|
Name |
Accession |
Description |
Interval |
E-value |
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
8-559 |
8.93e-137 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 409.16 E-value: 8.93e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 8 MIRPVVWSLLLAILVGTISTLSSISLMGLSAWLIASAALQPPLYVLSLAIVGVRFCGVMRAVFRYLERYFTHKVGFSLFT 87
Cdd:COG4987 9 LLRPHRGRLLLGVLLGLLTLLAGIGLLALSGWLIAAAALAPPILNLFVPIVGVRAFAIGRTVFRYLERLVSHDATLRLLA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 88 SFRVFVLIKIIKALPFK-QQTENGDAFDLIVNAVDNLRDSFLRFFLPPIITTISVFILSIWFFLYSYDLMILLISSWLIF 166
Cdd:COG4987 89 DLRVRLYRRLEPLAPAGlARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALALVLALGLLLA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 167 MIVIPYMIWRRYLKLKKHKFLLTQEI----IEFYEGNRELSFYNYDKYRLKNINHSIEQYQQYQQNLFKLKLKVNLCSEF 242
Cdd:COG4987 169 GLLLPLLAARLGRRAGRRLAAARAALrarlTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 243 IMGAYLVICLAISIYLVNTQDFNPIMAITIILTYQAVLEVLAMMPSLIEHFDE---ASKRWQDlaifmqekkfIANTNNE 319
Cdd:COG4987 249 AAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRvraAARRLNE----------LLDAPPA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 320 IKSENQEDKQSKDVQLLLKDLAYGYD---KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKN 396
Cdd:COG4987 319 VTEPAEPAPAPGGPSLELEDVSFRYPgagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 397 YDDLAEKSIREHFAVAFQEHHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKH 474
Cdd:COG4987 399 LRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALpdGLDTWLGEGGRRLSGGERR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 475 RLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLL 554
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLA 558
|
....*
gi 2674892663 555 REDSY 559
Cdd:COG4987 559 QNGRY 563
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
9-525 |
8.85e-74 |
|
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: 244.58 E-value: 8.85e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 9 IRPVVWSLLLAILVGTISTLSSISLMGLSAWLIASAALQPPLYVLSLAIVGVRFCGVMRAVFRYLERYFTHKVGFSLFTS 88
Cdd:TIGR02868 8 LKPRRRRLALAVLLGALALGSAVALLGVSAWLISRAAEMPPVLYLSVAAVAVRAFGIGRAVFRYLERLVGHDAALRSLGA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 89 FRVFVLIKIIK-ALPFKQQTENGDAFDLIVNAVDNLRDSFLRFFLPPIIT--TISVFILSIWFFlySYDLMILLISSWLI 165
Cdd:TIGR02868 88 LRVRVYERLARqALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVAlvVGAAAVAAIAVL--SVPAALILAAGLLL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 166 FMIVIPYMIWR----RYLKLKKHKFLLTQEIIEFYEGNRELSFYNYDKYRLKNINHSIEQYQQYQQNLFKLKLKVNLCSE 241
Cdd:TIGR02868 166 AGFVAPLVSLRaaraAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALGAALTL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 242 FIMGA--YLVICLAISIYLVNTQDfnPIMAITIILTYQAVLEVLAMMPSLIEHFdeasKRWQDLAIFMQEKKFIANTNNE 319
Cdd:TIGR02868 246 LAAGLavLGALWAGGPAVADGRLA--PVTLAVLVLLPLAAFEAFAALPAAAQQL----TRVRAAAERIVEVLDAAGPVAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 320 IKSENQEDKQSKDVQLLLKDLAYGY--DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNY 397
Cdd:TIGR02868 320 GSAPAAGAVGLGKPTLELRDLSAGYpgAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 398 DDLAEKSIREHFAVAFQEHHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHR 475
Cdd:TIGR02868 400 SSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALpdGLDTVLGEGGARLSGGERQR 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2674892663 476 LQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHD 525
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
8-559 |
3.99e-68 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 230.82 E-value: 3.99e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 8 MIRPVVWSLLLAILVGTISTLSSISLMGLSAWLIASAALQPPLYVLSLAIVGVRFCGVMRAVFRYLERYFTHKVGFSLFT 87
Cdd:COG1132 15 YLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 88 SFRVFVLIKIIKaLPFKQQTEN--GDAFDLIVNAVDNLRDsFLRFFLPPIITTISVFILSIWFFLYSYDLMILLISSWLI 165
Cdd:COG1132 95 DLRRDLFEHLLR-LPLSFFDRRrtGDLLSRLTNDVDAVEQ-FLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 166 FMIVIPY----MIWRRYLKLKKHKFLLTQEIIEFYEGNRELSFYNYDKYRLKNINHSIEQYQQYQQNLFKLKLKVNLCSE 241
Cdd:COG1132 173 LLLLVLRlfgrRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLME 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 242 FIMGAYLVICLAISIYLVNTQDFNP---IMAITIILTYQAVLEVLAMMPSLIEhfdEASKRWQDLAIFMQEKKFIANTNN 318
Cdd:COG1132 253 LLGNLGLALVLLVGGLLVLSGSLTVgdlVAFILYLLRLFGPLRQLANVLNQLQ---RALASAERIFELLDEPPEIPDPPG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 319 EIKSENQEDkqskDVQLllKDLAYGY--DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKN 396
Cdd:COG1132 330 AVPLPPVRG----EIEF--ENVSFSYpgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 397 YDDLAEKSIREHFAVAFQEHHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKH 474
Cdd:COG1132 404 IRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALpdGYDTVVGERGVNLSGGQRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 475 RLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLL 554
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLA 563
|
....*
gi 2674892663 555 REDSY 559
Cdd:COG1132 564 RGGLY 568
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-559 |
4.38e-67 |
|
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: 230.88 E-value: 4.38e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 5 LSNMIRPVVWSLLLAILVGTISTLSSISLMGLSAWLI---ASAALQPPLYVLSLAIVGVrfcGVMRAVFRYLERYFTHKV 81
Cdd:COG2274 147 FLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIdrvLPNQDLSTLWVLAIGLLLA---LLFEGLLRLLRSYLLLRL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 82 GFSLFTSFRVFVLIKIIKaLPFKQqTENGDAFDLI--VNAVDNLRDSFLRFFLPPIITTISVFILSIWFFLYSYDLMILL 159
Cdd:COG2274 224 GQRIDLRLSSRFFRHLLR-LPLSF-FESRSVGDLAsrFRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVV 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 160 ISSWLIFMIVIPYMIWRRYLKLKKHKFLLTQE---IIEFYEGNRELSFYNYDKYRLKNINHSIEQYQQYQQNLFKLKLKV 236
Cdd:COG2274 302 LLLIPLYVLLGLLFQPRLRRLSREESEASAKRqslLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 237 NLCSEFIMGAYLVICLAISIYLVNTQDFNP--IMAITIILTYqavleVLAMMPSLIEHFDeaskRWQDLAIFMQEKKFIA 314
Cdd:COG2274 382 STLSGLLQQLATVALLWLGAYLVIDGQLTLgqLIAFNILSGR-----FLAPVAQLIGLLQ----RFQDAKIALERLDDIL 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 315 NTnneiKSENQEDKQSKDVQLL-----LKDLAYGYD---KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPL 386
Cdd:COG2274 453 DL----PPEREEGRSKLSLPRLkgdieLENVSFRYPgdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 387 KGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGND 464
Cdd:COG2274 529 SGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALpmGYDTVVGEG 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 465 GNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKII 544
Cdd:COG2274 609 GSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIV 688
|
570
....*....|....*
gi 2674892663 545 EQGNIKKLLLREDSY 559
Cdd:COG2274 689 EDGTHEELLARKGLY 703
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-553 |
3.31e-64 |
|
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: 220.01 E-value: 3.31e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 5 LSNMIRPVVWSLLLAILVGTISTLSSISLMGLSAWLIASAAL-QPPLYVLSLAIVGVRFCGVMRAVFRYLERYFTHKVGF 83
Cdd:COG4988 8 LKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIgGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRAAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 84 SLFTSFRVFVLIKIIKALP-FKQQTENGDAFDLIVNAVDNLrDSFLRFFLPPIITTISVFILsIWFFLYSYDL---MILL 159
Cdd:COG4988 88 RVKRRLRRRLLEKLLALGPaWLRGKSTGELATLLTEGVEAL-DGYFARYLPQLFLAALVPLL-ILVAVFPLDWlsgLILL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 160 ISSWLI--FMIVIPYMiwrrylklkkhkfllTQEIIE------------FYE---GNRELSFYNYDKYRLKNINHSIEQY 222
Cdd:COG4988 166 VTAPLIplFMILVGKG---------------AAKASRrqwralarlsghFLDrlrGLTTLKLFGRAKAEAERIAEASEDF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 223 QQyqqnlfklK----LKVNLCSEFIM--GAYLVICLA---ISIYLVNTQdfnpimaitiiLTYQAVLEVLAMMPSLIEHF 293
Cdd:COG4988 231 RK--------RtmkvLRVAFLSSAVLefFASLSIALVavyIGFRLLGGS-----------LTLFAALFVLLLAPEFFLPL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 294 DEASKRWQDLA--------IFmqekKFIANTNNEIKSENQEDKQSKDVQLLLKDLAYGYD--KVLLKDINLSIKKGNKTL 363
Cdd:COG4988 292 RDLGSFYHARAngiaaaekIF----ALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPggRPALDGLSLTIPPGERVA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 364 IVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRDNFKMLYENITDEEIYKSL 443
Cdd:COG4988 368 LVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAAL 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 444 ENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIV 521
Cdd:COG4988 448 EAAGLDEFVAALpdGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVIL 527
|
570 580 590
....*....|....*....|....*....|..
gi 2674892663 522 TSHDISLLRFFDDIIICGEEKIIEQGNIKKLL 553
Cdd:COG4988 528 ITHRLALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-559 |
1.73e-62 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 215.46 E-value: 1.73e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 14 WSLLLAILVGTISTLSSISLMGLSAWLIASAALQPPLYVLS----LAIVGVRFCGVMRAVFRYLERYFTHKVGFSLFTSF 89
Cdd:PRK11160 16 FMLSLGILLAIVTLLASIGLLTLSGWFLSASAVAGLAGLYSfnymLPAAGVRGAAIGRTAGRYGERLVSHDATFRVLTHL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 90 RVFVLIKIIKALPFKQQT-ENGDAFDLIVNAVDNLRDSFLRFfLPPIITTISVfILSIWFFLYSYD--LMILLISSWLIF 166
Cdd:PRK11160 96 RVFTFSKLLPLSPAGLARyRQGDLLNRLVADVDTLDHLYLRL-ISPLVAALVV-ILVLTIGLSFFDltLALTLGGILLLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 167 MIVIPymiWRRYLKLKKHKFLLTQE-------IIEFYEGNRELSFYNY-DKYRlKNINHSIEQYQQYQQNLFKLKLKVNL 238
Cdd:PRK11160 174 LLLLP---LLFYRLGKKPGQDLTHLraqyrvqLTEWLQGQAELTLFGAeDRYR-QQLEQTEQQWLAAQRRQANLTGLSQA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 239 CSEFIMGAYLVICLAISIYLVNTQDF-NPIMAItIILTYQAVLEVLAMMPSLIEHFDE---ASKRWQDLaifMQEKKfia 314
Cdd:PRK11160 250 LMILANGLTVVLMLWLAAGGVGGNAQpGALIAL-FVFAALAAFEALMPVAGAFQHLGQviaSARRINEI---TEQKP--- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 315 ntnnEIKSENQEDKQSKDVQLLLKDLAYGYDK---VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIF 391
Cdd:PRK11160 323 ----EVTFPTTSTAAADQVSLTLNNVSFTYPDqpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 392 IQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRDNFKMLYENITDEEIYKSLENV---YLLDfvNQVGLDYIVGNDGNKL 468
Cdd:PRK11160 399 LNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVgleKLLE--DDKGLNAWLGEGGRQL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 469 SGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGN 548
Cdd:PRK11160 477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGT 556
|
570
....*....|.
gi 2674892663 549 IKKLLLREDSY 559
Cdd:PRK11160 557 HQELLAQQGRY 567
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
338-555 |
2.24e-49 |
|
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: 170.48 E-value: 2.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 338 KDLAYGYD--KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQE 415
Cdd:cd03254 6 ENVNFSYDekKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 HHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDE 493
Cdd:cd03254 86 TFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 494 PTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLR 555
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
337-537 |
3.35e-45 |
|
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: 158.78 E-value: 3.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGYD---KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAF 413
Cdd:cd03225 2 LKNLSFSYPdgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 Q--EHHIFNLSIRD--NFKMLYENITDEEIYKSLENVylldfVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDII 489
Cdd:cd03225 82 QnpDDQFFGPTVEEevAFGLENLGLPEEEIEERVEEA-----LELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 490 LLDEPTAGLDIKTTNNIcSQLMEKYQKQ--TMIVTSHDISLLR-FFDDIII 537
Cdd:cd03225 157 LLDEPTAGLDPAGRREL-LELLKKLKAEgkTIIIVTHDLDLLLeLADRVIV 206
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
337-537 |
5.19e-45 |
|
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: 156.77 E-value: 5.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGYD---KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAF 413
Cdd:cd03228 3 FKNVSFSYPgrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 QEHHIFNLSIRDNFkmlyenitdeeiykslenvylldfvnqvgldyivgndgnkLSGGQKHRLQLAICLAKQKDIILLDE 493
Cdd:cd03228 83 QDPFLFSGTIRENI----------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2674892663 494 PTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIII 537
Cdd:cd03228 123 ATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIV 166
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
337-559 |
1.07e-42 |
|
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: 152.77 E-value: 1.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGYD--KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQ 414
Cdd:cd03253 3 FENVTFAYDpgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 EHHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLD 492
Cdd:cd03253 83 DTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFpdGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2674892663 493 EPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLREDSY 559
Cdd:cd03253 163 EATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLY 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
337-559 |
4.21e-41 |
|
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: 148.53 E-value: 4.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGYDK---VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAF 413
Cdd:cd03251 3 FKNVTFRYPGdgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 QEHHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:cd03251 83 QDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2674892663 492 DEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLREDSY 559
Cdd:cd03251 163 DEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVY 230
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
337-557 |
7.94e-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: 147.48 E-value: 7.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY--DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQ 414
Cdd:COG1122 3 LENLSFSYpgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 --EHHIFNLSIRD-------NFKMLYENItDEEIYKSLENVYLLDFvnqvgLDYIVgndgNKLSGGQKHRLQLAICLAKQ 485
Cdd:COG1122 83 npDDQLFAPTVEEdvafgpeNLGLPREEI-RERVEEALELVGLEHL-----ADRPP----HELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2674892663 486 KDIILLDEPTAGLDIKTTNNIcSQLMEKYQKQ--TMIVTSHDISLL-RFFDDIIICGEEKIIEQGNIKKLLLRED 557
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRREL-LELLKRLNKEgkTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
9-559 |
1.34e-40 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 155.26 E-value: 1.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 9 IRPVVWSLLLAIL-----VGTISTLSSIS---LMGLSAWLIASAALQPPLYVLSLAIVgvrfcgvmRAVFRYLERYFTHK 80
Cdd:TIGR02203 9 VRPYKAGLVLAGVamilvAATESTLAALLkplLDDGFGGRDRSVLWWVPLVVIGLAVL--------RGICSFVSTYLLSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 81 VGFSLFTSFRVFVLIKIIKaLP--FKQQTENGDAFDLIVNAVDNLRDSFLRFFLPPIITTISVFILSIWFFLYSYDLMil 158
Cdd:TIGR02203 81 VSNKVVRDIRVRMFEKLLG-LPvsFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLT-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 159 lisswLIFMIVIPYMIW--RRYLKLKKHKFLLTQEII--------EFYEGNRELSFYNYDKYRLKninhsieQYQQYQQN 228
Cdd:TIGR02203 158 -----LIVVVMLPVLSIlmRRVSKRLRRISKEIQNSMgqvttvaeETLQGYRVVKLFGGQAYETR-------RFDAVSNR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 229 LFKLKLKV----NLCSEFIMgayLVICLAISIylvntqdfnpIMAITIILT---YQAVLEVLAMMPSLIEHFDeASKRWQ 301
Cdd:TIGR02203 226 NRRLAMKMtsagSISSPITQ---LIASLALAV----------VLFIALFQAqagSLTAGDFTAFITAMIALIR-PLKSLT 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 302 DLAIFMQEKKFIANTNNEIKSENQE-DKQSKDVQLLLKDLAY--------GYDKVLLKDINLSIKKGNKTLIVGTSGCGK 372
Cdd:TIGR02203 292 NVNAPMQRGLAAAESLFTLLDSPPEkDTGTRAIERARGDVEFrnvtfrypGRDRPALDSISLVIEPGETVALVGRSGSGK 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 373 STLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRDNFKmlY---ENITDEEIYKSLENVYLL 449
Cdd:TIGR02203 372 STLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIA--YgrtEQADRAEIERALAAAYAQ 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 450 DFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDIS 527
Cdd:TIGR02203 450 DFVDKLplGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLS 529
|
570 580 590
....*....|....*....|....*....|..
gi 2674892663 528 LLRFFDDIIICGEEKIIEQGNIKKLLLREDSY 559
Cdd:TIGR02203 530 TIEKADRIVVMDDGRIVERGTHNELLARNGLY 561
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
23-299 |
7.57e-40 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 146.86 E-value: 7.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 23 GTISTLSSISLMGLSAWLIASAALQP---PLYVLSLAIVGVRFCGVMRAVFRYLERYFTHKVGFSLFTSFRVFVLIKIIK 99
Cdd:cd18585 1 GLLTLLASIGLLALSGWFISAAALAGlaaPTFNYFTPAAGVRGFAITRTAGRYGERLVSHDATFRLLSNLRVWFYRKLEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 100 ALPFK-QQTENGDAFDLIVNAVDNLRDSFLRFFLPPIITTISVFILSIWFFLYSYDLMILLISSWLIFMIVIPYMIWRRY 178
Cdd:cd18585 81 LAPARlQKYRSGDLLNRIVADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILLAGLLLAGVVIPLLFYRLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 179 LKLKKHKFLLT----QEIIEFYEGNRELSFYNYDKYRLKNINHSIEQYQQYQQNLFKLKLKVNLCSEFIMGAYLVICLAI 254
Cdd:cd18585 161 KKIGQQLVQLRaelrTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQALMILLSGLTVWLVLWL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2674892663 255 SIYLVNTQDFNPIMAITIILTYQAVLEVLAMMPSLIEHFDE---ASKR 299
Cdd:cd18585 241 GAPLVQNGALDGALLAMLVFAVLASFEAVAPLPLAFQYLGEtraAARR 288
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-536 |
8.95e-40 |
|
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: 152.06 E-value: 8.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 16 LLLAILVGTISTLSSISLMGLSAWLIASAALQ-PPLYVLSLAIVGVRFCGVMRAVFRYLERYFTHKVGFSLFTSFRVFVL 94
Cdd:TIGR02857 5 LALLALLGVLGALLIIAQAWLLARVVDGLISAgEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 95 IKIIKALPFKQQTEN-GDAFDLIVNAVDNLRDSFLRFfLPPII--TTISVFILSIWFFLYSYDLMILLISSWLI--FMIV 169
Cdd:TIGR02857 85 EAVAALGPRWLQGRPsGELATLALEGVEALDGYFARY-LPQLVlaVIVPLAILAAVFPQDWISGLILLLTAPLIpiFMIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 170 IPYMIWRRYLKLKKHKFLLTQEIIEFYEGNRELSFYNYDKYRLKNINHSIEQYQQYQQNLFKLKlkvnlcseFIMGAYLV 249
Cdd:TIGR02857 164 IGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIA--------FLSSAVLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 250 ICLAISIYLVntqdfnpimAITI-------ILTYQAVLEVLAMMPSLIEHFDEASKRWQDLAIFMQEKKFIANT--NNEI 320
Cdd:TIGR02857 236 LFATLSVALV---------AVYIgfrllagDLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVldAAPR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 321 KSENQEDKQSKD-VQLLLKDL--AYGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNY 397
Cdd:TIGR02857 307 PLAGKAPVTAAPaSSLEFSGVsvAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 398 DDLAEKSIREHFAVAFQEHHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHR 475
Cdd:TIGR02857 387 ADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALpqGLDTPIGEGGAGLSGGQAQR 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 476 LQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDII 536
Cdd:TIGR02857 467 LALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIV 527
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
310-548 |
1.91e-38 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 149.22 E-value: 1.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 310 KKFIANTNNEIKSENQEDKQSKDVQLLLKDLA-YGYD-KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLyPLK 387
Cdd:PRK11174 325 VTFLETPLAHPQQGEKELASNDPVTIEAEDLEiLSPDgKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 388 GNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDG 465
Cdd:PRK11174 404 GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLpqGLDTPIGDQA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 466 NKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIE 545
Cdd:PRK11174 484 AGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQ 563
|
...
gi 2674892663 546 QGN 548
Cdd:PRK11174 564 QGD 566
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
337-547 |
4.79e-38 |
|
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: 139.65 E-value: 4.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGYD---KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAF 413
Cdd:cd03245 5 FRNVSFSYPnqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 QEHHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQ--VGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:cd03245 85 QDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKhpNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 492 DEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQG 547
Cdd:cd03245 165 DEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
337-564 |
9.94e-37 |
|
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: 136.65 E-value: 9.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEK---SIREHFAVA 412
Cdd:COG1127 8 VRNLTKSFgDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRRRIGML 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 413 FQEHHIF-NLSIRDN--FKML-YENITDEEIYKSLENVylldfVNQVGLDyivgNDGNK----LSGGQKHRLQLAICLAK 484
Cdd:COG1127 88 FQGGALFdSLTVFENvaFPLReHTDLSEAEIRELVLEK-----LELVGLP----GAADKmpseLSGGMRKRVALARALAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 485 QKDIILLDEPTAGLDIKTTNNIcSQLMEKYQKQ---TMIVTSHDI-SLLRFFDDIIICGEEKIIEQGNIKKLLLREDSYL 560
Cdd:COG1127 159 DPEILLYDEPTAGLDPITSAVI-DELIRELRDElglTSVVVTHDLdSAFAIADRVAVLADGKIIAEGTPEELLASDDPWV 237
|
....
gi 2674892663 561 NKLI 564
Cdd:COG1127 238 RQFL 241
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
337-556 |
1.74e-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: 136.33 E-value: 1.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGYD-KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQE 415
Cdd:COG1120 4 AENLSVGYGgRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 HHI-FNLSIRD-----------NFKMLYEniTDEEI-YKSLEnvylldfvnQVGLDYIVGNDGNKLSGGQKHRLQLAICL 482
Cdd:COG1120 84 PPApFGLTVRElvalgryphlgLFGRPSA--EDREAvEEALE---------RTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 483 AKQKDIILLDEPTAGLDIKttNNIcsQLME------KYQKQTMIVTSHDISL-LRFFDDIIICGEEKIIEQGNIKKLLLR 555
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLA--HQL--EVLEllrrlaRERGRTVVMVLHDLNLaARYADRLVLLKDGRIVAQGPPEEVLTP 228
|
.
gi 2674892663 556 E 556
Cdd:COG1120 229 E 229
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
335-549 |
2.52e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 134.56 E-value: 2.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYD-KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAF 413
Cdd:COG4619 1 LELEGLSFRVGgKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 QEHHIFNLSIRDNFKMLY----ENITDEEIYKSLEnvylldfvnQVGLD-YIVGNDGNKLSGGQKHRLQLAICLAKQKDI 488
Cdd:COG4619 81 QEPALWGGTVRDNLPFPFqlreRKFDRERALELLE---------RLGLPpDILDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2674892663 489 ILLDEPTAGLDIKTTNNICsQLMEKYQKQ---TMIVTSHDISLLRFFDDIIICgeekiIEQGNI 549
Cdd:COG4619 152 LLLDEPTSALDPENTRRVE-ELLREYLAEegrAVLWVSHDPEQIERVADRVLT-----LEAGRL 209
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
349-559 |
8.37e-36 |
|
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: 134.20 E-value: 8.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRDNFK 428
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 429 MLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNI 506
Cdd:cd03249 99 YGKPDATDEEVEEAAKKANIHDFIMSLpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLV 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 507 CSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLREDSY 559
Cdd:cd03249 179 QEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVY 231
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
337-552 |
1.33e-35 |
|
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: 133.07 E-value: 1.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLY-----PLKGNIFIQGKNYDDLAEK--SIREH 408
Cdd:cd03260 3 LRDLNVYYgDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvlELRRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 409 FAVAFQEHHIFNLSIRDN-------FKMLYENITDEEIYKSLENVYLLDFVNQvgldyivGNDGNKLSGGQKHRLQLAIC 481
Cdd:cd03260 83 VGMVFQKPNPFPGSIYDNvayglrlHGIKLKEELDERVEEALRKAALWDEVKD-------RLHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 482 LAKQKDIILLDEPTAGLDIKTTNNIcSQLMEKYQKQ-TMIVTSHDIS-LLRFFDDIIICGEEKIIEQGNIKKL 552
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKI-EELIAELKKEyTIVIVTHNMQqAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
349-548 |
1.54e-35 |
|
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: 132.62 E-value: 1.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRDNfk 428
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSGTIRSN-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 429 mL--YENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTN 504
Cdd:cd03244 98 -LdpFGEYSDEELWQALERVGLKEFVESLpgGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2674892663 505 NICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGN 548
Cdd:cd03244 177 LIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
337-561 |
6.66e-35 |
|
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: 131.47 E-value: 6.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEK---SIREHFAVA 412
Cdd:cd03261 3 LRGLTKSFgGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRRRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 413 FQEHHIFN-LSIRDN--FkMLYEN--ITDEEIYKSlenvyLLDFVNQVGLdyivGNDGNK----LSGGQKHRLQLAICLA 483
Cdd:cd03261 83 FQSGALFDsLTVFENvaF-PLREHtrLSEEEIREI-----VLEKLEAVGL----RGAEDLypaeLSGGMKKRVALARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 484 KQKDIILLDEPTAGLDIKTTNNIcSQLMEKYQKQ---TMIVTSHDI-SLLRFFDDIIICGEEKIIEQGNIKKLLLREDSY 559
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVI-DDLIRSLKKElglTSIMVTHDLdTAFAIADRIAVLYDGKIVAEGTPEELRASDDPL 231
|
..
gi 2674892663 560 LN 561
Cdd:cd03261 232 VR 233
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
337-547 |
1.24e-34 |
|
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: 128.71 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQe 415
Cdd:cd03214 2 VENLSVGYgGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 hhifnlsirdnfkmlyenitdeeiykSLENVYLLDFVNQvgldyivgnDGNKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:cd03214 81 --------------------------ALELLGLAHLADR---------PFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2674892663 496 AGLDIKTTNNICSQLME--KYQKQTMIVTSHDISL-LRFFDDIIICGEEKIIEQG 547
Cdd:cd03214 126 SHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNLaARYADRVILLKDGRIVAQG 180
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
339-555 |
1.28e-34 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 138.17 E-value: 1.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 339 DLAYGYD--KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEH 416
Cdd:PRK13657 339 DVSFSYDnsRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 417 HIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFV--NQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEP 494
Cdd:PRK13657 419 GLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIerKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEA 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 495 TAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLR 555
Cdd:PRK13657 499 TSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVAR 559
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
349-496 |
1.38e-34 |
|
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: 127.76 E-value: 1.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFN-LSIRDN- 426
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENl 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2674892663 427 -----FKMLYENITDEEIYKSLENVYLLDFVNQVgldyiVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTA 496
Cdd:pfam00005 81 rlgllLKGLSKREKDARAEEALEKLGLGDLADRP-----VGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
342-561 |
1.29e-33 |
|
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: 127.99 E-value: 1.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGYD-KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFN 420
Cdd:cd03252 10 YKPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 LSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGL 498
Cdd:cd03252 90 RSIRDNIALADPGMSMERVIEAAKLAGAHDFISELpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 499 DIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLREDSYLN 561
Cdd:cd03252 170 DYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAY 232
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
349-549 |
1.84e-33 |
|
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: 126.84 E-value: 1.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSI----REHFAVAFQEHH-IFNLSI 423
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafrRRHIGFVFQSFNlLPDLTA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 424 RDN--FKMLYENITDEEIYKSLEnvYLLDfvnQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIK 501
Cdd:cd03255 100 LENveLPLLLAGVPKKERRERAE--ELLE---RVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2674892663 502 TTNNICSQLME--KYQKQTMIVTSHDISLLRFFDDIIicgeekIIEQGNI 549
Cdd:cd03255 175 TGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRII------ELRDGKI 218
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
335-547 |
7.73e-33 |
|
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: 123.96 E-value: 7.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGY---DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLaEKSIREHFAV 411
Cdd:cd03247 1 LSINNVSFSYpeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 412 AFQEHHIFNLSIRDNFkmlyenitdeeiykslenvylldfvnqvgldyivgndGNKLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:cd03247 80 LNQRPYLFDTTLRNNL-------------------------------------GRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 492 DEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQG 547
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
349-536 |
1.06e-32 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 125.16 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSI----REHFAVAFQEHHIF-NLSI 423
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlrRRHIGFVFQFFNLLpELTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 424 RDNFKM--LYENITDEEIYKSLEnvYLLDfvnQVGLDYIVGNDGNKLSGGQKHRlqLAIC--LAKQKDIILLDEPTAGLD 499
Cdd:COG1136 104 LENVALplLLAGVSRKERRERAR--ELLE---RVGLGDRLDHRPSQLSGGQQQR--VAIAraLVNRPKLILADEPTGNLD 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 2674892663 500 IKTTNNICSQLME--KYQKQTMIVTSHDISLLRFFDDII 536
Cdd:COG1136 177 SKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVI 215
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
337-536 |
1.25e-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: 124.57 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGYD-KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDlaeksIREHFAVAFQE 415
Cdd:cd03235 2 VEDLTVSYGgHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 HHI---FNLSIRD----------NFKMLYENITDEEIYKSLENVYLLDFVN-QVGldyivgndgnKLSGGQKHRLQLAIC 481
Cdd:cd03235 77 RSIdrdFPISVRDvvlmglyghkGLFRRLSKADKAKVDEALERVGLSELADrQIG----------ELSGGQQQRVLLARA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2674892663 482 LAKQKDIILLDEPTAGLDIKTTNNICSqLMEKYQKQ--TMIVTSHDI-SLLRFFDDII 536
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYE-LLRELRREgmTILVVTHDLgLVLEYFDRVL 203
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
337-549 |
1.30e-32 |
|
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: 125.36 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGYDKVL-LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKsIREHFAVAFQE 415
Cdd:COG4555 4 VENLSKKYGKVPaLKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 HHIF-NLSIRDNFKMLYE--NITDEEIYKSLEN-VYLLDFVNQvgLDYIVGndgnKLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:COG4555 83 RGLYdRLTVRENIRYFAElyGLFDEELKKRIEElIELLGLEEF--LDRRVG----ELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 492 DEPTAGLDIKTTNNICSQLME-KYQKQTMIVTSHDISLL-RFFDDIIICGEEKIIEQGNI 549
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEVeALCDRVVILHKGKVVAQGSL 216
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
343-559 |
1.61e-32 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 131.68 E-value: 1.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 343 GYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLS 422
Cdd:PRK11176 353 GKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDT 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 IRDNFKMLYENI-TDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD 499
Cdd:PRK11176 433 IANNIAYARTEQySREQIEEAARMAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 500 IKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLREDSY 559
Cdd:PRK11176 513 TESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVY 572
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
337-536 |
2.60e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 124.43 E-value: 2.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGYD-KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKsirehfaVAF-- 413
Cdd:COG1121 9 LENLTVSYGgRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR-------IGYvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 QEHHI---FNLSIRDNFKM-LYENI--------TD-EEIYKSLENVYLLDFVN-QVGldyivgndgnKLSGGQKHRLQLA 479
Cdd:COG1121 82 QRAEVdwdFPITVRDVVLMgRYGRRglfrrpsrADrEAVDEALERVGLEDLADrPIG----------ELSGGQQQRVLLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 480 ICLAKQKDIILLDEPTAGLDIKTTNNIcSQLMEKYQKQ--TMIVTSHDISLLR-FFDDII 536
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEAL-YELLRELRREgkTILVVTHDLGAVReYFDRVL 210
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
342-561 |
2.78e-32 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 124.02 E-value: 2.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKsIREHFAVAFQEHHIF-N 420
Cdd:COG1131 10 YG-DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYVPQEPALYpD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 LSIRDNFKM---LY---ENITDEEIYKSLENVYLLDFVNQ-VGldyivgndgnKLSGGQKHRLQLAICLAKQKDIILLDE 493
Cdd:COG1131 88 LTVRENLRFfarLYglpRKEARERIDELLELFGLTDAADRkVG----------TLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 494 PTAGLDIKTTNNICsQLMEKYQKQ--TMIVTSHDISLL-RFFDDIIICGEEKIIEQGNIKKLLLR--EDSYLN 561
Cdd:COG1131 158 PTSGLDPEARRELW-ELLRELAAEgkTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKARllEDVFLE 229
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
337-553 |
5.59e-32 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 131.14 E-value: 5.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY---DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAF 413
Cdd:TIGR03375 466 FRNVSFAYpgqETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVP 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 QEHHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQ--VGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:TIGR03375 546 QDPRLFYGTLRDNIALGAPYADDEEILRAAELAGVTEFVRRhpDGLDMQIGERGRSLSGGQRQAVALARALLRDPPILLL 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 492 DEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLL 553
Cdd:TIGR03375 626 DEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADGPKDQVL 687
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
337-537 |
6.09e-32 |
|
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: 120.81 E-value: 6.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQe 415
Cdd:cd00267 2 IENLSFRYgGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 hhifnlsirdnfkmlyenitdeeiykslenvylldfvnqvgldyivgndgnkLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:cd00267 81 ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2674892663 496 AGLDIKTTNNIcSQLMEKYQKQ--TMIVTSHDISLLRFFDDIII 537
Cdd:cd00267 109 SGLDPASRERL-LELLRELAEEgrTVIIVTHDPELAELAADRVI 151
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
335-537 |
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: 121.14 E-value: 8.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKS--IREHFAV 411
Cdd:cd03229 1 LELKNVSKRYgQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 412 AFQEHHIF-NLSIRDNFKMLyenitdeeiykslenvylldfvnqvgldyivgndgnkLSGGQKHRLQLAICLAKQKDIIL 490
Cdd:cd03229 81 VFQDFALFpHLTVLENIALG-------------------------------------LSGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2674892663 491 LDEPTAGLDIKTTNNIcSQLMEKYQKQ---TMIVTSHDISLLRFFDDIII 537
Cdd:cd03229 124 LDEPTSALDPITRREV-RALLKSLQAQlgiTVVLVTHDLDEAARLADRVV 172
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
342-536 |
4.37e-31 |
|
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: 121.14 E-value: 4.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGK---NYDDLAEKSIREHFAVAFQEHHI 418
Cdd:cd03256 10 YPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinKLKGKALRQLRRQIGMIFQQFNL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 419 FN-LSIRDN-----------FKMLYENITDEEIYKSLEnvyLLDfvnQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQK 486
Cdd:cd03256 90 IErLSVLENvlsgrlgrrstWRSLFGLFPKEEKQRALA---ALE---RVGLLDKAYQRADQLSGGQQQRVAIARALMQQP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 487 DIILLDEPTAGLDIKTTNNICSQLMEKYQKQ--TMIVTSHDISL-LRFFDDII 536
Cdd:cd03256 164 KLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLaREYADRIV 216
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-559 |
4.67e-31 |
|
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: 128.32 E-value: 4.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 2 VQILSNMIRPVVWSLLLAILVGTISTLSSISLMGLsawlIASAALQPPLYVLSLAIVGVRFCGVMRAVFRYLERYFTHKV 81
Cdd:TIGR01193 148 IPLITRQKKLIVNIVIAAIIVTLISIAGSYYLQKI----IDTYIPHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 82 GFSLfTSFRVFVLIKIIKALPF-----KQQTENGDAFDLIVNAVDNLRDSFLRFFLP-PIITTISVFILsiwfFLYSYDL 155
Cdd:TIGR01193 224 GQRL-SIDIILSYIKHLFELPMsffstRRTGEIVSRFTDASSIIDALASTILSLFLDmWILVIVGLFLV----RQNMLLF 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 156 MILLISSWLIFMIVIPYM--IWRRYLKLKKHKFLLTQEIIEFYEGNRELSFYNYDKYRLKNINHSIEQY---------QQ 224
Cdd:TIGR01193 299 LLSLLSIPVYAVIIILFKrtFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYlnksfkyqkAD 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 225 YQQNLFKLKLKVNLcSEFIM--GAYLVICLAISIYLVntqdfnpimaitiiLTYQAvlevlammpsLIEHFDEASKRWQD 302
Cdd:TIGR01193 379 QGQQAIKAVTKLIL-NVVILwtGAYLVMRGKLTLGQL--------------ITFNA----------LLSYFLTPLENIIN 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 303 LAIFMQEKKFIANTNNEI---KSENQEDKQSKDVQLLLKDL-------AYGYDKVLLKDINLSIKKGNKTLIVGTSGCGK 372
Cdd:TIGR01193 434 LQPKLQAARVANNRLNEVylvDSEFINKKKRTELNNLNGDIvindvsySYGYGSNILSDISLTIKMNSKTTIVGMSGSGK 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 373 STLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRDNFKM-LYENITDEEIYKSLENVYLLDF 451
Cdd:TIGR01193 514 STLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLgAKENVSQDEIWAACEIAEIKDD 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 452 VNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMeKYQKQTMIVTSHDISLL 529
Cdd:TIGR01193 594 IENMplGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLL-NLQDKTIIFVAHRLSVA 672
|
570 580 590
....*....|....*....|....*....|
gi 2674892663 530 RFFDDIIICGEEKIIEQGNIKKLLLREDSY 559
Cdd:TIGR01193 673 KQSDKIIVLDHGKIIEQGSHDELLDRNGFY 702
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
349-547 |
8.27e-31 |
|
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: 119.92 E-value: 8.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAE---KSIREHFAVAFQE-HHIFN--LS 422
Cdd:cd03257 21 LDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlrKIRRKEIQMVFQDpMSSLNprMT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 IRDNFKMLYENITDEEIYKSLENVYLLDFVnQVGLDYIVGND-GNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIK 501
Cdd:cd03257 101 IGEQIAEPLRIHGKLSKKEARKEAVLLLLV-GVGLPEEVLNRyPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 502 TTNNICsQLMEKYQKQ---TMIVTSHDISLLRFF-DDIII--CGeeKIIEQG 547
Cdd:cd03257 180 VQAQIL-DLLKKLQEElglTLLFITHDLGVVAKIaDRVAVmyAG--KIVEEG 228
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
342-537 |
6.78e-30 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 117.78 E-value: 6.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIRE---HFAVAFQEHH- 417
Cdd:TIGR02315 11 YPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKlrrRIGMIFQHYNl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 418 IFNLSIRDN-----------FKMLYENITDEEIYKSLenvYLLDFVNQVGLDYIvgnDGNKLSGGQKHRLQLAICLAKQK 486
Cdd:TIGR02315 91 IERLTVLENvlhgrlgykptWRSLLGRFSEEDKERAL---SALERVGLADKAYQ---RADQLSGGQQQRVAIARALAQQP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 487 DIILLDEPTAGLDIKTTNNICSQLMEKYQKQ--TMIVTSHDISLLRFFDDIII 537
Cdd:TIGR02315 165 DLILADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVDLAKKYADRIV 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
321-553 |
1.53e-29 |
|
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: 122.32 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 321 KSENQEDKQSKDVQLLLKDLAYGY------DKVLLKDINLSIKKGnKTL-IVGTSGCGKSTLFYVLMRLLYPLKGNIFIQ 393
Cdd:COG1123 247 RGRAAPAAAAAEPLLEVRNLSKRYpvrgkgGVRAVDDVSLTLRRG-ETLgLVGESGSGKSTLARLLLGLLRPTSGSILFD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 394 GKNYDDLAEKSIRE---HFAVAFQE-HHIFN--LSIRD-------NFKMLYENITDEEIYKSLEnvylldfvnQVGLDYi 460
Cdd:COG1123 326 GKDLTKLSRRSLRElrrRVQMVFQDpYSSLNprMTVGDiiaeplrLHGLLSRAERRERVAELLE---------RVGLPP- 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 461 vgNDGNK----LSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICsQLMEKYQKQ---TMIVTSHDISLLRFF- 532
Cdd:COG1123 396 --DLADRypheLSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQIL-NLLRDLQRElglTYLFISHDLAVVRYIa 472
|
250 260
....*....|....*....|.
gi 2674892663 533 DDIIICGEEKIIEQGNIKKLL 553
Cdd:COG1123 473 DRVAVMYDGRIVEDGPTEEVF 493
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
342-549 |
5.32e-29 |
|
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: 112.88 E-value: 5.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKsIREHFAVAFQEHhifnl 421
Cdd:cd03230 10 YG-KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIGYLPEEP----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 422 sirdnfkMLYENITdeeiykslenvylldfvnqvGLDYIvgndgnKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIK 501
Cdd:cd03230 83 -------SLYENLT--------------------VRENL------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 502 TTNNIcSQLMEKYQKQ--TMIVTSHDISLL-RFFDDIIicgeekIIEQGNI 549
Cdd:cd03230 130 SRREF-WELLRELKKEgkTILLSSHILEEAeRLCDRVA------ILNNGRI 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
335-555 |
3.19e-28 |
|
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: 118.47 E-value: 3.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGY---DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYP---LKGNIFIQGKNYDDLAEKSIREH 408
Cdd:COG1123 5 LEVRDLSVRYpggDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 409 FAVAFQE--HHIFNLSIRDN--FKMLYENITDEEIYKSLENvyLLDfvnQVGLDYIVGNDGNKLSGGQKHRLQLAICLAK 484
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQiaEALENLGLSRAEARARVLE--LLE---AVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2674892663 485 QKDIILLDEPTAGLDIKTTNNIcSQLMEKYQKQ---TMIVTSHDISL-LRFFDDIIICGEEKIIEQGNIKKLLLR 555
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEI-LDLLRELQRErgtTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
344-551 |
4.76e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 113.60 E-value: 4.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 344 YDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDD--LAEKSIREHFAVAFQ--EHHIF 419
Cdd:PRK13637 18 FEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIRKKVGLVFQypEYQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 420 NLSIRDN--FKMLYENITDEEIYKSLENVylldfVNQVGLDYIVGNDGN--KLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:PRK13637 98 EETIEKDiaFGPINLGLSEEEIENRVKRA-----MNIVGLDYEDYKDKSpfELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 496 AGLDIKTTNNICSQ---LMEKYqKQTMIVTSH---DISllRFFDDIIICGEEKIIEQGNIKK 551
Cdd:PRK13637 173 AGLDPKGRDEILNKikeLHKEY-NMTIILVSHsmeDVA--KLADRIIVMNKGKCELQGTPRE 231
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
338-559 |
4.83e-28 |
|
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: 118.77 E-value: 4.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 338 KDLAYGYD--KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQE 415
Cdd:COG5265 361 ENVSFGYDpeRPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQD 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 HHIFNLSIRDNfkMLY--ENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:COG5265 441 TVLFNDTIAYN--IAYgrPDASEEEVEAAARAAQIHDFIESLpdGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIF 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2674892663 492 DEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLREDSY 559
Cdd:COG5265 519 DEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLY 586
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
332-553 |
6.02e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 113.40 E-value: 6.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 332 DVQLLLKDLAYGYD--KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGK--NYDDLAEKSIRE 407
Cdd:PRK13636 3 DYILKVEELNYNYSdgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 408 HFAVAFQ--EHHIFNLSIRDN--FKMLYENITDEEIYKSLENVylldfVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLA 483
Cdd:PRK13636 83 SVGMVFQdpDNQLFSASVYQDvsFGAVNLKLPEDEVRKRVDNA-----LKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 484 KQKDIILLDEPTAGLDIKTTNNICSQLME--KYQKQTMIVTSHDISLLRFF-DDIIICGEEKIIEQGNIKKLL 553
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEmqKELGLTIIIATHDIDIVPLYcDNVFVMKEGRVILQGNPKEVF 230
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
338-559 |
1.15e-27 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 117.90 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 338 KDLAYGY----DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAF 413
Cdd:TIGR00958 482 QDVSFSYpnrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVG 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 QEHHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:TIGR00958 562 QEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFpnGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLIL 641
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2674892663 492 DEPTAGLDIKtTNNICSQLMEKYQKqTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLREDSY 559
Cdd:TIGR00958 642 DEATSALDAE-CEQLLQESRSRASR-TVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCY 707
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
341-559 |
1.80e-27 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 116.74 E-value: 1.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 341 AYGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLlYPL-KGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIF 419
Cdd:PRK10790 349 AYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGY-YPLtEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVL 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 420 NLSIRDNFKmLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAG 497
Cdd:PRK10790 428 ADTFLANVT-LGRDISEEQVWQALETVQLAELARSLpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATAN 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 498 LDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLREDSY 559
Cdd:PRK10790 507 IDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRY 568
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
342-536 |
4.22e-27 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 110.15 E-value: 4.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREH---FAVAFQEHHI 418
Cdd:COG3638 12 YPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrrrIGMIFQQFNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 419 F-NLSIRDN-----------FKMLYENITDEEI---YKSLENVYLLDFVNQ-VGldyivgndgnKLSGGQKHRLQLAICL 482
Cdd:COG3638 92 VpRLSVLTNvlagrlgrtstWRSLLGLFPPEDReraLEALERVGLADKAYQrAD----------QLSGGQQQRVAIARAL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2674892663 483 AKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQ--TMIVTSHDISL-LRFFDDII 536
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQVDLaRRYADRII 218
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
337-547 |
1.01e-26 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 109.85 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGYD------KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKN---YDDLAEKSIRE 407
Cdd:TIGR04521 3 LKNVSYIYQpgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDitaKKKKKLKDLRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 408 HFAVAFQ--EHHIFNLSIRD-------NFKMlyeniTDEEI----YKSLEnvylldfvnQVGLDY-IVGNDGNKLSGGQK 473
Cdd:TIGR04521 83 KVGLVFQfpEHQLFEETVYKdiafgpkNLGL-----SEEEAeervKEALE---------LVGLDEeYLERSPFELSGGQM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2674892663 474 HRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQ--TMIVTSHDIS-LLRFFDDIIICGEEKIIEQG 547
Cdd:TIGR04521 149 RRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKglTVILVTHSMEdVAEYADRVIVMHKGKIVLDG 225
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
334-525 |
1.06e-26 |
|
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: 107.56 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 334 QLLLKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEkSIREHFAVA 412
Cdd:COG4133 2 MLEAENLSCRRgERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-DYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 413 FQEHHIF-NLSIRDN----FKMLYENITDEEIYKSLENVYLLDFvnqvgLDYIVGNdgnkLSGGQKHRLQLAICLAKQKD 487
Cdd:COG4133 81 GHADGLKpELTVRENlrfwAALYGLRADREAIDEALEAVGLAGL-----ADLPVRQ----LSAGQKRRVALARLLLSPAP 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2674892663 488 IILLDEPTAGLDiKTTNNICSQLMEKYQKQ--TMIVTSHD 525
Cdd:COG4133 152 LWLLDEPFTALD-AAGVALLAELIAAHLARggAVLLTTHQ 190
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
335-547 |
1.36e-26 |
|
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: 107.61 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYDKV-LLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKsiREHFAVAF 413
Cdd:cd03259 1 LELKGLSKTYGSVrALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 QEHHIF-NLSIRDN--FKMLYENITDEEIYKSLENVYLLdfvnqVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIIL 490
Cdd:cd03259 79 QDYALFpHLTVAENiaFGLKLRGVPKAEIRARVRELLEL-----VGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 491 LDEPTAGLDIKTTNNICSQLmEKYQKQ---TMIVTSHDIS-LLRFFDDIIICGEEKIIEQG 547
Cdd:cd03259 154 LDEPLSALDAKLREELREEL-KELQRElgiTTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
348-537 |
1.67e-26 |
|
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: 106.78 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 348 LLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnyddlaeksirehFAVAFQEHHIFNLSIRDN- 426
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-------------IAYVSQEPWIQNGTIRENi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 427 -FKMLYenitDEEIYKS-LENVYLL-DFVNQVGLD-YIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKT 502
Cdd:cd03250 87 lFGKPF----DEERYEKvIKACALEpDLEILPDGDlTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2674892663 503 TNNI-----CSQLMEkyqKQTMIVTSHDISLLRFFDDIII 537
Cdd:cd03250 163 GRHIfenciLGLLLN---NKTRILVTHQLQLLPHADQIVV 199
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
347-555 |
1.88e-26 |
|
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: 107.67 E-value: 1.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 347 VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIRE---HFAVAFQEhhiFNLSi 423
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKarrRIGMIFQH---FNLL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 424 rdNFKMLYENIT---------DEEIYKSLENvyLLDFvnqVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEP 494
Cdd:cd03258 95 --SSRTVFENVAlpleiagvpKAEIEERVLE--LLEL---VGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2674892663 495 TAGLDIKTTNNICsQLMEKYQKQ---TMIVTSHDISLLR-FFDDIIICGEEKIIEQGNIKKLLLR 555
Cdd:cd03258 168 TSALDPETTQSIL-ALLRDINRElglTIVLITHEMEVVKrICDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
335-558 |
4.57e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 106.38 E-value: 4.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYDkVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDL--AEKSIrehfAVA 412
Cdd:COG3840 2 LRLDDLTYRYG-DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALppAERPV----SML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 413 FQEHHIFN-LSIRDNF------KMlyeNITDEEIYKslenvyLLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQ 485
Cdd:COG3840 77 FQENNLFPhLTVAQNIglglrpGL---KLTAEQRAQ------VEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 486 KDIILLDEPTAGLD-------IKTTNNICSQlmekyQKQTMIVTSHDIS-LLRFFDDIIICGEEKIIEQGNIKKLLLRED 557
Cdd:COG3840 148 RPILLLDEPFSALDpalrqemLDLVDELCRE-----RGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALLDGEP 222
|
.
gi 2674892663 558 S 558
Cdd:COG3840 223 P 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
340-530 |
6.26e-26 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 105.90 E-value: 6.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 340 LAYGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSI---REHFAVAFQEH 416
Cdd:COG2884 9 KRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIpylRRRIGVVFQDF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 417 H-IFNLSIRDN--FKMLYENITDEEIYKSLENVylLDfvnQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDE 493
Cdd:COG2884 89 RlLPDRTVYENvaLPLRVTGKSRKEIRRRVREV--LD---LVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADE 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 2674892663 494 PTAGLDIKTTNNICsQLMEKYQKQ--TMIVTSHDISLLR 530
Cdd:COG2884 164 PTGNLDPETSWEIM-ELLEEINRRgtTVLIATHDLELVD 201
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
337-537 |
7.32e-26 |
|
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: 105.30 E-value: 7.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDL--AYGyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEK--SIREHFAVA 412
Cdd:cd03262 3 IKNLhkSFG-DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 413 FQEHHIF-NLSIRDNFKM-------LYENITDEEIYKSLENVYLLDFVNQvgldYIvgndgNKLSGGQKHRLQLAICLAK 484
Cdd:cd03262 82 FQQFNLFpHLTVLENITLapikvkgMSKAEAEERALELLEKVGLADKADA----YP-----AQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 485 QKDIILLDEPTAGLD---IKTTNNICSQLMEkyQKQTMIVTSHDISLLR-------FFDDIII 537
Cdd:cd03262 153 NPKVMLFDEPTSALDpelVGEVLDVMKDLAE--EGMTMVVVTHEMGFARevadrviFMDDGRI 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
337-544 |
1.05e-25 |
|
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: 104.65 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGYDKV--LLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNyddLAEKSIREHFAVAFQ 414
Cdd:cd03226 2 IENISFSYKKGteILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 E--HHIFNLSIRD----NFKMLYENITD-EEIYKSLEnvyLLDFVNQVGLDyivgndgnkLSGGQKHRLQLAICLAKQKD 487
Cdd:cd03226 79 DvdYQLFTDSVREelllGLKELDAGNEQaETVLKDLD---LYALKERHPLS---------LSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 488 IILLDEPTAGLDIKTTNNICsQLMEKYQKQ--TMIVTSHDISLL-RFFDDIIICGEEKII 544
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVG-ELIRELAAQgkAVIVITHDYEFLaKVCDRVLLLANGAIV 205
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
338-543 |
2.26e-25 |
|
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: 104.48 E-value: 2.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 338 KDLAYGY----DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAF 413
Cdd:cd03248 15 QNVTFAYptrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 QEHHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVN--QVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:cd03248 95 QEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISelASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 492 DEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKI 543
Cdd:cd03248 175 DEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
349-547 |
2.47e-25 |
|
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: 103.65 E-value: 2.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRDNFK 428
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSNLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 429 MlYENITDEEIYKSLEnvylldfvnqvgldyiVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICS 508
Cdd:cd03369 104 P-FDEYSDEEIYGALR----------------VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQK 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 2674892663 509 QLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQG 547
Cdd:cd03369 167 TIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
339-524 |
2.85e-25 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 105.12 E-value: 2.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 339 DLAYGyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRL--LYP---LKGNIFIQGKN-YD---DLAEksIREHF 409
Cdd:COG1117 18 NVYYG-DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPgarVEGEILLDGEDiYDpdvDVVE--LRRRV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 410 AVAFQEHHIFNLSIrdnfkmlYENIT--------------DEEIYKSLENVYLLDFV----NQVGLdyivgndgnKLSGG 471
Cdd:COG1117 95 GMVFQKPNPFPKSI-------YDNVAyglrlhgikskselDEIVEESLRKAALWDEVkdrlKKSAL---------GLSGG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2674892663 472 QKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICsQLMEKYQKQ-TMIVTSH 524
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIE-ELILELKKDyTIVIVTH 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
345-526 |
2.89e-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: 103.74 E-value: 2.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGknYDDLAE-KSIREHFAVAFQEHHIF-NLS 422
Cdd:cd03263 14 TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING--YSIRTDrKAARQSLGYCPQFDALFdELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 IRDN------FKMLYENITDEEIYKSLENVYLLDFVN-QVGldyivgndgnKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:cd03263 92 VREHlrfyarLKGLPKSEIKEEVELLLRVLGLTDKANkRAR----------TLSGGMKRKLSLAIALIGGPSVLLLDEPT 161
|
170 180 190
....*....|....*....|....*....|.
gi 2674892663 496 AGLDIKTTNNICSQLMEKYQKQTMIVTSHDI 526
Cdd:cd03263 162 SGLDPASRRAIWDLILEVRKGRSIILTTHSM 192
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
335-527 |
8.44e-25 |
|
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: 102.55 E-value: 8.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYD-----KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnyddlAEKSIREHF 409
Cdd:cd03293 1 LEVRNVSKTYGggggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-----PVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 410 AVAFQEHHIFN-LSIRDNFKMLYE--NITDEEIYKslenvYLLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQK 486
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLElqGVPKAEARE-----RAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2674892663 487 DIILLDEPTAGLDIKTTNNICSQLME--KYQKQTMIVTSHDIS 527
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDID 193
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
345-553 |
9.68e-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: 103.34 E-value: 9.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQE-------HH 417
Cdd:COG1124 17 RVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDpyaslhpRH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 418 IFNLSIRDNFKMLYENITDEEIYKSLEnvylldfvnQVGLD------YIvgndgNKLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:COG1124 97 TVDRILAEPLRIHGLPDREERIAELLE---------QVGLPpsfldrYP-----HQLSGGQRQRVAIARALILEPELLLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 492 DEPTAGLDIKTTNNICsQLMEKYQKQ---TMIVTSHDISLLRFF-DDIIICGEEKIIEQGNIKKLL 553
Cdd:COG1124 163 DEPTSALDVSVQAEIL-NLLKDLREErglTYLFVSHDLAVVAHLcDRVAVMQNGRIVEELTVADLL 227
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
338-552 |
1.33e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 103.62 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 338 KDLAYGYDK--VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGK--NYDDLAEKSIREHFAVAF 413
Cdd:PRK13639 5 RDLKYSYPDgtEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpiKYDKKSLLEVRKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 Q--EHHIFNLSIRDN--FKMLYENITDEEIYK----SLENVYLLDFVNQVGldyivgndgNKLSGGQKHRLQLAICLAKQ 485
Cdd:PRK13639 85 QnpDDQLFAPTVEEDvaFGPLNLGLSKEEVEKrvkeALKAVGMEGFENKPP---------HHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 486 KDIILLDEPTAGLDIKTTNNIcSQLMEKYQKQ--TMIVTSHDISLLRFF-DDIIICGEEKIIEQGNIKKL 552
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQI-MKLLYDLNKEgiTIIISTHDVDLVPVYaDKVYVMSDGKIIKEGTPKEV 224
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
334-564 |
3.62e-24 |
|
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: 102.24 E-value: 3.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 334 QLLLKDLAYGYDK---VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYpLKGNIFIQGKNYDDLAEKSIREHFA 410
Cdd:cd03289 2 QMTVKDLTAKYTEggnAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 411 VAFQEHHIFNLSIRDNFKMlYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDI 488
Cdd:cd03289 81 VIPQKVFIFSGTFRKNLDP-YGKWSDEEIWKVAEEVGLKSVIEQFpgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 489 ILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDIsllrffDDIIICGEEKIIEQGNIKKL-----LLREDSYLNKL 563
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRI------EAMLECQRFLVIEENKVRQYdsiqkLLNEKSHFKQA 233
|
.
gi 2674892663 564 I 564
Cdd:cd03289 234 I 234
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
342-528 |
1.05e-23 |
|
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: 99.40 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSI---REHFAVAFQEHH- 417
Cdd:cd03292 10 YPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIpylRRKIGVVFQDFRl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 418 IFNLSIRDN--FKMLYENITDEEIYKSLENVylldfVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:cd03292 90 LPDRNVYENvaFALEVTGVPPREIRKRVPAA-----LELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPT 164
|
170 180 190
....*....|....*....|....*....|....*
gi 2674892663 496 AGLDIKTTNNIcSQLMEKYQKQ--TMIVTSHDISL 528
Cdd:cd03292 165 GNLDPDTTWEI-MNLLKKINKAgtTVVVATHAKEL 198
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
334-565 |
1.43e-23 |
|
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: 99.98 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 334 QLLLKDLAYGYD---KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFA 410
Cdd:cd03288 19 EIKIHDLCVRYEnnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 411 VAFQEHHIFNLSIRDNFKMlYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDI 488
Cdd:cd03288 99 IILQDPILFSGSIRFNLDP-ECKCTDDRLWEALEIAQLKNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2674892663 489 ILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLREDSYLNKLIR 565
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVR 254
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
347-553 |
1.54e-23 |
|
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: 105.80 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 347 VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRDN 426
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 427 FKMlYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTN 504
Cdd:TIGR00957 1380 LDP-FSQYSDEEVWWALELAHLKTFVSALpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN 1458
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2674892663 505 NICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLL 553
Cdd:TIGR00957 1459 LIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLL 1507
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
337-547 |
2.30e-23 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 98.91 E-value: 2.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDL--AYGyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYD----DLAEksIREHFA 410
Cdd:COG1126 4 IENLhkSFG-DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskkDINK--LRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 411 VAFQEHHIF-NLSIRdnfkmlyENIT-----------DEEIYKSLEnvyLLDfvnQVGLdyivgndGNK-------LSGG 471
Cdd:COG1126 81 MVFQQFNLFpHLTVL-------ENVTlapikvkkmskAEAEERAME---LLE---RVGL-------ADKadaypaqLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 472 QKHRLQLAICLAKQKDIILLDEPTAGLD----------IKttnnicsQLMEkyQKQTMIVTSHDISLLR-------FFDD 534
Cdd:COG1126 141 QQQRVAIARALAMEPKVMLFDEPTSALDpelvgevldvMR-------DLAK--EGMTMVVVTHEMGFARevadrvvFMDG 211
|
250
....*....|...
gi 2674892663 535 iiicGEekIIEQG 547
Cdd:COG1126 212 ----GR--IVEEG 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
331-553 |
2.48e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 99.68 E-value: 2.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 331 KDVQLLLKDLAYGYD---KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIRE 407
Cdd:PRK13632 4 KSVMIKVENVSFSYPnseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 408 HFAVAFQ--EHHIFNLSIRDNFKMLYEN--ITDEEIYKSLEnvyllDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLA 483
Cdd:PRK13632 84 KIGIIFQnpDNQFIGATVEDDIAFGLENkkVPPKKMKDIID-----DLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 484 KQKDIILLDEPTAGLDIKTTNNIcSQLMEKYQKQ---TMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLL 553
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREI-KKIMVDLRKTrkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
335-552 |
4.16e-23 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 97.62 E-value: 4.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYdKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKsiREHFAVAFQ 414
Cdd:TIGR01277 1 LALDKVRYEY-EHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPY--QRPVSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 EHHIF-NLSIRDNFKMlyeNITDEEIYKSLENVYLLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDE 493
Cdd:TIGR01277 78 ENNLFaHLTVRQNIGL---GLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 494 PTAGLD-------IKTTNNICSQlmekyQKQTMIVTSHDISllrffDDIIICGEEKIIEQGNIKKL 552
Cdd:TIGR01277 155 PFSALDpllreemLALVKQLCSE-----RQRTLLMVTHHLS-----DARAIASQIAVVSQGKIKVV 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
335-549 |
8.58e-23 |
|
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: 95.36 E-value: 8.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGY---DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAV 411
Cdd:cd03246 1 LEVENVSFRYpgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 412 AFQEHHIFNLSIRDNFkmlyenitdeeiykslenvylldfvnqvgldyivgndgnkLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:cd03246 81 LPQDDELFSGSIAENI----------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2674892663 492 DEPTAGLDIKTTNNICSQL-MEKYQKQTMIVTSHDISLLRFFDDIIicgeekIIEQGNI 549
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIaALKAAGATRIVIAHRPETLASADRIL------VLEDGRV 173
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
349-528 |
1.29e-22 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 95.57 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGK--NYDDLAEKSIREHFAVAFQ--EHHIFNLSIR 424
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEplDYSRKGLLERRQRVGLVFQdpDDQLFAADVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 425 DN--FKMLYENITDEEIYKSLENVYLLdfvnqVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKT 502
Cdd:TIGR01166 88 QDvaFGPLNLGLSEAEVERRVREALTA-----VGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAG 162
|
170 180
....*....|....*....|....*..
gi 2674892663 503 TNNICSQLME-KYQKQTMIVTSHDISL 528
Cdd:TIGR01166 163 REQMLAILRRlRAEGMTVVISTHDVDL 189
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
334-547 |
2.59e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 96.62 E-value: 2.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 334 QLLLKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVA 412
Cdd:PRK11231 2 TLRTENLTVGYgTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 413 FQeHHIFNLSI---------RDNFKMLYENITDEE---IYKSLENVYLLDFVNQVGLDyivgndgnkLSGGQKHRLQLAI 480
Cdd:PRK11231 82 PQ-HHLTPEGItvrelvaygRSPWLSLWGRLSAEDnarVNQAMEQTRINHLADRRLTD---------LSGGQRQRAFLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 481 CLAKQKDIILLDEPTAGLDIKTTNNICSqLMEKYQKQ--TMIVTSHDIS-LLRFFDDIIICGEEKIIEQG 547
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDINHQVELMR-LMRELNTQgkTVVTVLHDLNqASRYCDHLVVLANGHVMAQG 220
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
342-555 |
2.89e-22 |
|
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: 95.83 E-value: 2.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIF-N 420
Cdd:cd03295 10 YGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQIGLFpH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 LSIRDNF-------KMLYENItDEEIYKSLEnvylldfvnQVGLD--YIVGNDGNKLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:cd03295 90 MTVEENIalvpkllKWPKEKI-RERADELLA---------LVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2674892663 492 DEPTAGLDIKTTNNIcSQLMEKYQKQ---TMIVTSHDI-SLLRFFDDIIICGEEKIIEQGNIKKLLLR 555
Cdd:cd03295 160 DEPFGALDPITRDQL-QEEFKRLQQElgkTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
325-545 |
3.87e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.14 E-value: 3.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 325 QEDKQSKDVqLLLKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIfIQGKN----Ydd 399
Cdd:COG0488 307 PPERLGKKV-LELEGLSKSYgDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-KLGETvkigY-- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 400 laeksirehFAvafQEHHIF--NLSIRDNFKMLYENITDEEIYKslenvYLLDFvnqvGLDyivGNDGNK----LSGGQK 473
Cdd:COG0488 383 ---------FD---QHQEELdpDKTVLDELRDGAPGGTEQEVRG-----YLGRF----LFS---GDDAFKpvgvLSGGEK 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 474 HRLQLAICLAKQKDIILLDEPTAGLDIKTTnnicsQLMEKYQKQ---TMIVTSHDISLL-RFFDDIIICGEEKIIE 545
Cdd:COG0488 439 ARLALAKLLLSPPNVLLLDEPTNHLDIETL-----EALEEALDDfpgTVLLVSHDRYFLdRVATRILEFEDGGVRE 509
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
330-526 |
9.66e-22 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 94.77 E-value: 9.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 330 SKDVQLLLKDLAYGY-----DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnyddlAEKS 404
Cdd:COG1116 3 AAAPALELRGVSKRFptgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK-----PVTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 405 IREHFAVAFQEHHIFN-LSIRDN--FKMLYENITDEEIYKSLEnvYLLDfvnQVGLdyivGNDGNK----LSGGQKHRLQ 477
Cdd:COG1116 78 PGPDRGVVFQEPALLPwLTVLDNvaLGLELRGVPKAERRERAR--ELLE---LVGL----AGFEDAyphqLSGGMRQRVA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 478 LAICLAKQKDIILLDEPTAGLDIKTTNNICSQLME--KYQKQTMI-VTsHDI 526
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLfVT-HDV 199
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
349-547 |
1.05e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 95.47 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFI------QGKNYDDLaeKSIREHFAVAFQ--EHHIFN 420
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKL--KPLRKKVGIVFQfpEHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 LSI-RD------NFKMLYEnitdEEIYKSLENVYLldfvnqVGLDY-IVGNDGNKLSGGQKHRLQLAICLAKQKDIILLD 492
Cdd:PRK13634 101 ETVeKDicfgpmNFGVSEE----DAKQKAREMIEL------VGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 493 EPTAGLDIKTTNNIcsqlME------KYQKQTMIVTSHDIS-LLRFFDDIIICGEEKIIEQG 547
Cdd:PRK13634 171 EPTAGLDPKGRKEM----MEmfyklhKEKGLTTVLVTHSMEdAARYADQIVVMHKGTVFLQG 228
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
330-553 |
1.39e-21 |
|
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: 94.63 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 330 SKDVQLLLKDLAYGYDK----------VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDD 399
Cdd:cd03294 11 GKNPQKAFKLLAKGKSKeeilkktgqtVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 400 LAEKSIRE----HFAVAFQEHHIF-NLSIRDN--FKMLYENITDEEIY----KSLENVYLLDFVNQvgldYIvgndgNKL 468
Cdd:cd03294 91 MSRKELRElrrkKISMVFQSFALLpHRTVLENvaFGLEVQGVPRAEREeraaEALELVGLEGWEHK----YP-----DEL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 469 SGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLME--KYQKQTMIVTSHD-ISLLRFFDDIIICGEEKIIE 545
Cdd:cd03294 162 SGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRlqAELQKTIVFITHDlDEALRLGDRIAIMKDGRLVQ 241
|
....*...
gi 2674892663 546 QGNIKKLL 553
Cdd:cd03294 242 VGTPEEIL 249
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
349-547 |
1.49e-21 |
|
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: 93.13 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIK---KGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDlAEKSI-----REHFAVAFQEHHIF- 419
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFD-SRKKInlppqQRKIGLVFQQYALFp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 420 NLSIRdnfkmlyENItdEEIYKSLENVYLLDFVNQV----GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:cd03297 89 HLNVR-------ENL--AFGLKRKRNREDRISVDELldllGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 496 AGLDiKTTNNICSQLMEKYQKQ---TMIVTSHDIS-LLRFFDDIIICGEEKIIEQG 547
Cdd:cd03297 160 SALD-RALRLQLLPELKQIKKNlniPVIFVTHDLSeAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
332-526 |
2.10e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 94.08 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 332 DVQLLLKDLAYGYDKVL-LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRL--LYP---LKGNIFIQGKN-YD-DLAEK 403
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLaVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPgfrVEGKVTFHGKNlYApDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 404 SIREHFAVAFQEHHIFNLSIRDNFKML-----YENITDEEIYKSLENVYLLDFV----NQVGLdyivgndgnKLSGGQKH 474
Cdd:PRK14243 88 EVRRRIGMVFQKPNPFPKSIYDNIAYGaringYKGDMDELVERSLRQAALWDEVkdklKQSGL---------SLSGGQQQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 475 RLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDI 526
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
189-537 |
3.31e-21 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 98.56 E-value: 3.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 189 TQEIIE-FYEGNRELSFYNYDKYRLKNINHSIEQYQQY--QQNLFKlKLKVNLCSEFIMGAY---------LVICLAISI 256
Cdd:PTZ00265 235 TMSIIEeALVGIRTVVSYCGEKTILKKFNLSEKLYSKYilKANFME-SLHIGMINGFILASYafgfwygtrIIISDLSNQ 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 257 YLVNtqDFNPIMAITIILTYQAVLEVLAMMPSLIEHFDEASKRWQDLAIFMQEKKFIANtnneikseNQEDKQSKDVQ-L 335
Cdd:PTZ00265 314 QPNN--DFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVEN--------NDDGKKLKDIKkI 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 336 LLKDLAYGYDK----VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQ-GKNYDDLAEKSIREHFA 410
Cdd:PTZ00265 384 QFKNVRFHYDTrkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWWRSKIG 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 411 VAFQEHHIFNLSIRDNFKML---------------------------------------------------------YEN 433
Cdd:PTZ00265 464 VVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrknYQT 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 434 ITDEEIYKSLENVYLLDFVNQVGLDY--IVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD-------IKTTN 504
Cdd:PTZ00265 544 IKDSEVVDVSKKVLIHDFVSALPDKYetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDnkseylvQKTIN 623
|
410 420 430
....*....|....*....|....*....|...
gi 2674892663 505 NicsqlMEKYQKQTMIVTSHDISLLRFFDDIII 537
Cdd:PTZ00265 624 N-----LKGNENRITIIIAHRLSTIRYANTIFV 651
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
335-498 |
3.65e-21 |
|
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: 92.11 E-value: 3.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYDKV-LLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLA-EKSIREHFAVA 412
Cdd:cd03224 1 LEVENLNAGYGKSqILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 413 FQEHHIF-NLSIRDNFKMLYENITDEEIYKSLENVY-----LLDFVNQVGldyivGNdgnkLSGGQkhRLQLAIC--LAK 484
Cdd:cd03224 81 PEGRRIFpELTVEENLLLGAYARRRAKRKARLERVYelfprLKERRKQLA-----GT----LSGGE--QQMLAIAraLMS 149
|
170
....*....|....
gi 2674892663 485 QKDIILLDEPTAGL 498
Cdd:cd03224 150 RPKLLLLDEPSEGL 163
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
344-563 |
5.05e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 93.31 E-value: 5.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 344 YDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQG----KNYDDLAEKSIREHFAVAFQ--EHH 417
Cdd:PRK13646 18 YEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIRPVRKRIGMVFQfpESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 418 IFNLSIR-------DNFKMLYENITDeeiykslenvYLLDFVNQVGLDY-IVGNDGNKLSGGQKHRLQLAICLAKQKDII 489
Cdd:PRK13646 98 LFEDTVEreiifgpKNFKMNLDEVKN----------YAHRLLMDLGFSRdVMSQSPFQMSGGQMRKIAIVSILAMNPDII 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2674892663 490 LLDEPTAGLDIKTTNNICSqLMEKYQ---KQTMIVTSHDIS-LLRFFDDIIICGEEKIIEQGNIKKlLLREDSYLNKL 563
Cdd:PRK13646 168 VLDEPTAGLDPQSKRQVMR-LLKSLQtdeNKTIILVSHDMNeVARYADEVIVMKEGSIVSQTSPKE-LFKDKKKLADW 243
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
334-564 |
5.32e-21 |
|
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: 97.67 E-value: 5.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 334 QLLLKDLAYGYD---KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLyPLKGNIFIQGKNYDDLAEKSIREHFA 410
Cdd:TIGR01271 1217 QMDVQGLTAKYTeagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTWRKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 411 VAFQEHHIFNLSIRDNFKMlYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDI 488
Cdd:TIGR01271 1296 VIPQKVFIFSGTFRKNLDP-YEQWSDEEIWKVAEEVGLKSVIEQFpdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKI 1374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 489 ILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKlLLREDSYLNKLI 564
Cdd:TIGR01271 1375 LLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQK-LLNETSLFKQAM 1449
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
330-547 |
8.92e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 92.56 E-value: 8.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 330 SKDVQLLLKDLAYGY---DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYP---LKGNIFIQGKNYDDLAEK 403
Cdd:PRK13640 1 MKDNIVEFKHVSFTYpdsKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 404 SIREHFAVAFQ--EHHIFNLSIRDNFKMLYEN--ITDEEIYKSLENVylldfVNQVG-LDYIVGNDGNkLSGGQKHRLQL 478
Cdd:PRK13640 81 DIREKVGIVFQnpDNQFVGATVGDDVAFGLENraVPRPEMIKIVRDV-----LADVGmLDYIDSEPAN-LSGGQKQRVAI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 479 AICLAKQKDIILLDEPTAGLDIKTTNNICS---QLMEKYQkQTMIVTSHDISLLRFFDDIIICGEEKIIEQG 547
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKlirKLKKKNN-LTVISITHDIDEANMADQVLVLDDGKLLAQG 225
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
349-565 |
9.79e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 97.12 E-value: 9.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRDNFK 428
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLD 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 429 MLYENiTDEEIYKSLENVYLLDFV--NQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNI 506
Cdd:PLN03130 1335 PFNEH-NDADLWESLERAHLKDVIrrNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALI 1413
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2674892663 507 CSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLREDSYLNKLIR 565
Cdd:PLN03130 1414 QKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQ 1472
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
337-557 |
1.38e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 91.72 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY--DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQ 414
Cdd:PRK13647 7 VEDLHFRYkdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 --EHHIFNLSIRDN--FKMLYENITDEEIYKSLEnvyllDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIIL 490
Cdd:PRK13647 87 dpDDQVFSSTVWDDvaFGPVNMGLDKDEVERRVE-----EALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2674892663 491 LDEPTAGLDIKTTNNICSQLMEKYQK-QTMIVTSHDISL-LRFFDDIIICGEEKIIEQGNiKKLLLRED 557
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDLaAEWADQVIVLKEGRVLAEGD-KSLLTDED 229
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
345-553 |
1.39e-20 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 91.30 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGN-IFIQGKNYD--DLAEksIREHFAV---AFQEHHI 418
Cdd:COG1119 15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGgeDVWE--LRKRIGLvspALQLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 419 FNLSIRDnfkM----------LYENITDEEIYKSLEnvyLLDFvnqVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDI 488
Cdd:COG1119 93 RDETVLD---VvlsgffdsigLYREPTDEQRERARE---LLEL---LGLAHLADRPFGTLSQGEQRRVLIARALVKDPEL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2674892663 489 ILLDEPTAGLDIKTT---NNICSQLMEKYQKQTMIVTsHDIS-LLRFFDDIIICGEEKIIEQGNIKKLL 553
Cdd:COG1119 164 LILDEPTAGLDLGARellLALLDKLAAEGAPTLVLVT-HHVEeIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
335-536 |
1.51e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.61 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGK--NYDDLAEKSIREHFAV 411
Cdd:PRK13638 2 LATSDLWFRYqDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 412 AFQ--EHHIFNLSIRDNFKMLYEN--ITDEEIYKSLENVYLLdfvnqVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKD 487
Cdd:PRK13638 82 VFQdpEQQIFYTDIDSDIAFSLRNlgVPEAEITRRVDEALTL-----VDAQHFRHQPIQCLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2674892663 488 IILLDEPTAGLDIKTTNNICSQLME-KYQKQTMIVTSHDISLLRFFDDII 536
Cdd:PRK13638 157 YLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEISDAV 206
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
335-536 |
1.65e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 90.54 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYD-KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAF 413
Cdd:PRK10247 8 LQLQNVGYLAGdAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 QEHHIFNLSIRDNFKMLYE--NITDEEiykslenVYLLDFVNQVGL-DYIVGNDGNKLSGGQKHRLQLAICLAKQKDIIL 490
Cdd:PRK10247 88 QTPTLFGDTVYDNLIFPWQirNQQPDP-------AIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2674892663 491 LDEPTAGLD---IKTTNNICSQLMEKYQKQTMIVTsHDISLLRFFDDII 536
Cdd:PRK10247 161 LDEITSALDesnKHNVNEIIHRYVREQNIAVLWVT-HDKDEINHADKVI 208
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
340-555 |
2.41e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 90.74 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 340 LAYGYDKVLlKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRL--LYP---LKGNIFIQGKNYDDLAEKSIREHFAVAFQ 414
Cdd:PRK14247 11 VSFGQVEVL-DGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPearVSGEVYLDGQDIFKMDVIELRRRVQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 -EHHIFNLSIRDNFKM------LYENITD--EEIYKSLENVYLLDFVNQvGLDYIVGndgnKLSGGQKHRLQLAICLAKQ 485
Cdd:PRK14247 90 iPNPIPNLSIFENVALglklnrLVKSKKElqERVRWALEKAQLWDEVKD-RLDAPAG----KLSGGQQQRLCIARALAFQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 486 KDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSH-DISLLRFFDDIIICGEEKIIEQGNIKKLLLR 555
Cdd:PRK14247 165 PEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
342-547 |
3.27e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 90.07 E-value: 3.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGYDKVLLkDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYD---DLAEKSIRE---HFAVAFQE 415
Cdd:PRK11124 12 YGAHQALF-DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfskTPSDKAIRElrrNVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 HHIF-NLSIRDNF-----KM--LYENITDEEIYKSLENVYLLDFVNQVGLdyivgndgnKLSGGQKHRLQLAICLAKQKD 487
Cdd:PRK11124 91 YNLWpHLTVQQNLieapcRVlgLSKDQALARAEKLLERLRLKPYADRFPL---------HLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 488 IILLDEPTAGLDIKTTNNICSQLMEKYQKQ-TMIVTSHDISLLRFFDDIIICGEE-KIIEQG 547
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGiTQVIVTHEVEVARKTASRVVYMENgHIVEQG 223
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
330-548 |
4.29e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 90.84 E-value: 4.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 330 SKDVqlLLKDLAYGYDKVL------LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQG----KNYDD 399
Cdd:PRK13645 4 SKDI--ILDNVSYTYAKKTpfefkaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 400 LAE-KSIREHFAVAFQ--EHHIFNLSIRDN--FKMLYENITDEEIYKSLENvyLLDFVnQVGLDYiVGNDGNKLSGGQKH 474
Cdd:PRK13645 82 IKEvKRLRKEIGLVFQfpEYQLFQETIEKDiaFGPVNLGENKQEAYKKVPE--LLKLV-QLPEDY-VKRSPFELSGGQKR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2674892663 475 RLQLAICLAKQKDIILLDEPTAGLDIKTTN---NICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGN 548
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
348-565 |
5.03e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 94.66 E-value: 5.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 348 LLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRDNF 427
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 428 KMLYENiTDEEIYKSLENVYLLDFV--NQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNN 505
Cdd:PLN03232 1331 DPFSEH-NDADLWEALERAHIKDVIdrNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSL 1409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 506 ICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLREDSYLNKLIR 565
Cdd:PLN03232 1410 IQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVH 1469
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
335-526 |
6.21e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 88.87 E-value: 6.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYDKVLLKdINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKsiREHFAVAFQ 414
Cdd:PRK10771 2 LKLTDITWLYHHLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 EHHIFN-LSIRDNFKM-LYENIT-DEEIYKSLEnvyllDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:PRK10771 79 ENNLFShLTVAQNIGLgLNPGLKlNAAQREKLH-----AIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2674892663 492 DEPTAGLD-------IKTTNNICSQlmekyQKQTMIVTSHDI 526
Cdd:PRK10771 154 DEPFSALDpalrqemLTLVSQVCQE-----RQLTLLMVSHSL 190
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
335-525 |
6.29e-20 |
|
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: 88.47 E-value: 6.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYDKVL-LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDL--AEKSIrehfAV 411
Cdd:cd03301 1 VELENVTKRFGNVTaLDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLppKDRDI----AM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 412 AFQEHHIF-NLSIRDN--FKMLYENITDEEIYKSLENVYLLdfvnqVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDI 488
Cdd:cd03301 77 VFQNYALYpHMTVYDNiaFGLKLRKVPKDEIDERVREVAEL-----LQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 2674892663 489 ILLDEPTAGLDIKTTNNICSQL--MEKYQKQTMIVTSHD 525
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELkrLQQRLGTTTIYVTHD 190
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
340-556 |
8.15e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 89.28 E-value: 8.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 340 LAYGyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQ----- 414
Cdd:PRK10253 15 LGYG-KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQnattp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 -EHHIFNLSIRDNF--KMLYENITDEEiykslenvylLDFVNQ----VGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKD 487
Cdd:PRK10253 94 gDITVQELVARGRYphQPLFTRWRKED----------EEAVTKamqaTGITHLADQSVDTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 488 IILLDEPTAGLDIKTTNNICSQLME--KYQKQTMIVTSHDIS-LLRFFDDIIICGEEKIIEQGNIKKLLLRE 556
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLSElnREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVTAE 235
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
337-532 |
1.22e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.05 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGK--------NYDDLAEKSIRE 407
Cdd:COG0488 1 LENLSKSFgGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGlrigylpqEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 408 HFAVAFQEhhifNLSIRDNFKMLYENITDEEI----YKSLENVY--------------LLDfvnqvGLDyIVGNDGNK-- 467
Cdd:COG0488 81 TVLDGDAE----LRALEAELEELEAKLAEPDEdlerLAELQEEFealggweaearaeeILS-----GLG-FPEEDLDRpv 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 468 --LSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTnnicsQLMEKYQKQ---TMIVTSHDisllRFF 532
Cdd:COG0488 151 seLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESI-----EWLEEFLKNypgTVLVVSHD----RYF 211
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
349-537 |
1.40e-19 |
|
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: 87.91 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGK--------------NYDDLAEKSIREHFAVAfq 414
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKqitepgpdrmvvfqNYSLLPWLTVRENIALA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 ehhiFNLSIRDNFKMLYENITDEEIykslenvylldfvNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEP 494
Cdd:TIGR01184 79 ----VDRVLPDLSKSERRAIVEEHI-------------ALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEP 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2674892663 495 TAGLDIKTTNNICSQLMEKYQKQ--TMIVTSHDISLLRFFDDIII 537
Cdd:TIGR01184 142 FGALDALTRGNLQEELMQIWEEHrvTVLMVTHDVDEALLLSDRVV 186
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
351-553 |
1.56e-19 |
|
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: 89.73 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 351 DINLSIKKGnKTL-IVGTSGCGKSTLFYVLMRLLYPL---KGNIFIQGKNYDDLAEKSIRE----HFAVAFQE-HHIFN- 420
Cdd:COG0444 23 GVSFDVRRG-ETLgLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELRKirgrEIQMIFQDpMTSLNp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 -LSIRDNFK---MLYENITDEEIY-KSLEnvyLLDfvnQVGLDyivgnDGNK--------LSGGQKHRLQLAICLAKQKD 487
Cdd:COG0444 102 vMTVGDQIAeplRIHGGLSKAEAReRAIE---LLE---RVGLP-----DPERrldrypheLSGGMRQRVMIARALALEPK 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2674892663 488 IILLDEPTAGLDIkTTnnicsQ-----LMEKYQKQ---TMIVTSHDISLLRFF-DDIII--CGeeKIIEQGNIKKLL 553
Cdd:COG0444 171 LLIADEPTTALDV-TI-----QaqilnLLKDLQRElglAILFITHDLGVVAEIaDRVAVmyAG--RIVEEGPVEELF 239
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
340-536 |
1.75e-19 |
|
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: 87.39 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 340 LAYGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDD--LAEKSIREHFAVAF--QE 415
Cdd:cd03290 8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEpsFEATRSRNRYSVAYaaQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 HHIFNLSIRDNfkMLYENITDEEIYK------SLE-NVYLLDFVNQVGldyiVGNDGNKLSGGQKHRLQLAICLAKQKDI 488
Cdd:cd03290 88 PWLLNATVEEN--ITFGSPFNKQRYKavtdacSLQpDIDLLPFGDQTE----IGERGINLSGGQRQRICVARALYQNTNI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 489 ILLDEPTAGLDIKTTNNICSQLMEKY---QKQTMIVTSHDISLLRFFDDII 536
Cdd:cd03290 162 VFLDDPFSALDIHLSDHLMQEGILKFlqdDKRTLVLVTHKLQYLPHADWII 212
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
349-559 |
2.03e-19 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 87.39 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLaeKSIREHFAVAFQEHHIF-NLSIRDN- 426
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNL--PPEKRDISYVPQNYALFpHMTVYKNi 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 427 -FKMLYENITDEEIYKSLENVylldfVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNN 505
Cdd:cd03299 93 aYGLKKRKVDKKEIERKVLEI-----AEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 506 ICSQLME--KYQKQTMIVTSHDisllrfFDDIIICGEE-------KIIEQGNIKKLLLREDSY 559
Cdd:cd03299 168 LREELKKirKEFGVTVLHVTHD------FEEAWALADKvaimlngKLIQVGKPEEVFKKPKNE 224
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
346-557 |
2.35e-19 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 91.64 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 346 KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRD 425
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 426 NFKMLYENITDEEIYKS--LENVY--LLDFVNqvGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIK 501
Cdd:TIGR01842 411 NIARFGENADPEKIIEAakLAGVHelILRLPD--GYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEE 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2674892663 502 TTNNICSQLME-KYQKQTMIVTSHDISLLRFFDDIIicgeekIIEQGNIKKLLLRED 557
Cdd:TIGR01842 489 GEQALANAIKAlKARGITVVVITHRPSLLGCVDKIL------VLQDGRIARFGERDE 539
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
335-554 |
2.39e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 87.91 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRL--LYP---LKGNIFIQGKN-YDDLAEK-SIR 406
Cdd:PRK14239 6 LQVSDLSVYYnKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNiYSPRTDTvDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 407 EHFAVAFQEHHIFNLSIRDNfkMLY---------ENITDEEIYKSLENVYLLDFVNQVGLDYIVGndgnkLSGGQKHRLQ 477
Cdd:PRK14239 86 KEIGMVFQQPNPFPMSIYEN--VVYglrlkgikdKQVLDEAVEKSLKGASIWDEVKDRLHDSALG-----LSGGQQQRVC 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2674892663 478 LAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLL-RFFDDIIICGEEKIIEQGNIKKLLL 554
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQMFM 236
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
349-538 |
2.85e-19 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 87.11 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREH-FAVAFQEHHIF-NLSIRDN 426
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRTFQIPRLFpELTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 427 ------------FKMLYENITDEEIYKSLENvyLLDFVnqvGL----DYIVGNdgnkLSGGQKHRLQLAICLAKQKDIIL 490
Cdd:cd03219 96 vmvaaqartgsgLLLARARREEREARERAEE--LLERV---GLadlaDRPAGE----LSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2674892663 491 LDEPTAGLDIKTTNNICSQLME-KYQKQTMIVTSHDISLLRFFDDIIIC 538
Cdd:cd03219 167 LDEPAAGLNPEETEELAELIRElRERGITVLLVEHDMDVVMSLADRVTV 215
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
341-525 |
2.88e-19 |
|
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: 86.91 E-value: 2.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 341 AYGyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKsiREHFAVAFQEHHIF- 419
Cdd:cd03300 9 FYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVFQNYALFp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 420 NLSIRDN------FKMLYENITDEEIYKSLENVYLLDFVNQvgldyivgnDGNKLSGGQKHRLQLAICLAKQKDIILLDE 493
Cdd:cd03300 86 HLTVFENiafglrLKKLPKAEIKERVAEALDLVQLEGYANR---------KPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 2674892663 494 PTAGLDIKTTNNICSQLMEkYQKQ---TMIVTSHD 525
Cdd:cd03300 157 PLGALDLKLRKDMQLELKR-LQKElgiTFVFVTHD 190
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
283-568 |
4.27e-19 |
|
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: 91.93 E-value: 4.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 283 LAMMPSLIEHFDEASKRWQDLAIFMQEKkfiantnnEIKSENQEDKQSKD---VQLLLKDLAYGYDKVL---LKDINLSI 356
Cdd:TIGR00957 590 LNILPMVISSIVQASVSLKRLRIFLSHE--------ELEPDSIERRTIKPgegNSITVHNATFTWARDLpptLNGITFSI 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 357 KKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGknyddlaeksirehfAVAF--QEHHIFNLSIRDNfkMLYENI 434
Cdd:TIGR00957 662 PEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG---------------SVAYvpQQAWIQNDSLREN--ILFGKA 724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 435 TDEEIYKS-LENVYLL-DFVNQVGLDYI-VGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQL- 510
Cdd:TIGR00957 725 LNEKYYQQvLEACALLpDLEILPSGDRTeIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVi 804
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 511 --MEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLREDSYLNKLIRYKN 568
Cdd:TIGR00957 805 gpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAP 864
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
337-547 |
4.68e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 87.38 E-value: 4.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY---DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnydDLAEKS---IREHFA 410
Cdd:PRK13635 8 VEHISFRYpdaATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETvwdVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 411 VAFQ--EHHIFNLSIRDNFKMLYEN--ITDEEIYKSLEnvyllDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQK 486
Cdd:PRK13635 85 MVFQnpDNQFVGATVQDDVAFGLENigVPREEMVERVD-----QALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 487 DIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTS--HDISLLRFFDDIIICGEEKIIEQG 547
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSitHDLDEAAQADRVIVMNKGEILEEG 222
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
335-525 |
7.49e-19 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 88.23 E-value: 7.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYDKVL-LKDINLSIKKGNKTLIVGTSGCGKSTlfyvLMRLLY----PLKGNIFIQGKNYDDL-AEKsiReH 408
Cdd:COG3842 6 LELENVSKRYGDVTaLDDVSLSIEPGEFVALLGPSGCGKTT----LLRMIAgfetPDSGRILLDGRDVTGLpPEK--R-N 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 409 FAVAFQEHHIF-NLSIRDN--F--KMLyeNITDEEIYKSLENvyLLDfvnQVGLD-----YIvgndgNKLSGGQKHRLQL 478
Cdd:COG3842 79 VGMVFQDYALFpHLTVAENvaFglRMR--GVPKAEIRARVAE--LLE---LVGLEgladrYP-----HQLSGGQQQRVAL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 479 AICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEkYQKQ---TMI-VTsHD 525
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALDAKLREEMREELRR-LQRElgiTFIyVT-HD 195
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
342-547 |
9.07e-19 |
|
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: 84.96 E-value: 9.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIRehfAVAFQEHHIF-- 419
Cdd:cd03268 10 YG-KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR---IGALIEAPGFyp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 420 NLSIRDNFKM--LYENITDEEIYKSLEnvylldfvnQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAG 497
Cdd:cd03268 86 NLTARENLRLlaRLLGIRKKRIDEVLD---------VVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 498 LDIKTTNNIcSQLMEKYQKQ--TMIVTSHDIS-LLRFFDDIIICGEEKIIEQG 547
Cdd:cd03268 157 LDPDGIKEL-RELILSLRDQgiTVLISSHLLSeIQKVADRIGIINKGKLIEEG 208
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
343-553 |
9.32e-19 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 89.77 E-value: 9.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 343 GYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLS 422
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 IRDNFKMLYENITDEEIykslENVYLLDFVNQ------VGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTA 496
Cdd:PRK10789 405 VANNIALGRPDATQQEI----EHVARLASVHDdilrlpQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2674892663 497 GLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLL 553
Cdd:PRK10789 481 AVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLA 537
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
349-553 |
1.34e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 88.17 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIRE----HFAVAFQEHHIF-NLSI 423
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMpHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 424 RDN--FKMLYENITDEEIYKSlenvyLLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD-- 499
Cdd:PRK10070 124 LDNtaFGMELAGINAEERREK-----ALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDpl 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 500 IKT-TNNICSQLMEKYQKqTMIVTSHDI-SLLRFFDDIIICGEEKIIEQGNIKKLL 553
Cdd:PRK10070 199 IRTeMQDELVKLQAKHQR-TIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
346-553 |
1.36e-18 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 86.01 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 346 KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDL---AEKSIREHFAVAFQE-HHIFN- 420
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQDsPSAVNp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 -LSIRDNFKMLYENITDeeIYKSLENVYLLDFVNQVGLDyivGNDGNK----LSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:TIGR02769 104 rMTVRQIIGEPLRHLTS--LDESEQKARIAELLDMVGLR---SEDADKlprqLSGGQLQRINIARALAVKPKLIVLDEAV 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 496 AGLDIKTTNNICsQLMEKYQKQ---TMIVTSHDISLL-RFFDDIIICGEEKIIEQGNIKKLL 553
Cdd:TIGR02769 179 SNLDMVLQAVIL-ELLRKLQQAfgtAYLFITHDLRLVqSFCQRVAVMDKGQIVEECDVAQLL 239
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
349-501 |
1.59e-18 |
|
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: 85.08 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnydDLAEKSIRE-HFAVAFQEHHIF-NLSIRDN 426
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE---DATDVPVQErNVGFVFQHYALFrHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 427 F------KMLYENITDEEIYKSLENvyLLDFvnqVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDI 500
Cdd:cd03296 95 VafglrvKPRSERPPEAEIRAKVHE--LLKL---VQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDA 169
|
.
gi 2674892663 501 K 501
Cdd:cd03296 170 K 170
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
345-558 |
1.60e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 87.08 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGknyDDLAEKSIREH-FAVAFQEHHIF-NLS 422
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG---EDVTHRSIQQRdICMVFQSYALFpHMS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 IRDN----FKMLyeNITDEEIYKSL-ENVYLLD-------FVNQVgldyivgndgnklSGGQKHRLQLAICLAKQKDIIL 490
Cdd:PRK11432 95 LGENvgygLKML--GVPKEERKQRVkEALELVDlagfedrYVDQI-------------SGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2674892663 491 LDEPTAGLDIkttnNICSQLMEK---YQKQ---TMIVTSHDISllRFF---DDIIICGEEKIIEQGNIKKLLLREDS 558
Cdd:PRK11432 160 FDEPLSNLDA----NLRRSMREKireLQQQfniTSLYVTHDQS--EAFavsDTVIVMNKGKIMQIGSPQELYRQPAS 230
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
349-555 |
2.53e-18 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 86.29 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIRE---HFAVAFQehHiFNL---- 421
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAarrKIGMIFQ--H-FNLlssr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 422 SIRDN--FKMLYENITDEEIYKSLENvyLLDFVnqvGLdyivgndGNK-------LSGGQKHRLQLAICLAKQKDIILLD 492
Cdd:COG1135 98 TVAENvaLPLEIAGVPKAEIRKRVAE--LLELV---GL-------SDKadaypsqLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 493 EPTAGLDIKTTNNICsQLMEKYQKQ---TMIVTSHDIsllrffdDII--IC--------GeeKIIEQGNIKKLLLR 555
Cdd:COG1135 166 EATSALDPETTRSIL-DLLKDINRElglTIVLITHEM-------DVVrrICdrvavlenG--RIVEQGPVLDVFAN 231
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
351-547 |
3.39e-18 |
|
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: 83.31 E-value: 3.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 351 DINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYD--DLAEKSIrehfAVAFQEHHIF-NLSIRDNF 427
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTaaPPADRPV----SMLFQENNLFaHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 428 KM-----LYENITDEEIYKSLenvylldfVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKT 502
Cdd:cd03298 92 GLglspgLKLTAEDRQAIEVA--------LARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2674892663 503 TNNICSQLMEKYQKQTM---IVTSHDISLLRFFDDIIICGEEKIIEQG 547
Cdd:cd03298 164 RAEMLDLVLDLHAETKMtvlMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
342-548 |
3.82e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 83.91 E-value: 3.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGYDKVLlKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYD---DLAEKSIRE---HFAVAFQE 415
Cdd:COG4161 12 YGSHQAL-FDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAIRLlrqKVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 HHIF-NLSIRDNF-----KMLYEN--ITDEEIYKSLENVYLLDFVNQVGLdyivgndgnKLSGGQKHRLQLAICLAKQKD 487
Cdd:COG4161 91 YNLWpHLTVMENLieapcKVLGLSkeQAREKAMKLLARLRLTDKADRFPL---------HLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 488 IILLDEPTAGLDIKTTNNICSQLMEKYQKQ-TMIVTSHDISLLRFFDDIIICGEE-KIIEQGN 548
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTGiTQVIVTHEVEFARKVASQVVYMEKgRIIEQGD 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
331-547 |
3.88e-18 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 82.60 E-value: 3.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 331 KDVQLLLKDLAYGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLM--RLLYPLKGNIFIQGKNYDdlaEKSIREH 408
Cdd:cd03213 7 RNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLD---KRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 409 FAVAFQE-HHIFNLSIRDNfkmlyenitdeeiykslenvylldfvnqvgLDYIVGNDGnkLSGGQKHRLQLAICLAKQKD 487
Cdd:cd03213 84 IGYVPQDdILHPTLTVRET------------------------------LMFAAKLRG--LSGGERKRVSIALELVSNPS 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2674892663 488 IILLDEPTAGLDIKTTNNIcSQLMEKYQKQ--TMIVTSHDIS--LLRFFDDIIICGEEKIIEQG 547
Cdd:cd03213 132 LLFLDEPTSGLDSSSALQV-MSLLRRLADTgrTIICSIHQPSseIFELFDKLLLLSQGRVIYFG 194
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
337-542 |
4.93e-18 |
|
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: 80.96 E-value: 4.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIfiqgknyddlaeksirehfavafqe 415
Cdd:cd03221 3 LENLSKTYgGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 hhifnlsirdnfkmlyenitdeEIYKSLENVYLldfvnqvgldyivgndgNKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:cd03221 58 ----------------------TWGSTVKIGYF-----------------EQLSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2674892663 496 AGLDIKTtnniCSQLME--KYQKQTMIVTSHDISLL-RFFDDIIICGEEK 542
Cdd:cd03221 99 NHLDLES----IEALEEalKEYPGTVILVSHDRYFLdQVATKIIELEDGK 144
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
345-547 |
6.57e-18 |
|
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: 83.09 E-value: 6.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLL---YPLKGNIFIQGKnydDLAEKSIREHFAVAFQeHHIF-- 419
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQ---PRKPDQFQKCVAYVRQ-DDILlp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 420 NLSIRD------NFKMLYENiTDEEIYKSLENVYLLDFVN-QVGLDYIVGndgnkLSGGQKHRLQLAICLAKQKDIILLD 492
Cdd:cd03234 95 GLTVREtltytaILRLPRKS-SDAIRKKRVEDVLLRDLALtRIGGNLVKG-----ISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 493 EPTAGLDIKTTNNIC---SQLMEKyqKQTMIVTSHD--ISLLRFFDDIIICGEEKIIEQG 547
Cdd:cd03234 169 EPTSGLDSFTALNLVstlSQLARR--NRIVILTIHQprSDLFRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
349-552 |
8.69e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 84.11 E-value: 8.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGK----NYDDLAEKSIREHFAVAFQ--EHHIF-NL 421
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitpETGNKNLKKLRKKVSLVFQfpEAQLFeNT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 422 SIRD-NFKMLYENITDEEIYKSLenvylLDFVNQVGLDYIVGNDGN-KLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD 499
Cdd:PRK13641 103 VLKDvEFGPKNFGFSEDEAKEKA-----LKWLKKVGLSEDLISKSPfELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2674892663 500 IKTTNNICsQLMEKYQK--QTMIVTSH---DISllRFFDDIIICGEEKIIEQGNIKKL 552
Cdd:PRK13641 178 PEGRKEMM-QLFKDYQKagHTVILVTHnmdDVA--EYADDVLVLEHGKLIKHASPKEI 232
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
349-548 |
9.15e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 83.65 E-value: 9.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQE-HHIFNLSI---- 423
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNpDNQFVGSIvkyd 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 424 ----RDNFKMLYENITdEEIYKSLENVYLLDFVNqvgldyivgNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD 499
Cdd:PRK13648 105 vafgLENHAVPYDEMH-RRVSEALKQVDMLERAD---------YEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 500 IKTTNNICSQLME-KYQKQ-TMIVTSHDISLLRFFDDIIICGEEKIIEQGN 548
Cdd:PRK13648 175 PDARQNLLDLVRKvKSEHNiTIISITHDLSEAMEADHVIVMNKGTVYKEGT 225
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
342-552 |
1.09e-17 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 83.98 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGknYDDLAE-KSIREHFAVAFQEHHIF- 419
Cdd:TIGR01188 3 YG-DFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAG--YDVVREpRKVRRSIGIVPQYASVDe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 420 NLSIRDNFKM---LY---ENITDEEIYKSLENVYLLDFVNQVGLDYivgndgnklSGGQKHRLQLAICLAKQKDIILLDE 493
Cdd:TIGR01188 80 DLTGRENLEMmgrLYglpKDEAEERAEELLELFELGEAADRPVGTY---------SGGMRRRLDIAASLIHQPDVLFLDE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 494 PTAGLDIKTTNNICSQLME-KYQKQTMIVTSHDISLL-RFFDDIIICGEEKIIEQGNIKKL 552
Cdd:TIGR01188 151 PTTGLDPRTRRAIWDYIRAlKEEGVTILLTTHYMEEAdKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
335-499 |
1.50e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.00 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLA--YGYDKVLlKDINLSIKKGNktlIV---GTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnydDLAEKSI--RE 407
Cdd:COG1137 4 LEAENLVksYGKRTVV-KDVSLEVNQGE---IVgllGPNGAGKTTTFYMIVGLVKPDSGRIFLDGE---DITHLPMhkRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 408 HFAVAF--QEHHIF-NLSIRDNFKMLYE--NITDEEIYKSLENvyLLDfvnQVGLDYIVGNDGNKLSGGQKHRLQLAICL 482
Cdd:COG1137 77 RLGIGYlpQEASIFrKLTVEDNILAVLElrKLSKKEREERLEE--LLE---EFGITHLRKSKAYSLSGGERRRVEIARAL 151
|
170
....*....|....*..
gi 2674892663 483 AKQKDIILLDEPTAGLD 499
Cdd:COG1137 152 ATNPKFILLDEPFAGVD 168
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
349-525 |
1.57e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 85.93 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSI----REHFAVAFQEHHIF-NLSI 423
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLsHLTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 424 RDNFKMlyenitdEEIYKSLENVYLL----DFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD 499
Cdd:PRK10535 104 AQNVEV-------PAVYAGLERKQRLlraqELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALD 176
|
170 180
....*....|....*....|....*....
gi 2674892663 500 IKTTN---NICSQLMEkyQKQTMIVTSHD 525
Cdd:PRK10535 177 SHSGEevmAILHQLRD--RGHTVIIVTHD 203
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
334-564 |
1.66e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 83.60 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 334 QLLLKDLAYGYDKVL------LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAE----- 402
Cdd:PRK13651 2 QIKVKNIVKIFNKKLptelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKtkeke 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 403 -------------------KSIREHFAVAFQ--EHHIFNLSIRDN--FKMLYENITDEEIYKSLenvylLDFVNQVGLD- 458
Cdd:PRK13651 82 kvleklviqktrfkkikkiKEIRRRVGVVFQfaEYQLFEQTIEKDiiFGPVSMGVSKEEAKKRA-----AKYIELVGLDe 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 459 -YIVGNDGNkLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQK-QTMIVTSHDI-SLLRFFDDI 535
Cdd:PRK13651 157 sYLQRSPFE-LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLdNVLEWTKRT 235
|
250 260 270
....*....|....*....|....*....|.
gi 2674892663 536 IICGEEKIIEQGNIKKlLLREDSYL--NKLI 564
Cdd:PRK13651 236 IFFKDGKIIKDGDTYD-ILSDNKFLieNNME 265
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
351-557 |
2.68e-17 |
|
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: 83.62 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 351 DINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDlAEKSI-----REHFAVAFQEHHIF-NLSIR 424
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFD-SRKGIflppeKRRIGYVFQEARLFpHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 425 DNFKMLYENITDEEIYKSLENVYLLdfvnqVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTN 504
Cdd:TIGR02142 94 GNLRYGMKRARPSERRISFERVIEL-----LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2674892663 505 NICSQLmEKYQKQT---MIVTSHDIS-LLRFFDDIIICGEEKIIEQGNIKKLLLRED 557
Cdd:TIGR02142 169 EILPYL-ERLHAEFgipILYVSHSLQeVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
346-548 |
4.92e-17 |
|
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: 80.66 E-value: 4.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 346 KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLaEKSIREHFAVAF--QEHHIF-NLS 422
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL-PMHKRARLGIGYlpQEASIFrKLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 IRDNFKMLYENITDEEIYKSLENVYLLDfvnQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKT 502
Cdd:cd03218 92 VEENILAVLEIRGLSKKEREEKLEELLE---EFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2674892663 503 TNNIcsQLMEKYQKQTMI---VTSHDIS-LLRFFDDIIICGEEKIIEQGN 548
Cdd:cd03218 169 VQDI--QKIIKILKDRGIgvlITDHNVReTLSITDRAYIIYEGKVLAEGT 216
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
348-528 |
5.27e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 80.63 E-value: 5.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 348 LLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDL---AEKSIREH-FAVAFQEHHIF-NLS 422
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaAKAELRNQkLGFIYQFHHLLpDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 IRDNFKM--LYENITDEEIYKSLenvylLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDI 500
Cdd:PRK11629 104 ALENVAMplLIGKKKPAEINSRA-----LEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDA 178
|
170 180 190
....*....|....*....|....*....|
gi 2674892663 501 KTTNNICSQLMEKYQKQ--TMIVTSHDISL 528
Cdd:PRK11629 179 RNADSIFQLLGELNRLQgtAFLVVTHDLQL 208
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
342-553 |
6.24e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 80.78 E-value: 6.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGYDKVLlKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKN-------------YDDLAEKSIREH 408
Cdd:PRK10619 15 YGEHEVL-KGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqlkvADKNQLRLLRTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 409 FAVAFQEhhiFNLSirdNFKMLYENITDEEIY-----KSLENVYLLDFVNQVGLDYIV-GNDGNKLSGGQKHRLQLAICL 482
Cdd:PRK10619 94 LTMVFQH---FNLW---SHMTVLENVMEAPIQvlglsKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2674892663 483 AKQKDIILLDEPTAGLD---IKTTNNICSQLMEkyQKQTMIVTSHDISLLRFFDD-IIICGEEKIIEQGNIKKLL 553
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDpelVGEVLRIMQQLAE--EGKTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAPEQLF 240
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
349-533 |
7.55e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 80.70 E-value: 7.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNyddlAEKSIREHFAVAFQEHHIFNLSirdnFK 428
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP----TRQALQKNLVAYVPQSEEVDWS----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 429 MLYENIT-----------------DEEIY-KSLENVYLLDFVN-QVGldyivgndgnKLSGGQKHRLQLAICLAKQKDII 489
Cdd:PRK15056 95 VLVEDVVmmgryghmgwlrrakkrDRQIVtAALARVDMVEFRHrQIG----------ELSGGQKKRVFLARAIAQQGQVI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2674892663 490 LLDEPTAGLDIKTTNNICSQLME-KYQKQTMIVTSHDI-SLLRFFD 533
Cdd:PRK15056 165 LLDEPFTGVDVKTEARIISLLRElRDEGKTMLVSTHNLgSVTEFCD 210
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
345-564 |
8.72e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 80.18 E-value: 8.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDdlAEKSI----------REHFAVAFQ 414
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITID--TARSLsqqkglirqlRQHVGFVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 EhhiFNLsirdnF--KMLYENIT-----------DEEIYKSLEnvylldFVNQVGLDYIVGNDGNKLSGGQKHRLQLAIC 481
Cdd:PRK11264 93 N---FNL-----FphRTVLENIIegpvivkgepkEEATARARE------LLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 482 LAKQKDIILLDEPTAGLDIKTTNNICS---QLMEkyQKQTMIVTSHDISLLR-FFDDIIICGEEKIIEQGNIKKLLL--- 554
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNtirQLAQ--EKRTMVIVTHEMSFARdVADRAIFMDQGRIVEQGPAKALFAdpq 236
|
250
....*....|..
gi 2674892663 555 --REDSYLNKLI 564
Cdd:PRK11264 237 qpRTRQFLEKFL 248
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
320-533 |
9.22e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 83.32 E-value: 9.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 320 IKSENQEDKQSKDVQLLLKDlaygyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLM--------RLLYPLKGNI- 390
Cdd:COG4178 355 IETSEDGALALEDLTLRTPD-----GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAglwpygsgRIARPAGARVl 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 391 FIQGKNYddLAEKSIREhfAVAFQEHHifnlsirdnfkmlyENITDEEIYKSLENVYLLDFVNQvgLDyiVGND-GNKLS 469
Cdd:COG4178 430 FLPQRPY--LPLGTLRE--ALLYPATA--------------EAFSDAELREALEAVGLGHLAER--LD--EEADwDQVLS 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2674892663 470 GGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFD 533
Cdd:COG4178 488 LGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHD 551
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
213-552 |
9.44e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 84.26 E-value: 9.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 213 KNINHSIEQYQQYQQNLFKLKLKVNLCSEFIMGAYLVICLAIS--IYLVNTQDFNPIMAITIILTYQAVLEVLAMMPSLI 290
Cdd:PLN03232 499 KSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSfgVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLL 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 291 EHFDEASKRWQDLA-IFMQEKKFIANtnneiksenQEDKQSKDVQLLLKDLAYGYD----KVLLKDINLSIKKGNKTLIV 365
Cdd:PLN03232 579 SQVVNANVSLQRIEeLLLSEERILAQ---------NPPLQPGAPAISIKNGYFSWDsktsKPTLSDINLEIPVGSLVAIV 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 366 GTSGCGKSTLFYVLMRLLYPLKGNIFIqgknyddlaeksIREHFAVAFQEHHIFNLSIRDNfkMLYENITDEEIYKSLEN 445
Cdd:PLN03232 650 GGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVAYVPQVSWIFNATVREN--ILFGSDFESERYWRAID 715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 446 VYLLdfvnQVGLDYIVGND-------GNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLM-EKYQKQ 517
Cdd:PLN03232 716 VTAL----QHDLDLLPGRDlteigerGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMkDELKGK 791
|
330 340 350
....*....|....*....|....*....|....*
gi 2674892663 518 TMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKL 552
Cdd:PLN03232 792 TRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
341-525 |
1.03e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 82.00 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 341 AYGyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTlfyvLMRLLYPLK----GNIFIQGKNYDDL--AEKSIrehfAVAFQ 414
Cdd:PRK11000 12 AYG-DVVISKDINLDIHEGEFVVFVGPSGCGKST----LLRMIAGLEditsGDLFIGEKRMNDVppAERGV----GMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 EHHIF-NLSIRDN--FKMLYENITDEEIYKSlenvylldfVNQVG----LDYIVGNDGNKLSGGQKHRLQLAICLAKQKD 487
Cdd:PRK11000 83 SYALYpHLSVAENmsFGLKLAGAKKEEINQR---------VNQVAevlqLAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2674892663 488 IILLDEPTAGLD----IKTTNNIcSQLMEKYQKqTMIVTSHD 525
Cdd:PRK11000 154 VFLLDEPLSNLDaalrVQMRIEI-SRLHKRLGR-TMIYVTHD 193
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
334-525 |
1.49e-16 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 81.27 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 334 QLLLKDLAYGYDKVL-LKDINLSIKKGNKTLIVGTSGCGKSTlfyvLMRLLYPL----KGNIFIQGKNYDDLAEKsiREH 408
Cdd:COG3839 3 SLELENVSKSYGGVEaLKDIDLDIEDGEFLVLLGPSGCGKST----LLRMIAGLedptSGEILIGGRDVTDLPPK--DRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 409 FAVAFQEHHIF-NLSIRDN--FKMLYENITDEEIYKSLENV-------YLLD-FVNQvgldyivgndgnkLSGGQKHRLQ 477
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENiaFPLKLRKVPKAEIDRRVREAaellgleDLLDrKPKQ-------------LSGGQRQRVA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 478 LAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMeKYQKQ---TMI-VTsHD 525
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIK-RLHRRlgtTTIyVT-HD 193
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
337-526 |
1.53e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 79.36 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnydDLAEKSIRE---HFAVA 412
Cdd:COG4604 4 IKNVSKRYgGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGL---DVATTPSRElakRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 413 FQEHHI-FNLSIRDnfkmLYE---------NITDEE---IYKSLENVYLLDFVNQvgldYIvgndgNKLSGGQKHRLQLA 479
Cdd:COG4604 81 RQENHInSRLTVRE----LVAfgrfpyskgRLTAEDreiIDEAIAYLDLEDLADR----YL-----DELSGGQRQRAFIA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2674892663 480 ICLAKQKDIILLDEPTAGLDIKTtnniCSQLM-------EKYQKQTMIVTsHDI 526
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKH----SVQMMkllrrlaDELGKTVVIVL-HDI 196
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
342-524 |
1.70e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 79.50 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGYDKVLlKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLL-----YPLKGNIFIQGKN--YDDLAEKSIREHFAVAFQ 414
Cdd:PRK14267 14 YGSNHVI-KGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNiySPDVDPIEVRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 EHHIF-NLSIRDN--FKMLYENIT------DEEIYKSLENVYLLDFVNQVGLDYivgndGNKLSGGQKHRLQLAICLAKQ 485
Cdd:PRK14267 93 YPNPFpHLTIYDNvaIGVKLNGLVkskkelDERVEWALKKAALWDEVKDRLNDY-----PSNLSGGQRQRLVIARALAMK 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 2674892663 486 KDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSH 524
Cdd:PRK14267 168 PKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
345-555 |
1.74e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 79.34 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLM-RLLY-PLKGNIFIQGKNYDDL-AEKSIREHFAVAFQ---EhhI 418
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMgHPKYeVTSGSILLDGEDILELsPDERARAGIFLAFQypvE--I 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 419 FNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQVGLD------YIvgNDGnkLSGGQKHRLQLAICLAKQKDIILLD 492
Cdd:COG0396 90 PGVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDedfldrYV--NEG--FSGGEKKRNEILQMLLLEPKLAILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2674892663 493 EPTAGLDI---KTTNNICSQLMEKyqKQTMIVTSHDISLLRFF--DDIIICGEEKIIEQGNiKKLLLR 555
Cdd:COG0396 166 ETDSGLDIdalRIVAEGVNKLRSP--DRGILIITHYQRILDYIkpDFVHVLVDGRIVKSGG-KELALE 230
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
338-557 |
1.93e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 79.85 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 338 KDLAYGY--DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQ- 414
Cdd:PRK13652 7 RDLCYSYsgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQn 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 -EHHIFNLSIRDN--FKMLYENITDEEIYKSLENVylldfVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:PRK13652 87 pDDQIFSPTVEQDiaFGPINLGLDEETVAHRVSSA-----LHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 492 DEPTAGLDIKTTNNI---CSQLMEKYqKQTMIVTSHDISLL-RFFDDIIICGEEKIIEQGNIKKLLLRED 557
Cdd:PRK13652 162 DEPTAGLDPQGVKELidfLNDLPETY-GMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
335-498 |
1.99e-16 |
|
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: 78.87 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYDKVL-LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDL-AEKSIREHFAVA 412
Cdd:COG0410 4 LEVENLHAGYGGIHvLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLpPHRIARLGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 413 FQEHHIF-NLSIRDNFKM-LYENITDEEIYKSLENVY-----LLDFVNQvgldyivgnDGNKLSGGQkhRLQLAIC--LA 483
Cdd:COG0410 84 PEGRRIFpSLTVEENLLLgAYARRDRAEVRADLERVYelfprLKERRRQ---------RAGTLSGGE--QQMLAIGraLM 152
|
170
....*....|....*
gi 2674892663 484 KQKDIILLDEPTAGL 498
Cdd:COG0410 153 SRPKLLLLDEPSLGL 167
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
337-553 |
2.36e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 79.65 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY--DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAE-KSIREHFAVAF 413
Cdd:PRK13644 4 LENVSYSYpdGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGIVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 Q--EHHIFNLSIRDNFKMLYENIT--DEEIYKSLENVylldfVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDII 489
Cdd:PRK13644 84 QnpETQFVGRTVEEDLAFGPENLClpPIEIRKRVDRA-----LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2674892663 490 LLDEPTAGLDIKTTNNICSQLMEKYQK-QTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLL 553
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
317-565 |
2.43e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 83.15 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 317 NNEIKSENQEDKQSKdvqLLLKDLAYGY----DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLlYPLK----- 387
Cdd:PTZ00265 1151 NGGIRIKNKNDIKGK---IEIMDVNFRYisrpNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRF-YDLKndhhi 1226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 388 --------------------------------------------------GNIFIQGKNYDDLAEKSIREHFAVAFQEHH 417
Cdd:PTZ00265 1227 vfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPM 1306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 418 IFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:PTZ00265 1307 LFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLpnKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEAT 1386
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2674892663 496 AGLDIKTTNNICSQLMEKYQK--QTMIVTSHDISLLRFFDDIIICGEEK-----IIEQGNIKKLLLREDSYLNKLIR 565
Cdd:PTZ00265 1387 SSLDSNSEKLIEKTIVDIKDKadKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLSVQDGVYKKYVK 1463
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
345-526 |
2.49e-16 |
|
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: 78.53 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNI----FIQGKNYDDLAEKsirehFAVAF--QEHHI 418
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrvagLVPWKRRKKFLRR-----IGVVFgqKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 419 FNLSIRDNFKMLYE--NITDEEIYKSLEN-VYLLDfvnqvgLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:cd03267 108 WDLPVIDSFYLLAAiyDLPPARFKKRLDElSELLD------LEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190
....*....|....*....|....*....|...
gi 2674892663 496 AGLDIKTTNNICSQLME--KYQKQTMIVTSHDI 526
Cdd:cd03267 182 IGLDVVAQENIRNFLKEynRERGTTVLLTSHYM 214
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
328-525 |
3.78e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 78.55 E-value: 3.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 328 KQSKDVQLLLKDLAYGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLL------YPLKGNIFIQGKNYDDLA 401
Cdd:PRK14246 5 KSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskIKVDGKVLYFGKDIFQID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 402 EKSIREHFAVAFQEHHIF-NLSIRDN--FKMLYENITDE-EIYKSLEnvyllDFVNQVGLDYIV----GNDGNKLSGGQK 473
Cdd:PRK14246 85 AIKLRKEVGMVFQQPNPFpHLSIYDNiaYPLKSHGIKEKrEIKKIVE-----ECLRKVGLWKEVydrlNSPASQLSGGQQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 474 HRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHD 525
Cdd:PRK14246 160 QRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHN 211
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
338-552 |
4.70e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 78.59 E-value: 4.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 338 KDLAYGY-------DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIqgKNYDDLAEKS---IRE 407
Cdd:PRK13633 8 KNVSYKYesneestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYV--DGLDTSDEENlwdIRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 408 HFAVAFQ--EHHIFNLSIRDNFKMLYEN--ITDEEIYKSLENVylldfVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLA 483
Cdd:PRK13633 86 KAGMVFQnpDNQIVATIVEEDVAFGPENlgIPPEEIRERVDES-----LKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 484 KQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQ--TMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKL 552
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
335-547 |
6.45e-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: 76.85 E-value: 6.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYDK-VLLKDINLSIKKGNKTLiVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGknYDDLAEKS-IREHFAVA 412
Cdd:cd03264 1 LQLENLTKRYGKkRALDGVSLTLGPGMYGL-LGPNGAGKTTLMRILATLTPPSSGTIRIDG--QDVLKQPQkLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 413 FQEHHIF-NLSIRD--NFKMLYENITD----EEIYKSLENVYLLDFVNqvglDYIvgndgNKLSGGQKHRLQLAICLAKQ 485
Cdd:cd03264 78 PQEFGVYpNFTVREflDYIAWLKGIPSkevkARVDEVLELVNLGDRAK----KKI-----GSLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 486 KDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFF-DDIIICGEEKIIEQG 547
Cdd:cd03264 149 PSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
338-552 |
6.55e-16 |
|
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: 77.02 E-value: 6.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 338 KDLAYGYDKVL-LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGknYDDLAE-KSIREHFAVAFQE 415
Cdd:cd03265 4 ENLVKKYGDFEaVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG--HDVVREpREVRRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 HHIFN-LSIRDNFKM---LY---ENITDEEIYKSLENVYLLDFVnqvglDYIVGNdgnkLSGGQKHRLQLAICLAKQKDI 488
Cdd:cd03265 82 LSVDDeLTGWENLYIharLYgvpGAERRERIDELLDFVGLLEAA-----DRLVKT----YSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2674892663 489 ILLDEPTAGLDIKTTNNICSQL--MEKYQKQTMIVTSHDISLL-RFFDDIIICGEEKIIEQGNIKKL 552
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIekLKEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
343-538 |
1.01e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 75.73 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 343 GYD-KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIfiqgknyddlaekSIREHFAVAFQEHHI--- 418
Cdd:NF040873 1 GYGgRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-------------RRAGGARVAYVPQRSevp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 419 --FNLSIRDNFKM-------LYENITDE---EIYKSLENVYLLDFVN-QVGldyivgndgnKLSGGQKHRLQLAICLAKQ 485
Cdd:NF040873 68 dsLPLTVRDLVAMgrwarrgLWRRLTRDdraAVDDALERVGLADLAGrQLG----------ELSGGQRQRALLAQGLAQE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2674892663 486 KDIILLDEPTAGLDIKTTNNIcSQLM--EKYQKQTMIVTSHDISLLRFFDDIIIC 538
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERI-IALLaeEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
345-547 |
1.08e-15 |
|
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: 76.17 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAeksiREHFAVAFQEHHIF-NLSI 423
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYpKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 424 RDNFKMLYE--NITDEEIYKS----LENVYLLDFVNQVgLDyivgndgnKLSGGQKHRLQLAICLAKQKDIILLDEPTAG 497
Cdd:cd03269 88 IDQLVYLAQlkGLKKEEARRRidewLERLELSEYANKR-VE--------ELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 498 LDIKTTNNICSQLME-KYQKQTMIVTSHDISLL-RFFDDIIICGEEKIIEQG 547
Cdd:cd03269 159 LDPVNVELLKDVIRElARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
346-547 |
1.16e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 77.12 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 346 KVLLKDINLSIKKGNKTLIVGTSGCGKSTLfyvlMRLL----YPLKGNIFIQGKnydDLAEKSIRE---HFAVAFQEHHI 418
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTL----LRALsgelSPDSGEVRLNGR---PLADWSPAElarRRAVLPQHSSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 419 -FNLSIRDNFKM-LY----ENITDEEIykslenvyLLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLA------KQK 486
Cdd:PRK13548 88 sFPFTVEEVVAMgRAphglSRAEDDAL--------VAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2674892663 487 DIILLDEPTAGLDIK---TTNNICSQLMEKyQKQTMIVTSHDISL-LRFFDDIIICGEEKIIEQG 547
Cdd:PRK13548 160 RWLLLDEPTSALDLAhqhHVLRLARQLAHE-RGLAVIVVLHDLNLaARYADRIVLLHQGRLVADG 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
345-524 |
1.30e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 79.85 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLM----------RLLY-----PLKGNIFIQGK-------------- 395
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRgmdqyeptsgRIIYhvalcEKCGYVERPSKvgepcpvcggtlep 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 396 ------NYDDLAEKSIREHFAVAFQEhhIFNLSIRDNfkmLYENITD--EEI-YKSLENVYL-LDFVNQVGLDYIVGNDG 465
Cdd:TIGR03269 92 eevdfwNLSDKLRRRIRKRIAIMLQR--TFALYGDDT---VLDNVLEalEEIgYEGKEAVGRaVDLIEMVQLSHRITHIA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 466 NKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLME--KYQKQTMIVTSH 524
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSH 227
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
346-543 |
1.43e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 80.59 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 346 KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIfiqgknyddLAEKSIrehfAVAFQEHHIFNLSIRD 425
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV---------WAERSI----AYVPQQAWIMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 426 NFKMLyenitDEEIYKSLENVY----LLDFVNQV--GLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD 499
Cdd:PTZ00243 740 NILFF-----DEEDAARLADAVrvsqLEADLAQLggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2674892663 500 IKTTNNICSQ-LMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKI 543
Cdd:PTZ00243 815 AHVGERVVEEcFLGALAGKTRVLATHQVHVVPRADYVVALGDGRV 859
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
345-553 |
1.64e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 76.28 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLA--EKSIREHFAVAFQEHHIF-NL 421
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKvdERLIRQEAGMVFQQFYLFpHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 422 SIRDNfkMLYENITDEEIYKSLENVYLLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD-- 499
Cdd:PRK09493 93 TALEN--VMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDpe 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 500 -----IKTTNNICSQLMekyqkqTMIVTSHDI-------SLLRFFDdiiiCGeeKIIEQGNIKKLL 553
Cdd:PRK09493 171 lrhevLKVMQDLAEEGM------TMVIVTHEIgfaekvaSRLIFID----KG--RIAEDGDPQVLI 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
331-525 |
1.88e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 75.21 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 331 KDVQLLLKDlaygydKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYP---LKGNIFIQGKNYDDL-AEksiR 406
Cdd:COG4136 5 ENLTITLGG------RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALpAE---Q 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 407 EHFAVAFQEHHIF-NLSIRDNFKM-LYENITDEE----IYKSLEnvylldfvnQVGLDYIVGNDGNKLSGGQKHRLQLAI 480
Cdd:COG4136 76 RRIGILFQDDLLFpHLSVGENLAFaLPPTIGRAQrrarVEQALE---------EAGLAGFADRDPATLSGGQRARVALLR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2674892663 481 CLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQ---TMIVTsHD 525
Cdd:COG4136 147 ALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRgipALLVT-HD 193
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
347-530 |
1.95e-15 |
|
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: 75.93 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 347 VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSI----REHFAVAFQehhifnls 422
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlrARHVGFVFQ-------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 irdNFkMLYENITdeeiykSLENVYL--------------LDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDI 488
Cdd:COG4181 98 ---SF-QLLPTLT------ALENVMLplelagrrdararaRALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAI 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2674892663 489 ILLDEPTAGLDIKTTNNICSQLMEKYQKQ--TMIVTSHDISLLR 530
Cdd:COG4181 168 LFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALAA 211
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
345-557 |
2.23e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 76.34 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEK---SIREHFAVAFQEHHIF-N 420
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSrlyTVRKRMSMLFQSGALFtD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 LSIRDN--FKMLYENITDEEIYKSLENVYLldfvNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGL 498
Cdd:PRK11831 99 MNVFDNvaYPLREHTQLPAPLLHSTVMMKL----EAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQ 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 499 DiKTTNNICSQLMEKYQKQ---TMIVTSHDI-SLLRFFDDIIICGEEKIIEQGNIKKLLLRED 557
Cdd:PRK11831 175 D-PITMGVLVKLISELNSAlgvTCVVVSHDVpEVLSIADHAYIVADKKIVAHGSAQALQANPD 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
349-547 |
2.46e-15 |
|
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: 78.96 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGnKTL-IVGTSGCGKSTLFYVLMRLLyPLKGNIFIQGKNYDDLAEK---SIREHFAVAFQE--------- 415
Cdd:COG4172 302 VDGVSLTLRRG-ETLgLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRalrPLRRRMQVVFQDpfgslsprm 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 ------------HHIfNLSIRDnfkmlyeniTDEEIYKSLEnvylldfvnQVGLDyivGNDGNK----LSGGQKHRLQLA 479
Cdd:COG4172 380 tvgqiiaeglrvHGP-GLSAAE---------RRARVAEALE---------EVGLD---PAARHRypheFSGGQRQRIAIA 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 480 ICLAKQKDIILLDEPTAGLDIKTTNNICsQLMEKYQKQ---TMIVTSHDISLLRFF-DDIIICGEEKIIEQG 547
Cdd:COG4172 438 RALILEPKLLVLDEPTSALDVSVQAQIL-DLLRDLQREhglAYLFISHDLAVVRALaHRVMVMKDGKVVEQG 508
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
349-524 |
2.75e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 76.32 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFI-------QGKNYDDlaeKSIREHFAVAFQ--EHHIF 419
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVddtlitsTSKNKDI---KQIRKKVGLVFQfpESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 420 NLSIRDNFKMLYEN--ITDEEIYK-SLENVYLldfvnqVGLDY-IVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:PRK13649 100 EETVLKDVAFGPQNfgVSQEEAEAlAREKLAL------VGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190
....*....|....*....|....*....|....
gi 2674892663 496 AGLDIKTTNnicsQLMEKYQK-----QTMIVTSH 524
Cdd:PRK13649 174 AGLDPKGRK----ELMTLFKKlhqsgMTIVLVTH 203
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
330-547 |
4.04e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 76.43 E-value: 4.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 330 SKDVQLLLKDLAYGYDK------VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQ----GKNYDD 399
Cdd:PRK13631 17 SDDIILRVKNLYCVFDEkqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 400 LAE------------KSIREHFAVAFQ--EHHIFNLSIRDN--FKMLYENITDEEIYKsLENVYLldfvNQVGLDY-IVG 462
Cdd:PRK13631 97 HELitnpyskkiknfKELRRRVSMVFQfpEYQLFKDTIEKDimFGPVALGVKKSEAKK-LAKFYL----NKMGLDDsYLE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 463 NDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLME-KYQKQTMIVTSHDI-SLLRFFDDIIICGE 540
Cdd:PRK13631 172 RSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDaKANNKTVFVITHTMeHVLEVADEVIVMDK 251
|
....*..
gi 2674892663 541 EKIIEQG 547
Cdd:PRK13631 252 GKILKTG 258
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
4-493 |
4.89e-15 |
|
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: 77.92 E-value: 4.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 4 ILSNMIRPVVWSLLLAILVGTISTLSSISLMGL-SAWLIASAALQPPLYVLSLAIVGVRFcgVMRAVFRYLERYFTHKVG 82
Cdd:COG4615 3 LLRLLLRESRWLLLLALLLGLLSGLANAGLIALiNQALNATGAALARLLLLFAGLLVLLL--LSRLASQLLLTRLGQHAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 83 FSLftsfRVFVLIKIIKAlPFKQQTENGDA--FDLIVNAVDNLRDSFlrFFLPPIITTISVFILSiwfFLYsydLMILli 160
Cdd:COG4615 81 ARL----RLRLSRRILAA-PLERLERIGAArlLAALTEDVRTISQAF--VRLPELLQSVALVLGC---LAY---LAWL-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 161 sSWLIFMIVIPYMI------WRRYLKLKKHKFLLTQEIIEFY-------EGNRELSFyNYDK---YRLKNINHSIEQYQQ 224
Cdd:COG4615 146 -SPPLFLLTLVLLGlgvagyRLLVRRARRHLRRAREAEDRLFkhfrallEGFKELKL-NRRRrraFFDEDLQPTAERYRD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 225 YQQNLFKLKLKVNLCSEFIMgaYLVICLAISIYLVNTQDFNPIMA-ITIILTY--QAVLEVLAMMPSLIEhFDEASKRWQ 301
Cdd:COG4615 224 LRIRADTIFALANNWGNLLF--FALIGLILFLLPALGWADPAVLSgFVLVLLFlrGPLSQLVGALPTLSR-ANVALRKIE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 302 DLaifmqEKKFiaNTNNEIKSENQEDKQSKDVQLL-LKDLAYGYDKVL------LKDINLSIKKGNKTLIVGTSGCGKST 374
Cdd:COG4615 301 EL-----ELAL--AAAEPAAADAAAPPAPADFQTLeLRGVTYRYPGEDgdegftLGPIDLTIRRGELVFIVGGNGSGKST 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 375 LFYVLMRLLYPLKGNIFIQGK-----NYDDLaeksiREHFAVAFQEHHIFnlsirDNFKMLYENITDEEIYKSLEnvyll 449
Cdd:COG4615 374 LAKLLTGLYRPESGEILLDGQpvtadNREAY-----RQLFSAVFSDFHLF-----DRLLGLDGEADPARARELLE----- 438
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2674892663 450 dfvnQVGLDYIVGNDGNK-----LSGGQKHRLQLAICLAKQKDIILLDE 493
Cdd:COG4615 439 ----RLELDHKVSVEDGRfsttdLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
349-506 |
5.84e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 76.38 E-value: 5.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIRE---HFAVAFQehHiFNL-SIR 424
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKarrQIGMIFQ--H-FNLlSSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 425 ---DN--FKMLYENITDEEIYKSLENvyLLDFVnqvGL----DYIVGNdgnkLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:PRK11153 98 tvfDNvaLPLELAGTPKAEIKARVTE--LLELV---GLsdkaDRYPAQ----LSGGQKQRVAIARALASNPKVLLCDEAT 168
|
170
....*....|.
gi 2674892663 496 AGLDIKTTNNI 506
Cdd:PRK11153 169 SALDPATTRSI 179
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
345-524 |
6.92e-15 |
|
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: 73.33 E-value: 6.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLM-RLLY-PLKGNIFIQGKnydDLAEKSIREHFA----VAFQEhhi 418
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMgHPKYeVTEGEILFKGE---DITDLPPEERARlgifLAFQY--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 419 fnlsirdnfkmlyenitDEEIykslENVYLLDFVNQVgldyivgNDGnkLSGGQKHRLQLAICLAKQKDIILLDEPTAGL 498
Cdd:cd03217 86 -----------------PPEI----PGVKNADFLRYV-------NEG--FSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180
....*....|....*....|....*..
gi 2674892663 499 DIKTTNNICSQLME-KYQKQTMIVTSH 524
Cdd:cd03217 136 DIDALRLVAEVINKlREEGKSVLIITH 162
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
337-561 |
7.01e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 75.15 E-value: 7.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGYD----KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGknyDDLAEKS---IREHF 409
Cdd:PRK13650 7 VKNLTFKYKedqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEENvwdIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 410 AVAFQ--EHHIFNLSIRDNFKMLYEN--ITDEEIYK----SLENVYLLDFVNQvgldyivgnDGNKLSGGQKHRLQLAIC 481
Cdd:PRK13650 84 GMVFQnpDNQFVGATVEDDVAFGLENkgIPHEEMKErvneALELVGMQDFKER---------EPARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 482 LAKQKDIILLDEPTAGLD-------IKTTNNIcsqlMEKYQkQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLL 554
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDpegrlelIKTIKGI----RDDYQ-MTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
....*..
gi 2674892663 555 REDSYLN 561
Cdd:PRK13650 230 RGNDLLQ 236
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
345-502 |
7.23e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 73.75 E-value: 7.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLaekSIREhfAVAFQEHHIF---NL 421
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDP---DVAE--ACHYLGHRNAmkpAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 422 SIRDN--FKMLYENITDEEIYKSLEnvylldfvnQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD 499
Cdd:PRK13539 89 TVAENleFWAAFLGGEELDIAAALE---------AVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
...
gi 2674892663 500 IKT 502
Cdd:PRK13539 160 AAA 162
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
348-549 |
7.62e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 75.95 E-value: 7.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 348 LLKDINLSIKKGNKTLIVGTSGCGKSTLfyvlMR----LLYPLKGNIFIQGKNYDdlAEKSIRE-HFAVAFQEHHIF-NL 421
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTL----LRiiagLETPDSGRIVLNGRDLF--TNLPPRErRVGFVFQHYALFpHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 422 SIRDN--FKMLYENITDEEIYKSLENvyLLDFVNQVGLD--YIvgndgNKLSGGQKHRLQLAICLAKQKDIILLDEPTAG 497
Cdd:COG1118 91 TVAENiaFGLRVRPPSKAEIRARVEE--LLELVQLEGLAdrYP-----SQLSGGQRQRVALARALAVEPEVLLLDEPFGA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 498 LDIKTTNNICSQLME---KYQKQTMIVTsHDISL-LRFFDDIIicgeekIIEQGNI 549
Cdd:COG1118 164 LDAKVRKELRRWLRRlhdELGGTTVFVT-HDQEEaLELADRVV------VMNQGRI 212
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
346-526 |
1.16e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 74.35 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 346 KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEK---------------------S 404
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYkrakyigrvfqdpmmgtapsmT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 405 IREHFAVAFQEHHIFNLSIRDNFKmlyenitDEEIYKS--------LENvyLLDfvNQVGLdyivgndgnkLSGGQKHRL 476
Cdd:COG1101 99 IEENLALAYRRGKRRGLRRGLTKK-------RRELFREllatlglgLEN--RLD--TKVGL----------LSGGQRQAL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 477 QLAICLAKQKDIILLDEPTAGLDIKTTNNI---CSQLMEKYQKQTMIVTsHDI 526
Cdd:COG1101 158 SLLMATLTKPKLLLLDEHTAALDPKTAALVlelTEKIVEENNLTTLMVT-HNM 209
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
349-530 |
1.36e-14 |
|
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: 73.92 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEksirehFAVA-------FQEHHIF-N 420
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP------HRIArlgiartFQNPRLFpE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 LSIRDNFKMLYENITDEEIYKSLENV---------------YLLDFVnqvGL----DYIVGNdgnkLSGGQKHRLQLAIC 481
Cdd:COG0411 94 LTVLENVLVAAHARLGRGLLAALLRLprarreereareraeELLERV---GLadraDEPAGN----LSYGQQRRLEIARA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 482 LAKQKDIILLDEPTAGLDIKTTNNICSQLME--KYQKQTMIVTSHDISLLR 530
Cdd:COG0411 167 LATEPKLLLLDEPAAGLNPEETEELAELIRRlrDERGITILLIEHDMDLVM 217
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
337-547 |
1.67e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 75.65 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQE 415
Cdd:PRK09536 6 VSDLSVEFgDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 HHI-FNLSIRDNFKM---------LYENITDEEIYKSLenvylldfVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQ 485
Cdd:PRK09536 86 TSLsFEFDVRQVVEMgrtphrsrfDTWTETDRAAVERA--------MERTGVAQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 486 KDIILLDEPTAGLDIK---TTNNICSQLMEkyQKQTMIVTSHDISL-LRFFDDIIICGEEKIIEQG 547
Cdd:PRK09536 158 TPVLLLDEPTASLDINhqvRTLELVRRLVD--DGKTAVAAIHDLDLaARYCDELVLLADGRVRAAG 221
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
348-547 |
1.84e-14 |
|
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: 72.30 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 348 LLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLL---YPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIR 424
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTegnVSVEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 425 DnfkmlyenitdeeiykslenvyLLDFVNQV-GLDYIVGndgnkLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTT 503
Cdd:cd03233 102 E----------------------TLDFALRCkGNEFVRG-----ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2674892663 504 NNI--CSQLMEKYQKQTMIVT----SHDISLLrfFDDIIICGEEKIIEQG 547
Cdd:cd03233 155 LEIlkCIRTMADVLKTTTFVSlyqaSDEIYDL--FDKVLVLYEGRQIYYG 202
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
351-547 |
2.00e-14 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 74.38 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 351 DINLSIKKGnKTL-IVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIRE---HFAVAFQE-HHIFN--LSI 423
Cdd:COG4608 36 GVSFDIRRG-ETLgLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQMVFQDpYASLNprMTV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 424 RD-------NFKMLYENITDEEIYKSLEnvylldfvnQVGLDyivGNDGNK----LSGGQKHRLQLAICLAKQKDIILLD 492
Cdd:COG4608 115 GDiiaeplrIHGLASKAERRERVAELLE---------LVGLR---PEHADRypheFSGGQRQRIGIARALALNPKLIVCD 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2674892663 493 EPTAGLDIkttnNICSQ---LMEKYQKQ---TMIVTSHDISLLRFF-DDIII--CGeeKIIEQG 547
Cdd:COG4608 183 EPVSALDV----SIQAQvlnLLEDLQDElglTYLFISHDLSVVRHIsDRVAVmyLG--KIVEIA 240
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
337-553 |
2.87e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 73.15 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGYD-KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLlYPLKGNIFIQGKNY---DDLAEKSI-----RE 407
Cdd:PRK14258 10 VNNLSFYYDtQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGRVEffnQNIYERRVnlnrlRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 408 HFAVAFQEHHIFNLSIRDNFKMLYENI-------TDEEIYKSLENVYLLDFVNQVgldyiVGNDGNKLSGGQKHRLQLAI 480
Cdd:PRK14258 89 QVSMVHPKPNLFPMSVYDNVAYGVKIVgwrpkleIDDIVESALKDADLWDEIKHK-----IHKSALDLSGGQQQRLCIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 481 CLAKQKDIILLDEPTAGLDIKTTNNICS--QLMEKYQKQTMIVTSHD---ISLLRFFDDIIICGEEKI---IEQGNIKKL 552
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESliQSLRLRSELTMVIVSHNlhqVSRLSDFTAFFKGNENRIgqlVEFGLTKKI 243
|
.
gi 2674892663 553 L 553
Cdd:PRK14258 244 F 244
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
329-549 |
3.15e-14 |
|
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: 72.18 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 329 QSKDVQLLLKDLAYGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAeksireh 408
Cdd:cd03220 18 SSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 409 FAVAFQEhhifNLSIRDN--FKMLYENITDEEIYKSLENVY----LLDFvnqvgLDYIVGNdgnkLSGGQKHRLQLAICL 482
Cdd:cd03220 91 LGGGFNP----ELTGRENiyLNGRLLGLSRKEIDEKIDEIIefseLGDF-----IDLPVKT----YSSGMKARLAFAIAT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2674892663 483 AKQKDIILLDEPTAGLDIKTTNNiCSQLMEKYQKQ--TMIVTSHDISLLRFFDDIIIcgeekIIEQGNI 549
Cdd:cd03220 158 ALEPDILLIDEVLAVGDAAFQEK-CQRRLRELLKQgkTVILVSHDPSSIKRLCDRAL-----VLEKGKI 220
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
349-549 |
3.46e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 73.23 E-value: 3.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAE----KSIREHFAVAFQ--EHHIFNLS 422
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqkeiKPVRKKVGVVFQfpESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 IRDNFKMLYEN--ITDEEIYKslenvYLLDFVNQVGLDYIVGNDGN-KLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD 499
Cdd:PRK13643 102 VLKDVAFGPQNfgIPKEKAEK-----IAAEKLEMVGLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 500 IKTTNNICSQLMEKYQK-QTMIVTSHDISLLRFFDDIIIcgeekIIEQGNI 549
Cdd:PRK13643 177 PKARIEMMQLFESIHQSgQTVVLVTHLMDDVADYADYVY-----LLEKGHI 222
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
347-564 |
3.85e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 75.97 E-value: 3.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 347 VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRDN 426
Cdd:PTZ00243 1324 LVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQN 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 427 FKMLYEnITDEEIYKSLENVYLLDFV--NQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQ-KDIILLDEPTAGLDIKTT 503
Cdd:PTZ00243 1404 VDPFLE-ASSAEVWAALELVGLRERVasESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKgSGFILMDEATANIDPALD 1482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 504 NNICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLLLREDSYLNKLI 564
Cdd:PTZ00243 1483 RQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMV 1543
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
335-525 |
4.40e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 74.10 E-value: 4.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYD-KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnydDLAE-KSIREHFAVA 412
Cdd:PRK11607 20 LEIRNLTKSFDgQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV---DLSHvPPYQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 413 FQEHHIF-NLSIRDN--FKMLYENITDEEIYKSLENVYLLdfvnqVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDII 489
Cdd:PRK11607 97 FQSYALFpHMTVEQNiaFGLKQDKLPKAEIASRVNEMLGL-----VHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 2674892663 490 LLDEPTAGLDIKTTNNICSQLMEKYQK--QTMIVTSHD 525
Cdd:PRK11607 172 LLDEPMGALDKKLRDRMQLEVVDILERvgVTCVMVTHD 209
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
352-551 |
4.97e-14 |
|
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: 74.84 E-value: 4.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 352 INLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQ-GKNYDDLAEKSI------REHFAVAFQEHHIF-NLSI 423
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPdgrgraKRYIGILHQEYDLYpHRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 424 RDNfkmLYENITDE---EIYKsLENVYLLdfvNQVGLD-----YIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:TIGR03269 383 LDN---LTEAIGLElpdELAR-MKAVITL---KMVGFDeekaeEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPT 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2674892663 496 AGLDIKTTNNICSQLMEKYQK--QTMIVTSHDISLLRffddiIICGEEKIIEQGNIKK 551
Cdd:TIGR03269 456 GTMDPITKVDVTHSILKAREEmeQTFIIVSHDMDFVL-----DVCDRAALMRDGKIVK 508
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
321-525 |
5.59e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.83 E-value: 5.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 321 KSENQEDKQSKDVQLLLKDLAYGYD-KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDD 399
Cdd:PRK09452 1 SKKLNKQPSSLSPLVELRGISKSFDgKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 400 L-AEKsirEHFAVAFQEHHIF-NLSIRDN--FKMLYENITDEEIYK----SLENVYLLDFVNQVGLDyivgndgnkLSGG 471
Cdd:PRK09452 81 VpAEN---RHVNTVFQSYALFpHMTVFENvaFGLRMQKTPAAEITPrvmeALRMVQLEEFAQRKPHQ---------LSGG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2674892663 472 QKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLmEKYQKQ---TMIVTSHD 525
Cdd:PRK09452 149 QQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNEL-KALQRKlgiTFVFVTHD 204
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
319-540 |
6.52e-14 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 75.33 E-value: 6.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 319 EIKSENQEDKQSK-DVQLLLKDLAYgYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKny 397
Cdd:TIGR01271 412 KIKQNNKARKQPNgDDGLFFSNFSL-YVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-- 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 398 ddlaeksirehFAVAFQEHHIFNLSIRDN--FKMLYenitDEEIYKSLENVYLLD-----FVNQvglDYIV-GNDGNKLS 469
Cdd:TIGR01271 489 -----------ISFSPQTSWIMPGTIKDNiiFGLSY----DEYRYTSVIKACQLEedialFPEK---DKTVlGEGGITLS 550
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 470 GGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEK-YQKQTMIVTSHDISLLRFFDDIIICGE 540
Cdd:TIGR01271 551 GGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKlMSNKTRILVTSKLEHLKKADKILLLHE 622
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
341-529 |
9.22e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 70.67 E-value: 9.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 341 AYGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSI---REHFAVAFQEHH 417
Cdd:PRK10908 10 AYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpflRRQIGMIFQDHH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 418 IF-NLSIRDNFKM--LYENITDEEIYK----SLENVYLLDFVNQVGLdyivgndgnKLSGGQKHRLQLAICLAKQKDIIL 490
Cdd:PRK10908 90 LLmDRTVYDNVAIplIIAGASGDDIRRrvsaALDKVGLLDKAKNFPI---------QLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2674892663 491 LDEPTAGLDIKTTNNICsQLMEKYQK--QTMIVTSHDISLL 529
Cdd:PRK10908 161 ADEPTGNLDDALSEGIL-RLFEEFNRvgVTVLMATHDIGLI 200
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
319-569 |
1.19e-13 |
|
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: 71.43 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 319 EIKSENQEDK-QSKDVQLLLKDLAYgYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKny 397
Cdd:cd03291 23 KAKQENNDRKhSSDDNNLFFSNLCL-VGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 398 ddlaeksirehFAVAFQEHHIFNLSIRDN--FKMLYenitDEEIYKSLENVYLL--DFVNQVGLDYIV-GNDGNKLSGGQ 472
Cdd:cd03291 100 -----------ISFSSQFSWIMPGTIKENiiFGVSY----DEYRYKSVVKACQLeeDITKFPEKDNTVlGEGGITLSGGQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 473 KHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQ-KQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKK 551
Cdd:cd03291 165 RARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMaNKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSE 244
|
250
....*....|....*...
gi 2674892663 552 LLLREDSYLNKLIRYKNF 569
Cdd:cd03291 245 LQSLRPDFSSKLMGYDTF 262
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
355-537 |
1.64e-13 |
|
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: 70.51 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 355 SIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNyddlaeksirehfaVAFQEHHI---FNLSIRDnfkMLY 431
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT--------------VSYKPQYIkadYEGTVRD---LLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 432 ENITDeeiyKSLENVYLLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKT---TNNICS 508
Cdd:cd03237 84 SITKD----FYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQrlmASKVIR 159
|
170 180
....*....|....*....|....*....
gi 2674892663 509 QLMEKYQKqTMIVTSHDISLLRFFDDIII 537
Cdd:cd03237 160 RFAENNEK-TAFVVEHDIIMIDYLADRLI 187
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
335-549 |
1.76e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 70.31 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYD-KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLA-EKSIREHFAVA 412
Cdd:PRK10895 4 LTAKNLAKAYKgRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 413 FQEHHIFN-LSIRDNFKMLYEniTDEEIYKSLENVYLLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:PRK10895 84 PQEASIFRrLSVYDNLMAVLQ--IRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 492 DEPTAGLDIKTTNNIcSQLMEKYQKQTM--IVTSHDISllrffDDIIICGEEKIIEQGNI 549
Cdd:PRK10895 162 DEPFAGVDPISVIDI-KRIIEHLRDSGLgvLITDHNVR-----ETLAVCERAYIVSQGHL 215
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
335-549 |
2.30e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 70.09 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIfIQGKNydDLAEksIREHFAVAF 413
Cdd:PRK11247 13 LLLNAVSKRYgERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTA--PLAE--AREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 QEHH-------IFN--LSIRDNFKmlyenitdEEIYKSLENVYLLDFVNqvglDYIVGndgnkLSGGQKHRLQLAICLAK 484
Cdd:PRK11247 88 QDARllpwkkvIDNvgLGLKGQWR--------DAALQALAAVGLADRAN----EWPAA-----LSGGQKQRVALARALIH 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2674892663 485 QKDIILLDEPTAGLDIKTTNNIcSQLMEKYQKQ---TMIVTSHDISLLRFFDDIIIcgeekIIEQGNI 549
Cdd:PRK11247 151 RPGLLLLDEPLGALDALTRIEM-QDLIESLWQQhgfTVLLVTHDVSEAVAMADRVL-----LIEEGKI 212
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
346-545 |
2.92e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 70.10 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 346 KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDL---AEKSIREHFAVAFQE------- 415
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDsisavnp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 HHIFNLSIRDNFKMLYENITDEEIYKSLEnvyLLDfvnQVGLD-YIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEP 494
Cdd:PRK10419 105 RKTVREIIREPLRHLLSLDKAERLARASE---MLR---AVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2674892663 495 TAGLDIKTTNNICSQLmEKYQKQT---MIVTSHDISLL-RFFDDIIICGEEKIIE 545
Cdd:PRK10419 179 VSNLDLVLQAGVIRLL-KKLQQQFgtaCLFITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
349-530 |
2.95e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.12 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEK-SIREHFAVAFQEHHIFN-LSIRDN 426
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGIIYQELSVIDeLTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 427 F--------KMLYENITDEEIYKSLENVYLLDFVNQVGLDYIVGNdgnkLSGGQKHRLQLAICLAKQKDIILLDEPTAGL 498
Cdd:PRK09700 101 LyigrhltkKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190
....*....|....*....|....*....|....*
gi 2674892663 499 DIKTTNN---ICSQLmeKYQKQTMIVTSHDISLLR 530
Cdd:PRK09700 177 TNKEVDYlflIMNQL--RKEGTAIVYISHKLAEIR 209
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
337-525 |
3.13e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 72.29 E-value: 3.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 337 LKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnyddlaeksirehFAVAFQE 415
Cdd:PRK11147 322 MENVNYQIdGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK-------------LEVAYFD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 HHIFNL----SIRDNfkmLYENITDEEIYKSLENV--YLLDFV-------NQVgldyivgndgNKLSGGQKHRLQLAICL 482
Cdd:PRK11147 389 QHRAELdpekTVMDN---LAEGKQEVMVNGRPRHVlgYLQDFLfhpkramTPV----------KALSGGERNRLLLARLF 455
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2674892663 483 AKQKDIILLDEPTAGLDIKTTnNICSQLMEKYQKQTMIVtSHD 525
Cdd:PRK11147 456 LKPSNLLILDEPTNDLDVETL-ELLEELLDSYQGTVLLV-SHD 496
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
339-497 |
5.08e-13 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 68.71 E-value: 5.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 339 DLAYGYDKVLlKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSiREHFAVAF--QEH 416
Cdd:TIGR03410 7 NVYYGQSHIL-RGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE-RARAGIAYvpQGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 417 HIF-NLSIRDNFKMLYENITD------EEIYkSLENVyLLDFVNQVGldyivgndGNkLSGGQkhRLQLAI--CLAKQKD 487
Cdd:TIGR03410 85 EIFpRLTVEENLLTGLAALPRrsrkipDEIY-ELFPV-LKEMLGRRG--------GD-LSGGQ--QQQLAIarALVTRPK 151
|
170
....*....|
gi 2674892663 488 IILLDEPTAG 497
Cdd:TIGR03410 152 LLLLDEPTEG 161
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
349-526 |
9.11e-13 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 68.74 E-value: 9.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDL-AEKsirehfAVAFQEHHIFN-LSIRDN 426
Cdd:COG4525 23 LQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPgADR------GVVFQKDALLPwLNVLDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 427 --FKMLYENITDEEIYKSLEnvyllDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTN 504
Cdd:COG4525 97 vaFGLRLRGVPKAERRARAE-----ELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTRE 171
|
170 180
....*....|....*....|....*
gi 2674892663 505 NICSQLMEKYQ---KQTMIVTsHDI 526
Cdd:COG4525 172 QMQELLLDVWQrtgKGVFLIT-HSV 195
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
339-553 |
9.64e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 68.58 E-value: 9.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 339 DLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLL-----YPLKGNIFIQGK---NYDDLAEksIREHF 409
Cdd:PRK14271 26 NLTLGFaGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdkvsgYRYSGDVLLGGRsifNYRDVLE--FRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 410 AVAFQEHHIFNLSIRDNF--KMLYENITDEEIYKSLENVYLldfvNQVGL-DYI---VGNDGNKLSGGQKHRLQLAICLA 483
Cdd:PRK14271 104 GMLFQRPNPFPMSIMDNVlaGVRAHKLVPRKEFRGVAQARL----TEVGLwDAVkdrLSDSPFRLSGGQQQLLCLARTLA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 484 KQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDIS-LLRFFDDIIICGEEKIIEQGNIKKLL 553
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLF 250
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
346-528 |
1.00e-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: 67.13 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 346 KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQEHHIFNLSIRD 425
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 426 NFKMLYENITDEEIYKSLENVYLLDFVnqvglDYIVgndgNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNN 505
Cdd:cd03231 93 NLRFWHADHSDEQVEEALARVGLNGFE-----DRPV----AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180
....*....|....*....|...
gi 2674892663 506 ICSQLMEKYQKQTMIVTSHDISL 528
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTHQDL 186
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
325-539 |
1.08e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.68 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 325 QEDKQSKDVQLLLKDLAYGYDKV---LLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLY--PLKGNIFIQGKNYDD 399
Cdd:COG2401 19 SVLDLSERVAIVLEAFGVELRVVeryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 400 laEKSIREHFAvafqehhifnlsIRDNFKmlyenitdeeiykslENVYLLdfvNQVGLdyivgNDG-------NKLSGGQ 472
Cdd:COG2401 99 --EASLIDAIG------------RKGDFK---------------DAVELL---NAVGL-----SDAvlwlrrfKELSTGQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 473 KHRLQLAICLAKQKDIILLDEPTAGLDiKTTNNICSQLMEKYQKQ---TMIVTSHDISLLRFF--DDIIICG 539
Cdd:COG2401 142 KFRFRLALLLAERPKLLVIDEFCSHLD-RQTAKRVARNLQKLARRagiTLVVATHHYDVIDDLqpDLLIFVG 212
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
349-541 |
1.15e-12 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 68.41 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLfyvLMRLLYP-LKGNIFIQGKNYDDLAEKSIREH------------------- 408
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSL---INDTLYPaLARRLHLKKEQPGNHDRIEGLEHidkvividqspigrtprsn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 409 ---FAVAFQEhhifnlsIRDNF--------------KMLYE--NITD------EEIYKSLENV----YLLDFVNQVGLDY 459
Cdd:cd03271 88 patYTGVFDE-------IRELFcevckgkrynretlEVRYKgkSIADvldmtvEEALEFFENIpkiaRKLQTLCDVGLGY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 460 I-VGNDGNKLSGGQKHRLQLAICLAKQ---KDIILLDEPTAGL---DIKTTNNICSQLMEKyqKQTMIVTSHDISLLRFF 532
Cdd:cd03271 161 IkLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLhfhDVKKLLEVLQRLVDK--GNTVVVIEHNLDVIKCA 238
|
....*....
gi 2674892663 533 DDIIICGEE 541
Cdd:cd03271 239 DWIIDLGPE 247
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
357-538 |
1.15e-12 |
|
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: 68.16 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 357 KKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNiFIQGKNYDDLaeksIREHFAVAFQEH--HIFNLSIRDNFKMLYENI 434
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK-FDDPPDWDEI----LDEFRGSELQNYftKLLEGDVKVIVKPQYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 435 --------TDEEIYKSLENVYLLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNI 506
Cdd:cd03236 99 ipkavkgkVGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNA 178
|
170 180 190
....*....|....*....|....*....|...
gi 2674892663 507 CSQLMEKYQ-KQTMIVTSHDISLLRFFDDIIIC 538
Cdd:cd03236 179 ARLIRELAEdDNYVLVVEHDLAVLDYLSDYIHC 211
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
334-499 |
1.24e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.39 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 334 QLLLKDLAYGYDK--VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAV 411
Cdd:PRK10522 322 TLELRNVTFAYQDngFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 412 AFQEHHIFN-LSIRDNFKmlyeniTDEEIYKS-LENvylLDFVNQVGLDyivgnDGN----KLSGGQKHRLQLAICLAKQ 485
Cdd:PRK10522 402 VFTDFHLFDqLLGPEGKP------ANPALVEKwLER---LKMAHKLELE-----DGRisnlKLSKGQKKRLALLLALAEE 467
|
170
....*....|....
gi 2674892663 486 KDIILLDEPTAGLD 499
Cdd:PRK10522 468 RDILLLDEWAADQD 481
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
349-512 |
2.44e-12 |
|
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: 65.53 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnydDLAEKSIREHFA--VAF-----QEHHIF-N 420
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGK---PVTRRSPRDAIRagIAYvpedrKREGLVlD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 LSIRDNFKMlyenitdeeiykslenvylldfvnqvgldyivgndGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDI 500
Cdd:cd03215 93 LSVAENIAL-----------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
170
....*....|..
gi 2674892663 501 KTTNNICSQLME 512
Cdd:cd03215 138 GAKAEIYRLIRE 149
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
349-526 |
2.50e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 67.03 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDL-AEKsirehfAVAFQEHHIFN-LSIRDN 426
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPgAER------GVVFQNEGLLPwRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 427 --FKMLYENITDEEiykslENVYLLDFVNQVGLD-----YIVgndgnKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD 499
Cdd:PRK11248 91 vaFGLQLAGVEKMQ-----RLEIAHQMLKKVGLEgaekrYIW-----QLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190
....*....|....*....|....*....|
gi 2674892663 500 IKTTNNICSQLMEKYQ---KQTMIVTsHDI 526
Cdd:PRK11248 161 AFTREQMQTLLLKLWQetgKQVLLIT-HDI 189
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
349-553 |
3.32e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.80 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKN-YDDlaEKSIREHFAVAF-QEHH-IFNLSIRD 425
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpFKR--RKEFARRIGVVFgQRSQlWWDLPAID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 426 NFKML---YEnITDEEIYKSLENvylldFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKT 502
Cdd:COG4586 116 SFRLLkaiYR-IPDAEYKKRLDE-----LVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVS 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 503 TNNIcSQLMEKYQKQ---TMIVTSHDIsllrffDDI-------IICGEEKIIEQGNIKKLL 553
Cdd:COG4586 190 KEAI-REFLKEYNRErgtTILLTSHDM------DDIealcdrvIVIDHGRIIYDGSLEELK 243
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
335-553 |
4.10e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 67.04 E-value: 4.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYDKV----LLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFA 410
Cdd:PRK13642 5 LEVENLVFKYEKEsdvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 411 VAFQ--EHHIFNLSIRDN--FKMLYENITDEEIYKSLEN----VYLLDFVNQvgldyivgnDGNKLSGGQKHRLQLAICL 482
Cdd:PRK13642 85 MVFQnpDNQFVGATVEDDvaFGMENQGIPREEMIKRVDEallaVNMLDFKTR---------EPARLSGGQKQRVAVAGII 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 483 AKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTS--HDISLLRFFDDIIICGEEKIIEQGNIKKLL 553
Cdd:PRK13642 156 ALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSitHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
239-552 |
4.17e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 69.38 E-value: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 239 CSEFIMGA--YLVICLAISIYLVNTQDFNPIMAITIILTYQAVLEVLAMMPSLIEHFDEAS---KRWQDLaiFMQEKKFI 313
Cdd:PLN03130 525 FNSFILNSipVLVTVVSFGVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANvslKRLEEL--LLAEERVL 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 314 AnTNNEIKSENQedkqskdvQLLLKDLAYGYD----KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGN 389
Cdd:PLN03130 603 L-PNPPLEPGLP--------AISIKNGYFSWDskaeRPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDA 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 390 IFIqgknyddlaeksIREHFAVAFQEHHIFNLSIRDNfkMLYENITDEEIYKSLENVYLLdfvnQVGLDYIVGND----- 464
Cdd:PLN03130 674 SVV------------IRGTVAYVPQVSWIFNATVRDN--ILFGSPFDPERYERAIDVTAL----QHDLDLLPGGDlteig 735
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 465 --GNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQ-LMEKYQKQTMIVTSHDISLLRFFDDIIICGEE 541
Cdd:PLN03130 736 erGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKcIKDELRGKTRVLVTNQLHFLSQVDRIILVHEG 815
|
330
....*....|.
gi 2674892663 542 KIIEQGNIKKL 552
Cdd:PLN03130 816 MIKEEGTYEEL 826
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
335-524 |
5.82e-12 |
|
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: 65.07 E-value: 5.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYD-KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnydDLAEKSIREHFAVAF 413
Cdd:TIGR01189 1 LAARNLACSRGeRMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT---PLAEQRDEPHENILY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 QEHH--IFN-LSIRDNFKMLYENITDEE--IYKSLENVYLLDFVnqvglDYIVgndgNKLSGGQKHRLQLAICLAKQKDI 488
Cdd:TIGR01189 78 LGHLpgLKPeLSALENLHFWAAIHGGAQrtIEDALAAVGLTGFE-----DLPA----AQLSAGQQRRLALARLWLSRRPL 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 2674892663 489 ILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIV-TSH 524
Cdd:TIGR01189 149 WILDEPTTALDKAGVALLAGLLRAHLARGGIVLlTTH 185
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
342-525 |
8.57e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 66.65 E-value: 8.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGYDKVLlKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnydDLAEKSIRE-HFAVAFQEHHIF- 419
Cdd:PRK10851 12 FGRTQVL-NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT---DVSRLHARDrKVGFVFQHYALFr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 420 NLSIRDN----FKML--YENITDEEIYKSLenVYLLDFVNqvgLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDE 493
Cdd:PRK10851 88 HMTVFDNiafgLTVLprRERPNAAAIKAKV--TQLLEMVQ---LAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190
....*....|....*....|....*....|....*
gi 2674892663 494 PTAGLDIKTTNNI---CSQLMEKYQKQTMIVTsHD 525
Cdd:PRK10851 163 PFGALDAQVRKELrrwLRQLHEELKFTSVFVT-HD 196
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
338-537 |
9.44e-12 |
|
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: 64.19 E-value: 9.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 338 KDLAY-----GYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLM--RLLYPLKGNIFIQGKNYDDLAEKSIrehfa 410
Cdd:cd03232 7 KNLNYtvpvkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILINGRPLDKNFQRST----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 411 vAFQEH---HIFNLSIRDnfkmlyenitdeeiykSLENVYLLdfvnqvgldyivgndgNKLSGGQKHRLQLAICLAKQKD 487
Cdd:cd03232 82 -GYVEQqdvHSPNLTVRE----------------ALRFSALL----------------RGLSVEQRKRLTIGVELAAKPS 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2674892663 488 IILLDEPTAGLDIKTTNNICsQLMEKY--QKQTMIVTSH--DISLLRFFDDIII 537
Cdd:cd03232 129 ILFLDEPTSGLDSQAAYNIV-RFLKKLadSGQAILCTIHqpSASIFEKFDRLLL 181
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
349-534 |
1.26e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 64.75 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnydDLAEKSirEHfAVA-------FQEHHIF-N 420
Cdd:COG4674 26 LNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGT---DLTGLD--EH-EIArlgigrkFQKPTVFeE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 LSIRDN-----------FKMLYENITDEE---IYKSLENVYLLDFvnqvgLDYIVGNdgnkLSGGQKHRLQLAICLAKQK 486
Cdd:COG4674 100 LTVFENlelalkgdrgvFASLFARLTAEErdrIEEVLETIGLTDK-----ADRLAGL----LSHGQKQWLEIGMLLAQDP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2674892663 487 DIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDISLLRFFDD 534
Cdd:COG4674 171 KLLLLDEPVAGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIAR 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
346-547 |
1.46e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.04 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 346 KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLyPLKGNIFIQGKNYDDLAEKS---IREHFAVAFQEHhifNLS 422
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQllpVRHRIQVVFQDP---NSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 IrdNFKMLYENITDEEI---YKSL----ENVYLLDFVNQVGLD------YivgndGNKLSGGQKHRLQLAICLAKQKDII 489
Cdd:PRK15134 375 L--NPRLNVLQIIEEGLrvhQPTLsaaqREQQVIAVMEEVGLDpetrhrY-----PAEFSGGQRQRIAIARALILKPSLI 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 490 LLDEPTAGLDIKTTNNICSQLMEKYQKQTM--IVTSHDISLLRFF-DDIIICGEEKIIEQG 547
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRALcHQVIVLRQGEVVEQG 508
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
349-550 |
1.46e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 64.72 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnyddLAekSIREhFAVAFQEhhifNLSIRDN-- 426
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR----VS--ALLE-LGAGFHP----ELTGRENiy 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 427 FKMLYENITDEEIYKSLENVylLDFVnQVGlDYI---VGNdgnkLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDI--- 500
Cdd:COG1134 111 LNGRLLGLSRKEIDEKFDEI--VEFA-ELG-DFIdqpVKT----YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAafq 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2674892663 501 -KttnniCSQLMEKYQKQ--TMIVTSHDISLLR-FFDDIIicgeekIIEQGNIK 550
Cdd:COG1134 183 kK-----CLARIRELRESgrTVIFVSHSMGAVRrLCDRAI------WLEKGRLV 225
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
352-549 |
1.49e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 67.73 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 352 INLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEkSIREHFAVAFQEHHIFN-LSIRDNFkML 430
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLD-AVRQSLGMCPQHNILFHhLTVAEHI-LF 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 431 YENI---TDEEIYKSLENVylldfVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNIC 507
Cdd:TIGR01257 1027 YAQLkgrSWEEAQLEMEAM-----LEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2674892663 508 SQLMEKYQKQTMIVTSHDISLLRFFDDIIicgeeKIIEQGNI 549
Cdd:TIGR01257 1102 DLLLKYRSGRTIIMSTHHMDEADLLGDRI-----AIISQGRL 1138
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
338-536 |
2.27e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.50 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 338 KDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMrllyplkgnifiqGKNYDDLAEKSIREHFAVAFQEH 416
Cdd:TIGR03719 326 ENLTKAFgDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMIT-------------GQEQPDSGTIEIGETVKLAYVDQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 417 HIFNLsirDNFKMLYENITDeeiykslenvylldfvnqvGLDYIV------------------GNDGNK----LSGGQKH 474
Cdd:TIGR03719 393 SRDAL---DPNKTVWEEISG-------------------GLDIIKlgkreipsrayvgrfnfkGSDQQKkvgqLSGGERN 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 475 RLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKyqKQTMIVTSHDisllRFFDDII 536
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHD----RWFLDRI 506
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
351-553 |
4.15e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.50 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 351 DINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLL------YPlKGNIFIQGKNYDDLAEKSIR----EHFAVAFQEHHIFN 420
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSVTALSILRLLpsppvvYP-SGDIRFHGESLLHASEQTLRgvrgNKIAMIFQEPMVSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 LSIRDNFKMLYENIT----------DEEIYKSLENV-------YLLDFVNQvgldyivgndgnkLSGGQKHRLQLAICLA 483
Cdd:PRK15134 106 NPLHTLEKQLYEVLSlhrgmrreaaRGEILNCLDRVgirqaakRLTDYPHQ-------------LSGGERQRVMIAMALL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 484 KQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTM--IVTSHDISLLR-FFDDIIICGEEKIIEQGNIKKLL 553
Cdd:PRK15134 173 TRPELLIADEPTTALDVSVQAQILQLLRELQQELNMglLFITHNLSIVRkLADRVAVMQNGRCVEQNRAATLF 245
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
338-533 |
4.34e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.90 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 338 KDLAY-----GYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLL---YPLKGNIFIQGKNYDDLAEKSIRehf 409
Cdd:TIGR00956 763 RNLTYevkikKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVttgVITGGDRLVNGRPLDSSFQRSIG--- 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 410 AVAFQEHHIFNLSIRDNFKM-----LYENITDEEIYKSLENVY-LLDFVNQVglDYIVGNDGNKLSGGQKHRLQLAICL- 482
Cdd:TIGR00956 840 YVQQQDLHLPTSTVRESLRFsaylrQPKSVSKSEKMEYVEEVIkLLEMESYA--DAVVGVPGEGLNVEQRKRLTIGVELv 917
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2674892663 483 AKQKDIILLDEPTAGLDIKTTNNICsQLMEKYQK--QTMIVTSHDISLLRF--FD 533
Cdd:TIGR00956 918 AKPKLLLFLDEPTSGLDSQTAWSIC-KLMRKLADhgQAILCTIHQPSAILFeeFD 971
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
345-549 |
5.21e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.12 E-value: 5.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRllYP----LKGNIFIQGKNYDDLaEKSIREHFAV--AFQEH-H 417
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPaykiLEGDILFKGESILDL-EPEERAHLGIflAFQYPiE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 418 IFNLSIRDNFKMLYENITDEEIYKSLENVYLLDFVNQ----VGLD--YIVGNDGNKLSGGQKHR---LQLAICLAKqkdI 488
Cdd:CHL00131 96 IPGVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEklklVGMDpsFLSRNVNEGFSGGEKKRneiLQMALLDSE---L 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 489 ILLDEPTAGLDI---KTTNNICSQLMEKyqKQTMIVTSHDISLLRFF--DDIIICGEEKIIEQGNI 549
Cdd:CHL00131 173 AILDETDSGLDIdalKIIAEGINKLMTS--ENSIILITHYQRLLDYIkpDYVHVMQNGKIIKTGDA 236
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
345-538 |
7.10e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.82 E-value: 7.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIfiqgknyddlaEKSIREHFAVAFQEHHI---FNL 421
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYVPQKLYLdttLPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 422 SIRdNFKMLYENITDEEIYKSLENV---YLLDFVNQvgldyivgndgnKLSGGQKHRLQLAICLAKQKDIILLDEPTAGL 498
Cdd:PRK09544 85 TVN-RFLRLRPGTKKEDILPALKRVqagHLIDAPMQ------------KLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2674892663 499 DIK---TTNNICSQLMEKYQKQTMIVtSHDISLLRFFDDIIIC 538
Cdd:PRK09544 152 DVNgqvALYDLIDQLRRELDCAVLMV-SHDLHLVMAKTDEVLC 193
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
339-530 |
7.47e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.89 E-value: 7.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 339 DLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYD-DLAeksirehfavAFQEH 416
Cdd:PRK13540 6 ELDFDYhDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKkDLC----------TYQKQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 417 HIF---------NLSIRDNfkMLYenitdeEIYKSLENVYLLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKD 487
Cdd:PRK13540 76 LCFvghrsginpYLTLREN--CLY------DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2674892663 488 IILLDEPTAGLDIKTTNNICSQLME-KYQKQTMIVTSH-DISLLR 530
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQEhRAKGGAVLLTSHqDLPLNK 192
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
325-553 |
1.21e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 62.11 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 325 QEDKQSKDVQLLLKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEK 403
Cdd:PRK10575 2 QEYTNHSDTTFALRNVSFRVpGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 404 S-------------------IREHFAVAFQEHH--IFNLSIRDNFKMlyenitDEEIykslenvylldfvNQVGLDYIVG 462
Cdd:PRK10575 82 AfarkvaylpqqlpaaegmtVRELVAIGRYPWHgaLGRFGAADREKV------EEAI-------------SLVGLKPLAH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 463 NDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICS--QLMEKYQKQTMIVTSHDISL-LRFFDDIIICG 539
Cdd:PRK10575 143 RLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLAlvHRLSQERGLTVIAVLHDINMaARYCDYLVALR 222
|
250
....*....|....
gi 2674892663 540 EEKIIEQGNIKKLL 553
Cdd:PRK10575 223 GGEMIAQGTPAELM 236
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
295-524 |
1.70e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 62.54 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 295 EASKRWQDLAIFMQEKKFIANTNNEIKSenqeDKQSKDVQLLLKDLAYGyDKVLLKDINLSIKKGNKTLIVGTSGCGKST 374
Cdd:PRK13536 8 EEAPRRLELSPIERKHQGISEAKASIPG----SMSTVAIDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 375 LFYVLMRLLYPLKGNIFIQGKNYDDLAeKSIREHFAVAFQEHHI-FNLSIRDN-------FKMLYENItdEEIYKSLenv 446
Cdd:PRK13536 83 IARMILGMTSPDAGKITVLGVPVPARA-RLARARIGVVPQFDNLdLEFTVRENllvfgryFGMSTREI--EAVIPSL--- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2674892663 447 ylLDFVNqvgLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQK-QTMIVTSH 524
Cdd:PRK13536 157 --LEFAR---LESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARgKTILLTTH 230
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
349-537 |
2.03e-10 |
|
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: 59.36 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnyddlaeksirehfAVAFqehhifnLSIRDnfk 428
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK--------------EVSF-------ASPRD--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 429 mlyenitdeeiykSLEN-VYLldfVNQvgldyivgndgnkLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNIC 507
Cdd:cd03216 72 -------------ARRAgIAM---VYQ-------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLF 122
|
170 180 190
....*....|....*....|....*....|...
gi 2674892663 508 sQLMEKYQKQ--TMIVTSHDIS-LLRFFDDIII 537
Cdd:cd03216 123 -KVIRRLRAQgvAVIFISHRLDeVFEIADRVTV 154
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
349-553 |
2.06e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 61.39 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLfyvLMRL--LYPLKGNIFIQGKNYDDLAEKSIREHFAVAFQE---------HH 417
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTL---LARMagLLPGQGEILLNGRPLSDWSAAELARHRAYLSQQqsppfampvFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 418 IFNLSIRDNfkmlyeniTDEEIYKSLenvyLLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLA-ICLakQKD--------I 488
Cdd:COG4138 89 YLALHQPAG--------ASSEAVEQL----LAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAaVLL--QVWptinpegqL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2674892663 489 ILLDEPTAGLDI---KTTNNICSQLMEkyQKQTMIVTSHDISL-LRFFDDIIICGEEKIIEQGNIKKLL 553
Cdd:COG4138 155 LLLDEPMNSLDVaqqAALDRLLRELCQ--QGITVVMSSHDLNHtLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
347-547 |
2.47e-10 |
|
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: 60.46 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 347 VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGknYDDLAEK-SIREHFAVAFQEHHIFN-LSIR 424
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPaEARRRLGFVSDSTGLYDrLTAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 425 DN---FKMLY----ENITD--EEIYKSLENVYLLDfvnqvgldyivgNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:cd03266 97 ENleyFAGLYglkgDELTArlEELADRLGMEELLD------------RRVGGFSTGMRQKVAIARALVHDPPVLLLDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2674892663 496 AGLDIKTTNNICSQLME-KYQKQTMIVTSHDIS-LLRFFDDIIICGEEKIIEQG 547
Cdd:cd03266 165 TGLDVMATRALREFIRQlRALGKCILFSTHIMQeVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
349-549 |
2.67e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 61.18 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLL---------YPLKGN-IFIQGKNYDDLaEKSiREHFAVAFQEHHI 418
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdksagshIELLGRtVQREGRLARDI-RKS-RANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 419 FN-LSIRDNfkMLYENITDEEIYKS-------LENVYLLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIIL 490
Cdd:PRK09984 98 VNrLSVLEN--VLIGALGSTPFWRTcfswftrEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 491 LDEPTAGLDIKTTNNICSQLMEKYQKQ--TMIVTSHDISL-LRFFDDIIicgeekIIEQGNI 549
Cdd:PRK09984 176 ADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYaLRYCERIV------ALRQGHV 231
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
318-537 |
3.56e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.52 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 318 NEIKSENQEDKQSKDVQLLLK--DLAYGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGK 395
Cdd:PRK13409 322 EPIEFEERPPRDESERETLVEypDLTKKLGDFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 396 nyddlaeksirehfaVAFQEHHI---FNLSIRDNFKMLYENItDEEIYKSlenvyllDFVNQVGLDYIVGNDGNKLSGGQ 472
Cdd:PRK13409 402 ---------------ISYKPQYIkpdYDGTVEDLLRSITDDL-GSSYYKS-------EIIKPLQLERLLDKNVKDLSGGE 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2674892663 473 KHRLQLAICLAKQKDIILLDEPTAGLD----IKTTNNIcSQLMEKyQKQTMIVTSHDISLLRFFDDIII 537
Cdd:PRK13409 459 LQRVAIAACLSRDADLYLLDEPSAHLDveqrLAVAKAI-RRIAEE-REATALVVDHDIYMIDYISDRLM 525
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
349-553 |
4.45e-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: 62.01 E-value: 4.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGnKTL-IVGTSGCGKSTLFYVLMRLL-YP---LKGNIFIQGKNYDDLAEKSIRE----HFAVAFQE---- 415
Cdd:COG4172 26 VKGVSFDIAAG-ETLaLVGESGSGKSVTALSILRLLpDPaahPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEpmts 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 ----HHIFN-----LsirdnfkMLYENITDEEI-YKSLEnvyLLDfvnQVGLDyivgNDGNK-------LSGGQKHRLQL 478
Cdd:COG4172 105 lnplHTIGKqiaevL-------RLHRGLSGAAArARALE---LLE---RVGIP----DPERRldayphqLSGGQRQRVMI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2674892663 479 AICLAKQKDIILLDEPTAGLDIKTTNNICsQLMEKYQKQT---MIVTSHDISLLR-FFDDIIICGEEKIIEQGNIKKLL 553
Cdd:COG4172 168 AMALANEPDLLIADEPTTALDVTVQAQIL-DLLKDLQRELgmaLLLITHDLGVVRrFADRVAVMRQGEIVEQGPTAELF 245
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
332-528 |
4.57e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.79 E-value: 4.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 332 DVQLLLKDLAYGYDKV-LLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEK---SIR- 406
Cdd:PRK10584 8 EVHHLKKSVGQGEHELsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRa 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 407 EHFAVAFQEHhifnlsirdnfkMLYENITdeeiykSLENVYL----------------LDFVNQVGLDYIVGNDGNKLSG 470
Cdd:PRK10584 88 KHVGFVFQSF------------MLIPTLN------ALENVELpallrgessrqsrngaKALLEQLGLGKRLDHLPAQLSG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 471 GQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQL--MEKYQKQTMIVTSHDISL 528
Cdd:PRK10584 150 GEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfsLNREHGTTLILVTHDLQL 209
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
364-547 |
4.80e-10 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 61.36 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 364 IVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKsiREHFAVAFQEHHIF-NLSIRDN--FKMLYENITDEEI- 439
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH--LRHINMVFQSYALFpHMTVEENvaFGLKMRKVPRAEIk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 440 ---YKSLENVYLLDFvnqvGLDYIvgndgNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLmEKYQK 516
Cdd:TIGR01187 79 prvLEALRLVQLEEF----ADRKP-----HQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLEL-KTIQE 148
|
170 180 190
....*....|....*....|....*....|....*
gi 2674892663 517 Q---TMIVTSHDIS-LLRFFDDIIICGEEKIIEQG 547
Cdd:TIGR01187 149 QlgiTFVFVTHDQEeAMTMSDRIAIMRKGKIAQIG 183
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
349-547 |
5.21e-10 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 62.34 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYvlmRLLYPLKGNIFIQGK----NYDDL--AEK------------------- 403
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLIN---DTLYPALANRLNGAKtvpgRYTSIegLEHldkvihidqspigrtprsn 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 404 ---------SIREHFA-------VAFQEHHI-FN--------------LSIRDNF-----------------------KM 429
Cdd:TIGR00630 701 patytgvfdEIRELFAetpeakvRGYTPGRFsFNvkggrceacqgdgvIKIEMHFlpdvyvpcevckgkrynretlevKY 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 430 LYENITD------EEIYKSLENV----YLLDFVNQVGLDYI-VGNDGNKLSGGQKHRLQLAICLAKQ---KDIILLDEPT 495
Cdd:TIGR00630 781 KGKNIADvldmtvEEAYEFFEAVpsisRKLQTLCDVGLGYIrLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPT 860
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 496 AGL---DIKTTNNICSQLMEkyQKQTMIVTSHDISLLRFFDDIIICGEE------KIIEQG 547
Cdd:TIGR00630 861 TGLhfdDIKKLLEVLQRLVD--KGNTVVVIEHNLDVIKTADYIIDLGPEggdgggTVVASG 919
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
352-547 |
5.91e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 60.00 E-value: 5.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 352 INLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREHFAV-AFQEHHIF-NLSIRDN--- 426
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVrTFQHVRLFrEMTVIENllv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 427 --------------FKM-LYENITDEEIYKS---LENVYLLDFVNQVGldyivgndGNkLSGGQKHRLQLAICLAKQKDI 488
Cdd:PRK11300 104 aqhqqlktglfsglLKTpAFRRAESEALDRAatwLERVGLLEHANRQA--------GN-LAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 489 ILLDEPTAGLDIKTT---NNICSQLMEKYQkQTMIVTSHDISLLRFFDDIIIcgeekIIEQG 547
Cdd:PRK11300 175 LMLDEPAAGLNPKETkelDELIAELRNEHN-VTVLLIEHDMKLVMGISDRIY-----VVNQG 230
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
349-553 |
1.36e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 59.03 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGK--NYDDLAEKSIRehFAVAFQE----------- 415
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplHFGDYSYRSQR--IRMIFQDpstslnprqri 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 416 HHIFNLSIRDNFKMLYENiTDEEIYKSLENVYLL-DFVNQVgldyivgndGNKLSGGQKHRLQLAICLAKQKDIILLDEP 494
Cdd:PRK15112 107 SQILDFPLRLNTDLEPEQ-REKQIIETLRQVGLLpDHASYY---------PHMLAPGQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 495 TAGLDIKTTN---NICSQLMEKYQKQTMIVTSHDISLLRFFDDIIICGEEKIIEQGNIKKLL 553
Cdd:PRK15112 177 LASLDMSMRSqliNLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
362-536 |
1.38e-09 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 58.00 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 362 TLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLA-EKSIREHFAVAFqehhifnlsiRDNFKMLYENITDEEIY 440
Cdd:cd03240 25 TLIVGQNGAGKTTIIEALKYALTGELPPNSKGGAHDPKLIrEGEVRAQVKLAF----------ENANGKKYTITRSLAIL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 441 kslENVYlldFVNQVGLDYIVGNDGNKLSGGQK------HRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKY 514
Cdd:cd03240 95 ---ENVI---FCHQGESNWPLLDMRGRCSGGEKvlasliIRLALAETFGSNCGILALDEPTTNLDEENIEESLAEIIEER 168
|
170 180
....*....|....*....|....*
gi 2674892663 515 QKQT---MIVTSHDISLLRFFDDII 536
Cdd:cd03240 169 KSQKnfqLIVITHDEELVDAADHIY 193
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
349-552 |
1.45e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.64 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNI-----FIQGKNYD--DLAEKSIRE-------HFAVAFQ 414
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmLLRRRSRQviELSEQSAAQmrhvrgaDMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 E-----HHIFNL------SIRdnfkmLYENITDEEiyKSLENVYLLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLA 483
Cdd:PRK10261 112 EpmtslNPVFTVgeqiaeSIR-----LHQGASREE--AMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALS 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 484 KQKDIILLDEPTAGLDIKTTNNICsQLMEKYQKQT---MIVTSHDISLL-RFFDDIIICGEEKIIEQGNIKKL 552
Cdd:PRK10261 185 CRPAVLIADEPTTALDVTIQAQIL-QLIKVLQKEMsmgVIFITHDMGVVaEIADRVLVMYQGEAVETGSVEQI 256
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
355-537 |
1.67e-09 |
|
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: 60.57 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 355 SIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIfiqgknyddlaEKSIRehfaVAFQEHHI---FNLSIRDNFKMLY 431
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----------DEDLK----ISYKPQYIspdYDGTVEEFLRSAN 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 432 ENITDEEIYKSlenvyllDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD----IKTTNNIc 507
Cdd:COG1245 427 TDDFGSSYYKT-------EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrLAVAKAI- 498
|
170 180 190
....*....|....*....|....*....|
gi 2674892663 508 SQLMEKYQKQTMIVtSHDISLLRFFDDIII 537
Cdd:COG1245 499 RRFAENRGKTAMVV-DHDIYLIDYISDRLM 527
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
341-502 |
2.13e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.13 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 341 AYGyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIfiqgknyddlaekSIREHFAVAFQEHHIFN 420
Cdd:PRK11819 333 SFG-DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI-------------KIGETVKLAYVDQSRDA 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 LsirDNFKMLYENITDeeiykslenvylldfvnqvGLDYI-VGN-----------------DGNK----LSGGQKHRLQL 478
Cdd:PRK11819 399 L---DPNKTVWEEISG-------------------GLDIIkVGNreipsrayvgrfnfkggDQQKkvgvLSGGERNRLHL 456
|
170 180
....*....|....*....|....
gi 2674892663 479 AICLAKQKDIILLDEPTAGLDIKT 502
Cdd:PRK11819 457 AKTLKQGGNVLLLDEPTNDLDVET 480
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
349-547 |
2.44e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.82 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGnKTL-IVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKN---YDDLAEKSIREHFAVAFQehhifNLSIR 424
Cdd:PRK11308 31 LDGVSFTLERG-KTLaVVGESGCGKSTLARLLTMIETPTGGELYYQGQDllkADPEAQKLLRQKIQIVFQ-----NPYGS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 425 DNFKMLYENITDE--EIYKSL------ENVylLDFVNQVGLD------YivgndGNKLSGGQKHRLQLAICLAKQKDIIL 490
Cdd:PRK11308 105 LNPRKKVGQILEEplLINTSLsaaerrEKA--LAMMAKVGLRpehydrY-----PHMFSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2674892663 491 LDEPTAGLDIkttnNICSQ---LMEKYQKQ---TMIVTSHDISLLRFF-DDIIICGEEKIIEQG 547
Cdd:PRK11308 178 ADEPVSALDV----SVQAQvlnLMMDLQQElglSYVFISHDLSVVEHIaDEVMVMYLGRCVEKG 237
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
335-530 |
2.63e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.80 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGY-DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIfiqgknydDLAeKSIREHFavaF 413
Cdd:PRK10636 313 LKMEKVSAGYgDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI--------GLA-KGIKLGY---F 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 414 QEHHIFNLSIRDNFKMLYENITDEEIYKSLENvYLLDFvnqvgldyivGNDGNKL-------SGGQKHRLQLAICLAKQK 486
Cdd:PRK10636 381 AQHQLEFLRADESPLQHLARLAPQELEQKLRD-YLGGF----------GFQGDKVteetrrfSGGEKARLVLALIVWQRP 449
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2674892663 487 DIILLDEPTAGLDIKTTNNICSQLMEKyqKQTMIVTSHDISLLR 530
Cdd:PRK10636 450 NLLLLDEPTNHLDLDMRQALTEALIDF--EGALVVVSHDRHLLR 491
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
345-543 |
3.09e-09 |
|
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: 56.39 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRlLYPL-KGNIfiqgknyddlaekSIREHFAVAF--QEHHIFNL 421
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPWgSGRI-------------GMPEGEDLLFlpQRPYLPLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 422 SIRDNFkmlyenitdeeiykslenVYLLDFVnqvgldyivgndgnkLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIK 501
Cdd:cd03223 79 TLREQL------------------IYPWDDV---------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2674892663 502 TTNNICSQLMEKyqKQTMIVTSHDISLLRFFDDII-ICGEEKI 543
Cdd:cd03223 126 SEDRLYQLLKEL--GITVISVGHRPSLWKFHDRVLdLDGEGGW 166
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
347-531 |
5.31e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 58.99 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 347 VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLM--------RLLYPLKGNIF-IQGKNYDDLAeksirehfavAFQEHH 417
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLFyVPQRPYMTLG----------TLRDQI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 418 IFNLSIRDNFKmlyENITDEEIYKSLENVYLLDFVNQ-VGLDyIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTA 496
Cdd:TIGR00954 536 IYPDSSEDMKR---RGLSDKDLEQILDNVQLTHILEReGGWS-AVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTS 611
|
170 180 190
....*....|....*....|....*....|....*
gi 2674892663 497 GLDIKTTNNICSQLMEKyqKQTMIVTSHDISLLRF 531
Cdd:TIGR00954 612 AVSVDVEGYMYRLCREF--GITLFSVSHRKSLWKY 644
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
334-558 |
5.36e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 57.02 E-value: 5.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 334 QLLLKDLAYGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYP----LKGNIFIQGKnydDLAEKSIR-EH 408
Cdd:PRK10418 4 QIELRNIALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGK---PVAPCALRgRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 409 FAV-------AFQEHHIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDfvnqvgLDYIVGNDGNKLSGGQKHRLQLAIC 481
Cdd:PRK10418 81 IATimqnprsAFNPLHTMHTHARETCLALGKPADDATLTAALEAVGLEN------AARVLKLYPFEMSGGMLQRMMIALA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 482 LAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQT--MIVTSHDISLL-RFFDDIIICGEEKIIEQGNIKKLLLREDS 558
Cdd:PRK10418 155 LLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFNAPKH 234
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
342-556 |
8.07e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 57.12 E-value: 8.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSiREHFAVAFQEHHIF-N 420
Cdd:PRK13537 17 YG-DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVVPQFDNLDpD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 LSIRDNFKML--YENITDEEIYKSLENvyLLDFVN-QVGLDYIVGndgnKLSGGQKHRLQLAICLAKQKDIILLDEPTAG 497
Cdd:PRK13537 95 FTVRENLLVFgrYFGLSAAAARALVPP--LLEFAKlENKADAKVG----ELSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 498 LDIKTTNNICSQLMEKYQK-QTMIVTSHDI-SLLRFFDDIIICGEEKIIEQGNIKKLLLRE 556
Cdd:PRK13537 169 LDPQARHLMWERLRSLLARgKTILLTTHFMeEAERLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
342-552 |
8.11e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 57.04 E-value: 8.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 342 YGyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDlaeksirehfavafqehhifnl 421
Cdd:COG4152 11 FG-DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP---------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 422 SIRDNF-----------KM------LY----ENITDEEIYKSLEnvYLLDfvnQVGL-DYIvgNDG-NKLSGGQKHRLQL 478
Cdd:COG4152 68 EDRRRIgylpeerglypKMkvgeqlVYlarlKGLSKAEAKRRAD--EWLE---RLGLgDRA--NKKvEELSKGNQQKVQL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 479 AICLAKQKDIILLDEPTAGLDIKTTNNICSQLME-KYQKQTMIVTSHDISLL-RFFDDIIICGEEKIIEQGNIKKL 552
Cdd:COG4152 141 IAALLHDPELLILDEPFSGLDPVNVELLKDVIRElAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEI 216
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
339-529 |
1.13e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.95 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 339 DLAYGY--DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFiqgknyddlaeKSIREHFAVaFQEH 416
Cdd:PLN03073 513 DASFGYpgGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----------RSAKVRMAV-FSQH 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 417 HIFNLSIRDNfKMLYenitdeeIYKSLENVYLLDFVNQVGLDYIVGNDGNK----LSGGQKHRLQLAICLAKQKDIILLD 492
Cdd:PLN03073 581 HVDGLDLSSN-PLLY-------MMRCFPGVPEQKLRAHLGSFGVTGNLALQpmytLSGGQKSRVAFAKITFKKPHILLLD 652
|
170 180 190
....*....|....*....|....*....|....*..
gi 2674892663 493 EPTAGLDIKTTNNICSQLMeKYQKQTMIVtSHDISLL 529
Cdd:PLN03073 653 EPSNHLDLDAVEALIQGLV-LFQGGVLMV-SHDEHLI 687
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
341-534 |
1.31e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 57.64 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 341 AYGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQ-GKNYDDLA-------EKSIREHFAVA 412
Cdd:TIGR03719 13 VVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIKVGYLPqepqldpTKTVRENVEEG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 413 FQEhhifNLSIRDNFKMLYENITDE------------EIYKSLENVYLLDFVNQVGL----------DYIVgndgNKLSG 470
Cdd:TIGR03719 93 VAE----IKDALDRFNEISAKYAEPdadfdklaaeqaELQEIIDAADAWDLDSQLEIamdalrcppwDADV----TKLSG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2674892663 471 GQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTnnicsQLMEKYQKQ---TMIVTSHDisllRFFDD 534
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESV-----AWLERHLQEypgTVVAVTHD----RYFLD 222
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
448-536 |
1.93e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 448 LLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTSHDIS 527
Cdd:PRK13409 193 LDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDLA 272
|
....*....
gi 2674892663 528 LLRFFDDII 536
Cdd:PRK13409 273 VLDYLADNV 281
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
348-551 |
2.22e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.43 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 348 LLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKgnIFIQGK-NYDDLAEKSIREHFA-----VAFQEHHIFNL 421
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFH--IGVEGViTYDGITPEEIKKHYRgdvvyNAETDVHFPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 422 SIRDNFKML---------YENITDEEIYKSLENVYLLDFvnqvGLDY----IVGNDGNK-LSGGQKHRLQLAICLAKQKD 487
Cdd:TIGR00956 154 TVGETLDFAarcktpqnrPDGVSREEYAKHIADVYMATY----GLSHtrntKVGNDFVRgVSGGERKRVSIAEASLGGAK 229
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 488 IILLDEPTAGLDIKTTNNI--CSQLMEKYQKQTMIVT----SHDISLLrfFDDIIICGEEKIIEQGNIKK 551
Cdd:TIGR00956 230 IQCWDNATRGLDSATALEFirALKTSANILDTTPLVAiyqcSQDAYEL--FDKVIVLYEGYQIYFGPADK 297
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
326-512 |
2.31e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.57 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 326 EDKQSKDVQLLLKDLAYGYDK--VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEK 403
Cdd:COG3845 249 APAEPGEVVLEVENLSVRDDRgvPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 404 SIREHfAVAF--QEHH----IFNLSIRDNfkMLYENITDEEIYKSLenvyLLDF---------------VNQVGLDYIVG 462
Cdd:COG3845 329 ERRRL-GVAYipEDRLgrglVPDMSVAEN--LILGRYRRPPFSRGG----FLDRkairafaeelieefdVRTPGPDTPAR 401
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 463 NdgnkLSGG--QKhrLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLME 512
Cdd:COG3845 402 S----LSGGnqQK--VILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLE 447
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
352-525 |
2.31e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 55.32 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 352 INLSIKKGNKTLIVGTSGCGKSTLfyvLMRL--LYPLKGNIFIQGKNYDDLAEKSIREHFA-VAFQEHHIFNLSIrdnFK 428
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTL---LARMagLLPGSGSIQFAGQPLEAWSAAELARHRAyLSQQQTPPFAMPV---FQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 429 ML----YENITDEEIYKSLENVylldfVNQVGLDYIVGNDGNKLSGGQKHRLQLA-ICLAKQKDI------ILLDEPTAG 497
Cdd:PRK03695 89 YLtlhqPDKTRTEAVASALNEV-----AEALGLDDKLGRSVNQLSGGEWQRVRLAaVVLQVWPDInpagqlLLLDEPMNS 163
|
170 180 190
....*....|....*....|....*....|
gi 2674892663 498 LDIkTTNNICSQLMEKYQKQ--TMIVTSHD 525
Cdd:PRK03695 164 LDV-AQQAALDRLLSELCQQgiAVVMSSHD 192
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
349-536 |
2.73e-08 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 54.57 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYvlmrllyplkGNIFIQG-KNYDDLAEKSIReHFAVAFQE---HHIFNLS-- 422
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAF----------DTIYAEGqRRYVESLSAYAR-QFLGQMDKpdvDSIEGLSpa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 -------IRDNFKMLYENITdeEIYKSLENVYL-------LDFVNQVGLDYI-VGNDGNKLSGGQKHRLQLAICLAKQKD 487
Cdd:cd03270 80 iaidqktTSRNPRSTVGTVT--EIYDYLRLLFArvgirerLGFLVDVGLGYLtLSRSAPTLSGGEAQRIRLATQIGSGLT 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 488 IIL--LDEPTAGLDIKTTNNICSQLME-KYQKQTMIVTSHDISLLRFFDDII 536
Cdd:cd03270 158 GVLyvLDEPSIGLHPRDNDRLIETLKRlRDLGNTVLVVEHDEDTIRAADHVI 209
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
357-536 |
2.77e-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: 56.72 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 357 KKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNifiqgknYDDLAEKS-IREHFA-VAFQEHhifnlsirdnFKMLYENi 434
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGD-------YDEEPSWDeVLKRFRgTELQDY----------FKKLANG- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 435 tdeEI---YKS-----------------LENV----YLLDFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIIL 490
Cdd:COG1245 159 ---EIkvaHKPqyvdlipkvfkgtvrelLEKVdergKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2674892663 491 LDEPTAGLDIKTTNNICSQLME--KYQKQTMIVtSHDISLLRFFDDII 536
Cdd:COG1245 236 FDEPSSYLDIYQRLNVARLIRElaEEGKYVLVV-EHDLAILDYLADYV 282
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
351-499 |
3.14e-08 |
|
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: 55.88 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 351 DINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDlAEKSI-----REHFAVAFQEHHIF-NLSIR 424
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQD-SARGIflpphRRRIGYVFQEARLFpHLSVR 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2674892663 425 DNFKMLYENITDEEIYKSLENVylldfVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD 499
Cdd:COG4148 96 GNLLYGRKRAPRAERRISFDEV-----VELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
346-547 |
3.52e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 56.21 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 346 KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLM-RLLYPLK--GNIFIQGKNYDdlaEKSIREHFAVAfQEHHIF--N 420
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAfRSPKGVKgsGSVLLNGMPID---AKEMRAISAYV-QQDDLFipT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 LSIRDN------FKMlyenitDEEIYKSLENVYLLDFVNQVGL----DYIVGNDGNK--LSGGQKHRLQLAICLAKQKDI 488
Cdd:TIGR00955 114 LTVREHlmfqahLRM------PRRVTKKEKRERVDEVLQALGLrkcaNTRIGVPGRVkgLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 489 ILLDEPTAGLDIKTTNNICSQLMEKYQK-QTMIVTSHDIS--LLRFFDDIIICGEEKIIEQG 547
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLAQKgKTIICTIHQPSseLFELFDKIILMAEGRVAYLG 249
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
335-525 |
4.07e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.05 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYD-KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNI----------FIQGKNYDDLAEK 403
Cdd:PRK15064 320 LEVENLTKGFDnGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenanigyYAQDHAYDFENDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 404 SIREHFAVAFQEHHIfNLSIRDNF-KMLYeniTDEEIYKSLENvylldfvnqvgldyivgndgnkLSGGQKHRLQLAICL 482
Cdd:PRK15064 400 TLFDWMSQWRQEGDD-EQAVRGTLgRLLF---SQDDIKKSVKV----------------------LSGGEKGRMLFGKLM 453
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2674892663 483 AKQKDIILLDEPTAGLD---IKTTNNIcsqlMEKYqKQTMIVTSHD 525
Cdd:PRK15064 454 MQKPNVLVMDEPTNHMDmesIESLNMA----LEKY-EGTLIFVSHD 494
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
467-537 |
6.34e-08 |
|
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: 52.57 E-value: 6.34e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2674892663 467 KLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNIC---SQLMEKYQKqTMIVTSHDISLLRFFDDIII 537
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAAraiRRLSEEGKK-TALVVEHDLAVLDYLSDRIH 143
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
349-547 |
6.94e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 52.71 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLfyvlmrllyplkgnifiqgknyddlaeksIREHFAVAFQEHHIFNLSIRDNFK 428
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL-----------------------------VNEGLYASGKARLISFLPKFSRNK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 429 MLYenitdeeiykslenVYLLDFVNQVGLDYI-VGNDGNKLSGGQKHRLQLAICLAKQKD--IILLDEPTAGLDikttNN 505
Cdd:cd03238 62 LIF--------------IDQLQFLIDVGLGYLtLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH----QQ 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 506 ICSQLMEKY-----QKQTMIVTSHDISLLRFFDDIIICGE------EKIIEQG 547
Cdd:cd03238 124 DINQLLEVIkglidLGNTVILIEHNLDVLSSADWIIDFGPgsgksgGKVVFSG 176
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
350-534 |
7.80e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 54.33 E-value: 7.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 350 KDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEK---SIREHFAVAFQEhHIFNLS---- 422
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDewrAVRSDIQMIFQD-PLASLNprmt 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 ----IRDNFKMLYENITDEEIYKSLENVYLldfvnQVGLdyiVGNDGNK----LSGGQKHRLQLAICLAKQKDIILLDEP 494
Cdd:PRK15079 117 igeiIAEPLRTYHPKLSRQEVKDRVKAMML-----KVGL---LPNLINRypheFSGGQCQRIGIARALILEPKLIICDEP 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2674892663 495 TAGLDIkttnNICSQ---LMEKYQKQ---TMIVTSHDISLLRFFDD 534
Cdd:PRK15079 189 VSALDV----SIQAQvvnLLQQLQREmglSLIFIAHDLAVVKHISD 230
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
335-530 |
1.05e-07 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 53.27 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDL--AYGYDKVLlKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYD------------DL 400
Cdd:COG4598 9 LEVRDLhkSFGDLEVL-KGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgelvpaDR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 401 AE-KSIREHFAVAFQEhhiFNL----SIRdnfkmlyENIT-----------DEEIYKSLEnvyLLDfvnQVGL----DYI 460
Cdd:COG4598 88 RQlQRIRTRLGMVFQS---FNLwshmTVL-------ENVIeapvhvlgrpkAEAIERAEA---LLA---KVGLadkrDAY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 461 VGNdgnkLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD----------IKttnnicsQLMEkyQKQTMIVTSHDISLLR 530
Cdd:COG4598 152 PAH----LSGGQQQRAAIARALAMEPEVMLFDEPTSALDpelvgevlkvMR-------DLAE--EGRTMLVVTHEMGFAR 218
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
349-498 |
1.61e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.16 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLlYP---LKGNIFIQGKnydDLAEKSIREH----FAVAFQEHHIF-N 420
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPhgtYEGEIIFEGE---ELQASNIRDTeragIAIIHQELALVkE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 LSIRDNFKMLYE-----NITDEEIYksLENVYLLdfvNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:PRK13549 97 LSVLENIFLGNEitpggIMDYDAMY--LRAQKLL---AQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
...
gi 2674892663 496 AGL 498
Cdd:PRK13549 172 ASL 174
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
349-499 |
4.09e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 52.71 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLfyvlMRLL---YPL-KGNIFIQGKNYDDLAEKSIREH-FAVAFQEHHIF-NLS 422
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTL----MKILsgvYQPdSGEILLDGEPVRFRSPRDAQAAgIAIIHQELNLVpNLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 IRDNFKMLYEN-----ITDEEIYKSLENvyLLDfvnQVGLDY----IVGNdgnkLSGGQKHRLQLAICLAKQKDIILLDE 493
Cdd:COG1129 96 VAENIFLGREPrrgglIDWRAMRRRARE--LLA---RLGLDIdpdtPVGD----LSVAQQQLVEIARALSRDARVLILDE 166
|
....*.
gi 2674892663 494 PTAGLD 499
Cdd:COG1129 167 PTASLT 172
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
340-530 |
4.26e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.65 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 340 LAYGyDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLM--------RLLY------------PLKGnifIQGKNYDD 399
Cdd:PRK11147 11 LSFS-DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNgevllddgRIIYeqdlivarlqqdPPRN---VEGTVYDF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 400 LAE--KSIREHFAvafQEHHIFNLSIRD-NFKMLYENitdEEIYKSLE--NVYLLDF-VNQV----GLDyivgNDG--NK 467
Cdd:PRK11147 87 VAEgiEEQAEYLK---RYHDISHLVETDpSEKNLNEL---AKLQEQLDhhNLWQLENrINEVlaqlGLD----PDAalSS 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 468 LSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTnnicsQLMEKYQKQ---TMIVTSHDISLLR 530
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETI-----EWLEGFLKTfqgSIIFISHDRSFIR 217
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
349-525 |
5.74e-07 |
|
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: 50.90 E-value: 5.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLfyvlMRLLY----PLKGNIFIQ-GKNYDDLAEKSirehfavafqEHHIfnLSI 423
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTL----LKCIYgnylPDSGSILVRhDGGWVDLAQAS----------PREI--LAL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 424 RDNfkmlyenitdeEI-YKS-----LENVYLLDFVNQVGLDYIVGNDG-----------------------NKLSGGQKH 474
Cdd:COG4778 91 RRR-----------TIgYVSqflrvIPRVSALDVVAEPLLERGVDREEarararellarlnlperlwdlppATFSGGEQQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2674892663 475 RLQLAICLAKQKDIILLDEPTAGLDIKTTNNICsQLMEKYQKQ--TMIVTSHD 525
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVV-ELIEEAKARgtAIIGIFHD 211
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
334-501 |
7.31e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 51.38 E-value: 7.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 334 QLLLKDLAYGYD-KVL-LKDINLSIKKGNKTLIVGTSGCGKSTlfyvLMRLLYPLK----GNIFIQGKNYDDL--AEKSI 405
Cdd:PRK11650 3 GLKLQAVRKSYDgKTQvIKGIDLDVADGEFIVLVGPSGCGKST----LLRMVAGLEritsGEIWIGGRVVNELepADRDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 406 rehfAVAFQEH----HifnLSIRDNfkMLY---------ENITD--EEIYKSLENVYLLDfvnqvgldyivgNDGNKLSG 470
Cdd:PRK11650 79 ----AMVFQNYalypH---MSVREN--MAYglkirgmpkAEIEErvAEAARILELEPLLD------------RKPRELSG 137
|
170 180 190
....*....|....*....|....*....|.
gi 2674892663 471 GQKHRLQLAICLAKQKDIILLDEPTAGLDIK 501
Cdd:PRK11650 138 GQRQRVAMGRAIVREPAVFLFDEPLSNLDAK 168
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
346-536 |
8.74e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 48.90 E-value: 8.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 346 KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFyvlmrllyplkgnifiqgknyDDLAeksirehFAVAFQEHHIFnlsird 425
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTIL---------------------DAIG-------LALGGAQSATR------ 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 426 nfKMLYENITDEEIYKSLENVYLLDfvnqvgldyivgndgnKLSGGQKHRLQLAICLAKQK----DIILLDEPTAGLDIK 501
Cdd:cd03227 54 --RRSGVKAGCIVAAVSAELIFTRL----------------QLSGGEKELSALALILALASlkprPLYILDEIDRGLDPR 115
|
170 180 190
....*....|....*....|....*....|....*.
gi 2674892663 502 TTNNICSQLMEKYQKQ-TMIVTSHDISLLRFFDDII 536
Cdd:cd03227 116 DGQALAEAILEHLVKGaQVIVITHLPELAELADKLI 151
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
341-534 |
1.02e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.66 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 341 AYGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQgKNY-----------DDlaEKSIREHF 409
Cdd:PRK11819 15 VVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPA-PGIkvgylpqepqlDP--EKTVRENV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 410 AVAFQEhhIFNLsiRDNFKMLYENITDEEIYKS--------LENvyLLDFVNQVGLDYIV------------GNDGNKLS 469
Cdd:PRK11819 92 EEGVAE--VKAA--LDRFNEIYAAYAEPDADFDalaaeqgeLQE--IIDAADAWDLDSQLeiamdalrcppwDAKVTKLS 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 470 GGQKHRLqlAIC--LAKQKDIILLDEPTAGLDIKTTnnicsQLMEKYQKQ---TMIVTSHDisllRFFDD 534
Cdd:PRK11819 166 GGERRRV--ALCrlLLEKPDMLLLDEPTNHLDAESV-----AWLEQFLHDypgTVVAVTHD----RYFLD 224
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
335-499 |
1.46e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.10 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 335 LLLKDLAYGYDKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIrehfavAFQ 414
Cdd:PRK13541 2 LSLHQLQFNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC------TYI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 415 EHHI---FNLSIRDNFKMLyenitdEEIYKSLENVYLLdfVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILL 491
Cdd:PRK13541 76 GHNLglkLEMTVFENLKFW------SEIYNSAETLYAA--IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLL 147
|
....*...
gi 2674892663 492 DEPTAGLD 499
Cdd:PRK13541 148 DEVETNLS 155
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
348-499 |
1.46e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.39 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 348 LLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLM--RLLYPLKGNIFIQG--KNYDDLA------EKSIREHFAVAFQEHH 417
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAgrKTGGYIEGDIRISGfpKKQETFArisgycEQNDIHSPQVTVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 418 IFNLSIRdnfkmLYENITDEEIYKSLENVylLDFVNQVGL-DYIVGNDG-NKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:PLN03140 975 IYSAFLR-----LPKEVSKEEKMMFVDEV--MELVELDNLkDAIVGLPGvTGLSTEQRKRLTIAVELVANPSIIFMDEPT 1047
|
....
gi 2674892663 496 AGLD 499
Cdd:PLN03140 1048 SGLD 1051
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
333-498 |
1.46e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 49.49 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 333 VQLLLKDLAYGYDKV-LLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSI-REHFA 410
Cdd:PRK11614 4 VMLSFDKVSAHYGKIqALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKImREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 411 VAFQEHHIFN-LSIRDNFKMLYENITDEEIYKSLENVYLLdFVNqvgLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDII 489
Cdd:PRK11614 84 IVPEGRRVFSrMTVEENLAMGGFFAERDQFQERIKWVYEL-FPR---LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
....*....
gi 2674892663 490 LLDEPTAGL 498
Cdd:PRK11614 160 LLDEPSLGL 168
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
352-547 |
1.50e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.51 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 352 INLSIKKGNKTLIVGTSGCGKSTLFYVLMRLL-YPLK---GNIFIQGKNYDDLAEKSIRE----HFAVAFQEHHI-FNLS 422
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdYPGRvmaEKLEFNGQDLQRISEKERRNlvgaEVAMIFQDPMTsLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 IRDNFKMLYENITDEEIYKSLENVYLLDFVNQVG-------LDyivgNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:PRK11022 106 YTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGipdpasrLD----VYPHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2674892663 496 AGLDIKTTNNICSQLMEKYQKQTM--IVTSHDISLL-RFFDDIIICGEEKIIEQG 547
Cdd:PRK11022 182 TALDVTIQAQIIELLLELQQKENMalVLITHDLALVaEAAHKIIVMYAGQVVETG 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
349-500 |
1.53e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 50.79 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNktlIVGTSG---CGKSTLFYVLMRLLYPLKGNIFIQGKnydDLAEKSIREhfA----VAF-----QEH 416
Cdd:COG1129 268 VRDVSFSVRAGE---ILGIAGlvgAGRTELARALFGADPADSGEIRLDGK---PVRIRSPRD--AiragIAYvpedrKGE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 417 HIF-NLSIRDNFkmlyeNITdeeIYKSLENVYLLDF--VNQVGLDYI-------------VGNdgnkLSGG--QKhrLQL 478
Cdd:COG1129 340 GLVlDLSIRENI-----TLA---SLDRLSRGGLLDRrrERALAEEYIkrlriktpspeqpVGN----LSGGnqQK--VVL 405
|
170 180
....*....|....*....|..
gi 2674892663 479 AICLAKQKDIILLDEPTAGLDI 500
Cdd:COG1129 406 AKWLATDPKVLILDEPTRGIDV 427
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
346-553 |
2.06e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.44 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 346 KVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLL--------YPLKGNIFIQGKNYDDL-AEKSIREHFAVAFQEH 416
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgARVTGDVTLNGEPLAAIdAPRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 417 HIFNLSIRDNFKM-LYEN--------ITDEEI-YKSLEnvylldfvnQVGLDYIVGNDGNKLSGGQKHRLQLAICLAK-- 484
Cdd:PRK13547 94 PAFAFSAREIVLLgRYPHarragaltHRDGEIaWQALA---------LAGATALVGRDVTTLSGGELARVQFARVLAQlw 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2674892663 485 -----QKD--IILLDEPTAGLDIKTTNNICSQLMEKYQKQTMIVTS--HDISL-LRFFDDIIICGEEKIIEQGNIKKLL 553
Cdd:PRK13547 165 pphdaAQPprYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAivHDPNLaARHADRIAMLADGAIVAHGAPADVL 243
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
353-525 |
2.22e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.28 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 353 NLSIK--KGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQ-----GKNYDDlaeksireHFAvaFQEHHIFNLSI-- 423
Cdd:PRK15064 19 NISVKfgGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpnerlGKLRQD--------QFA--FEEFTVLDTVImg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 424 ----------RDNFKMLYEnITDEEIYK--SLENVY---------------LLdfvnQVGLDyIVGNDG--NKLSGGQKH 474
Cdd:PRK15064 89 htelwevkqeRDRIYALPE-MSEEDGMKvaDLEVKFaemdgytaearagelLL----GVGIP-EEQHYGlmSEVAPGWKL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 475 RLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQLMEKyqKQTMIVTSHD 525
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNER--NSTMIIISHD 211
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
349-529 |
3.71e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.85 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAE---KSIREHFAVAFQE-------HHI 418
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQDpyasldpRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 419 FNLSIRDNFK---MLYENITDEEIYKSLENVYLLDfvnQVGLDYivgndGNKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:PRK10261 420 VGDSIMEPLRvhgLLPGKAAAARVAWLLERVGLLP---EHAWRY-----PHEFSGGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190
....*....|....*....|....*....|....*..
gi 2674892663 496 AGLDIKTTNNICSQLMEkYQKQ---TMIVTSHDISLL 529
Cdd:PRK10261 492 SALDVSIRGQIINLLLD-LQRDfgiAYLFISHDMAVV 527
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
348-547 |
6.18e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.46 E-value: 6.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 348 LLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLM-----------RLLY---------PLKGNIFIQ-------------- 393
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAgkldpslkvsgEITYngyrlnefvPRKTSAYISqndvhvgvmtvket 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 394 ----------GKNYDDLAEKSIREHFAVAFQEHHIfnlsirdnfKMLYENITDEEIYKSLENVYLLDFVnqvGLDY---- 459
Cdd:PLN03140 260 ldfsarcqgvGTRYDLLSELARREKDAGIFPEAEV---------DLFMKATAMEGVKSSLITDYTLKIL---GLDIckdt 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 460 IVGNDGNK-LSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNI--CSQLMEKYQKQTMIVtshdiSLLR------ 530
Cdd:PLN03140 328 IVGDEMIRgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIvkCLQQIVHLTEATVLM-----SLLQpapetf 402
|
250
....*....|....*...
gi 2674892663 531 -FFDDIIICGEEKIIEQG 547
Cdd:PLN03140 403 dLFDDIILLSEGQIVYQG 420
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
347-530 |
7.08e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.89 E-value: 7.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 347 VLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLaeKSIREH----FAVAfQEHHIF-NL 421
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL--TPAKAHqlgiYLVP-QEPLLFpNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 422 SIRDNfkMLYENITDEEIYKSLENvyLLDFVN-QVGLDYIVGNdgnkLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDI 500
Cdd:PRK15439 102 SVKEN--ILFGLPKRQASMQKMKQ--LLAALGcQLDLDSSAGS----LEVADRQIVEILRGLMRDSRILILDEPTASLTP 173
|
170 180 190
....*....|....*....|....*....|.
gi 2674892663 501 KTTNNICSQLMEKYQKQTMIV-TSHDISLLR 530
Cdd:PRK15439 174 AETERLFSRIRELLAQGVGIVfISHKLPEIR 204
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
389-561 |
9.51e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.86 E-value: 9.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 389 NIFIQGKNYDDLAEKSIREhfavafqEHHIFNLSIRDNFKmlyENITDE---EIYKSLEnvYLLDfvnqVGLDYI-VGND 464
Cdd:TIGR00630 422 AVTVGGKSIADVSELSIRE-------AHEFFNQLTLTPEE---KKIAEEvlkEIRERLG--FLID----VGLDYLsLSRA 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 465 GNKLSGGQKHRLQLAICLAKQKDIIL--LDEPTAGLDIKTTNNICSQLME-KYQKQTMIVTSHDISLLRFFDDII----- 536
Cdd:TIGR00630 486 AGTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQRDNRRLINTLKRlRDLGNTLIVVEHDEDTIRAADYVIdigpg 565
|
170 180 190
....*....|....*....|....*....|.
gi 2674892663 537 --ICGEEkIIEQGNIKKLLLREDS----YLN 561
Cdd:TIGR00630 566 agEHGGE-VVASGTPEEILANPDSltgqYLS 595
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
346-549 |
1.08e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.24 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 346 KVLLKDINLSIKKGNKTLIVGTSGCGKSTLfyvlmrlLYPLKGNIFIQGKNYddlaekSIREHFAVAF--QEHHIFNLSI 423
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTL-------LALLKNEISADGGSY------TFPGNWQLAWvnQETPALPQPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 424 RDnfkmlYENITDEEiYKSLENVylLDFVNQVgldyivgNDGN-------KL---------------------------- 468
Cdd:PRK10636 81 LE-----YVIDGDRE-YRQLEAQ--LHDANER-------NDGHaiatihgKLdaidawtirsraasllhglgfsneqler 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 469 -----SGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTnnicsQLMEKYQKQ---TMIVTSHDisllRFFDDIIIcge 540
Cdd:PRK10636 146 pvsdfSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAV-----IWLEKWLKSyqgTLILISHD----RDFLDPIV--- 213
|
250
....*....|.
gi 2674892663 541 EKI--IEQGNI 549
Cdd:PRK10636 214 DKIihIEQQSL 224
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
358-537 |
1.47e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.06 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 358 KGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIqgknyddlaeksirehfavafqehhifnlsirdnfkmlyenITDE 437
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-----------------------------------------IDGE 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 438 EIYKSLENVYLLDfvnqvgldyIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQL------- 510
Cdd:smart00382 40 DILEEVLDQLLLI---------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllll 110
|
170 180 190
....*....|....*....|....*....|...
gi 2674892663 511 MEKYQKQTMIVTSHDIS------LLRFFDDIII 537
Cdd:smart00382 111 LKSEKNLTVILTTNDEKdlgpalLRRRFDRRIV 143
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
345-547 |
2.93e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 46.80 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 345 DKVLLKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYP--LKGNIFIQGKNyddLAEKSIREHFAVAFQEHHIFNLS 422
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGnnFTGTILANNRK---PTKQILKRTGFVTQDDILYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 423 IRDNFKM-----LYENITDEEIYKSLENVylldfVNQVGL----DYIVGNDGNK-LSGGQKHRLQLAICLAKQKDIILLD 492
Cdd:PLN03211 157 VRETLVFcsllrLPKSLTKQEKILVAESV-----ISELGLtkceNTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2674892663 493 EPTAGLDIKTTNNICSQLMEKYQKQTMIVTS-HDIS--LLRFFDDIIICGEEKIIEQG 547
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLAQKGKTIVTSmHQPSsrVYQMFDSVLVLSEGRCLFFG 289
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
455-541 |
4.13e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 455 VGLDYI-VGNDGNKLSGGQKHRLQLAICL---AKQKDIILLDEPTAGL---DIKTTNNICSQLMekYQKQTMIVTSHDIS 527
Cdd:PRK00635 796 LGLDYLpLGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLhthDIKALIYVLQSLT--HQGHTVVIIEHNMH 873
|
90
....*....|....
gi 2674892663 528 LLRFFDDIIICGEE 541
Cdd:PRK00635 874 VVKVADYVLELGPE 887
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
449-541 |
4.86e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 449 LDFVNQVGLDYIV-GNDGNKLSGGQKHRLQLAICLAKQ-KDII-LLDEPTAGLDIKTTNNICSQLMEKY-QKQTMIVTSH 524
Cdd:PRK00635 1368 LTFIDKVGLSYITlGQEQDTLSDGEHYRLHLAKKISSNlTDIIyLLEDPLSGLHPQDAPTLLQLIKELVtNNNTVIATDR 1447
|
90
....*....|....*..
gi 2674892663 525 DISLLRFFDDIIICGEE 541
Cdd:PRK00635 1448 SGSLAEHADHLIHLGPG 1464
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
16-259 |
6.22e-05 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 45.23 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 16 LLLAILVGTISTLSSISLMGLSAWLIASAALQPPLYVLSLAIVGVRFCGVMRAVFRYLERYFTHKVGFSLFTSFRVFVLI 95
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 96 KIIKaLP--FKQQTENGDAFDLIVNAVDNLRDSFLRFFLPPIITTISVFILSIWFFLYSYDLMILLISSWLIFMIVIPYM 173
Cdd:cd07346 81 HLQR-LSlsFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 174 ---IWRRYLKLKKHKFLLTQEIIEFYEGNRELSFYNYDKYRLKNINHSIEQYQQYQQNLFKLKLKVNLCSEFIMGAYLVI 250
Cdd:cd07346 160 rrrIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTAL 239
|
....*....
gi 2674892663 251 CLAISIYLV 259
Cdd:cd07346 240 VLLYGGYLV 248
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
349-503 |
7.29e-05 |
|
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: 45.59 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLlYP---LKGNIFIQGKnydDLAEKSIREH----FAVAFQEHHIF-N 420
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPhgtWDGEIYWSGS---PLKASNIRDTeragIVIIHQELTLVpE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 421 LSIRDNFKMLYEnIT-------DEEIYKSLENVylldfVNQVGLDYI-VGNDGNKLSGGQKHRLQLAICLAKQKDIILLD 492
Cdd:TIGR02633 93 LSVAENIFLGNE-ITlpggrmaYNAMYLRAKNL-----LRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQARLLILD 166
|
170
....*....|.
gi 2674892663 493 EPTAGLDIKTT 503
Cdd:TIGR02633 167 EPSSSLTEKET 177
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
349-498 |
1.11e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 45.02 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTlfyvLMRLLY----PLKGNIFIQGKnyddlaEKSIRE-HFAVA------FQeHh 417
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKST----LMKILYglyqPDSGEILIDGK------PVRIRSpRDAIAlgigmvHQ-H- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 418 iFnlsirdnfkMLYENITdeeiykSLENVYL-------------------LDFVNQVGL----DYIVGNdgnkLSGGQKH 474
Cdd:COG3845 89 -F---------MLVPNLT------VAENIVLgleptkggrldrkaarariRELSERYGLdvdpDAKVED----LSVGEQQ 148
|
170 180
....*....|....*....|....
gi 2674892663 475 RLQLAICLAKQKDIILLDEPTAGL 498
Cdd:COG3845 149 RVEILKALYRGARILILDEPTAVL 172
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
394-501 |
1.28e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.02 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 394 GKNYDDLAEKSIREhfAVAFqehhifnlsirdnFkmlyENITdeEIYKSLEnvYLLDfvnqVGLDYI-VGNDGNKLSGGQ 472
Cdd:COG0178 779 GKNIADVLDMTVEE--ALEF-------------F----ENIP--KIARKLQ--TLQD----VGLGYIkLGQPATTLSGGE 831
|
90 100 110
....*....|....*....|....*....|....*
gi 2674892663 473 KHRLQLAICLAK---QKDIILLDEPTAGL---DIK 501
Cdd:COG0178 832 AQRVKLASELSKrstGKTLYILDEPTTGLhfhDIR 866
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
450-552 |
1.93e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.96 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 450 DFVNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNICSQL--MEKYQKQTMIVTSHDIS 527
Cdd:NF000106 127 ELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVrsMVRDGATVLLTTQYMEE 206
|
90 100
....*....|....*....|....*
gi 2674892663 528 LLRFFDDIIICGEEKIIEQGNIKKL 552
Cdd:NF000106 207 AEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
349-551 |
3.21e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.88 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGknyddlaeksirEHFAVAFQEHHIFNLSIRDN-- 426
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------------EVSVIAISAGLSGQLTGIENie 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 427 FKMLYENITDEEIYKSLENVY----LLDFVNQvgldyivgnDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKT 502
Cdd:PRK13546 108 FKMLCMGFKRKEIKAMTPKIIefseLGEFIYQ---------PVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTF 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2674892663 503 TNNICSQLME-KYQKQTMIVTSHDISLLRFFddiiiCGEEKIIEQGNIKK 551
Cdd:PRK13546 179 AQKCLDKIYEfKEQNKTIFFVSHNLGQVRQF-----CTKIAWIEGGKLKD 223
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
351-547 |
4.93e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 42.22 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 351 DINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGK--NYDDLAEKSIREHFAVAFQEHHIFNLSIRDNFK 428
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgQLRDLYALSEAERRRLLRTEWGFVHQHPRDGLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 429 ML------------------YENITDEEiykslenvylLDFVNQVGLDYI-VGNDGNKLSGGQKHRLQLAICLAKQKDII 489
Cdd:PRK11701 104 MQvsaggnigerlmavgarhYGDIRATA----------GDWLERVEIDAArIDDLPTTFSGGMQQRLQIARNLVTHPRLV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2674892663 490 LLDEPTAGLDIKTTN---NICSQLMEKYQKQTMIVTsHDISLLRFFDD-IIICGEEKIIEQG 547
Cdd:PRK11701 174 FMDEPTGGLDVSVQArllDLLRGLVRELGLAVVIVT-HDLAVARLLAHrLLVMKQGRVVESG 234
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
449-501 |
6.60e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.75 E-value: 6.60e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 449 LDFVNQVGLDYI-VGNDGNKLSGGQKHRLQLAICLAKQ---KDIILLDEPTAGL---DIK 501
Cdd:PRK00349 811 LQTLVDVGLGYIkLGQPATTLSGGEAQRVKLAKELSKRstgKTLYILDEPTTGLhfeDIR 870
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
468-565 |
7.27e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 42.35 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 468 LSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNIcSQLMEKYQKQ--TMIVTSHDISLLRFFDDIIIcgeekIIE 545
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDI-YQLIRSIAAQnvAVLFISSDLEEIEQMADRVL-----VMH 477
|
90 100
....*....|....*....|
gi 2674892663 546 QGNIKKLLLREDSYLNKLIR 565
Cdd:PRK15439 478 QGEISGALTGAAINVDTIMR 497
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
349-552 |
1.02e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.02 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDDLAEKSIREH-FAVAFQE-HHIFNLSIRDN 426
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENgISMVHQElNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 427 F-------KMLYenITDEEIYKSLENVYlldfvNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLD 499
Cdd:PRK10982 94 MwlgryptKGMF--VDQDKMYRDTKAIF-----DELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2674892663 500 IKTTNNICSqLMEKYQKQ--TMIVTSHDI-SLLRFFDDIIICGEEKIIEQGNIKKL 552
Cdd:PRK10982 167 EKEVNHLFT-IIRKLKERgcGIVYISHKMeEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
358-391 |
1.04e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.58 E-value: 1.04e-03
10 20 30
....*....|....*....|....*....|....
gi 2674892663 358 KGNkTLIVGTSGCGKSTLFYVLMRLLYPLKGNIF 391
Cdd:pfam13555 22 RGN-TLLTGPSGSGKSTLLDAIQTLLVPAKRARF 54
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
21-175 |
1.40e-03 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 40.88 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 21 LVGTISTLSSISLMGLSAWLIASA-------ALQPPLYVLSLAIVGVrfcGVMRAVFRYLERYFTHKVGFSLFTSFRVFV 93
Cdd:cd18542 2 LLAILALLLATALNLLIPLLIRRIidsviggGLRELLWLLALLILGV---ALLRGVFRYLQGYLAEKASQKVAYDLRNDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 94 LIKIIKaLPF----KQQTenGDAFDLIVNAVDNLRDsFLRFFLPPIITTISVFILSIWfflysydlmILLISSW---LIF 166
Cdd:cd18542 79 YDHLQR-LSFsfhdKART--GDLMSRCTSDVDTIRR-FLAFGLVELVRAVLLFIGALI---------IMFSINWkltLIS 145
|
....*....
gi 2674892663 167 MIVIPYMIW 175
Cdd:cd18542 146 LAIIPFIAL 154
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
351-543 |
1.44e-03 |
|
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: 41.35 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 351 DINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLlYPLK--GNIFIQGKNYD-DLAEKSIREHFAVAFQEH----------- 416
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGA-YPGKfeGNVFINGKPVDiRNPAQAIRAGIAMVPEDRkrhgivpilgv 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 417 -HIFNLSIRDNFKMLYENITDEEIYKSLENVYLLDfVNQVGLDYIVGndgnKLSGGQKHRLQLAICLAKQKDIILLDEPT 495
Cdd:TIGR02633 357 gKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLK-VKTASPFLPIG----RLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2674892663 496 AGLDIKTTNNIcSQLMEKYQKQ--TMIVTSHDIS-LLRFFDDIIICGEEKI 543
Cdd:TIGR02633 432 RGVDVGAKYEI-YKLINQLAQEgvAIIVVSSELAeVLGLSDRVLVIGEGKL 481
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
15-280 |
1.80e-03 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 40.32 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 15 SLLLAILVGTISTLSSISLMGLSAWLIASAALQP-PLYVLSLAIVGVrfcGVMRAVFRYLERYFTHKVGFSLFTSFRVFV 93
Cdd:pfam00664 4 AILLAILSGAISPAFPLVLGRILDVLLPDGDPETqALNVYSLALLLL---GLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 94 LIKIIKA-LPFKQQTENGDAFDLIVNAVDNLRDSFLRFFLPPIITTISVFILSIWFFLYSYDLMILLISSWLIFMIVIPY 172
Cdd:pfam00664 81 FKKILRQpMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 173 ---MIWRRYLKLKKHKFLLTQEIIEFYEGNRELSFYNYDKYRLKNINHSIEQYQQYQQNLFKLKLKVNLCSEFIMGAYLV 249
Cdd:pfam00664 161 fakILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|.
gi 2674892663 250 ICLAISIYLVNTQDFNPIMAITIIlTYQAVL 280
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFL-SLFAQL 270
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
437-524 |
1.86e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 437 EEIYKSLEnvyLLDFVNQ--------VGLDY---IVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNN 505
Cdd:PLN03073 306 EEIYKRLE---LIDAYTAearaasilAGLSFtpeMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLW 382
|
90
....*....|....*....
gi 2674892663 506 ICSQLMeKYQKqTMIVTSH 524
Cdd:PLN03073 383 LETYLL-KWPK-TFIVVSH 399
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
16-175 |
1.93e-03 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 40.48 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 16 LLLAILVGTISTLSSISLMGLSAWLIASAALQPP---LYVLSLAIVGVrfcGVMRAVFRYLERYFTHKVGFSLFTSFRVF 92
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDleaLLLVPLAIIGL---FLLRGLASYLQTYLMAYVGQRVVRDLRND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 93 VLIKIIKA-LPFKQQTENGDAFDLIVNAVDNLRDSFLRFFLPPIITTISVFILSIWFFLYSYDLMillisswLIFMIVIP 171
Cdd:cd18552 78 LFDKLLRLpLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLT-------LIALVVLP 150
|
....
gi 2674892663 172 YMIW 175
Cdd:cd18552 151 LAAL 154
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
364-526 |
2.00e-03 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 41.15 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 364 IVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKnyddlaekSIREHFAVAFQehhifNLSIRDNFKMLYENITDEE---IY 440
Cdd:TIGR01257 1970 LLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK--------SILTNISDVHQ-----NMGYCPQFDAIDDLLTGREhlyLY 2036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 441 KSLENVYLLDF-------VNQVGLDYIVGNDGNKLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTT----NNICSQ 509
Cdd:TIGR01257 2037 ARLRGVPAEEIekvanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARrmlwNTIVSI 2116
|
170
....*....|....*..
gi 2674892663 510 LMEkyqKQTMIVTSHDI 526
Cdd:TIGR01257 2117 IRE---GRAVVLTSHSM 2130
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
457-553 |
2.92e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 40.37 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 457 LDYIVGNdgnkLSGGQKHRLQLAICLAKQKDIILLDEPTAGLDIKTTNNIcSQLMEKYQKQTM---IVTSHDISLLRFFD 533
Cdd:PRK10762 389 MEQAIGL----LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEI-YQLINQFKAEGLsiiLVSSEMPEVLGMSD 463
|
90 100
....*....|....*....|....*
gi 2674892663 534 DIIICGEEKI-----IEQGNIKKLL 553
Cdd:PRK10762 464 RILVMHEGRIsgeftREQATQEKLM 488
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
390-561 |
4.23e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.06 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 390 IFIQGKNYDDLAEKSIREhfAVAFQEhhifNLSIRDNFKMLYENITdEEIYKSLEnvylldFVNQVGLDYI-VGNDGNKL 468
Cdd:PRK00349 424 VKVGGKNIGEVSELSIGE--ALEFFE----NLKLSEQEAKIAEPIL-KEIRERLK------FLVDVGLDYLtLSRSAGTL 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 469 SGGQKHRlqlaICLAKQkdI------IL--LDEPTAGL---D----IKTTNNicsqLMEKyqKQTMIVTSHDISLLRFFD 533
Cdd:PRK00349 491 SGGEAQR----IRLATQ--IgsgltgVLyvLDEPSIGLhqrDndrlIETLKH----LRDL--GNTLIVVEHDEDTIRAAD 558
|
170 180 190
....*....|....*....|....*....|....*...
gi 2674892663 534 DII-I---CGEE--KIIEQGNIKKLLLREDS----YLN 561
Cdd:PRK00349 559 YIVdIgpgAGVHggEVVASGTPEEIMKNPNSltgqYLS 596
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
349-537 |
8.84e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 38.94 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 349 LKDINLSIKKGNKTLIVGTSGCGKSTLFYVLMRLLYPLKGNIFIQGKNYDD-LAEKSIREHFAVAFQEHH---IF-NLSI 423
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhNANEAINHGFALVTEERRstgIYaYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674892663 424 rdNFKMLYENITDeeiYKS----LENVYLLDFVNQVGLDYIVGNDGNK-----LSGGQKHRLQLAICLAKQKDIILLDEP 494
Cdd:PRK10982 344 --GFNSLISNIRN---YKNkvglLDNSRMKSDTQWVIDSMRVKTPGHRtqigsLSGGNQQKVIIGRWLLTQPEILMLDEP 418
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2674892663 495 TAGLDIKTTNNICSQLME--KYQKQTMIVTSHDISLLRFFDDIII 537
Cdd:PRK10982 419 TRGIDVGAKFEIYQLIAElaKKDKGIIIISSEMPELLGITDRILV 463
|
|
|