNKTRIL-VTHQL-QLLPHADQIVVLDNGR 204
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
254-495 |
4.86e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 67.28 E-value: 4.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 254 KENVSNLAHETVFEVRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRS 331
Cdd:PRK09452 3 KLNKQPSSLSPLVELRGISkSFDGKEViSNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 332 PldavkkgmayitESRRDN------GFFPNFSIAQNMAISRSLKdggykgamglfhEVDEQRTAENQRELLALK--CHSV 403
Cdd:PRK09452 83 A------------ENRHVNtvfqsyALFPHMTVFENVAFGLRMQ------------KTPAAEITPRVMEALRMVqlEEFA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 404 NQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGID----VGAKAEIYKVMRQLaddGKVILMVSSELPEIITVCDRI 479
Cdd:PRK09452 139 QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDyklrKQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRI 215
|
250
....*....|....*.
gi 16131913 480 AVFCEGRLTQILTNRD 495
Cdd:PRK09452 216 VVMRDGRIEQDGTPRE 231
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
279-472 |
5.63e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 64.56 E-value: 5.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRlngkdispRSPLDAVkkgmAYITESRRDNGFFPnFSI 358
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR--------RAGGARV----AYVPQRSEVPDSLP-LTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 359 AQNMAISRSLKDGGYKGamglfHEVDEQRTAENQRELLALKCHSVNQnITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
Cdd:NF040873 75 RDLVAMGRWARRGLWRR-----LTRDDRAAVDDALERVGLADLAGRQ-LGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190
....*....|....*....|....*....|....
gi 16131913 439 GIDVGAKAEIYKVMRQLADDGKVILMVSSELPEI 472
Cdd:NF040873 149 GLDAESRERIIALLAEEHARGATVVVVTHDLELV 182
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
267-489 |
6.55e-12 |
|
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: 65.32 E-value: 6.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT-SRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRsPLDAVKKGMAYI 343
Cdd:cd03254 4 EFENVNfSYDEKKpvLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI-SRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 344 TEsrrDNGFFPNfSIAQNMAISRSL-KDGGYKGAMGLFHEVDEQRTAENQREllalkcHSVNQNITELSGGNQQKVLISK 422
Cdd:cd03254 83 LQ---DTFLFSG-TIMENIRLGRPNaTDEEVIEAAKEAGAHDFIMKLPNGYD------TVLGENGGNLSQGERQLLAIAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELpEIITVCDRIAVFCEGRLTQ 489
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAHRL-STIKNADKILVLDDGKIIE 217
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
272-487 |
7.16e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 66.01 E-value: 7.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgmayiteSRRDNG 351
Cdd:PRK13641 16 TPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKK-------LRKKVS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 352 FFPNFSIAQnMAISRSLKDGGYkGAMGL-FHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEV 430
Cdd:PRK13641 89 LVFQFPEAQ-LFENTVLKDVEF-GPKNFgFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 431 IIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-221 |
8.39e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 65.91 E-value: 8.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTI-------TINNIsYNKLDHklaaqlgIGIIYQE----- 88
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdllTEENV-WDIRHK-------IGMVFQNpdnqf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 89 --LSVIDELTV-LENlyigrhltkkicgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
Cdd:PRK13650 95 vgATVEDDVAFgLEN--------------KGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIrRICDRYTVMKDG 221
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNG 216
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
281-487 |
8.71e-12 |
|
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: 64.44 E-value: 8.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAvKKGMAYitesrRDNGFFPNFSIAQ 360
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADR-PVSMLF-----QENNLFAHLTVEQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 361 NMAISRS--LKdggykgamglFHEVDEQRTAENQREL-LALKchsVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
Cdd:cd03298 90 NVGLGLSpgLK----------LTAEDRQAIEVALARVgLAGL---EKRLPGELSGGERQRVALARVLVRDKPVLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16131913 438 RGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:cd03298 157 AALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
21-209 |
9.19e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 64.12 E-value: 9.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLdhklaAQLGIGIIYQELSVIDELTVLEN 100
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-----AKPYCTYIGHNLGLKLEMTVFEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 101 LYIgrhltkkicgvniidWREM-----RVRAAMMLLRvgLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
Cdd:PRK13541 91 LKF---------------WSEIynsaeTLYAAIHYFK--LHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETN 153
|
170 180 190
....*....|....*....|....*....|....
gi 16131913 176 LTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIR 209
Cdd:PRK13541 154 LSKENRDLLNNLIVMKANSGGIVLLSSHLESSIK 187
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
253-493 |
1.08e-11 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 65.06 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 253 MKENVSNlaHETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCL-------FGVdkRAGGEIRLN 323
Cdd:COG1117 1 MTAPAST--LEPKIEVRNLNVYygDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndliPGA--RVEGEILLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 324 GKDI-SPRSPLDAVKK--GMAyitesrrdngF-----FPnFSIAQNMAISrsLKDGGYKGAmglfHEVDEqrTAENqrel 395
Cdd:COG1117 77 GEDIyDPDVDVVELRRrvGMV----------FqkpnpFP-KSIYDNVAYG--LRLHGIKSK----SELDE--IVEE---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 396 lALK--------CHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVIlmvss 467
Cdd:COG1117 134 -SLRkaalwdevKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIV----- 207
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 16131913 468 elpeIIT--------VCDRIAVFCEGRL------TQILTN 493
Cdd:COG1117 208 ----IVThnmqqaarVSDYTAFFYLGELvefgptEQIFTN 243
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
263-492 |
1.12e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 65.42 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 263 ETVFEVRNVTSR----DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKK 338
Cdd:PRK13635 3 EEIIRVEHISFRypdaATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 339 -GMAYiteSRRDNGFFPN-------FSIaQNMAISRSLkdggykgamgLFHEVDEQRTAENQRELLALKCHSvnqniteL 410
Cdd:PRK13635 83 vGMVF---QNPDNQFVGAtvqddvaFGL-ENIGVPREE----------MVERVDQALRQVGMEDFLNREPHR-------L 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 411 SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIITVcDRIAVFCEGRLTQ 489
Cdd:PRK13635 142 SGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGItVLSITHDLDEAAQA-DRVIVMNKGEILE 220
|
...
gi 16131913 490 ILT 492
Cdd:PRK13635 221 EGT 223
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-221 |
1.18e-11 |
|
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: 62.47 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI---NNISYnkldhklaaqlgi 82
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWgstVKIGY------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 83 giiYQELSvideltvlenlyiGrhltkkicGvniidWReMRVRaammllrvglkvdldekvanlsishkqmleIAKTLML 162
Cdd:cd03221 68 ---FEQLS-------------G--------G-----EK-MRLA------------------------------LAKLLLE 87
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 163 DAKVIIMDEPTSSLTNKEVDYLfliMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:cd03221 88 NPNLLLLDEPTNHLDLESIEAL---EEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-203 |
1.60e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.82 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE--PTKGTITINNISynkldhklaaqlgigiIYQELSVIDELt 96
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQ----------------FGREASLIDAI- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 97 vlenlyigrhltkkicgvniidWREMRVRAAMMLL-RVGLK--VDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
Cdd:COG2401 107 ----------------------GRKGDFKDAVELLnAVGLSdaVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190
....*....|....*....|....*....|...
gi 16131913 174 SSL---TNKEVDYLFLIMnqLRKEGTAIVYISH 203
Cdd:COG2401 165 SHLdrqTAKRVARNLQKL--ARRAGITLVVATH 195
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
16-232 |
2.22e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.13 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 16 GPVHALKSVNLTVYPGEIHALLGENGAGKS----TLMKVLS--GIhepTKGTITIN-----NISYNKLDHKLAAQlgIGI 84
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAanGR---IGGSATFNgreilNLPEKELNKLRAEQ--ISM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 85 IYQelsviDELTVLeNLY--IGRHLTKKIC---GVNIIDWREMRVRaamMLLRVglKVDLDEKVANL-----SISHKQML 154
Cdd:PRK09473 102 IFQ-----DPMTSL-NPYmrVGEQLMEVLMlhkGMSKAEAFEESVR---MLDAV--KMPEARKRMKMyphefSGGMRQRV 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 155 EIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:PRK09473 171 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
279-489 |
2.29e-11 |
|
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: 63.66 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYITEsrrDNGFFpNFSI 358
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADP-AWLRRQVGVVLQ---ENVLF-NRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 359 AQNMAISRSlkdggykgAMGLFHEVDEQRTA---ENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
Cdd:cd03252 93 RDNIALADP--------GMSMERVIEAAKLAgahDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131913 436 PTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
Cdd:cd03252 165 ATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKNA-DRIIVMEKGRIVE 216
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-224 |
3.57e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 65.43 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNklDHKLAA-QLGIGIIYQELSVIDElTVL 98
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR--DYTLASlRNQVALVSQNVHLFND-TIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 99 ENLYIGRhlTKKICgvniidwREMRVRAAMML--------LRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMD 170
Cdd:PRK11176 435 NNIAYAR--TEQYS-------REQIEEAARMAyamdfinkMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILD 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131913 171 EPTSSLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSV 224
Cdd:PRK11176 506 EATSALDTESERAIQAALDELQKNRTSLV-IAHRLSTIEK-ADEILVVEDGEIV 557
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
253-487 |
3.84e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 63.95 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 253 MKENVSNLAHEtvFEVRnvTSRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFGVDKragGEIRLNGKDISP 329
Cdd:PRK13651 1 MQIKVKNIVKI--FNKK--LPTELKALDNVSVEINQGEFIAIIGQTGSGKTtfiEHLNALLLPDT---GTIEWIFKDEKN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 330 RSPLDAVKKGMA-------------YITESRRDNGFFPNFSIAQnMAISRSLKDGGYkGA--MGLFHEVDEQRTAEnQRE 394
Cdd:PRK13651 74 KKKTKEKEKVLEklviqktrfkkikKIKEIRRRVGVVFQFAEYQ-LFEQTIEKDIIF-GPvsMGVSKEEAKKRAAK-YIE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 395 LLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIIT 474
Cdd:PRK13651 151 LVGLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLE 230
|
250
....*....|...
gi 16131913 475 VCDRIAVFCEGRL 487
Cdd:PRK13651 231 WTKRTIFFKDGKI 243
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
263-482 |
4.40e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 63.26 E-value: 4.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 263 ETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK-----RAGGEIRLNGKDISPrSPLDA 335
Cdd:PRK14243 8 ETVLRTENLNVYygSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYA-PDVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 336 VkkgmayitESRRDNGF-------FPNfSIAQNMAISRSLKdgGYKGAMglfHEVDEqrTAENQRELLALKCHSVNQNIT 408
Cdd:PRK14243 87 V--------EVRRRIGMvfqkpnpFPK-SIYDNIAYGARIN--GYKGDM---DELVE--RSLRQAALWDEVKDKLKQSGL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVF 482
Cdd:PRK14243 151 SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFF 223
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-221 |
5.39e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.38 E-value: 5.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 17 PVhaLKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISynkldhklAAQLGIGIIYQELSVIDELT 96
Cdd:PLN03232 1250 PV--LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCD--------VAKFGLTDLRRVLSIIPQSP 1319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 97 VLENLYIgRHLTKKICGVNIID-WREMR---VRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
Cdd:PLN03232 1320 VLFSGTV-RFNIDPFSEHNDADlWEALErahIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEA 1398
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16131913 173 TSSLtnkEVDYLFLIMNQLRKE--GTAIVYISHKLAEIRRiCDRYTVMKDG 221
Cdd:PLN03232 1399 TASV---DVRTDSLIQRTIREEfkSCTMLVIAHRLNTIID-CDKILVLSSG 1445
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-203 |
5.77e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 64.96 E-value: 5.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN---ISYnkLDHKLAAQLGI 82
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGEtvkLAY--VDQSRDALDPN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 83 GIIYQELSviDELTVLEnlyIGRhltkkicgvniidwREMRVRAamMLLRVGLK-VDLDEKVANLSISHKQMLEIAKTLM 161
Cdd:TIGR03719 401 KTVWEEIS--GGLDIIK---LGK--------------REIPSRA--YVGRFNFKgSDQQKKVGQLSGGERNRVHLAKTLK 459
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16131913 162 LDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRK-EGTAIVyISH 203
Cdd:TIGR03719 460 SGGNVLLLDEPTNDL---DVETLRALEEALLNfAGCAVV-ISH 498
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
281-488 |
6.33e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 63.22 E-value: 6.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKK-----GMAY-ITESR------- 347
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQirkkvGLVFqFPESQlfeetvl 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 348 RDNGFFPnfsiaQNMAISRSlkdggykgamglfhevDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCC 427
Cdd:PRK13649 105 KDVAFGP-----QNFGVSQE----------------EAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAME 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913 428 PEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLT 488
Cdd:PRK13649 164 PKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
265-487 |
7.24e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.41 E-value: 7.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 265 VFEVRNVT-SRDRKKVRDISFSVCRGEILGFAGLVGSGRTelMNCLFGVD------KRAGGEIRLNGKdisPRSPLDAVK 337
Cdd:PRK10418 4 QIELRNIAlQAAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLLDGK---PVAPCALRG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 338 KGMAYITESRRdNGFFPNFSIAQNmAISRSLKDGGYKGAMGLFHEVDEQRTAENQRellALKCHSVnqnitELSGGNQQK 417
Cdd:PRK10418 79 RKIATIMQNPR-SAFNPLHTMHTH-ARETCLALGKPADDATLTAALEAVGLENAAR---VLKLYPF-----EMSGGMLQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913 418 VLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYK-VMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:PRK10418 149 MMIALALLCEAPFIIADEPTTDLDVVAQARILDlLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
20-227 |
8.78e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 62.72 E-value: 8.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN------NISYNKLDHKLAAQLGIGIIYQELSVID 93
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaipaNLKKIKEVKRLRKEIGLVFQFPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 94 ElTVLENLYIGR-HLTKkicgvniiDWREMRVRAAMMLLRVGLKVDLDEKVA-NLSISHKQMLEIAKTLMLDAKVIIMDE 171
Cdd:PRK13645 106 E-TIEKDIAFGPvNLGE--------NKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 172 PTSSLTNK-EVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:PRK13645 177 PTGGLDPKgEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
6-227 |
9.09e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 62.72 E-value: 9.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN--ISYNKLDhKLAAQLGIG 83
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRG-LLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 84 IIYQE------LSVIDELTV--LENLYIGR-HLTKKIC-GVNIIDWREMRvraammllrvglkvdlDEKVANLSISHKQM 153
Cdd:PRK13638 81 TVFQDpeqqifYTDIDSDIAfsLRNLGVPEaEITRRVDeALTLVDAQHFR----------------HQPIQCLSHGQKKR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:PRK13638 145 VAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHG 218
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
274-487 |
9.12e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 61.97 E-value: 9.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 274 RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDA-VKKGMAYIT-ESrrdnG 351
Cdd:COG1137 14 GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIT-HLPMHKrARLGIGYLPqEA----S 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 352 FFPNFSIAQN-MAIsrsLKdggykgamglFHEVDEQRTAENQRELLA---LKcHSVNQNITELSGGNQQKVLISKWLCCC 427
Cdd:COG1137 89 IFRKLTVEDNiLAV---LE----------LRKLSKKEREERLEELLEefgIT-HLRKSKAYSLSGGERRRVEIARALATN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913 428 PEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILM----VSselpEIITVCDRIAVFCEGRL 487
Cdd:COG1137 155 PKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLItdhnVR----ETLGICDRAYIISEGKV 214
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
289-486 |
9.45e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 64.30 E-value: 9.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 289 GEILGFAGLVGSGRTELMNCLF-----GVDKraGGEIRLNGKDISprspLDAVKKGMAYItesRRDNGFFPNFSIAQNMA 363
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAfrspkGVKG--SGSVLLNGMPID----AKEMRAISAYV---QQDDLFIPTLTVREHLM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 364 ISRSLKdggykgaMGLFHEVDEQRTAENQ--RELLALKCHS----VNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
Cdd:TIGR00955 122 FQAHLR-------MPRRVTKKEKRERVDEvlQALGLRKCANtrigVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131913 438 RGIDVGAKAEIYKVMRQLADDGKVILMV----SSELPEIItvcDRIAVFCEGR 486
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKGKTIICTihqpSSELFELF---DKIILMAEGR 244
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-227 |
9.85e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 64.08 E-value: 9.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHklaAQL--GIGIIYQELSVID 93
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE---AALrqAISVVSQRVHLFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 94 ElTVLENLYIGRHltkkicgvNIIDWREMRVraammLLRVGLK--VDLDEKVAN--------LSISHKQMLEIAKTLMLD 163
Cdd:PRK11160 428 A-TLRDNLLLAAP--------NASDEALIEV-----LQQVGLEklLEDDKGLNAwlgeggrqLSGGEQRRLGIARALLHD 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 164 AKVIIMDEPTSSL---TNKEvdylflIMNQLRK--EGTAIVYISHKLAEIRRIcDRYTVMKDGSSVCSG 227
Cdd:PRK11160 494 APLLLLDEPTEGLdaeTERQ------ILELLAEhaQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQG 555
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
267-464 |
1.15e-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: 60.97 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSplDAVKKGMAYIT 344
Cdd:cd03231 2 EADELTcERDGRALfSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR--DSIARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 ESrrdNGFFPNFSIAQNMAISRSlkdggykgamglFHEVDEQRTAENQRELLALKCHSVNQniteLSGGNQQKVLISKWL 424
Cdd:cd03231 80 HA---PGIKTTLSVLENLRFWHA------------DHSDEQVEEALARVGLNGFEDRPVAQ----LSAGQQRRVALARLL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16131913 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILM 464
Cdd:cd03231 141 LSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVL 180
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
267-487 |
1.35e-10 |
|
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: 61.48 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT---SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpLDAVKKGMAYI 343
Cdd:cd03253 2 EFENVTfayDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT-LDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 344 TEsrrDNGFFpNFSIAQNMAISRSlkdggykGAmglfheVDEQ-----RTAENQRELLALK---CHSVNQNITELSGGNQ 415
Cdd:cd03253 81 PQ---DTVLF-NDTIGYNIRYGRP-------DA------TDEEvieaaKAAQIHDKIMRFPdgyDTIVGERGLKLSGGEK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 416 QKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIITvCDRIAVFCEGRL 487
Cdd:cd03253 144 QRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVN-ADKIIVLKDGRI 213
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
272-495 |
1.51e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.10 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSP---LDAVKK--GMAY-ITE 345
Cdd:PRK13646 16 TPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyIRPVRKriGMVFqFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 346 SR-------RDNGFFP-NFsiaqNMAISRsLKDGGYKGAMGLFHEvdeqrtaenqRELLAlkchsvnQNITELSGGNQQK 417
Cdd:PRK13646 96 SQlfedtveREIIFGPkNF----KMNLDE-VKNYAHRLLMDLGFS----------RDVMS-------QSPFQMSGGQMRK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 418 VLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLA-DDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
Cdd:PRK13646 154 IAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKE 232
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
263-487 |
1.53e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 61.57 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 263 ETVFEVRNV--TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGV---DKRAGGEIRLNGKDISPRSPLdavk 337
Cdd:PRK09984 2 QTIIRVEKLakTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRL---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 338 kgMAYITESRRDNGF-FPNFSIAQNMAISRSLKDGGYkGAMGLFHEVDEQRT-AENQRELLALK----CHSVNQNITELS 411
Cdd:PRK09984 78 --ARDIRKSRANTGYiFQQFNLVNRLSVLENVLIGAL-GSTPFWRTCFSWFTrEQKQRALQALTrvgmVHFAHQRVSTLS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 412 GGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:PRK09984 155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-213 |
1.61e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.59 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE-----PTKGTITI--NNISYNKLD-HK 75
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFfnQNIYERRVNlNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 76 LAAQlgIGIIYQELSVIdELTVLENLYIGrhltkkicgVNIIDWR---------EMRVRAAMMLLRVglKVDLDEKVANL 146
Cdd:PRK14258 86 LRRQ--VSMVHPKPNLF-PMSVYDNVAYG---------VKIVGWRpkleiddivESALKDADLWDEI--KHKIHKSALDL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913 147 SISHKQMLEIAKTLMLDAKVIIMDEPTSSL---TNKEVDYlfLIMN-QLRKEGTaIVYISHKLAEIRRICD 213
Cdd:PRK14258 152 SGGQQQRLCIARALAVKPKVLLMDEPCFGLdpiASMKVES--LIQSlRLRSELT-MVIVSHNLHQVSRLSD 219
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
265-503 |
1.78e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 61.63 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 265 VFEVRNVTSR---DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS-PRSPLDAVKKGM 340
Cdd:PRK13639 1 ILETRDLKYSypdGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 341 AYITESRRDNGFFPnfSIAQNMAIsrslkdggykGAM--GLFHEVDEQRTAEnqrellALKCHSV----NQNITELSGGN 414
Cdd:PRK13639 81 GIVFQNPDDQLFAP--TVEEDVAF----------GPLnlGLSKEEVEKRVKE------ALKAVGMegfeNKPPHHLSGGQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 415 QQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNR 494
Cdd:PRK13639 143 KKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPK 222
|
....*....
gi 16131913 495 DDMSEEEIM 503
Cdd:PRK13639 223 EVFSDIETI 231
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-442 |
2.33e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.05 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN--------------NISYNK 71
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEqdlivarlqqdpprNVEGTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 72 LDH---KLAAQLGIGIIYQELSVideltVLENLYIGRHLTKKICGVNIID----WR-EMRVRAAMMLlrvgLKVDLDEKV 143
Cdd:PRK11147 84 YDFvaeGIEEQAEYLKRYHDISH-----LVETDPSEKNLNELAKLQEQLDhhnlWQlENRINEVLAQ----LGLDPDAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 144 ANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYL--FLimnqLRKEGtAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLegFL----KTFQG-SIIFISHDRSFIRNMATRIVDLDRG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 222 SsvcsgIVSDVSNDDIV------RLMVgRELQN---------------------------RFNAMKE---------NV-- 257
Cdd:PRK11147 230 K-----LVSYPGNYDQYllekeeALRV-EELQNaefdrklaqeevwirqgikarrtrnegRVRALKAlrrerserrEVmg 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 258 -SNLAHET-------VFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK-D 326
Cdd:PRK11147 304 tAKMQVEEasrsgkiVFEMENVNYQidGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 327 IS----PRSPLDAVKKGMAYITESRRD---NGffpnfsiaQNMAISRSLKDggykgamGLFHEvdeqrtaenQRELLALK 399
Cdd:PRK11147 384 VAyfdqHRAELDPEKTVMDNLAEGKQEvmvNG--------RPRHVLGYLQD-------FLFHP---------KRAMTPVK 439
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 16131913 400 ChsvnqniteLSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDV 442
Cdd:PRK11147 440 A---------LSGGERNRLLLARLFLKPSNLLILDEPTNDLDV 473
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
259-495 |
2.70e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 60.93 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 259 NLAHETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS--PRSPLD 334
Cdd:PRK11831 1 EQSVANLVDMRGVSFTrgNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPamSRSRLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 335 AVKKGMAYITESrrdNGFFPNFSIAQNMAIsrSLKDggykgamglfHevdEQRTAENQRELLALKCHSV------NQNIT 408
Cdd:PRK11831 81 TVRKRMSMLFQS---GALFTDMNVFDNVAY--PLRE----------H---TQLPAPLLHSTVMMKLEAVglrgaaKLMPS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDR---IA---V 481
Cdd:PRK11831 143 ELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHayiVAdkkI 222
|
250
....*....|....
gi 16131913 482 FCEGRLTQILTNRD 495
Cdd:PRK11831 223 VAHGSAQALQANPD 236
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
15-199 |
2.85e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.25 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 15 FGPVHalksvnLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDH-KLAAQLG-IGIIYQELSvi 92
Cdd:PRK13543 27 FGPLD------FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRsRFMAYLGhLPGLKADLS-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 93 deltVLENLYIgrhltkkICGVNIIDWREMRVRAammLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
Cdd:PRK13543 99 ----TLENLHF-------LCGLHGRRAKQMPGSA---LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
170 180
....*....|....*....|....*...
gi 16131913 173 TSSLTNKEVDYL-FLIMNQLRKEGTAIV 199
Cdd:PRK13543 165 YANLDLEGITLVnRMISAHLRGGGAALV 192
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
21-221 |
3.57e-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: 62.53 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHK-LAAQlgIGIIYQElsvidelTVLE 99
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAsLRAA--IGIVPQD-------TVLF 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 100 NLYIgrhltkkicGVNI----IDWREMRVRAA---------MMLL------RV---GLKvdldekvanLSISHKQMLEIA 157
Cdd:COG5265 445 NDTI---------AYNIaygrPDASEEEVEAAaraaqihdfIESLpdgydtRVgerGLK---------LSGGEKQRVAIA 506
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 158 KTLMLDAKVIIMDEPTSSL---TNKEvdylflIMNQLR---KEGTAIVyISHKLAEIRRiCDRYTVMKDG 221
Cdd:COG5265 507 RTLLKNPPILIFDEATSALdsrTERA------IQAALRevaRGRTTLV-IAHRLSTIVD-ADEILVLEAG 568
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
10-203 |
4.04e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.22 E-value: 4.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTI--TIN-NISYNKLDHklAAQLGigiiy 86
Cdd:PRK15064 324 NLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwSENaNIGYYAQDH--AYDFE----- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 87 QELSVIDELTvlenlyigrhltkkicgvniiDWR-----EMRVRAAM--MLLRvglKVDLDEKVANLSISHKQMLEIAKT 159
Cdd:PRK15064 397 NDLTLFDWMS---------------------QWRqegddEQAVRGTLgrLLFS---QDDIKKSVKVLSGGEKGRMLFGKL 452
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16131913 160 LMLDAKVIIMDEPTSSLTNKEVDYLfliMNQLRK-EGTAIvYISH 203
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMDMESIESL---NMALEKyEGTLI-FVSH 493
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-278 |
4.18e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 62.22 E-value: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIsynkldhklAAQLGIGI-IYQELSVIDELTv 97
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS---------AALIAISSgLNGQLTGIENIE- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 98 LENLYIGrhLTK-KICGV--NIIDWREmrvraammllrvgLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
Cdd:PRK13545 108 LKGLMMG--LTKeKIKEIipEIIEFAD-------------IGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 175 ----SLTNKEVDYlfliMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSN--DDIVRLMVGRELQN 248
Cdd:PRK13545 173 vgdqTFTKKCLDK----MNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDhyDEFLKKYNQMSVEE 248
|
250 260 270
....*....|....*....|....*....|
gi 16131913 249 RFNAMKENVSNLAHETVFEVRNVTSRDRKK 278
Cdd:PRK13545 249 RKDFREEQISQFQHGLLQEDQTGRERKRKK 278
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-217 |
4.61e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.11 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 26 LTVYPGEIH-----ALLGENGAGKSTLMKVLSGIHEPTKGTITIN-NISYNKldhklaaqlgigiiyQELSVIDELTVLE 99
Cdd:COG1245 356 LEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlKISYKP---------------QYISPDYDGTVEE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 100 NLY--IGRHLTKKICGVNIIDwremrvraammllRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLt 177
Cdd:COG1245 421 FLRsaNTDDFGSSYYKTEIIK-------------PLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHL- 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16131913 178 nkEVDYLFLIMNQLR-----KEGTAIVyISHKLAEIRRICDRYTV 217
Cdd:COG1245 487 --DVEQRLAVAKAIRrfaenRGKTAMV-VDHDIYLIDYISDRLMV 528
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
275-495 |
4.72e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 59.93 E-value: 4.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCL-----FGVDKRAGGEIRLNGKDISPrspldavkkgMAYITESRRD 349
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQDIFK----------MDVIELRRRV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 350 NGFF------PNFSIAQNMAISRSLkDGGYKGAMGLFHEVdeqRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKW 423
Cdd:PRK14247 85 QMVFqipnpiPNLSIFENVALGLKL-NRLVKSKKELQERV---RWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
276-491 |
4.76e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.44 E-value: 4.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 276 RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK-----RAGGEIRLNGKDISPRS-PLDAVKKGMAYITESrrd 349
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYERRvNLNRLRRQVSMVHPK--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 350 NGFFPnFSIAQNMAISrsLKDGGYKGAMglfhEVDE-QRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCP 428
Cdd:PRK14258 97 PNLFP-MSVYDNVAYG--VKIVGWRPKL----EIDDiVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 429 EVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIITVCDRIAVF--CEGRLTQIL 491
Cdd:PRK14258 170 KVLLMDEPCFGLDPIASMKVESLIQSLRLRSELtMVIVSHNLHQVSRLSDFTAFFkgNENRIGQLV 235
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
289-485 |
4.92e-10 |
|
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: 62.34 E-value: 4.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 289 GEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprspldavkkgMAYITESRRDNGFFPNFSIAQNMAISRS- 367
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI------------LTNISDVHQNMGYCPQFDAIDDLLTGREh 2032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 368 --LkdggYKGAMGLFHEvDEQRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAK 445
Cdd:TIGR01257 2033 lyL----YARLRGVPAE-EIEKVANWSIQSLGLSLYA-DRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16131913 446 AEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEG 485
Cdd:TIGR01257 2107 RMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
261-487 |
5.21e-10 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 61.62 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 261 AHETVFEVRNVT------SRDRKKVRDISFSVCRGEILGFAGLVGSGRT----ELMNCLFGVDKRAGGEIRLNGKDIspr 330
Cdd:COG4172 2 MSMPLLSVEDLSvafgqgGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 331 spLDAVKKGMAYItesR-RDNGF-F--------PNFSIAQNMAISRSLKDGgykgaMGlfhevdeqRTAENQR--ELLA- 397
Cdd:COG4172 79 --LGLSERELRRI---RgNRIAMiFqepmtslnPLHTIGKQIAEVLRLHRG-----LS--------GAAARARalELLEr 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 398 ---------LKC--HsvnqnitELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMV 465
Cdd:COG4172 141 vgipdperrLDAypH-------QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLI 213
|
250 260
....*....|....*....|..
gi 16131913 466 SSELPEIITVCDRIAVFCEGRL 487
Cdd:COG4172 214 THDLGVVRRFADRVAVMRQGEI 235
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
279-486 |
5.38e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 60.00 E-value: 5.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRdngFFPNFSI 358
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQHVR---LFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 359 AQNM--AISRSLKDGGYKgamGLFH-------EVDEQRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWLCCCPE 429
Cdd:PRK11300 98 IENLlvAQHQQLKTGLFS---GLLKtpafrraESEALDRAATWLERVGLLEHA-NRQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 430 VIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIITVCDRIAVFCEGR 486
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEHNVtVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
267-490 |
5.78e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 60.89 E-value: 5.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavkkgmayit 344
Cdd:PRK11432 8 VLKNITKRFGSNTviDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSI------------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 eSRRD-------NGFFPNFSIAQNMaisrslkdgGYKGAM-GLFHEVDEQRTAEnQRELLALKCHSvNQNITELSGGNQQ 416
Cdd:PRK11432 76 -QQRDicmvfqsYALFPHMSLGENV---------GYGLKMlGVPKEERKQRVKE-ALELVDLAGFE-DRYVDQISGGQQQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
Cdd:PRK11432 144 RVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQI 218
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
267-490 |
6.18e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 61.72 E-value: 6.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT---SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFG---VDkraGGEIRLNGKDIspRS-PLDAVKKG 339
Cdd:COG1132 341 EFENVSfsyPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRfydPT---SGRILIDGVDI--RDlTLESLRRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 340 MAYITEsrrDNGFFpNFSIAQNMAISRSlkdggykgamglfhEVDEQRTAEnqrellALK---CHS------------VN 404
Cdd:COG1132 416 IGVVPQ---DTFLF-SGTIRENIRYGRP--------------DATDEEVEE------AAKaaqAHEfiealpdgydtvVG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 405 QNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELpEIITVCDRIAVFCE 484
Cdd:COG1132 472 ERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRL-STIRNADRILVLDD 549
|
....*.
gi 16131913 485 GRLTQI 490
Cdd:COG1132 550 GRIVEQ 555
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
265-499 |
6.51e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 60.11 E-value: 6.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 265 VFEVRNVTSR-----DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKK- 338
Cdd:PRK13642 4 ILEVENLVFKyekesDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 339 GMAYITESRRDNGFFPNFSIA---QNMAISRSlkdggykgamGLFHEVDEQRTAENqreLLALKchsvNQNITELSGGNQ 415
Cdd:PRK13642 84 GMVFQNPDNQFVGATVEDDVAfgmENQGIPRE----------EMIKRVDEALLAVN---MLDFK----TREPARLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 416 QKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIITvCDRIAVFCEGRL------T 488
Cdd:PRK13642 147 QRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLtVLSITHDLDEAAS-SDRILVMKAGEIikeaapS 225
|
250
....*....|.
gi 16131913 489 QILTNRDDMSE 499
Cdd:PRK13642 226 ELFATSEDMVE 236
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
21-199 |
7.32e-10 |
|
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: 58.41 E-value: 7.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGihEPTKGTITiNNISYNKLDHKLAAQLGIGIIYQELSVIDELTVLEN 100
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVIT-GEILINGRPLDKNFQRSTGYVEQQDVHSPNLTVREA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 101 LyigrhltkkicgvniidwremRVRAammLLRvglkvdldekvaNLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKE 180
Cdd:cd03232 100 L---------------------RFSA---LLR------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
170 180
....*....|....*....|..
gi 16131913 181 VdylFLIMNQLRK---EGTAIV 199
Cdd:cd03232 144 A---YNIVRFLKKladSGQAIL 162
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-204 |
7.43e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.81 E-value: 7.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKldHKLAAQLGIGIIYQELSVIDELTVLEN 100
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK--DLCTYQKQLCFVGHRSGINPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 101 LYIGRHLTKKICGVNiidwremrvraamMLLRV-GLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNK 179
Cdd:PRK13540 95 CLYDIHFSPGAVGIT-------------ELCRLfSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
170 180
....*....|....*....|....*
gi 16131913 180 EVDYLFLIMNQLRKEGTAIVYISHK 204
Cdd:PRK13540 162 SLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
267-500 |
7.66e-10 |
|
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: 59.17 E-value: 7.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT----SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCL---FGVDKragGEIRLNGKDISPRSpLDAVKKG 339
Cdd:cd03251 2 EFKNVTfrypGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIprfYDVDS---GRILIDGHDVRDYT-LASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 340 MAYITEsrrdNGFFPNFSIAQNMAISRSlkdggykGAMGlfHEVDEQRTAENQRELLALKCHSVNQNITE----LSGGNQ 415
Cdd:cd03251 78 IGLVSQ----DVFLFNDTVAENIAYGRP-------GATR--EEVEEAARAANAHEFIMELPEGYDTVIGErgvkLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 416 QKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELpEIITVCDRIAVFCEGRLTQILTNRD 495
Cdd:cd03251 145 QRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKN-RTTFVIAHRL-STIENADRIVVLEDGKIVERGTHEE 222
|
....*
gi 16131913 496 DMSEE 500
Cdd:cd03251 223 LLAQG 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
279-492 |
7.67e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 60.82 E-value: 7.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSI 358
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 359 AQNMAISRSLKdggykgamGLFHEVDEQRTAENQREL-LALKCHSVNQnitELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
Cdd:PRK10070 124 LDNTAFGMELA--------GINAEERREKALDALRQVgLENYAHSYPD---ELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 438 RGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILT 492
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
249-498 |
8.20e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.43 E-value: 8.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 249 RFNAMKENVSN----LAHETVFEVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAG--GEIRL 322
Cdd:PLN03211 50 KFENMKNKGSNikriLGHKPKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 323 NGkdispRSPLDAVKKGMAYITEsrrDNGFFPNFSIAQNMA------ISRSLKdggykgamglfhEVDEQRTAENQRELL 396
Cdd:PLN03211 130 NN-----RKPTKQILKRTGFVTQ---DDILYPHLTVRETLVfcsllrLPKSLT------------KQEKILVAESVISEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 397 AL-KCHSV---NQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILmVSSELP-- 470
Cdd:PLN03211 190 GLtKCENTiigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIV-TSMHQPss 268
|
250 260
....*....|....*....|....*...
gi 16131913 471 EIITVCDRIAVFCEGRLTQILTNRDDMS 498
Cdd:PLN03211 269 RVYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
267-487 |
9.81e-10 |
|
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: 58.66 E-value: 9.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSRDRK----KVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAY 342
Cdd:cd03244 4 EFKNVSLRYRPnlppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIS-KIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 ITE-------SRRDNgFFPnFSIAQNMAISRSLKDGGYKGAMglfhevdeqrtaENQRELLALKCHSVNQNiteLSGGNQ 415
Cdd:cd03244 83 IPQdpvlfsgTIRSN-LDP-FGEYSDEELWQALERVGLKEFV------------ESLPGGLDTVVEEGGEN---LSVGQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131913 416 QKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITvCDRIAVFCEGRL 487
Cdd:cd03244 146 QLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGRV 215
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
274-487 |
1.04e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 59.25 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 274 RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK--DISPRSPLdAVKKGMAYITESRRDNG 351
Cdd:PRK13638 12 QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLL-ALRQQVATVFQDPEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 352 FFPNFsiaqNMAISRSLKDGGykgamglfheVDEQRTAENQRELLAL--KCHSVNQNITELSGGNQQKVLISKWLCCCPE 429
Cdd:PRK13638 91 FYTDI----DSDIAFSLRNLG----------VPEAEITRRVDEALTLvdAQHFRHQPIQCLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 430 VIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:PRK13638 157 YLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-232 |
1.26e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.79 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIhEPTKGTITINNIS----------------------------YNKL 72
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPleawsaaelarhraylsqqqtppfampvFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 73 DHKLAAQLGIGIIYQELSVIDELTVLENLyIGRHLTKKICGvniiDWRemRVRAAMMLlrvglkvdldekvanlsishkq 152
Cdd:PRK03695 91 TLHQPDKTRTEAVASALNEVAEALGLDDK-LGRSVNQLSGG----EWQ--RVRLAAVV---------------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 153 mLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:PRK03695 142 -LQVWPDINPAGQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-100 |
1.29e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.52 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 1 MATPYI-SMAGIGKSFGP-VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGtitinnisynklDHKLAA 78
Cdd:PRK11819 1 MMAQYIyTMNRVSKVVPPkKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG------------EARPAP 68
|
90 100
....*....|....*....|..
gi 16131913 79 QLGIGIIYQELSVIDELTVLEN 100
Cdd:PRK11819 69 GIKVGYLPQEPQLDPEKTVREN 90
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
265-504 |
1.33e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 59.05 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 265 VFEVRNVT---SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMA 341
Cdd:PRK13652 3 LIETRDLCysySGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT-KENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 342 YITESRRDNGFFPnfSIAQNMAISRSlkdggykgAMGLFHEVDEQRTAENQReLLALKcHSVNQNITELSGGNQQKVLIS 421
Cdd:PRK13652 82 LVFQNPDDQIFSP--TVEQDIAFGPI--------NLGLDEETVAHRVSSALH-MLGLE-ELRDRVPHHLSGGEKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEE 500
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
....
gi 16131913 501 EIMA 504
Cdd:PRK13652 230 DLLA 233
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
21-227 |
1.39e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 57.66 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPT---KGTITINNISYNKLDHKLAAQlgigIIY--QELSVIDEL 95
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGE----IIYvsEEDVHFPTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 96 TVLEnlyigrhltkkicgvniidwremrvraammLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPT-- 173
Cdd:cd03233 99 TVRE------------------------------TLDFALRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTrg 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 174 --SSLTNKEVDYLFLIMNQLRkeGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
Cdd:cd03233 149 ldSSTALEILKCIRTMADVLK--TTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
269-486 |
1.58e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 57.66 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 269 RNVTSRDRKK------VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGV---DKRAGGEIRLNG---KDISPRSPLDAV 336
Cdd:cd03233 7 RNISFTTGKGrskipiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNGipyKEFAEKYPGEII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 337 kkgmaYITESrrDNgFFPNFSIAQNMAISRSLKDggykgamglfhevdeqrtaenqrellalkchsvNQNITELSGGNQQ 416
Cdd:cd03233 87 -----YVSEE--DV-HFPTLTVRETLDFALRCKG---------------------------------NEFVRGISGGERK 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVS----SelPEIITVCDRIAVFCEGR 486
Cdd:cd03233 126 RVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSlyqaS--DEIYDLFDKVLVLYEGR 197
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
279-490 |
1.63e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 58.70 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCL-----FGVDKRAGGEIRLNGKDI-SPR-SPLDAVKK-GMAYITESRrdn 350
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIySPDvDPIEVRREvGMVFQYPNP--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 351 gfFPNFSIAQNMAISrsLKdggYKGAMGLFHEVDEQ-RTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPE 429
Cdd:PRK14267 97 --FPHLTIYDNVAIG--VK---LNGLVKSKKELDERvEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPK 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913 430 VIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSElPEIITVCDRIAVFCEGRLTQI 490
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSP-AQAARVSDYVAFLYLGKLIEV 229
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
410-489 |
1.92e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 58.57 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILmVSSELPEIITVCDRIAVFCEGRLTQ 489
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVII-VTHNLAQAARISDRAALFFDGRLVE 242
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-217 |
2.04e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 58.19 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 27 TVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN--ISYNKldhklaaqlgigiiyQELSVIDELTVLENLYig 104
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdtVSYKP---------------QYIKADYEGTVRDLLS-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 105 rhltKKICGVNIIDWREMRVRAAMMLLRVglkvdLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYL 184
Cdd:cd03237 84 ----SITKDFYTHPYFKTEIAKPLQIEQI-----LDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMA 154
|
170 180 190
....*....|....*....|....*....|....*
gi 16131913 185 FLIMNQ--LRKEGTAIVyISHKLAEIRRICDRYTV 217
Cdd:cd03237 155 SKVIRRfaENNEKTAFV-VEHDIIMIDYLADRLIV 188
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-208 |
2.11e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.80 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQlG 81
Cdd:PRK10247 4 NSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQ-Q 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 82 IGIIYQELSVIDElTVLENLyigrhltkkicgvnIIDW--REMRVRAAMM---LLRVGLKVD-LDEKVANLSISHKQMLE 155
Cdd:PRK10247 83 VSYCAQTPTLFGD-TVYDNL--------------IFPWqiRNQQPDPAIFlddLERFALPDTiLTKNIAELSGGEKQRIS 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 156 IAKTLMLDAKVIIMDEPTSSL--TNKE-VDYlfLIMNQLRKEGTAIVYISHKLAEI 208
Cdd:PRK10247 148 LIRNLQFMPKVLLLDEITSALdeSNKHnVNE--IIHRYVREQNIAVLWVTHDKDEI 201
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-232 |
2.38e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.30 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSG-IHEP-------TKGTITINNISYNKLDHKLAAQLGiGIIYQELSVI 92
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGgaprgarVTGDVTLNGEPLAAIDAPRLARLR-AVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 93 DELTVLENLYIGRHLTKKICGVNIIDWREMRVRAammLLRVGLKVDLDEKVANLSISHKQMLEIAKTL---------MLD 163
Cdd:PRK13547 96 FAFSAREIVLLGRYPHARRAGALTHRDGEIAWQA---LALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-211 |
2.50e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.12 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 25 NLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQL-------GIGiiyqelsviDELTV 97
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLlylghqpGIK---------TELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 98 LENLYIGRHLTKKIcgvniidwREMRVRAAmmLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLT 177
Cdd:PRK13538 92 LENLRFYQRLHGPG--------DDEALWEA--LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 16131913 178 NKEVDYLF-LIMNQLRKEGTAIVYISHKL----AEIRRI 211
Cdd:PRK13538 162 KQGVARLEaLLAQHAEQGGMVILTTHQDLpvasDKVRKL 200
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
282-500 |
2.74e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 57.64 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVdKRAGGEIRLNGKDISPRSPLD-AVKKgmAYITESRRdngffPNFSIAQ 360
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAElARHR--AYLSQQQT-----PPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 361 NMAISRSLKDGGykgamglfHEVDEQRTAENQRELLAL--KCHSvnqNITELSGGNQQKV-----LISKWLCCCPE--VI 431
Cdd:PRK03695 87 FQYLTLHQPDKT--------RTEAVASALNEVAEALGLddKLGR---SVNQLSGGEWQRVrlaavVLQVWPDINPAgqLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 432 IFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEE 500
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
263-489 |
3.05e-09 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 57.44 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 263 ETVFEVRNVTsrdrKKV----------RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSP 332
Cdd:COG4181 6 APIIELRGLT----KTVgtgageltilKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 333 lDAVKKGmayitesRRDN-GF-FPNFSIAQNM-------------------AISRSLKDggykgAMGLFHEVDeqrtaen 391
Cdd:COG4181 82 -DARARL-------RARHvGFvFQSFQLLPTLtalenvmlplelagrrdarARARALLE-----RVGLGHRLD------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 392 qrellalkcHSVNQniteLSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSElP 470
Cdd:COG4181 142 ---------HYPAQ----LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHD-P 207
|
250
....*....|....*....
gi 16131913 471 EIITVCDRIAVFCEGRLTQ 489
Cdd:COG4181 208 ALAARCDRVLRLRAGRLVE 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
279-487 |
3.58e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 57.69 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYItesrrdngffpnFSI 358
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIV------------FQN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 359 AQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENqRELLALKCHSV-NQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
Cdd:PRK13644 86 PETQFVGRTVEEDLAFGPENLCLPPIEIRKRVD-RALAEIGLEKYrHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16131913 438 RGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEiITVCDRIAVFCEGRL 487
Cdd:PRK13644 165 SMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKI 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
267-487 |
3.77e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 58.17 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT------SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSP--LDAVKK 338
Cdd:COG1135 3 ELENLSktfptkGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSEreLRAARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 339 GMAYItesrrdngfFPNF------SIAQNmaISRSLKDGGYKGAmglfhEVdEQRTAenqrELLALkchsV------NQN 406
Cdd:COG1135 83 KIGMI---------FQHFnllssrTVAEN--VALPLEIAGVPKA-----EI-RKRVA----ELLEL----VglsdkaDAY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 407 ITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEG 485
Cdd:COG1135 138 PSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENG 217
|
..
gi 16131913 486 RL 487
Cdd:COG1135 218 RI 219
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
18-259 |
4.14e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 57.80 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKlDHKLAAQLGIGIIYQElsvideltv 97
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA-ENVWNLRRKIGMVFQN--------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 98 LENLYIGRHLTKKIC-GVNI--IDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
Cdd:PRK13642 90 PDNQFVGATVEDDVAfGMENqgIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 175 SLTNKEVDYLFLIMNQLR-KEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGIVSDV--SNDDIVRlmVGRELQNRFN 251
Cdd:PRK13642 170 MLDPTGRQEIMRVIHEIKeKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELfaTSEDMVE--IGLDVPFSSN 246
|
....*...
gi 16131913 252 AMKENVSN 259
Cdd:PRK13642 247 LMKDLRKN 254
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-217 |
5.51e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.67 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 26 LTVYPGEIHA-----LLGENGAGKSTLMKVLSGIHEPTKGTITIN-NISYNKldhklaaqlgigiiyQELSVIDELTVLE 99
Cdd:PRK13409 355 LEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElKISYKP---------------QYIKPDYDGTVED 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 100 NLY-IGRHLTKKICGVNIIDwremrvraammllRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtn 178
Cdd:PRK13409 420 LLRsITDDLGSSYYKSEIIK-------------PLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHL-- 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16131913 179 kEVDYLFLIMNQLR-----KEGTAIVyISHKLAEIRRICDRYTV 217
Cdd:PRK13409 485 -DVEQRLAVAKAIRriaeeREATALV-VDHDIYMIDYISDRLMV 526
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
14-222 |
7.40e-09 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 56.19 E-value: 7.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 14 SFGP-VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNI---SYNKLDHKLAAQLGIGIIYQEL 89
Cdd:cd03290 9 SWGSgLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKnesEPSFEATRSRNRYSVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 90 SVIDElTVLENLYIGRHLTKKICGVnIIDwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
Cdd:cd03290 89 WLLNA-TVEENITFGSPFNKQRYKA-VTD--ACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 170 DEPTSSLTNKEVDYLFL--IMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGS 222
Cdd:cd03290 165 DDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDGS 218
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-232 |
8.02e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 56.39 E-value: 8.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHePTKGTITINNISYNKLD-HKLA---AQLGigiiyQELSVIDELT 96
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSaAELArhrAYLS-----QQQSPPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 97 VLEnlYIGRHLTKKIcgvniidwREMRVRAAMMLL--RVGLKVDLDEKVANLSISHKQMLEIAKTLM-------LDAKVI 167
Cdd:COG4138 86 VFQ--YLALHQPAGA--------SSEAVEQLLAQLaeALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 168 IMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:COG4138 156 LLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEV 220
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-204 |
8.41e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.58 E-value: 8.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGihEPTKGTITINNISYN--KLDHKLaaQLGIGIIYQELSVIDELTVL 98
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGGDRLVNgrPLDSSF--QRSIGYVQQQDLHLPTSTVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 99 ENL----YIGR--HLTK--KICGVN-IIDWREMRVRAAMMLLRVGlkvdldekvANLSISHKQMLEIAKTLMLDAKVII- 168
Cdd:TIGR00956 855 ESLrfsaYLRQpkSVSKseKMEYVEeVIKLLEMESYADAVVGVPG---------EGLNVEQRKRLTIGVELVAKPKLLLf 925
|
170 180 190
....*....|....*....|....*....|....*.
gi 16131913 169 MDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHK 204
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQ 961
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
268-487 |
1.01e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 56.63 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 268 VRNVTSRDRKK---VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRspldavkkgmayit 344
Cdd:COG4586 24 LKGLFRREYREveaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKR-------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 esRRDNgffpnfsiAQNMAI---SRS-------LKDgGYK--GAMglfHEVDEQRTAENQREL---LALKcHSVNQNITE 409
Cdd:COG4586 90 --RKEF--------ARRIGVvfgQRSqlwwdlpAID-SFRllKAI---YRIPDAEYKKRLDELvelLDLG-ELLDTPVRQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 410 LSGGnqQKV-------LISKwlcccPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAV 481
Cdd:COG4586 155 LSLG--QRMrcelaaaLLHR-----PKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIV 227
|
....*.
gi 16131913 482 FCEGRL 487
Cdd:COG4586 228 IDHGRI 233
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
255-502 |
1.14e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 56.55 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 255 ENVS-NLAHETVFEVRNVTSRDRKkvrdisfsVCRGEILGFAGLVGSGRTELMNCLFGVdkraggEIRLNGKDISPRSPL 333
Cdd:PRK13645 10 DNVSyTYAKKTPFEFKALNNTSLT--------FKKNKVTCVIGTTGSGKSTMIQLTNGL------IISETGQTIVGDYAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 334 DAVKKGMAYITESRRDNGF---FPNFSIAQNmAISRSLkdggykgAMGLFH-EVDEQRTAENQRELL---ALKCHSVNQN 406
Cdd:PRK13645 76 PANLKKIKEVKRLRKEIGLvfqFPEYQLFQE-TIEKDI-------AFGPVNlGENKQEAYKKVPELLklvQLPEDYVKRS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 407 ITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEG 485
Cdd:PRK13645 148 PFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEG 227
|
250 260
....*....|....*....|...
gi 16131913 486 RLT------QILTNRDDMSEEEI 502
Cdd:PRK13645 228 KVIsigspfEIFSNQELLTKIEI 250
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-208 |
1.28e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 57.65 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLD-HKLAAQlgIGIIYQElSVIDELTVLE 99
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGlHDLRFK--ITIIPQD-PVLFSGSLRM 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 100 NL-YIGRHLTKKIcgvniidWREMR---VRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
Cdd:TIGR00957 1379 NLdPFSQYSDEEV-------WWALElahLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAA 1451
|
170 180 190
....*....|....*....|....*....|...
gi 16131913 176 LtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEI 208
Cdd:TIGR00957 1452 V-DLETDNLIQSTIRTQFEDCTVLTIAHRLNTI 1483
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
24-65 |
1.32e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 57.12 E-value: 1.32e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 16131913 24 VNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN 65
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLD 392
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
30-204 |
1.63e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 57.20 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 30 PGEIHALLGENGAGKSTLMKVLSG-IHEPT-KGTITINNisyNKLDHKLAAQLGI----GIIYQELSVIDELTVLENLYI 103
Cdd:PLN03211 93 PGEILAVLGPSGSGKSTLLNALAGrIQGNNfTGTILANN---RKPTKQILKRTGFvtqdDILYPHLTVRETLVFCSLLRL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 104 GRHLTKKicgvniidwrEMRVRAAMMLLRVGLKVDLDEKVAN-----LSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTN 178
Cdd:PLN03211 170 PKSLTKQ----------EKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180
....*....|....*....|....*.
gi 16131913 179 KEVDYLFLIMNQLRKEGTAIVYISHK 204
Cdd:PLN03211 240 TAAYRLVLTLGSLAQKGKTIVTSMHQ 265
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-486 |
1.67e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.44 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI--NNISynklDHKLAAQLGIG 83
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlgGDMA----DARHRRAVCPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 84 IIY--QEL--SVIDELTVLENL-YIGR---HltkkicgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLE 155
Cdd:NF033858 78 IAYmpQGLgkNLYPTLSVFENLdFFGRlfgQ-----------DAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 156 IAKTLMLDAKVIIMDEPTSSltnkeVDYL----F--LImNQLRKEG---TAIV---YIShklaEIRRiCDRYTVMKDGSS 223
Cdd:NF033858 147 LCCALIHDPDLLILDEPTTG-----VDPLsrrqFweLI-DRIRAERpgmSVLVataYME----EAER-FDWLVAMDAGRV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 224 VCSGIVSDV----SNDDI----VRLM-VGRELQNRFNAMKENVSNLAHETVFEVRNVTSR--DRKKVRDISFSVCRGEIL 292
Cdd:NF033858 216 LATGTPAELlartGADTLeaafIALLpEEKRRGHQPVVIPPRPADDDDEPAIEARGLTMRfgDFTAVDHVSFRIRRGEIF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 293 GFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRsplD-AVKKGMAYITESrrdngffpnFS------IAQNMAI- 364
Cdd:NF033858 296 GFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAG---DiATRRRVGYMSQA---------FSlygeltVRQNLELh 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 365 SRslkdggykgamgLFHeVDEQRTAENQRELLA---LKCHsVNQNITELSGGNQQKV-----LISKwlcccPEVIIFDEP 436
Cdd:NF033858 364 AR------------LFH-LPAAEIAARVAEMLErfdLADV-ADALPDSLPLGIRQRLslavaVIHK-----PELLILDEP 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 437 TRGIDVGAKAEIYKVMRQLADDGKVILMVSS------ELpeiitvCDRIAVFCEGR 486
Cdd:NF033858 425 TSGVDPVARDMFWRLLIELSREDGVTIFISThfmneaER------CDRISLMHAGR 474
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
283-487 |
1.72e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 54.97 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 283 SFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavkkgmayiteSRR-------DNGFFPN 355
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPP-------------SRRpvsmlfqENNLFSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 356 FSIAQNMAIsrslkdgGYKGAMGLFHEvdeqrtaenQRELLALKCHSV------NQNITELSGGNQQKVLISKWLCCCPE 429
Cdd:PRK10771 86 LTVAQNIGL-------GLNPGLKLNAA---------QREKLHAIARQMgiedllARLPGQLSGGQRQRVALARCLVREQP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 430 VIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:PRK10771 150 ILLLDEPFSALDPALRQEMLTLVSQVCQERQLtLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-221 |
2.02e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.06 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 17 PVhaLKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKL---DHKLAaqlgIGIIYQElSVID 93
Cdd:PLN03130 1253 PV--LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFglmDLRKV----LGIIPQA-PVLF 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 94 ELTVLENL-YIGRHltkkicgvNIIDWREMRVRAAMM-LLR---VGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVII 168
Cdd:PLN03130 1326 SGTVRFNLdPFNEH--------NDADLWESLERAHLKdVIRrnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILV 1397
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 169 MDEPTSSLtnkEVDYLFLIMNQLRKEGTA--IVYISHKLAEIrrI-CDRYTVMKDG 221
Cdd:PLN03130 1398 LDEATAAV---DVRTDALIQKTIREEFKSctMLIIAHRLNTI--IdCDRILVLDAG 1448
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
10-176 |
2.03e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN---ISY-----NKLDHKlaaqlg 81
Cdd:PRK11819 329 NLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGEtvkLAYvdqsrDALDPN------ 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 82 iGIIYQELSviDEltvLENLYIGRhltkkicgvniidwREMRVRAamMLLRVGLK-VDLDEKVANLSISHKQMLEIAKTL 160
Cdd:PRK11819 403 -KTVWEEIS--GG---LDIIKVGN--------------REIPSRA--YVGRFNFKgGDQQKKVGVLSGGERNRLHLAKTL 460
|
170
....*....|....*.
gi 16131913 161 MLDAKVIIMDEPTSSL 176
Cdd:PRK11819 461 KQGGNVLLLDEPTNDL 476
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
271-469 |
2.23e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 55.12 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 271 VTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRlngkdispRSPldavKKGMAYITESRRDN 350
Cdd:PRK09544 12 VSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------RNG----KLRIGYVPQKLYLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 351 GFFPnfsiaqnMAISR--SLKDGGYKGAMglfhevdeqrtaenqreLLALK----CHSVNQNITELSGGNQQKVLISKWL 424
Cdd:PRK09544 80 TTLP-------LTVNRflRLRPGTKKEDI-----------------LPALKrvqaGHLIDAPMQKLSGGETQRVLLARAL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16131913 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSEL 469
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDL 181
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
276-488 |
2.26e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 54.50 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 276 RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS----PRSPLDAVKKGMAYitesrRDNG 351
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknREVPFLRRQIGMIF-----QDHH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 352 FFPNFSIAQNMAISRSLKdggykGAMGlfheVDEQRTAENQRELLALKCHSVNQNItELSGGNQQKVLISKWLCCCPEVI 431
Cdd:PRK10908 90 LLMDRTVYDNVAIPLIIA-----GASG----DDIRRRVSAALDKVGLLDKAKNFPI-QLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 432 IFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLT 488
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
279-487 |
2.28e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 55.08 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPrspLDAVKKGmAYitesRRD--------- 349
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAK---LNRAQRK-AF----RRDiqmvfqdsi 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 350 NGFFPNFSIAQNMAIS-RSLKDggykgamglfheVDEQRTAENQRELL---ALKCHSVNQNITELSGGNQQKVLISKWLC 425
Cdd:PRK10419 100 SAVNPRKTVREIIREPlRHLLS------------LDKAERLARASEMLravDLDDSVLDKRPPQLSGGQLQRVCLARALA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131913 426 CCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:PRK10419 168 VEPKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
253-487 |
2.70e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 55.18 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 253 MKENVSNlaHETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPR 330
Cdd:PRK10575 1 MQEYTNH--SDTTFALRNVSFRvpGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 331 SPlDAVKKGMAYITEsrrdngffpNFSIAQNMAISRSLKDGGY--KGAMGLFHEVDEQRTaENQRELLALKCHSvNQNIT 408
Cdd:PRK10575 79 SS-KAFARKVAYLPQ---------QLPAAEGMTVRELVAIGRYpwHGALGRFGAADREKV-EEAISLVGLKPLA-HRLVD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:PRK10575 147 SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEM 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
275-479 |
3.15e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 54.33 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYIT-------ESR 347
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP-EIYRQQVSYCAqtptlfgDTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 348 RDNGFFPnFSIAQNmaisrslkdggykgamglfhEVDEQRTAEN-QRelLALKCHSVNQNITELSGGNQQKVLISKWLCC 426
Cdd:PRK10247 98 YDNLIFP-WQIRNQ--------------------QPDPAIFLDDlER--FALPDTILTKNIAELSGGEKQRISLIRNLQF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131913 427 CPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEiITVCDRI 479
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIaVLWVTHDKDE-INHADKV 207
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
281-469 |
3.30e-08 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 54.25 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKkgmayITESRRDNG-------FF 353
Cdd:COG4161 20 DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKA-----IRLLRQKVGmvfqqynLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 354 PNFSIAQNM--AISRSL---KDGGYKGAMGLFHEVDEQRTAEnqrellALKCHsvnqniteLSGGNQQKVLISKWLCCCP 428
Cdd:COG4161 95 PHLTVMENLieAPCKVLglsKEQAREKAMKLLARLRLTDKAD------RFPLH--------LSGGQQQRVAIARALMMEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16131913 429 EVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSEL 469
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEV 201
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-203 |
3.42e-08 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 52.93 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI---NNISYnkLDHK-------LAAQlgigIIY---Q 87
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpegEDLLF--LPQRpylplgtLREQ----LIYpwdD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 88 ELSvideltvlenlyigrhltkkicgvniidwremrvraammllrvglkvdLDEkvanlsishKQMLEIAKTLMLDAKVI 167
Cdd:cd03223 91 VLS------------------------------------------------GGE---------QQRLAFARLLLHKPKFV 113
|
170 180 190
....*....|....*....|....*....|....*.
gi 16131913 168 IMDEPTSSLTnkeVDYLFLIMNQLRKEGTAIVYISH 203
Cdd:cd03223 114 FLDEATSALD---EESEDRLYQLLKELGITVISVGH 146
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
17-232 |
4.59e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 54.75 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 17 PVHALKSVNLTVYPGEIHALLGENGAGKS-TLMKVLSGIHEPtkGTITINNISYNKLD-HKLAAQLGIGIIYQELSVI-- 92
Cdd:PRK11022 19 PFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMAEKLEFNGQDlQRISEKERRNLVGAEVAMIfq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 93 DELTVLENLY-IGRHLTKKICGVNIIDWREMRVRAAMMLLRVGL---KVDLDEKVANLSISHKQMLEIAKTLMLDAKVII 168
Cdd:PRK11022 97 DPMTSLNPCYtVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 169 MDEPTSSL-TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:PRK11022 177 ADEPTTALdVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
267-487 |
4.60e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 54.81 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT------SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPrspLDAvkkgm 340
Cdd:PRK11153 3 ELKNISkvfpqgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTA---LSE----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 341 AYITESRRDNGF-FPNFsiaqNMAISRSLKDggyKGAMGLfhEVDEQRTAE-NQR--ELLALkchsV------NQNITEL 410
Cdd:PRK11153 75 KELRKARRQIGMiFQHF----NLLSSRTVFD---NVALPL--ELAGTPKAEiKARvtELLEL----VglsdkaDRYPAQL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 411 SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:PRK11153 142 SGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
264-487 |
5.70e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 54.01 E-value: 5.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 264 TVFEVRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLD-AVKKGM 340
Cdd:PRK13548 1 AMLEARNLSvRLGGRTLlDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 341 ----AYITesrrdngfFPnFSIAQNMaisrslkdggykgAMGL----FHEVDEQRTAENQRELLALkCHSVNQNITELSG 412
Cdd:PRK13548 81 lpqhSSLS--------FP-FTVEEVV-------------AMGRaphgLSRAEDDALVAAALAQVDL-AHLAGRDYPQLSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 413 GNQQKVLISKWLCCC------PEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVilmvsselpeiiTVC---------- 476
Cdd:PRK13548 138 GEQQRVQLARVLAQLwepdgpPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGL------------AVIvvlhdlnlaa 205
|
250
....*....|....
gi 16131913 477 ---DRIAVFCEGRL 487
Cdd:PRK13548 206 ryaDRIVLLHQGRL 219
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
263-487 |
6.13e-08 |
|
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: 53.24 E-value: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 263 ETVFEVRNVT----SR-DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP------RS 331
Cdd:cd03248 9 KGIVKFQNVTfaypTRpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyehkylHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 332 PLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQrtaenqrellalkchsVNQNITELS 411
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTE----------------VGEKGSQLS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 412 GGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKViLMVSSELpEIITVCDRIAVFCEGRL 487
Cdd:cd03248 153 GGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTV-LVIAHRL-STVERADQILVLDGGRI 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
267-469 |
6.19e-08 |
|
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: 55.06 E-value: 6.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR---DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavkkgmayi 343
Cdd:TIGR02868 336 ELRDLSAGypgAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQ----------- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 344 TESRRDNGFFPN----F--SIAQNMAISRSlkdggykgamglfhEVDEQRTAENQR-----ELLALKCHSVNQNITE--- 409
Cdd:TIGR02868 405 DEVRRRVSVCAQdahlFdtTVRENLRLARP--------------DATDEELWAALErvglaDWLRALPDGLDTVLGEgga 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913 410 -LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSEL 469
Cdd:TIGR02868 471 rLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-236 |
6.28e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 54.00 E-value: 6.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 24 VNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN--NISYNKLDHKLAAQLGIGIIYQELSVIDELTVLEN- 100
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDgeNIPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFDNv 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 101 ---LYIGRHLTKKIcgvniidwreMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLT 177
Cdd:PRK11831 106 aypLREHTQLPAPL----------LHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913 178 NKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV-SNDD 236
Cdd:PRK11831 176 PITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALqANPD 236
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
262-499 |
6.28e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 53.99 E-value: 6.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 262 HETVFEVRNVT----SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldavk 337
Cdd:PRK13648 4 KNSIIVFKNVSfqyqSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDN------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 338 kgmayITESRRDNGFFpnFSIAQNMAISRSLKdggYKGAMGLfhEVDEQRTAENQREllalkchsVNQNITE-------- 409
Cdd:PRK13648 78 -----FEKLRKHIGIV--FQNPDNQFVGSIVK---YDVAFGL--ENHAVPYDEMHRR--------VSEALKQvdmlerad 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 410 -----LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEI-----ITVCDR 478
Cdd:PRK13648 138 yepnaLSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNItIISITHDLSEAmeadhVIVMNK 217
|
250 260
....*....|....*....|.
gi 16131913 479 IAVFCEGRLTQILTNRDDMSE 499
Cdd:PRK13648 218 GTVYKEGTPTEIFDHAEELTR 238
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
296-488 |
7.02e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 54.50 E-value: 7.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 296 GLVGSGRTELMNCLFGVDKRAGGEIRLNGK---DISPRSPLDAVKKGMAYITESRRdngFFPNFSIAQNMAIsrslkdgG 372
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKGICLPPEKRRIGYVFQDAR---LFPHYKVRGNLRY-------G 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 373 YKGAM-GLFHEVdeqrtaenqRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKV 451
Cdd:PRK11144 101 MAKSMvAQFDKI---------VALLGIE-PLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPY 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 16131913 452 MRQLADDGKV-ILMVSSELPEIITVCDRIAVFCEGRLT 488
Cdd:PRK11144 171 LERLAREINIpILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-482 |
8.68e-08 |
|
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: 54.79 E-value: 8.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 30 PGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITiNNISYNK-LDH-----------KLAAQlgigiiyqELSV------ 91
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYD-EEPSWDEvLKRfrgtelqdyfkKLANG--------EIKVahkpqy 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 92 IDEL------TVlenlyigRHLTKKIcgvniiDWREMrvrAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
Cdd:COG1245 169 VDLIpkvfkgTV-------RELLEKV------DERGK---LDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKdGSSVCSGIVSDVSNddiVRlmVGre 245
Cdd:COG1245 233 FYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHILY-GEPGVYGVVSKPKS---VR--VG-- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 246 lqnrFNAM------KENVSNLAHETVFEVRnvTSRDRKKVRDI-----------SFS-------VCRGEILGFAGLVGSG 301
Cdd:COG1245 305 ----INQYldgylpEENVRIRDEPIEFEVH--APRREKEEETLveypdltksygGFSleveggeIREGEVLGIVGPNGIG 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 302 RTELMNCLFGVDKRAGGEIRLNGKdIS--PRspldavkkgmaYItesrrdngffpnfSIAQNMAIsRSLKDGGYKGAMG- 378
Cdd:COG1245 379 KTTFAKILAGVLKPDEGEVDEDLK-ISykPQ-----------YI-------------SPDYDGTV-EEFLRSANTDDFGs 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 379 --LFHEVDEQrtaenqrelLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLA 456
Cdd:COG1245 433 syYKTEIIKP---------LGLE-KLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFA 502
|
490 500
....*....|....*....|....*..
gi 16131913 457 DD-GKVILMVSSELPEIITVCDRIAVF 482
Cdd:COG1245 503 ENrGKTAMVVDHDIYLIDYISDRLMVF 529
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
277-483 |
9.10e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 54.04 E-value: 9.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKR----AGGEIRLNGKDI---SPRSPLDAVKKGMAYI---TES 346
Cdd:PRK15093 21 KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLlrlSPRERRKLVGHNVSMIfqePQS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 347 RRDngffPNFSIAQNMAisRSLKDGGYKGAMglfhevdEQRTAENQR---ELL---ALKCHS--VNQNITELSGGNQQKV 418
Cdd:PRK15093 101 CLD----PSERVGRQLM--QNIPGWTYKGRW-------WQRFGWRKRraiELLhrvGIKDHKdaMRSFPYELTEGECQKV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 419 LISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAV-FC 483
Cdd:PRK15093 168 MIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVlYC 234
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
21-270 |
9.49e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 53.32 E-value: 9.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEpTKGTITINNISYNKLDHKlAAQLGIGIIYQELSVIDElTVLEN 100
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQ-KWRKAFGVIPQKVFIFSG-TFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 101 L-YIGRHLTKKIcgvniidWR---EMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
Cdd:cd03289 97 LdPYGKWSDEEI-------WKvaeEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 177 TNKEVDYLFLIMNQLRKEGTaIVYISHKLAEIRRiCDRYTVMKDGS-----------SVCSGIVSDVSNDDIVRLMVGRE 245
Cdd:cd03289 170 DPITYQVIRKTLKQAFADCT-VILSEHRIEAMLE-CQRFLVIEENKvrqydsiqkllNEKSHFKQAISPSDRLKLFPRRN 247
|
250 260
....*....|....*....|....*
gi 16131913 246 LQNRFNAMKENVSNLAHETVFEVRN 270
Cdd:cd03289 248 SSKSKRKPRPQIQALQEETEEEVQD 272
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-221 |
9.86e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 54.08 E-value: 9.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 1 MATpyISMAGIGKSF-GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDhklAAQ 79
Cdd:PRK11650 1 MAG--LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELE---PAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 80 LGIGIIYQELSVIDELTVLENLYIGrhLtkKICGVNiIDWREMRVRAAMMLLRVG-LkvdLDEKVANLSISHKQMLEIAK 158
Cdd:PRK11650 76 RDIAMVFQNYALYPHMSVRENMAYG--L--KIRGMP-KAEIEERVAEAARILELEpL---LDRKPRELSGGQRQRVAMGR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913 159 TLMLDAKVIIMDEPTSSLTNKevdylflIMNQLRKE--------GTAIVYISHKLAEIRRICDRYTVMKDG 221
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDAK-------LRVQMRLEiqrlhrrlKTTSLYVTHDQVEAMTLADRVVVMNGG 211
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
263-502 |
9.87e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.20 E-value: 9.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 263 ETVFEVRNVTSR---DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRS-------- 331
Cdd:PRK13647 2 DNIIEVEDLHFRykdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENekwvrskv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 332 ------PLDAVKKGMAYitesrRDNGFFPnfsiaQNMAISRSlkdggykgamglfhEVDEqRTAEnqrellALKchSVN- 404
Cdd:PRK13647 82 glvfqdPDDQVFSSTVW-----DDVAFGP-----VNMGLDKD--------------EVER-RVEE------ALK--AVRm 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 405 QNITE-----LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRI 479
Cdd:PRK13647 129 WDFRDkppyhLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQV 208
|
250 260
....*....|....*....|....*...
gi 16131913 480 AVFCEGRL-----TQILTNRDDMSEEEI 502
Cdd:PRK13647 209 IVLKEGRVlaegdKSLLTDEDIVEQAGL 236
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
281-468 |
1.09e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 52.71 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKkgmayITESRRDNG-------FF 353
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKA-----IRELRRNVGmvfqqynLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 354 PNFSIAQNMaISRSLKDGGykgamglfheVDEQRTAENQRELLA---LKCHSvNQNITELSGGNQQKVLISKWLCCCPEV 430
Cdd:PRK11124 95 PHLTVQQNL-IEAPCRVLG----------LSKDQALARAEKLLErlrLKPYA-DRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 16131913 431 IIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSE 468
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHE 200
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
265-463 |
1.80e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 51.80 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 265 VFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprsPLDAVKKGMAY 342
Cdd:PRK13539 2 MLEGEDLACVrgGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI----DDPDVAEACHY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 ITESrrdNGFFPNFSIAQNMAISRSLKDGGYKG------AMGLFHevdeqrtaenqreLLALKCHsvnqnitELSGGNQQ 416
Cdd:PRK13539 78 LGHR---NAMKPALTVAENLEFWAAFLGGEELDiaaaleAVGLAP-------------LAHLPFG-------YLSAGQKR 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16131913 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMR-QLADDGKVIL 463
Cdd:PRK13539 135 RVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRaHLAQGGIVIA 182
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
409-486 |
2.65e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.17 E-value: 2.65e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGR 486
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
21-87 |
2.78e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 51.72 E-value: 2.78e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGI--HEPTKGTITINNISYNKLDHKLAAQLGIGIIYQ 87
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQ 85
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
277-481 |
2.90e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.40 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLD--AVKKGMAYITESrrdngffP 354
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEwrAVRSDIQMIFQD-------P 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 355 NFSIAQNMA----ISRSLKdggykgamgLFH-EVDEQRTAENQRELLA---LKCHSVNQNITELSGGNQQKVLISKWLCC 426
Cdd:PRK15079 108 LASLNPRMTigeiIAEPLR---------TYHpKLSRQEVKDRVKAMMLkvgLLPNLINRYPHEFSGGQCQRIGIARALIL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 427 CPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAV 481
Cdd:PRK15079 179 EPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLV 234
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
374-469 |
4.10e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 51.21 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 374 KGAMG-LFHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVM 452
Cdd:cd03236 104 KGKVGeLLKKKDERGKLDELVDQLELR-HVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLI 182
|
90
....*....|....*..
gi 16131913 453 RQLADDGKVILMVSSEL 469
Cdd:cd03236 183 RELAEDDNYVLVVEHDL 199
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-62 |
4.12e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.48 E-value: 4.12e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 3 TPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTI 62
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI 369
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
15-213 |
4.60e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 51.32 E-value: 4.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 15 FGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNklDHKLAAQ--------LGIGIIY 86
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFH--GKNLYAPdvdpvevrRRIGMVF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 87 QELSVIDElTVLENLYIGrhltKKICG--VNIIDWREMRVRAAMMLLRVglKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
Cdd:PRK14243 98 QKPNPFPK-SIYDNIAYG----ARINGykGDMDELVERSLRQAALWDEV--KDKLKQSGLSLSGGQQQRLCIARAIAVQP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16131913 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLrKEGTAIVYISHKLAEIRRICD 213
Cdd:PRK14243 171 EVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHNMQQAARVSD 218
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
24-232 |
4.80e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 51.24 E-value: 4.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 24 VNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEP----TKGTITINnisynkldhklaaqlGIGIIYQELSVIDELTVLE 99
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLD---------------GKPVAPCALRGRKIATIMQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 100 N-------LYIGRHLTKKICGVNIIDWREMRVRAAMMllRVGLkvDLDEKVANL-----SISHKQMLEIAKTLMLDAKVI 167
Cdd:PRK10418 87 NprsafnpLHTMHTHARETCLALGKPADDATLTAALE--AVGL--ENAARVLKLypfemSGGMLQRMMIALALLCEAPFI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 168 IMDEPTSSLTN-KEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDV 232
Cdd:PRK10418 163 IADEPTTDLDVvAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
279-503 |
4.93e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 51.24 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 279 VRDISFSVCRGEILGFAGLVGSGRTEL---MNCLFgvdKRAGGEIRLNGKDISPRSPLDAVKK--GM----------AYI 343
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALL---IPSEGKVYVDGLDTSDEENLWDIRNkaGMvfqnpdnqivATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 344 TEsrRDNGFFP-NFSIAQNMAISRslkdggykgamglfheVDEQRTAENQRELLALKCHSvnqniteLSGGNQQKVLISK 422
Cdd:PRK13633 103 VE--EDVAFGPeNLGIPPEEIRER----------------VDESLKKVGMYEYRRHAPHL-------LSGGQKQRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVcDRIAVFCEGRLTQILTNRDDMSEEE 501
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkYGITIILITHYMEEAVEA-DRIIVMDSGKVVMEGTPKEIFKEVE 236
|
..
gi 16131913 502 IM 503
Cdd:PRK13633 237 MM 238
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
263-495 |
6.71e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 50.89 E-value: 6.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 263 ETVFEVRNVTSR-----DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVK 337
Cdd:PRK13650 2 SNIIEVKNLTFKykedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 338 K-GMAYiteSRRDNGFfpnfsiaqnmaISRSLKDggyKGAMGLFHE-VDEQRTAENQRELLALKCHS--VNQNITELSGG 413
Cdd:PRK13650 82 KiGMVF---QNPDNQF-----------VGATVED---DVAFGLENKgIPHEEMKERVNEALELVGMQdfKEREPARLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 414 NQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEiITVCDRIAVFCEGRLTQILT 492
Cdd:PRK13650 145 QKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDE-VALSDRVLVMKNGQVESTST 223
|
...
gi 16131913 493 NRD 495
Cdd:PRK13650 224 PRE 226
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
267-463 |
7.07e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.80 E-value: 7.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIspRSPLDAVKKGMAYIT 344
Cdd:PRK13538 3 EARNLAcERDERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI--RRQRDEYHQDLLYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 345 ESrrdNGFFPNFSIAQNMAIsrslkdggykgAMGLFHEVDEQRTaenqRELLA---------LKCHSvnqniteLSGGNQ 415
Cdd:PRK13538 81 HQ---PGIKTELTALENLRF-----------YQRLHGPGDDEAL----WEALAqvglagfedVPVRQ-------LSAGQQ 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16131913 416 QKVLISK-WLCCCPeVIIFDEPTRGIDVGAKAEIYKVMRQ-LADDGKVIL 463
Cdd:PRK13538 136 RRVALARlWLTRAP-LWILDEPFTAIDKQGVARLEALLAQhAEQGGMVIL 184
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-176 |
7.48e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.22 E-value: 7.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEpTKGTITINNISYNKLDHKlAAQLGIGIIYQELSVIDElTVLEN 100
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQ-TWRKAFGVIPQKVFIFSG-TFRKN 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 101 L-YIGRHLTKKIcgvniidWR---EMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
Cdd:TIGR01271 1312 LdPYEQWSDEEI-------WKvaeEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHL 1384
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
257-487 |
7.70e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 51.89 E-value: 7.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 257 VSNLAHETVFEvrNVT-SRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpL 333
Cdd:PRK13657 328 LGRVKGAVEFD--DVSfSYDNSRqgVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT-R 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 334 DAVKKGMAYITEsrrDNGFFpNFSIAQNMAISRSlkdggykGAMGlfHEVDEQRTAENQRELLALKCHSVNQNITE---- 409
Cdd:PRK13657 405 ASLRRNIAVVFQ---DAGLF-NRSIEDNIRVGRP-------DATD--EEMRAAAERAQAHDFIERKPDGYDTVVGErgrq 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIykvmrQLADD----GKVILMVSSELPEIITVcDRIAVFCEG 485
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALDVETEAKV-----KAALDelmkGRTTFIIAHRLSTVRNA-DRILVFDNG 545
|
..
gi 16131913 486 RL 487
Cdd:PRK13657 546 RV 547
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-203 |
1.40e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 50.74 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN--ISYNKLDHklaaqlgigiiYQEL--SVIDEL 95
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGkpVTAEQPED-----------YRKLfsAVFTDF 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 96 tvlenlyigrHLTKKICGVNIIDWREMRVRAAMMLLRVGLKVDL-DEKVANLSISHKQMLEIAKTLMLDAK--VIIMDE- 171
Cdd:PRK10522 407 ----------HLFDQLLGPEGKPANPALVEKWLERLKMAHKLELeDGRISNLKLSKGQKKRLALLLALAEErdILLLDEw 476
|
170 180 190
....*....|....*....|....*....|....*..
gi 16131913 172 -----PTSsltnKEVDYLFLiMNQLRKEGTAIVYISH 203
Cdd:PRK10522 477 aadqdPHF----RREFYQVL-LPLLQEMGKTIFAISH 508
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
18-210 |
1.49e-06 |
|
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: 48.47 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLmkVLSGIHEPTKGTitinnisYNKLDHKLAAQLGIgiiyqelsVIDELTV 97
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYASGKAR-------LISFLPKFSRNKLI--------FIDQLQF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 98 LENLYIGrHLTkkicgvniidwremrvraammllrvglkvdLDEKVANLSISHKQMLEIAKTLMLDAK--VIIMDEPTSS 175
Cdd:cd03238 71 LIDVGLG-YLT------------------------------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTG 119
|
170 180 190
....*....|....*....|....*....|....*
gi 16131913 176 LTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRR 210
Cdd:cd03238 120 LHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS 154
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
6-249 |
1.61e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.12 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAG--KSTLMKVLSGihePTKGTITINNISYNKLDHKLAAQLGIG 83
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCANRRALRRTIG*H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 84 IIYQElSVIDELTVLENLY-IGRHLTkkicgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
Cdd:NF000106 91 RPVR*-GRRESFSGRENLYmIGR*LD--------LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVsdvsnDDIVRLMV 242
Cdd:NF000106 162 RPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKV-----DELKTKVG 236
|
....*..
gi 16131913 243 GRELQNR 249
Cdd:NF000106 237 GRTLQIR 243
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
267-487 |
2.28e-06 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 48.29 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVD--KRAGGEIRLNGKDISPRSPLDAVKKGMay 342
Cdd:cd03217 2 EIKDLHVSvgGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLGI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 itesrrdngfFPNFsiaQNMAisrslkdggykgamglfhEVDEQRTAENQRellalkchSVNQNiteLSGGNQQKVLISK 422
Cdd:cd03217 80 ----------FLAF---QYPP------------------EIPGVKNADFLR--------YVNEG---FSGGEKKRNEILQ 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVS--SELPEIITVcDRIAVFCEGRL 487
Cdd:cd03217 118 LLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIIThyQRLLDYIKP-DRVHVLYDGRI 183
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-482 |
2.47e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.19 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 27 TVYPGEIHALLGENGAGKSTLMKVLSGI---------HEPT--------KGTITIN---NISYNKLD--HK-----LAAQ 79
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGElipnlgdyeEEPSwdevlkrfRGTELQNyfkKLYNGEIKvvHKpqyvdLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 80 LGIGIIYQELSVIDELTVLENLyigrhltkkicgvniIDwremrvraammllRVGLKVDLDEKVANLSISHKQMLEIAKT 159
Cdd:PRK13409 175 VFKGKVRELLKKVDERGKLDEV---------------VE-------------RLGLENILDRDISELSGGELQRVAIAAA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 160 LMLDAKVIIMDEPTSSLTNKEvdyLFLIMNQLRK--EGTAIVYISHKLAEIRRICDRYTVMKDGSSVcSGIVSDVSNddi 237
Cdd:PRK13409 227 LLRDADFYFFDEPTSYLDIRQ---RLNVARLIRElaEGKYVLVVEHDLAVLDYLADNVHIAYGEPGA-YGVVSKPKG--- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 238 VRlmVG------RELQNrfnamkENVSNLAHETVFEVRNVTSRDRKKV----RDIS-----FS-------VCRGEILGFA 295
Cdd:PRK13409 300 VR--VGineylkGYLPE------ENMRIRPEPIEFEERPPRDESERETlveyPDLTkklgdFSleveggeIYEGEVIGIV 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 296 GLVGSGRTELMNCLFGVDKRAGGEIRLNGK------DISPRSPLdAVKKGMAYITESRRDNGFFPNfsIAQNMAISRSLk 369
Cdd:PRK13409 372 GPNGIGKTTFAKLLAGVLKPDEGEVDPELKisykpqYIKPDYDG-TVEDLLRSITDDLGSSYYKSE--IIKPLQLERLL- 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 370 dggykgamglfhevdeqrtaenqrellalkchsvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIY 449
Cdd:PRK13409 448 ----------------------------------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVA 493
|
490 500 510
....*....|....*....|....*....|....
gi 16131913 450 KVMRQLADD-GKVILMVSSELPEIITVCDRIAVF 482
Cdd:PRK13409 494 KAIRRIAEErEATALVVDHDIYMIDYISDRLMVF 527
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
266-488 |
2.60e-06 |
|
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: 47.69 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 266 FEVRNVT----SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprSPLDAVKKGMA 341
Cdd:cd03247 1 LSINNVSfsypEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVS--DLEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 342 YITESrrdnGFFPNFSIAQNMAisrslkdggykgamglfhevdeqrtaenqrellalkchsvnqniTELSGGNQQKVLIS 421
Cdd:cd03247 79 VLNQR----PYLFDTTLRNNLG--------------------------------------------RRFSGGERQRLALA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131913 422 KWLCCCPEVIIFDEPTRGIDvgAKAEiYKVMRQLAD--DGKVILMVSSELPEIITVcDRIAVFCEGRLT 488
Cdd:cd03247 111 RILLQDAPIVLLDEPTVGLD--PITE-RQLLSLIFEvlKDKTLIWITHHLTGIEHM-DKILFLENGKII 175
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-93 |
3.32e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.51 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI-NNISYNKLDHKLAAqlgigi 84
Cdd:PRK15064 2 LSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLdPNERLGKLRQDQFA------ 75
|
....*....
gi 16131913 85 iYQELSVID 93
Cdd:PRK15064 76 -FEEFTVLD 83
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
269-490 |
3.51e-06 |
|
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: 47.91 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 269 RNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisPRSPLDAvkkGMayitesrr 348
Cdd:cd03220 28 RKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR---VSSLLGL---GG-------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 349 dnGFFPNFSIAQNMAIsrslkdggykgaMGLFHEVDEQRTAENQRELLAL----KChsVNQNITELSGGNQQKVLISKWL 424
Cdd:cd03220 94 --GFNPELTGRENIYL------------NGRLLGLSRKEIDEKIDEIIEFselgDF--IDLPVKTYSSGMKARLAFAIAT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
Cdd:cd03220 158 ALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
410-499 |
3.56e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.63 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAE 215
|
90
....*....|
gi 16131913 490 ILTNRDDMSE 499
Cdd:PRK10938 216 TGEREEILQQ 225
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
267-462 |
3.83e-06 |
|
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: 49.94 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVTSRDRKKV----RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgmay 342
Cdd:TIGR00957 1286 EFRNYCLRYREDLdlvlRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFK---- 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 343 ITESRRDNGFFPNfSIAQNMAISRSLKDGGYKGAMGLFHEVDeqrTAENQRELLALKCHSVNQNiteLSGGNQQKVLISK 422
Cdd:TIGR00957 1362 ITIIPQDPVLFSG-SLRMNLDPFSQYSDEEVWWALELAHLKT---FVSALPDKLDHECAEGGEN---LSVGQRQLVCLAR 1434
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16131913 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVI 462
Cdd:TIGR00957 1435 ALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVL 1474
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
286-487 |
3.92e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 47.85 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 286 VCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP-----RSPLDAvkKGMAYITESRRdngFFPNFSIAQ 360
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeeaRAKLRA--KHVGFVFQSFM---LIPTLNALE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 361 NMAISrslkdggykgamGLFHEVDEQRTAENQRELLALK--CHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
Cdd:PRK10584 108 NVELP------------ALLRGESSRQSRNGAKALLEQLglGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16131913 439 GIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:PRK10584 176 NLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-206 |
4.73e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 48.13 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 30 PGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITiNNISYNK-LDHKLAAQLGIgiiYQELSVIDELTVLENLYIGRHLT 108
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD-DPPDWDEiLDEFRGSELQN---YFTKLLEGDVKVIVKPQYVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 109 KKICG--VNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFL 186
Cdd:cd03236 101 KAVKGkvGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAAR 180
|
170 180
....*....|....*....|
gi 16131913 187 IMNQLRKEGTAIVYISHKLA 206
Cdd:cd03236 181 LIRELAEDDNYVLVVEHDLA 200
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
267-486 |
5.46e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 48.95 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 267 EVRNVT--SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYI 343
Cdd:PRK10790 342 DIDNVSfaYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH-SVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 344 tesRRD-----NGFFPNFSIAQNMA---------------ISRSLKDggykgamGLFHEVDEQ--RTAENQRELLALKch 401
Cdd:PRK10790 421 ---QQDpvvlaDTFLANVTLGRDISeeqvwqaletvqlaeLARSLPD-------GLYTPLGEQgnNLSVGQKQLLALA-- 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 402 svnqnitelsggnqqKVLISKwlcccPEVIIFDEPTRGIDVGAKAEIYKVMRQLADdgKVILMVSSELPEIITVCDRIAV 481
Cdd:PRK10790 489 ---------------RVLVQT-----PQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVEADTILV 546
|
....*
gi 16131913 482 FCEGR 486
Cdd:PRK10790 547 LHRGQ 551
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
21-176 |
6.01e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.07 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGihEPTKGTIT--INNISYNKLDHKLAAQLGigiiYQELSVID--ELT 96
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEgdIRISGFPKKQETFARISG----YCEQNDIHspQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 97 VLENLYIGRHLTKKIcgvNIIDWREMRVRAAMMLLrvglkVDLDE---------KVANLSISHKQMLEIAKTLMLDAKVI 167
Cdd:PLN03140 970 VRESLIYSAFLRLPK---EVSKEEKMMFVDEVMEL-----VELDNlkdaivglpGVTGLSTEQRKRLTIAVELVANPSII 1041
|
....*....
gi 16131913 168 IMDEPTSSL 176
Cdd:PLN03140 1042 FMDEPTSGL 1050
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
282-500 |
7.06e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.82 E-value: 7.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYITES--------RRDNGFF 353
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA-KFGLTDLRRVLSIIPQSpvlfsgtvRFNIDPF 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 354 PNFSIAQNM-AISRS-LKDGGYKGAMGLFHEVDE--QRTAENQRELLALKchsvnqnitelsggnqqKVLISKwlcccPE 429
Cdd:PLN03232 1334 SEHNDADLWeALERAhIKDVIDRNPFGLDAEVSEggENFSVGQRQLLSLA-----------------RALLRR-----SK 1391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913 430 VIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITvCDRIAVFCEGRLTQILTNRDDMSEE 500
Cdd:PLN03232 1392 ILVLDEATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
409-507 |
1.19e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 46.94 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
Cdd:PRK13634 145 ELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTV 224
|
90 100
....*....|....*....|.
gi 16131913 488 TQILTNRDDMSE-EEIMAWAL 507
Cdd:PRK13634 225 FLQGTPREIFADpDELEAIGL 245
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-203 |
1.31e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 47.88 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEihALL--GENGAGKSTLMKVLSGIHEPTKGTITinnisYNKLDHKL-AAQ---LGIG-----IIY--Q 87
Cdd:COG4178 379 LEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRIA-----RPAGARVLfLPQrpyLPLGtlreaLLYpaT 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 88 ELSVIDEltvlenlyigrhltkkicgvniidwremRVRAAmmLLRVGL---KVDLDEKVA---NLSISHKQMLEIAKTLM 161
Cdd:COG4178 452 AEAFSDA----------------------------ELREA--LEAVGLghlAERLDEEADwdqVLSLGEQQRLAFARLLL 501
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16131913 162 LDAKVIIMDEPTSSLTNKEVDYLfliMNQLRKE--GTAIVYISH 203
Cdd:COG4178 502 HKPDWLFLDEATSALDEENEAAL---YQLLREElpGTTVISVGH 542
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
12-214 |
1.51e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 46.73 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 12 GKSFgpvHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN-NISYNKLDHKLAAQlgigiiyqels 90
Cdd:PRK13546 34 NKTF---FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNgEVSVIAISAGLSGQ----------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 91 videLTVLENLYIgrhltKKICgvniIDWREMRVRAAM--MLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVII 168
Cdd:PRK13546 100 ----LTGIENIEF-----KMLC----MGFKRKEIKAMTpkIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16131913 169 MDEPTS----SLTNKEVDYLFlimnQLRKEGTAIVYISHKLAEIRRICDR 214
Cdd:PRK13546 167 IDEALSvgdqTFAQKCLDKIY----EFKEQNKTIFFVSHNLGQVRQFCTK 212
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
411-492 |
1.85e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.04 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 411 SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEI------ITVCDRIAVFCE 484
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAeqlaheLTVIDRGRVIAD 225
|
....*...
gi 16131913 485 GRLTQILT 492
Cdd:NF000106 226 GKVDELKT 233
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
17-256 |
2.14e-05 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 46.39 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 17 PVhaLKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN-NISYNkldhklaaqlgigiiyQELSVIDEL 95
Cdd:cd03291 51 PV--LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSgRISFS----------------SQFSWIMPG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 96 TVLENLyigrhltkkICGVNIIDWREMRVRAAMMLLRVGLKVD------LDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
Cdd:cd03291 113 TIKENI---------IFGVSYDEYRYKSVVKACQLEEDITKFPekdntvLGEGGITLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 170 DEPTSSL---TNKEVdylF------LIMNQLRkegtaiVYISHKLAEIRRiCDRYTVMKDGSSVCSGIVSDVSND--DIV 238
Cdd:cd03291 184 DSPFGYLdvfTEKEI---FescvckLMANKTR------ILVTSKMEHLKK-ADKILILHEGSSYFYGTFSELQSLrpDFS 253
|
250
....*....|....*...
gi 16131913 239 RLMVGRELQNRFNAMKEN 256
Cdd:cd03291 254 SKLMGYDTFDQFSAERRN 271
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-256 |
2.16e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 47.60 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 17 PVhaLKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN-ISYNKldhklaaqlgigiiyqELSVIDEL 95
Cdd:TIGR01271 440 PV--LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGrISFSP----------------QTSWIMPG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 96 TVLENLyigrhltkkICGVNIIDWREMRVRAA------MMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
Cdd:TIGR01271 502 TIKDNI---------IFGLSYDEYRYTSVIKAcqleedIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLL 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 170 DEPTSSL---TNKEVdylF------LIMNQLRkegtaiVYISHKLAEIRRiCDRYTVMKDGSSVCSGIVSDVSND--DIV 238
Cdd:TIGR01271 573 DSPFTHLdvvTEKEI---FesclckLMSNKTR------ILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSELQAKrpDFS 642
|
250
....*....|....*...
gi 16131913 239 RLMVGRELQNRFNAMKEN 256
Cdd:TIGR01271 643 SLLLGLEAFDNFSAERRN 660
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
269-490 |
2.56e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 45.84 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 269 RNVTSRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdISPrsPLDavkKGMayitesr 347
Cdd:COG1134 31 RRRTRREEFWAlKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VSA--LLE---LGA------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 348 rdnGFFPNFSIAQNMAISRSLkdggykgaMGLFHEVDEQRTAEnqrellalkchsvnqnITELSG-GN--QQKV------ 418
Cdd:COG1134 98 ---GFHPELTGRENIYLNGRL--------LGLSRKEIDEKFDE----------------IVEFAElGDfiDQPVktyssg 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 419 ----L---ISkwLCCCPEVIIFDEptrGIDVG-----AKAeiYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
Cdd:COG1134 151 mrarLafaVA--TAVDPDILLVDE---VLAVGdaafqKKC--LARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
....
gi 16131913 487 LTQI 490
Cdd:COG1134 224 LVMD 227
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-176 |
2.81e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.03 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITiNNISYNKLD-HKLAAQLGIGIIY-QELSV-IDELTV 97
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVE-GVITYDGITpEEIKKHYRGDVVYnAETDVhFPHLTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 98 LENL-YIGRHLT--KKICGVNIIDWREMRVRAAMMLLrvGLKVDLDEKVAN-----LSISHKQMLEIAKTLMLDAKVIIM 169
Cdd:TIGR00956 156 GETLdFAARCKTpqNRPDGVSREEYAKHIADVYMATY--GLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCW 233
|
....*..
gi 16131913 170 DEPTSSL 176
Cdd:TIGR00956 234 DNATRGL 240
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
277-489 |
4.49e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.50 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 277 KKVRDISFSVCRGEILGFAGLVGSGRT----ELMNCLFGVDKRAGGEIRLNGKD---ISPRSPLDAVKKGMAYITESRRd 349
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDlqrISEKERRNLVGAEVAMIFQDPM- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 350 NGFFPNFSIAqnMAISRSLK--DGGYKGAMglfhevdEQRTAEnqreLLAL-----KCHSVNQNITELSGGNQQKVLISK 422
Cdd:PRK11022 100 TSLNPCYTVG--FQIMEAIKvhQGGNKKTR-------RQRAID----LLNQvgipdPASRLDVYPHQLSGGMSQRVMIAM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131913 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
Cdd:PRK11022 167 AIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVE 234
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
288-482 |
4.84e-05 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 45.09 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 288 RGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS-------PRSPLdAVKKGMAYITESRRDNGFFpNFSIAQ 360
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqyikADYEG-TVRDLLSSITKDFYTHPYF-KTEIAK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 361 NMAISRSLkdggykgamglfhevdeqrtaenqrellalkchsvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGI 440
Cdd:cd03237 102 PLQIEQIL-----------------------------------DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16131913 441 DVGAKAEIYKVMRQLADDGKVILMVSSELPEIIT-VCDRIAVF 482
Cdd:cd03237 147 DVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDyLADRLIVF 189
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
253-503 |
5.13e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 45.18 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 253 MKENVSNLAHETVfevrnvTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFGVDKRAGGEIRLNGKDI 327
Cdd:PRK13640 1 MKDNIVEFKHVSF------TYPDSKKpaLNDISFSIPRGSWTALIGHNGSGKStisKLINGLLLPDDNPNSKITVDGITL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 328 SPRSPLDAVKKgmAYITESRRDNGFfpnfsiaqnmaISRSLKDggyKGAMGLfhevdEQRTAENQrELLALKCHSVNQ-- 405
Cdd:PRK13640 75 TAKTVWDIREK--VGIVFQNPDNQF-----------VGATVGD---DVAFGL-----ENRAVPRP-EMIKIVRDVLADvg 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 406 -------NITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLA-DDGKVILMVSSELPEiITVCD 477
Cdd:PRK13640 133 mldyidsEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkKNNLTVISITHDIDE-ANMAD 211
|
250 260
....*....|....*....|....*.
gi 16131913 478 RIAVFCEGRLTQILTNRDDMSEEEIM 503
Cdd:PRK13640 212 QVLVLDDGKLLAQGSPVEIFSKVEML 237
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
276-487 |
1.04e-04 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 45.12 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 276 RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldavkkgmayITESRRDNGFFPN 355
Cdd:TIGR01193 487 SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID-----------RHTLRQFINYLPQ 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 356 FSIAQNMAISRSLKDGGYKGAMGlfHEVDEQ-RTAENQREL--LALKCH-SVNQNITELSGGNQQKVLISKWLCCCPEVI 431
Cdd:TIGR01193 556 EPYIFSGSILENLLLGAKENVSQ--DEIWAAcEIAEIKDDIenMPLGYQtELSEEGSSISGGQKQRIALARALLTDSKVL 633
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 432 IFDEPTRGIDVGAKAEIYKVMRQLADdgKVILMVSSELpEIITVCDRIAVFCEGRL 487
Cdd:TIGR01193 634 ILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRL-SVAKQSDKIIVLDHGKI 686
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
145-243 |
1.55e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.63 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 145 NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL-TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSS 223
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLdSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNPDR 1436
|
90 100
....*....|....*....|
gi 16131913 224 VCSGIVSDVSNDDIVRLMVG 243
Cdd:PTZ00265 1437 TGSFVQAHGTHEELLSVQDG 1456
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
21-221 |
1.61e-04 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 43.36 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLD-HKLAAQLGIgiIYQElSVIDELTVLE 99
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPlHTLRSRLSI--ILQD-PILFSGSIRF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 100 NLYIGRHLTKKICgvniidWREMRVRAAMMLLRV---GLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
Cdd:cd03288 114 NLDPECKCTDDRL------WEALEIAQLKNMVKSlpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASI 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16131913 177 TNKEVDYLFLIMNQLRKEGTaIVYISHKLAEIRRiCDRYTVMKDG 221
Cdd:cd03288 188 DMATENILQKVVMTAFADRT-VVTIAHRVSTILD-ADLVLVLSRG 230
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-221 |
2.82e-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: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNisynkldhklaaqlGIGIIYQElSVIDELTVLEN 100
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--------------SVAYVPQQ-AWIQNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 101 LYIGRHLTKKIcgvniidWREMRVRAAMM----LLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
Cdd:TIGR00957 719 ILFGKALNEKY-------YQQVLEACALLpdleILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131913 177 TNKEVDYLF--------LIMNQLRkegtaiVYISHKLAEIRRIcDRYTVMKDG 221
Cdd:TIGR00957 792 DAHVGKHIFehvigpegVLKNKTR------ILVTHGISYLPQV-DVIIVMSGG 837
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
289-509 |
3.46e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.56 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 289 GEILGFAGLVGSGRTELMNCL----FGVDKRAGGEIRLNG---KDISPRSPLDAVkkgmaYITESrrDNgFFPNFSIAQN 361
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGitpEEIKKHYRGDVV-----YNAET--DV-HFPHLTVGET 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 362 MAISRSLKDGG--YKGamglfheVDEQRTAENQRELLALK---CHSVNQN-----ITELSGGNQQKVLISKWLCCCPEVI 431
Cdd:TIGR00956 159 LDFAARCKTPQnrPDG-------VSREEYAKHIADVYMATyglSHTRNTKvgndfVRGVSGGERKRVSIAEASLGGAKIQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 432 IFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVS--SELPEIITVCDRIAVFCEGRltQILTNRDDMSEE--EIMAWAL 507
Cdd:TIGR00956 232 CWDNATRGLDSATALEFIRALKTSANILDTTPLVAiyQCSQDAYELFDKVIVLYEGY--QIYFGPADKAKQyfEKMGFKC 309
|
..
gi 16131913 508 PQ 509
Cdd:TIGR00956 310 PD 311
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
227-463 |
5.22e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.79 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 227 GIVSDVSNDDIVRLMV--GRELQNRFNAMKENV--SNLAHETVFEVRNVT------SRDRKKVRDISFSVCRGEILGFAG 296
Cdd:TIGR00956 717 GETSASNKNDIEAGEVlgSTDLTDESDDVNDEKdmEKESGEDIFHWRNLTyevkikKEKRVILNNVDGWVKPGTLTALMG 796
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 297 LVGSGRTELMNCLFGvdkRAGGEIRLNGKDISPRSPLDA-------------VKKGMAYITESRRdngffpnFSIA--QN 361
Cdd:TIGR00956 797 ASGAGKTTLLNVLAE---RVTTGVITGGDRLVNGRPLDSsfqrsigyvqqqdLHLPTSTVRESLR-------FSAYlrQP 866
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 362 MAISRSLKDggykgamglfhevdeqRTAENQRELLALKchSVNQNITELSGG----NQQKVL-ISKWLCCCPEVIIF-DE 435
Cdd:TIGR00956 867 KSVSKSEKM----------------EYVEEVIKLLEME--SYADAVVGVPGEglnvEQRKRLtIGVELVAKPKLLLFlDE 928
|
250 260
....*....|....*....|....*...
gi 16131913 436 PTRGIDVGAKAEIYKVMRQLADDGKVIL 463
Cdd:TIGR00956 929 PTSGLDSQTAWSICKLMRKLADHGQAIL 956
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
402-479 |
6.28e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 40.77 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 402 SVNQNITELSGGNQQKVLISKWLCCCPE--VIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSElPEIITVCDRI 479
Cdd:cd03238 80 TLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN-LDVLSSADWI 158
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
396-479 |
6.51e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 396 LALKCHSVNQNITELSGGNQQKVLISKWLCCcpEVI----IFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSElPE 471
Cdd:PRK00635 463 LGLPYLTPERALATLSGGEQERTALAKHLGA--ELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQ 539
|
....*...
gi 16131913 472 IITVCDRI 479
Cdd:PRK00635 540 MISLADRI 547
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
282-490 |
1.00e-03 |
|
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: 41.85 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprspldavkkgMAYITEsrrdNGFFPNFSIAQN 361
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------------VAYVPQ----QAWIQNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 362 MAISRSLKDGGYKGAM---GLFHEVdEQRTAENQREllalkchsVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
Cdd:TIGR00957 719 ILFGKALNEKYYQQVLeacALLPDL-EILPSGDRTE--------IGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 439 GIDVGAKAEIYK----VMRQLADDGKVILMVS-SELPEIitvcDRIAVFCEGRLTQI 490
Cdd:TIGR00957 790 AVDAHVGKHIFEhvigPEGVLKNKTRILVTHGiSYLPQV----DVIIVMSGGKISEM 842
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
281-469 |
1.03e-03 |
|
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: 40.78 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKG---MAYITEsrrdNGFFPNFS 357
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNrysVAYAAQ----KPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 358 IAQNMAISRSLKDGGYKGamglfheVDEQRTAENQRELLALKCHS-VNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
Cdd:cd03290 95 VEENITFGSPFNKQRYKA-------VTDACSLQPDIDLLPFGDQTeIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190
....*....|....*....|....*....|....*
gi 16131913 437 TRGIDVGAKAEIYK--VMRQLADDGKVILMVSSEL 469
Cdd:cd03290 168 FSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKL 202
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
409-482 |
1.36e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 39.86 E-value: 1.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDG-KVILMVSSELPEIITVCDRIAVF 482
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
18-68 |
1.77e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 39.48 E-value: 1.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131913 18 VHALKSVNLTVYPGEIH-----ALLGENGAGKSTLMKVLSGIHEPTKGTITINNIS 68
Cdd:cd03222 7 VKRYGVFFLLVELGVVKegeviGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGIT 62
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
279-463 |
1.79e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 41.37 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGvDKRAG---GEIRLNGkdisprspLDAVKKGMAYITESRRDNGFF-P 354
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG-RKTGGyieGDIRISG--------FPKKQETFARISGYCEQNDIHsP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 355 NFSIAQNMAIS---RSLKDGGYKGAMGLFHEVDEQRTAENQRE-LLALKchsvnqNITELSGGNQQKVLISKWLCCCPEV 430
Cdd:PLN03140 967 QVTVRESLIYSaflRLPKEVSKEEKMMFVDEVMELVELDNLKDaIVGLP------GVTGLSTEQRKRLTIAVELVANPSI 1040
|
170 180 190
....*....|....*....|....*....|...
gi 16131913 431 IIFDEPTRGIDVGAKAEIYKVMRQLADDGKVIL 463
Cdd:PLN03140 1041 IFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVV 1073
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
270-470 |
2.39e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 39.16 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 270 NVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIspRSPLDAVKKGMAYITESrrd 349
Cdd:PRK13540 8 DFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI--KKDLCTYQKQLCFVGHR--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 350 NGFFPNFSIAQNMAISRSLKDGGYkgamglfhEVDEQRTAENQRELLALKCHSVNqnitelSGGNQQKVLISKWLCCCpE 429
Cdd:PRK13540 83 SGINPYLTLRENCLYDIHFSPGAV--------GITELCRLFSLEHLIDYPCGLLS------SGQKRQVALLRLWMSKA-K 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16131913 430 VIIFDEPTRGIDVGAKAEIY-KVMRQLADDGKVILMVSSELP 470
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIItKIQEHRAKGGAVLLTSHQDLP 189
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
4-62 |
2.57e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 2.57e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131913 4 PYISM--AGIGKSFGPVhALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTI 62
Cdd:PLN03073 507 PIISFsdASFGYPGGPL-LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV 566
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
280-325 |
2.64e-03 |
|
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: 39.37 E-value: 2.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 16131913 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK 325
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS 67
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
265-327 |
3.31e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.15 E-value: 3.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131913 265 VFEvrNVTSRDRKKV----RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDI 327
Cdd:PTZ00243 1310 VFE--GVQMRYREGLplvlRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREI 1374
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
409-455 |
4.05e-03 |
|
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: 38.29 E-value: 4.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 16131913 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL 455
Cdd:cd03223 91 VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL 137
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
410-482 |
4.32e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.01 E-value: 4.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131913 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDG-KVILMVSSELPEiITVCDRIAVF 482
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIAS-IKRSDKIVVF 1431
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-55 |
5.11e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 39.23 E-value: 5.11e-03
10 20 30
....*....|....*....|....*....|....*
gi 16131913 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIH 55
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH 310
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
281-340 |
6.28e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.10 E-value: 6.28e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIrlngkDISPRSPLDAVKKGM 340
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSAALIAISSGL 96
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
279-485 |
8.09e-03 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 38.30 E-value: 8.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdISPRSPLDAVKKGmayitesrrdngffpnfSI 358
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-ISFSSQFSWIMPG-----------------TI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131913 359 AQNMAISRSLKDGGYKGAMGLFH-EVDEQRTAENQRELLAlkchsvNQNITeLSGGNQQKVLISKWLCCCPEVIIFDEPT 437
Cdd:cd03291 115 KENIIFGVSYDEYRYKSVVKACQlEEDITKFPEKDNTVLG------EGGIT-LSGGQRARISLARAVYKDADLYLLDSPF 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16131913 438 RGIDVGAKAEIYK--VMRQLADdgKVILMVSSELpEIITVCDRIAVFCEG 485
Cdd:cd03291 188 GYLDVFTEKEIFEscVCKLMAN--KTRILVTSKM-EHLKKADKILILHEG 234
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
22-51 |
8.47e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 38.37 E-value: 8.47e-03
10 20 30
....*....|....*....|....*....|.
gi 16131913 22 KSV-NLTVYPGEIHALLGENGAGKSTLMKVL 51
Cdd:COG4637 11 KSLrDLELPLGPLTVLIGANGSGKSNLLDAL 41
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
279-332 |
9.79e-03 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 38.74 E-value: 9.79e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 16131913 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK-DISPRSP 332
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRiSFSPQTS 496
|
|
|